|
Name |
Accession |
Description |
Interval |
E-value |
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
20-538 |
0e+00 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 642.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 20 MIRHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQL 99
Cdd:cd12119 1 LLEHAARLHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLD-VKGWVVMTDKpADEIETTLENVVFYEDLIKDKPDTYDWPV 178
Cdd:cd12119 81 NPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPtVEHVVVMTDD-AAMPEPAGVGVLAYEELLAAESPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFD--DTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGK 256
Cdd:cd12119 160 FDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSesDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEFgaIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPqPPDLSGVRLVSGSSEPPLSMMRGFKEItGADVIHGYGATE 336
Cdd:cd12119 240 YLDPAS--LAELIEREGVTFAAGVPTVWQGLLDHLEANG-RDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 337 TTPLATTNWHIKPGLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQLPDNSERFL 416
Cdd:cd12119 316 TSPLGTVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 -DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEV 495
Cdd:cd12119 396 eDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATV 475
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1949187543 496 TRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd12119 476 TAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
12-537 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 596.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 12 SYQLNTTSMIRHAATVFGEQEVVYRnsDGswGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPG 91
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYF--DG--RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 92 LAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLD-VKGWVVMTDKPADEietTLENVVFYEDLIKDK 170
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAP---LAPEVGEYEELLAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 171 PDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAK 250
Cdd:PRK06187 156 SDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 251 LVLPGKFaaeEFGAIAKAFIAEKVTLANGAPAIFAPMLAmmKDMPQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVI 329
Cdd:PRK06187 236 QVIPRRF---DPENLLDLIETERVTFFFAVPTIWQMLLK--APRAYFVDFSSLRLViYGGAALPPALLREFKEKFGIDLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTPLATTNWhikpgLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQLP 409
Cdd:PRK06187 311 QGYGMTETSPVVSVLP-----PEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVV 488
Cdd:PRK06187 386 EATAETIdGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1949187543 489 AEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK06187 466 LKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
12-542 |
4.88e-171 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 494.61 E-value: 4.88e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 12 SYQLNTTSMIRHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPG 91
Cdd:PRK07008 7 DMPLLISSLIAHAARHAGDTEIVSRRVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 92 LAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKL-DVKGWVVMTDK---PADEIEttlenVVFYEDLI 167
Cdd:PRK07008 87 SGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQCpNVKGWVAMTDAahlPAGSTP-----LLCYETLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 168 KDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLA--ALGASFDDTIMPITPMFHVLSWGFPQNAV 245
Cdd:PRK07008 162 GAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRSTVLHAYGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 246 AAGAKLVLPGKfaAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDmpqppdlSGVRL------VSGSSEPPLSMMRG 319
Cdd:PRK07008 242 LTGAKLVLPGP--DLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMRE-------AGLRFstlrrtVIGGSACPPAMIRT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 320 FKEITGADVIHGYGATETTPLATTNWHIKPGLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGP 399
Cdd:PRK07008 313 FEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRELPWDGKAFGDLQVRGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 400 WITESYFQlpDNSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKW 479
Cdd:PRK07008 393 WVIDRYFR--GDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKW 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 480 QERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWED 542
Cdd:PRK07008 471 DERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
20-542 |
2.77e-150 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 441.88 E-value: 2.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 20 MIRHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQL 99
Cdd:PRK06018 15 IIDHAARIHGNREVVTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKL-DVKGWVVMTDKpADEIETTLENVVFYEDLIKDKPDTYDWPV 178
Cdd:PRK06018 95 NPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLpSVERYVVLTDA-AHMPQTTLKNAVAYEEWIAEADGDFAWKT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLA--ALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGk 256
Cdd:PRK06018 174 FDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNgdALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPG- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 fAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMM-KDMPQPPDLSGVrlVSGSSEPPLSMMRGFKEItGADVIHGYGAT 335
Cdd:PRK06018 253 -AKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMeKEGLKLPHLKMV--VCGGSAMPRSMIKAFEDM-GVEVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 ETTPLATTNwHIKPGL-DMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQLPDNser 414
Cdd:PRK06018 329 EMSPLGTLA-ALKPPFsKLPGDARLDVLQKQGYPPFGVEMKITDDAGKELPWDGKTFGRLKVRGPAVAAAYYRVDGE--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 415 FLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG 492
Cdd:PRK06018 405 ILDddGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPG 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1949187543 493 AEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWED 542
Cdd:PRK06018 485 ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
18-545 |
1.99e-136 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 403.04 E-value: 1.99e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 18 TSMIRHAATVFGEQEVVYRnsdgSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATML 97
Cdd:COG0318 2 ADLLRRAAARHPDRPALVF----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLNLRLAPEDLAYVVSHSKSDWIFVdesllpvaealapkldvkgwvvmtdkpadeiettlenvvfyedlikdkpdtydwp 177
Cdd:COG0318 78 PLNPRLTAEELAYILEDSGARALVT------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 vvdektaAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQN-AVAAGAKLVLPGK 256
Cdd:COG0318 103 -------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLaPLLAGATLVLLPR 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEFgaiAKAFIAEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGAT 335
Cdd:COG0318 176 FDPERV---LELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPlPPELLERFEERFGVRIVEGYGLT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 ETTPLATTNWhikpgldmdEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSER 414
Cdd:COG0318 251 ETSPVVTVNP---------EDPGERRPGSVGRPLPGVEVRIVDEDGRELPPG--EVGEIVVRGPNVMKGYWNDPEaTAEA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 415 FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAE 494
Cdd:COG0318 320 FRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAE 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 495 VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWEDAEA 545
Cdd:COG0318 400 LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
15-538 |
6.84e-117 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 354.30 E-value: 6.84e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 15 LNTTSMIRHAATVFGEQ-EVVYRNSdgswgRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLA 93
Cdd:cd12118 4 LTPLSFLERAAAVYPDRtSIVYGDR-----RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 94 ATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLpvaealapkldvkgwvvmtdkpadeiettlenvvfYEDLIKDKPDT 173
Cdd:cd12118 79 AVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE-----------------------------------YEDLLAEGDPD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 174 YDW-PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLV 252
Cdd:cd12118 124 FEWiPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LPGKFAAEE-FGAIAKafiaEKVTLANGAPAIFApMLAMMKDMPQPPDLSGVRLVSGSSEPPLSMMRGFKEItGADVIHG 331
Cdd:cd12118 204 CLRKVDAKAiYDLIEK----HKVTHFCGAPTVLN-MLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLATTN-WhiKPGLD-MDEEERWDFKRYQGLPVIGVE-VKVVDP-TGEELPRDGKSMGEVLMRGPWITESYFQ 407
Cdd:cd12118 278 YGLTETYGPATVCaW--KPEWDeLPTEERARLKARQGVRYVGLEeVDVLDPeTMKPVPRDGKTIGEIVFRGNIVMKGYLK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 408 LPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAY 486
Cdd:cd12118 356 NPEaTAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAF 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 487 VVAEDGAEVTRETIVEVLGDRFAKWQLPdEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd12118 436 VELKEGAKVTEEEIIAFCREHLAGFMVP-KTVVFGELPKTSTGKIQKFVLRD 486
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
15-544 |
5.78e-115 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 352.55 E-value: 5.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 15 LNTTSMIRHAATVFGEQEVVYRNSDGSwGRSNYADEFKRMAQLAHGL-TELGVGAGSMVGVLDWNSRRHFELYFAVPGLA 93
Cdd:PRK05620 10 LSLTRILEYGSTVHGDTTVTTWGGAEQ-EQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 94 ATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLlpvAEALAPKLD----VKGWVVMTDKPADEIETTLE---NVVFYEDL 166
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVIVADPRL---AEQLGEILKecpcVRAVVFIGPSDADSAAAHMPegiKVYSYEAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 167 IKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAA--LGASFDDTIMPITPMFHVLSWGFPQNA 244
Cdd:PRK05620 166 LDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVPLAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 245 VAAGAKLVLPGKFAAEEfgAIAKAFIAEKVTLANGAPAIFapMLAMMKDMPQPPDLSGVR--LVSGSSEPPLsMMRGFKE 322
Cdd:PRK05620 246 FMSGTPLVFPGPDLSAP--TLAKIIATAMPRVAHGVPTLW--IQLMVHYLKNPPERMSLQeiYVGGSAVPPI-LIKAWEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 323 ITGADVIHGYGATETTPLATTNwhiKPGLDMDEEERWDFKRYQGLPVIGVEVKVVDpTGEELPRDGKSMGEVLMRGPWIT 402
Cdd:PRK05620 321 RYGVDVVHVWGMTETSPVGTVA---RPPSGVSGEARWAYRVSQGRFPASLEYRIVN-DGQVMESTDRNEGEIQVRGNWVT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 403 ESYFQLP-----------------DNSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSP 464
Cdd:PRK05620 397 ASYYHSPteegggaastfrgedveDANDRFTaDGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 465 SVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET---IVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWE 541
Cdd:PRK05620 477 EVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
...
gi 1949187543 542 DAE 544
Cdd:PRK05620 557 DGD 559
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
21-533 |
1.69e-101 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 313.01 E-value: 1.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 21 IRHAATVFGEQeVVYRNSDGSWGrsnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLN 100
Cdd:cd17631 1 LRRRARRHPDR-TALVFGGRSLT---YAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 101 LRLAPEDLAYVVSHSKSDWIFVDESLLpvaealapkldvkgwvvMtdkpadeiettlenvvfyedlikdkpdtydwpvvd 180
Cdd:cd17631 77 FRLTPPEVAYILADSGAKVLFDDLALL-----------------M----------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 181 ektaayagYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAV-AAGAKLVLPGKFAA 259
Cdd:cd17631 105 --------YTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTlLRGGTVVILRKFDP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 260 EE-FGAIAKafiaEKVTLANGAPAifapMLAMMKDMPQP--PDLSGVRLVS-GSSEPPLSMMRGFKEItGADVIHGYGAT 335
Cdd:cd17631 177 ETvLDLIER----HRVTSFFLVPT----MIQALLQHPRFatTDLSSLRAVIyGGAPMPERLLRALQAR-GVKFVQGYGMT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 ETTPLATtnwhikpGLDMDEEERwdfK-RYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPD-NSE 413
Cdd:cd17631 248 ETSPGVT-------FLSPEDHRR---KlGSAGRPVFFVEVRIVDPDGREVPPGE--VGEIVVRGPHVMAGYWNRPEaTAA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 RFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGA 493
Cdd:cd17631 316 AFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGA 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1949187543 494 EVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDK 533
Cdd:cd17631 396 ELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
19-545 |
8.31e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 309.57 E-value: 8.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 19 SMIRHAATVFGEQ-EVVYRNSdgswgRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATML 97
Cdd:PRK08162 22 SFLERAAEVYPDRpAVIHGDR-----RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIETTLENVVFYEDLIKDKPDTYDW- 176
Cdd:PRK08162 97 TLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAFLASGDPDFAWt 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGasfddtiMP-------ITPMFHVLSWGFPQNAVAAGA 249
Cdd:PRK08162 177 LPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWG-------MPkhpvylwTLPMFHCNGWCFPWTVAARAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 KLVLPGKFAAEE-FGAIAKafiaEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSePPLSMMRGFKEItGADV 328
Cdd:PRK08162 250 TNVCLRKVDPKLiFDLIRE----HGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAA-PPAAVIAKMEEI-GFDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATET-TPLATTNWHikPGLD-MDEEERWDFKRYQGLPVIGVE-VKVVDP-TGEELPRDGKSMGEVLMRGPWITES 404
Cdd:PRK08162 324 THVYGLTETyGPATVCAWQ--PEWDaLPLDERAQLKARQGVRYPLQEgVTVLDPdTMQPVPADGETIGEIMFRGNIVMKG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 405 YFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERP 483
Cdd:PRK08162 402 YLKNPKaTEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVP 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 484 VAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTdELPRTSVGKLDKKLLRKTWEDAEA 545
Cdd:PRK08162 482 CAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFG-ELPKTSTGKIQKFVLREQAKSLKA 542
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
189-532 |
1.32e-94 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 291.88 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFgaiAKA 268
Cdd:cd04433 7 YTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA---LEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLANGAPAIFApmlAMMK-DMPQPPDLSGVR-LVSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTNwh 346
Cdd:cd04433 84 IEREKVTILLGVPTLLA---RLLKaPESAGYDLSSLRaLVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 347 ikpGLDMDEEERwdfkRYQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFL-DGWWRSGDV 425
Cdd:cd04433 159 ---PPDDDARKP----GSVGRPVPGVEVRIVDPDGGELPPGEI--GELVVRGPSVMKGYWNNPEATAAVDeDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLG 505
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 1949187543 506 DRFAKWQLPDEIIVTDELPRTSVGKLD 532
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-537 |
2.73e-89 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 282.53 E-value: 2.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRnsdgswgrsnyadEFKRMAQ-LAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNL 101
Cdd:cd05936 15 KTALIFMGRKLTYR-------------ELDALAEaFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESLlpvaealapkldvkgwvvmtdkpadeiettlenvvfyEDLIKDKPDTYDWPVVDE 181
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVSF-------------------------------------TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 182 KTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASF--DDTIMPITPMFHVLSWGFPQNA-VAAGAKLVLPGKFA 258
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLegDDVVLAALPLFHVFGLTVALLLpLALGATIVLIPRFR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 259 AEEF-GAIAKafiaEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGYGATE 336
Cdd:cd05936 205 PIGVlKEIRK----HRVTIFPGVPTMYIALLNAPEF--KKRDFSSLRLcISGGAPLPVEVAERFEELTGVPIVEGYGLTE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 337 TTPLATTN---WHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NS 412
Cdd:cd05936 279 TSPVVAVNpldGPRKPG-------------SIGIPLPGTEVKIVDDDGEELPPG--EVGELWVRGPQVMKGYWNRPEeTA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 413 ERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG 492
Cdd:cd05936 344 EAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1949187543 493 AEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05936 424 ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
21-447 |
1.40e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 278.81 E-value: 1.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 21 IRHAATVFGEQEVVYrnsDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLN 100
Cdd:pfam00501 1 LERQAARTPDKTALE---VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 101 LRLAPEDLAYVVSHSKSDWIFVDESL-LPVAEALAPKLDVKGWVVMTDKPADEIETTLenvvfYEDLIKDKPDTYDWPVV 179
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPL-----PEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 DEKTAAYAGYTTGTTGRPKGVYYSHRSI----YLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQN-AVAAGAKLVLP 254
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 GKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMmkDMPQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVIHGYG 333
Cdd:pfam00501 233 PGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEA--GAPKRALLSSLRLVlSGGAPLPPELARRFRELFGGALVNGYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 334 ATETTPLATTnwhikpglDMDEEERWDFKRYQGLPVIGVEVKVVDP-TGEELPRDGKsmGEVLMRGPWITESYFQLPD-N 411
Cdd:pfam00501 311 LTETTGVVTT--------PLPLDEDLRSLGSVGRPLPGTEVKIVDDeTGEPVPPGEP--GELCVRGPGVMKGYLNDPElT 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 1949187543 412 SERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSG 447
Cdd:pfam00501 381 AEAFDeDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
24-537 |
2.60e-80 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 262.09 E-value: 2.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 24 AATVFGEQ-EVVYRNSDGSWgrsnyADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLR 102
Cdd:PLN02479 29 AAVVHPTRkSVVHGSVRYTW-----AQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 103 LAPEDLAYVVSHSKSDWIFVDESLLPVAE-ALAPKLDVKGW-------VVMTDKPAD--EIETTL-ENVVFYEDLIKDKP 171
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEeALKILAEKKKSsfkppllIVIGDPTCDpkSLQYALgKGAIEYEKFLETGD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 172 DTYDW-PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQN-AVAAGA 249
Cdd:PLN02479 184 PEFAWkPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTlAALCGT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 KLVLPGKFAAEEFGAIAKAfiaeKVTLANGAPAIF-----APMLAMMKDMPQPPDLsgvrLVSGSSEPP--LSMM--RGF 320
Cdd:PLN02479 264 NICLRQVTAKAIYSAIANY----GVTHFCAAPVVLntivnAPKSETILPLPRVVHV----MTAGAAPPPsvLFAMseKGF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 321 KeitgadVIHGYGATET-TPLATTNWhiKPGLD-MDEEERWDFKRYQGLPVIGVE-VKVVDP-TGEELPRDGKSMGEVLM 396
Cdd:PLN02479 336 R------VTHTYGLSETyGPSTVCAW--KPEWDsLPPEEQARLNARQGVRYIGLEgLDVVDTkTMKPVPADGKTMGEIVM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 397 RGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVP 475
Cdd:PLN02479 408 RGNMVMKGYLKNPKaNEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARP 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 476 DEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLP----DEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PLN02479 488 DERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERLPaywvPKSVVFGPLPKTATGKIQKHVLR 553
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-543 |
6.33e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 257.17 E-value: 6.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRnsdgswgrsnyadEFKRMA-QLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRL 103
Cdd:PRK08316 29 ALVFGDRSWTYA-------------ELDAAVnRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 104 APEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIETTLENVvfyEDLIKDKPDTYDWPVVDEKT 183
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDF---ADWAEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 AAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH-----VlswgFPQNAVAAGAK-LVLPGKF 257
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHcaqldV----FLGPYLYVGATnVILDAPD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 258 AAEEFGAIAkafiAEKVTLANGAPAIFAPMLammkdmpQPPDLSGVRLVS------GSS---EPPLSMMRgfKEITGADV 328
Cdd:PRK08316 249 PELILRTIE----AERITSFFAPPTVWISLL-------RHPDFDTRDLSSlrkgyyGASimpVEVLKELR--ERLPGLRF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLATTnwhIKPGldmDEEERWDfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQL 408
Cdd:PRK08316 316 YNCYGQTEIAPLATV---LGPE---EHLRRPG---SAGRPVLNVETRVVDDDGNDVAPG--EVGEIVHRSPQLMLGYWDD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 409 PDNS-ERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYV 487
Cdd:PRK08316 385 PEKTaEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 488 VAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWEDA 543
Cdd:PRK08316 465 VPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
17-541 |
1.99e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 247.11 E-value: 1.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 17 TTSMIRHAATVFGEQEVVYRNSDGSwgrsnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATM 96
Cdd:PRK06145 5 SASIAFHARRTPDRAALVYRDQEIS-----YAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 97 LQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPK--LDVKGWVVMTDKPADEIETTLENVVFYEDLIKdkpdty 174
Cdd:PRK06145 80 LPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKivIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVR------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 175 dwpvvdektaayAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAV-AAGAKLVL 253
Cdd:PRK06145 154 ------------LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVlWVGGTLRI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEefgAIAKAFIAEKVTLANGAPAIFAPMLAMmkdmPQPP--DLSGVR-LVSGSSEPPLSMMRGFKEI-TGADVI 329
Cdd:PRK06145 222 HREFDPE---AVLAAIERHRLTCAWMAPVMLSRVLTV----PDRDrfDLDSLAwCIGGGEKTPESRIRDFTRVfTRARYI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTPLATTnwhikpgldMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLP 409
Cdd:PRK06145 295 DAYGLTETCSGDTL---------MEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMK--GEICMRGPKVTKGYWKDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSER-FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVV 488
Cdd:PRK06145 364 EKTAEaFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 489 AEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWE 541
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
46-538 |
4.38e-75 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 246.07 E-value: 4.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSrrhfeLYFAVPGLAATMLQ-----LNLRLAPEDLAYVVSHSKSDWI 120
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKKGDRVAIALPNG-----LEFVVAFLAAARAGavvapLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 121 FVD-ESLLPVAEAlAPKLDvkgwvvMTDKPADEIETTLENVVFYEDL---IKDKPDTYDWPVVDEKTAAYAGYTTGTTGR 196
Cdd:cd05926 91 LTPkGELGPASRA-ASKLG------LAILELALDVGVLIRAPSAESLsnlLADKKNAKSEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 197 PKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHV-------LSwgfpqnAVAAGAKLVLPGKFAAEEFgaiAKAF 269
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVhglvaslLS------TLAAGGSVVLPPRFSASTF---WPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 270 IAEKVTLANGAPAIFAPMLAMMKDMPQPPdLSGVRLV-SGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTN---- 344
Cdd:cd05926 235 RDYNATWYTAVPTIHQILLNRPEPNPESP-PPKLRFIrSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplpp 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 345 WHIKPGLdmdeeerwdfkryQGLPViGVEVKVVDPTGEELPrDGKSmGEVLMRGPWITESYFQLPD-NSERFL-DGWWRS 422
Cdd:cd05926 314 GPRKPGS-------------VGKPV-GVEVRILDEDGEILP-PGVV-GEICLRGPNVTRGYLNNPEaNAEAAFkDGWFRT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 423 GDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVE 502
Cdd:cd05926 378 GDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRA 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 1949187543 503 VLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05926 458 FCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
15-539 |
5.26e-75 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 246.35 E-value: 5.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 15 LNTTSMIRHAATVFGEQEVVYrnsDGSwGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAA 94
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYV---FGD-QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 95 TMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIETtlENVVFYEDLIKDKPDTY 174
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICETEEDDPHT--EKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 175 DWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNA-VAAGAKLVL 253
Cdd:PRK07656 159 RAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNApLMRGATILP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEE-FGAIAKafiaEKVTLANGAPAIFAPMLammkDMPQ--PPDLSGVRL-VSGSSEPPLSMMRGFKEITGAD-V 328
Cdd:PRK07656 239 LPVFDPDEvFRLIET----ERITVLPGPPTMYNSLL----QHPDrsAEDLSSLRLaVTGAASMPVALLERFESELGVDiV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLATTNwhiKPGldmdeEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQL 408
Cdd:PRK07656 311 LTGYGLSEASGVTTFN---RLD-----DDRKTVAGTIGTAIAGVENKIVNELGEEVPVG--EVGELLVRGPNVMKGYYDD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 409 PDNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAY 486
Cdd:PRK07656 381 PEATAAAIdaDGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAY 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 487 VVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKT 539
Cdd:PRK07656 461 VVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
44-537 |
9.62e-75 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 247.62 E-value: 9.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLPVAE---ALAPKLDVKG-----WVVMTDKPADEIETTLEnvvfYEDLIKD---KPDTYD--WPVVDEKTAAYAGYT 190
Cdd:PLN03102 119 RSFEPLARevlHLLSSEDSNLnlpviFIHEIDFPKRPSSEELD----YECLIQRgepTPSLVArmFRIQDEHDPISLNYT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 191 TGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEfgaIAKAFI 270
Cdd:PLN03102 195 SGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPE---IYKNIE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 271 AEKVTLANGAPAIFAPMLAMMKdMPQPPDLSGVRLVSGSSEPPLSMMRGFKEItGADVIHGYGATETT-PLATTNWHIKP 349
Cdd:PLN03102 272 MHNVTHMCCVPTVFNILLKGNS-LDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATgPVLFCEWQDEW 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 350 GlDMDEEERWDFKRYQGLPVIG---VEVKVVDpTGEELPRDGKSMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDV 425
Cdd:PLN03102 350 N-RLPENQQMELKARQGVSILGladVDVKNKE-TQESVPRDGKTMGEIVIKGSSIMKGYLKNPKaTSEAFKHGWLNTGDV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAE---------VT 496
Cdd:PLN03102 428 GVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETtkedrvdklVT 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1949187543 497 RE-TIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PLN03102 508 RErDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
39-531 |
1.95e-74 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 244.43 E-value: 1.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRS-NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKS 117
Cdd:cd05911 4 DADTGKElTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 118 DWIFVDESLLPVAEALAPKLDVKGWV-VMTDKPAD--EIETTLENVVFYEDlikdkpDTYDWPVVD-EKTAAYAGYTTGT 193
Cdd:cd05911 84 KVIFTDPDGLEKVKEAAKELGPKDKIiVLDDKPDGvlSIEDLLSPTLGEED------EDLPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 194 TGRPKGVYYSHRSIYLHTMGGLAALGASF--DDTIMPITPMFHVlsWGFPQ--NAVAAGAKLVLPGKFAAEEF-GAIAKa 268
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGNDgsNDVILGFLPLYHI--YGLFTtlASLLNGATVIIMPKFDSELFlDLIEK- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 fiaEKVTLANGAPAIfapMLAMMKD-MPQPPDLSGVR-LVSGSSepPLSmmRGFKE-----ITGADVIHGYGATETTPLA 341
Cdd:cd05911 235 ---YKITFLYLVPPI---AAALAKSpLLDKYDLSSLRvILSGGA--PLS--KELQEllakrFPNATIKQGYGMTETGGIL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 342 TTNwhikPGLDMDEEErwdfkryQGLPVIGVEVKVVDP-TGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFLD--G 418
Cdd:cd05911 305 TVN----PDGDDKPGS-------VGRLLPNVEAKIVDDdGKDSLGPNEP--GEICVRGPQVMKGYYNNPEATKETFDedG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 419 WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRE 498
Cdd:cd05911 372 WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEK 451
|
490 500 510
....*....|....*....|....*....|....
gi 1949187543 499 TIVEVLGDRFAKW-QLPDEIIVTDELPRTSVGKL 531
Cdd:cd05911 452 EVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKI 485
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
22-545 |
4.73e-68 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 229.61 E-value: 4.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 22 RHAATVfGEQE-VVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGLA---ATML 97
Cdd:COG0365 17 RHAEGR-GDKVaLIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIY---LPNIPEAVIAMLACArigAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLNLRLAPEDLAYVVSHSKSDWIFVDESLLP----------VAEALA--PKLDVkgwVVMTDKPADEIEttLENVVFYED 165
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLITADGGLRggkvidlkekVDEALEelPSLEH---VIVVGRTGADVP--MEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 166 LIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHT-MGGLAALGASFDDTIMPITPMFhvlsWGFPQ-N 243
Cdd:COG0365 168 LLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAaTTAKYVLDLKPGDVFWCTADIG----WATGHsY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 244 AV----AAGAKLVL-PGKFAAEEFGAIAKaFIAE-KVTLANGAPAIFApmlAMMKDMPQPP---DLSGVRLVSGSSEP-P 313
Cdd:COG0365 244 IVygplLNGATVVLyEGRPDFPDPGRLWE-LIEKyGVTVFFTAPTAIR---ALMKAGDEPLkkyDLSSLRLLGSAGEPlN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 314 LSMMRGFKEITGADVIHGYGATETT-PLATTNWH--IKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDGKs 390
Cdd:COG0365 320 PEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGlpVKPG-------------SMGKPVPGYDVAVVDEDGNPVPPGEE- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 391 mGEVLMRGPW--ITESYFQlpdNSERFLD-------GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAIL 461
Cdd:COG0365 386 -GELVIKGPWpgMFRGYWN---DPERYREtyfgrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 462 DSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT---RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:COG0365 462 SHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
....*..
gi 1949187543 539 TWEDAEA 545
Cdd:COG0365 542 IAEGRPL 548
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
47-536 |
7.19e-67 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 224.74 E-value: 7.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLT-ELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDES 125
Cdd:PRK06839 30 YKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 LLPVAEALAPKLDVKGWVVMTDkpadeiettlenvvfYEDLIKDKPDTYDWPvvDEKTAAYAGYTTGTTGRPKGVYYSHR 205
Cdd:PRK06839 110 FQNMALSMQKVSYVQRVISITS---------------LKEIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 SIYLHTMGGLAALGASFDDTIMPITPMFHVLSWG-FPQNAVAAGAKLVLPGKFAAEEfgaiAKAFI-AEKVTLANGAPAI 283
Cdd:PRK06839 173 NMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGVIIVPRKFEPTK----ALSMIeKHKVTVVMGVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 284 FAPMLAMMKDMPqpPDLSGVRLV-SGSSEPPLSMMRGFKEiTGADVIHGYGATETTPLATtnwhikpgldMDEEErwDFK 362
Cdd:PRK06839 249 HQALINCSKFET--TNLQSVRWFyNGGAPCPEELMREFID-RGFLFGQGFGMTETSPTVF----------MLSEE--DAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 363 RYQG---LPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPDNSERFL-DGWWRSGDVGVIFPNGYLKLTD 438
Cdd:PRK06839 314 RKVGsigKPVLFCDYELIDENKNKVEVGE--VGELLIRGPNVMKEYWNRPDATEETIqDGWLCTGDLARVDEDGFVYIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 439 RLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEII 518
Cdd:PRK06839 392 RKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIV 471
|
490
....*....|....*...
gi 1949187543 519 VTDELPRTSVGKLDKKLL 536
Cdd:PRK06839 472 FLKELPKNATGKIQKAQL 489
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
44-538 |
3.21e-66 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 221.10 E-value: 3.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESllpvaealapkldvkgwvvmtdkpadeiettlenvvFYEDLIKDKPDTydwpvvdektAAYAGYTTGTTGRPKGVYYS 203
Cdd:cd05903 81 ER------------------------------------FRQFDPAAMPDA----------VALLLFTSGTTGEPKGVMHS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFP-QNAVAAGAKLVLPGKFAAEEFGAIAKAfiaEKVTLANGAPA 282
Cdd:cd05903 115 HNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGfTLPLLLGAPVVLQDIWDPDKALALMRE---HGVTFMMGATP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 283 IFAPMLAMMKDmpQPPDLSGVR--LVSGSSEPPlSMMRGFKEITGADVIHGYGATETtPLATTNwhIKPGldmDEEERWd 360
Cdd:cd05903 192 FLTDLLNAVEE--AGEPLSRLRtfVCGGATVPR-SLARRAAELLGAKVCSAYGSTEC-PGAVTS--ITPA---PEDRRL- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 361 fkRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFL-DGWWRSGDVGVIFPNGYLKLTDR 439
Cdd:cd05903 262 --YTDGRPLPGVEIKVVDDTGATLAPG--VEGELLSRGPSVFLGYLDRPDLTADAApEGWFRTGDLARLDEDGYLRITGR 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 440 LKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVL-GDRFAKWQLPDEII 518
Cdd:cd05903 338 SKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLV 417
|
490 500
....*....|....*....|
gi 1949187543 519 VTDELPRTSVGKLDKKLLRK 538
Cdd:cd05903 418 HVDDLPRTPSGKVQKFRLRE 437
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-537 |
7.06e-65 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 217.16 E-value: 7.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDE-S 125
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDPaS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 LLpvaealapkldvkgwvvmtdkpadeiettlenvvfyedlikdkpdtydwpvvdektaayagYTTGTTGRPKGVYYSHR 205
Cdd:cd05934 86 IL-------------------------------------------------------------YTSGTTGPPKGVVITHA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 siYLHTMGGLAA--LGASFDDTIMPITPMFHV--LSWGFPQnAVAAGAKLVLPGKFAAEEF-GAIAKAfiaeKVTLANga 280
Cdd:cd05934 105 --NLTFAGYYSArrFGLGEDDVYLTVLPLFHInaQAVSVLA-ALSVGATLVLLPRFSASRFwSDVRRY----GATVTN-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 281 pAIFAPMLAMMKDMPQPPDLSG-VRLVSGSSEPPlSMMRGFKEITGADVIHGYGATETT-PLATTNwhikpgldmDEEER 358
Cdd:cd05934 176 -YLGAMLSYLLAQPPSPDDRAHrLRAAYGAPNPP-ELHEEFEERFGVRLLEGYGMTETIvGVIGPR---------DEPRR 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 359 WDfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRG--PWIT-ESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYL 434
Cdd:cd05934 245 PG---SIGRPAPGYEVRIVDDDGQELPAG--EPGELVIRGlrGWGFfKGYYNMPEaTAEAMRNGWFHTGDLGYRDADGFF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 435 KLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLP 514
Cdd:cd05934 320 YFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVP 399
|
490 500
....*....|....*....|...
gi 1949187543 515 DEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05934 400 RYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
189-538 |
1.26e-63 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 214.46 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNA-VAAGAKLVLPGKF-AAEEFGAIA 266
Cdd:cd05941 96 YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLFAGASVEFLPKFdPKEVAISRL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 267 KAFIaekvTLANGAPAIFAPMLAMMKDMPQPPD------LSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGYGATETTp 339
Cdd:cd05941 176 MPSI----TVFMGVPTIYTRLLQYYEAHFTDPQfaraaaAERLRLmVSGSAALPVPTLEEWEAITGHTLLERYGMTEIG- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 340 LATTNwhikpGLDmdeEERWDfkRYQGLPVIGVEVKVVDPTGEElPRDGKSMGEVLMRGPWITESYFQLPD-NSERF-LD 417
Cdd:cd05941 251 MALSN-----PLD---GERRP--GTVGMPLPGVQARIVDEETGE-PLPRGEVGEIQVRGPSVFKEYWNKPEaTKEEFtDD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 GWWRSGDVGVIFPNGYLKLTDRLK-DVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAE-V 495
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaL 399
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1949187543 496 TRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05941 400 SLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
47-538 |
3.44e-63 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 212.59 E-value: 3.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDwifvdesl 126
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 lpvaealapkldvkgwvvmtdkpADEIETTLenvvfyedlikdkpdtydwpvvdektaayagYTTGTTGRPKGVYYSHRS 206
Cdd:cd05912 76 -----------------------LDDIATIM-------------------------------YTSGTTGKPKGVQQTFGN 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 IYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEfgaIAKAFIAEKVTLANGAPAifap 286
Cdd:cd05912 102 HWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQ---VLHLINSGKVTIISVVPT---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 287 MLA-MMKDMPQ--PPDLSGVRLvsGSSEPPLSMMRGFKEiTGADVIHGYGATETTPLATT----NWHIKPGldmdeeerw 359
Cdd:cd05912 175 MLQrLLEILGEgyPNNLRCILL--GGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQIVTlspeDALNKIG--------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 360 dfkrYQGLPVIGVEVKVVDPTGEElprdgKSMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTD 438
Cdd:cd05912 243 ----SAGKPLFPVELKIEDDGQPP-----YEVGEILLKGPNVTKGYLNRPDaTEESFENGWFKTGDIGYLDEEGFLYVLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 439 RLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEdgAEVTRETIVEVLGDRFAKWQLPDEII 518
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIY 391
|
490 500
....*....|....*....|
gi 1949187543 519 VTDELPRTSVGKLDKKLLRK 538
Cdd:cd05912 392 FVDELPRTASGKLLRHELKQ 411
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
22-538 |
3.65e-63 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 215.80 E-value: 3.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 22 RHAATVFGEQEVVYRNSDGSWGrsnyaDEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNL 101
Cdd:PRK07786 25 RHALMQPDAPALRFLGNTTTWR-----ELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESLLPVAEA---LAPKLDVKgwVVMTDKPADeiettleNVVFYEDLIKDkpDTYDWPV 178
Cdd:PRK07786 100 RLTPPEIAFLVSDCGAHVVVTEAALAPVATAvrdIVPLLSTV--VVAGGSSDD-------SVLGYEDLLAE--AGPAHAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VD--EKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPIT-PMFHVLSWGFPQNAVAAGAKLVL-P 254
Cdd:PRK07786 169 VDipNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGvPLFHIAGIGSMLPGLLLGAPTVIyP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 -GKFAAeefGAIAKAFIAEKVTLANGAPAIFAPMLAMMKdmPQPPDLSgVRLVS-GSSEPPLSMMRGFKEI-TGADVIHG 331
Cdd:PRK07786 249 lGAFDP---GQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ--ARPRDLA-LRVLSwGAAPASDTLLRQMAATfPEAQILAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLATTnwhikpgLDMDEEERwdfKRYQ-GLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD 410
Cdd:PRK07786 323 FGQTEMSPVTCM-------LLGEDAIR---KLGSvGKVIPTVAARVVDENMNDVPVG--EVGEIVYRAPTLMSGYWNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 -NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYV-V 488
Cdd:PRK07786 391 aTAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaV 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1949187543 489 AEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK07786 471 RNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
18-537 |
5.05e-63 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 214.54 E-value: 5.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 18 TSMIRHAATVFGEQEVVYRNSDGSWgrsnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATML 97
Cdd:cd05959 7 TLVDLNLNEGRGDKTAFIDDAGSLT----YAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIETTLEnvvfYEDLIKDKPDTYDWP 177
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALL----LAELVAAEAEQLKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYlhTMGGLAA---LGASFDDTIMPITPMFHVLSWG----FPqnaVAAGAK 250
Cdd:cd05959 159 ATHADDPAFWLYSSGSTGRPKGVVHLHADIY--WTAELYArnvLGIREDDVCFSAAKLFFAYGLGnsltFP---LSVGAT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 251 LVL-PGKFAAEefgAIAKAFIAEKVTLANGAPAIFAPMLAmmKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADV 328
Cdd:cd05959 234 TVLmPERPTPA---AVFKRIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEAlPAEVGERWKARFGLDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLATTNwhikpgldmdeeeRWDFKRY--QGLPVIGVEVKVVDPTGEELPrDGKSmGEVLMRGPWITESYF 406
Cdd:cd05959 309 LDGIGSTEMLHIFLSN-------------RPGRVRYgtTGKPVPGYEVELRDEDGGDVA-DGEP-GELYVRGPSSATMYW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 407 QLPDNSER-FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVA 485
Cdd:cd05959 374 NNRDKTRDtFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1949187543 486 YVVAEDGA---EVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05959 454 FVVLRPGYedsEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
15-538 |
8.55e-62 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 211.52 E-value: 8.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 15 LNTTSMIRHAATVFGEQevVYRNSDGSWGRSNyadefKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAA 94
Cdd:cd05915 2 ERAAALFGRKEVVSRLH--TGEVHRTTYAEVY-----QRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 95 TMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVkgwvvMTDKPADEieTTLENvvfYEDLIKD-KPDT 173
Cdd:cd05915 75 VLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKT-----VQHFVVMD--EKAPE---GYLAYEEaLGEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 174 YDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTmgglAALGA--SFDDTIMPI----TPMFHVLSWGFPQNAVAA 247
Cdd:cd05915 145 ADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHS----LAASLvdGTALSEKDVvlpvVPMFHVNAWCLPYAATLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 248 GAKLVLPGKFAAEEfgAIAKAFIAEKVTLANGAPAIFApMLAMMKDMPQPPDLSGVRLVSGSSEPPLSMMRgFKEITGAD 327
Cdd:cd05915 221 GAKQVLPGPRLDPA--SLVELFDGEGVTFTAGVPTVWL-ALADYLESTGHRLKTLRRLVVGGSAAPRSLIA-RFERMGVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 VIHGYGATETTPLATTNWHIKPGLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQ 407
Cdd:cd05915 297 VRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 408 LPDNSER--FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVA 485
Cdd:cd05915 377 NEEATRSalTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLA 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 486 YVVAEDgAEVTRETIVEVLGDRFAKWQL-PDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05915 457 VVVPRG-EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
19-530 |
7.03e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 210.63 E-value: 7.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 19 SMIRHAATVFGEQEVVYrnsdgSWGRS-NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATML 97
Cdd:PRK05605 36 DLYDNAVARFGDRPALD-----FFGATtTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLN-LRLAPEDLAYVVSHSKSDWIFVDESLlPVAEALAP--KLDVKGWVVMTD------------------KPADEIETT 156
Cdd:PRK05605 111 EHNpLYTAHELEHPFEDHGARVAIVWDKVA-PTVERLRRttPLETIVSVNMIAampllqrlalrlpipalrKARAALTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 157 LENVVFYEDLIKDKP----DTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLA---ALGASfDDTIMPI 229
Cdd:PRK05605 190 APGTVPWETLVDAAIggdgSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAwvpGLGDG-PERVLAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 230 TPMFHVlsWGFPQN---AVAAGAKLVLpgkFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRL- 305
Cdd:PRK05605 269 LPMFHA--YGLTLCltlAVSIGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNa 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 306 VSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTN---WHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDP--T 380
Cdd:PRK05605 342 FSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNpmsDDRRPG-------------YVGVPFPDTEVRIVDPedP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 381 GEELPrDGKSmGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENA 459
Cdd:PRK05605 409 DETMP-DGEE-GELLVRGPQVFKGYWNRPEeTAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 460 ILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGK 530
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGK 557
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
46-536 |
7.77e-59 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 201.55 E-value: 7.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDES 125
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 LlpvaealapkldvkgwvvmtdkpadeiettlenvvfyEDLikdkpdtydwpvvdektaAYAGYTTGTTGRPKGVYYSHR 205
Cdd:cd05935 83 L-------------------------------------DDL------------------ALIPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 SIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQN-AVAAGAKLVLPGKFAAEefgAIAKAFIAEKVTLANGAPAIF 284
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNtAVYVGGTYVLMARWDRE---TALELIEKYKVTFWTNIPTML 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 285 APMLAMMKDmpQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATETTPLATTNWHIKPGLdmdeeerwdfkR 363
Cdd:cd05935 185 VDLLATPEF--KTRDLSSLKVLTGGGAPmPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKL-----------Q 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 364 YQGLPVIGVEVKVVDP-TGEELPrDGKSmGEVLMRGPWITESYFQLP-DNSERF--LDG--WWRSGDVGVIFPNGYLKLT 437
Cdd:cd05935 252 CLGIP*FGVDARVIDIeTGRELP-PNEV-GEIVVRGPQIFKGYWNRPeETEESFieIKGrrFFRTGDLGYMDEEGYFFFV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 438 DRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG--AEVTRETIVEVLGDRFAKWQLPD 515
Cdd:cd05935 330 DRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPR 409
|
490 500
....*....|....*....|.
gi 1949187543 516 EIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05935 410 EVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
39-536 |
9.59e-58 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 200.54 E-value: 9.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRS-NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKS 117
Cdd:cd05904 26 DAATGRAlTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 118 DWIFVDESLLPVAEALAPKLdvkgwVVMTDKPADEIEttlenvvFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRP 197
Cdd:cd05904 106 KLAFTTAELAEKLASLALPV-----VLLDSAEFDSLS-------FSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 198 KGVYYSHRSiylhtmggLAALGASF----------DDTIMPITPMFHV--LSWgFPQNAVAAGAKLVLPGKFAAEEFgai 265
Cdd:cd05904 174 KGVMLTHRN--------LIAMVAQFvagegsnsdsEDVFLCVLPMFHIygLSS-FALGLLRLGATVVVMPRFDLEEL--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 266 AKAFIAEKVTLANGAPAIfapMLAMMK-DMPQPPDLSGVRLVSgSSEPPLS--MMRGFKE-ITGADVIHGYGATETTPLA 341
Cdd:cd05904 242 LAAIERYKVTHLPVVPPI---VLALVKsPIVDKYDLSSLRQIM-SGAAPLGkeLIEAFRAkFPNVDLGQGYGMTESTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 342 TTNwhikpglDMDEEERwdfKRYQ--GLPVIGVEVKVVDP-TGEELPRdGKSmGEVLMRGPWITESYFQLPDNSERFLD- 417
Cdd:cd05904 318 AMC-------FAPEKDR---AKYGsvGRLVPNVEAKIVDPeTGESLPP-NQT-GELWIRGPSIMKGYLNNPEATAATIDk 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 -GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT 496
Cdd:cd05904 386 eGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLT 465
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1949187543 497 RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05904 466 EDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
177-537 |
3.23e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 198.29 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIyLHTMGGLA-ALGASFDDTIMPITPMFHV--LSWGFpQNAVAAGAKLVL 253
Cdd:PRK07787 123 PEPDPDAPALIVYTSGTTGPPKGVVLSRRAI-AADLDALAeAWQWTADDVLVHGLPLFHVhgLVLGV-LGPLRIGNRFVH 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEefgAIAKAfIAEKVTLANGAPAIFAPMLAmmkDMPQPPDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGY 332
Cdd:PRK07787 201 TGRPTPE---AYAQA-LSEGGTLYFGVPTVWSRIAA---DPEAARALRGARLlVSGSAALPVPVFDRLAALTGHRPVERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATETtpLATTNWHIkpgldmDEEERWDfkrYQGLPVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQLPD-N 411
Cdd:PRK07787 274 GMTET--LITLSTRA------DGERRPG---WVGLPLAGVETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLNRPDaT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 412 SERFL-DGWWRSGDVGVIFPNGYLKLTDRLK-DVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVA 489
Cdd:PRK07787 343 AAAFTaDGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVG 422
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1949187543 490 edGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK07787 423 --ADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
47-538 |
2.93e-56 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 195.95 E-value: 2.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:PRK03640 30 FMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDDF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 lpvaealAPKLDVKGWVVMTDKPadeiETTLENVVFYEDlikdkpdtydwpvVDEKTAAYAGYTTGTTGRPKGVYYSHRS 206
Cdd:PRK03640 110 -------EAKLIPGISVKFAELM----NGPKEEAEIQEE-------------FDLDEVATIMYTSGTTGKPKGVIQTYGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 IYLHTMGGLAALGASFDDTIMPITPMFHV--LSWGFPQnaVAAGAKLVLPGKFAAEEfgaIAKAFIAEKVTLANGAPAIF 284
Cdd:PRK03640 166 HWWSAVGSALNLGLTEDDCWLAAVPIFHIsgLSILMRS--VIYGMRVVLVEKFDAEK---INKLLQTGGVTIISVVSTML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 285 APMLAMMKDMPQPPDLSGVRLvsGSSEPPLSMMRGFKEiTGADVIHGYGATETTP----LATTNWHIKPGldmdeeerwd 360
Cdd:PRK03640 241 QRLLERLGEGTYPSSFRCMLL--GGGPAPKPLLEQCKE-KGIPVYQSYGMTETASqivtLSPEDALTKLG---------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 361 fkrYQGLPVIGVEVKVVDPTGEELPRDgksMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDR 439
Cdd:PRK03640 308 ---SAGKPLFPCELKIEKDGVVVPPFE---EGEIVVKGPNVTKGYLNREDaTRETFQDGWFKTGDIGYLDEEGFLYVLDR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 440 LKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAedGAEVTRETIVEVLGDRFAKWQLPDEIIV 519
Cdd:PRK03640 382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYF 459
|
490
....*....|....*....
gi 1949187543 520 TDELPRTSVGKLDKKLLRK 538
Cdd:PRK03640 460 VEELPRNASGKLLRHELKQ 478
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
24-539 |
7.32e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 196.53 E-value: 7.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 24 AATV--FGEQE-VVYRNSDGSWGRSNYADEFKRmaqLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLN 100
Cdd:PRK12583 25 DATVarFPDREaLVVRHQALRYTWRQLADAVDR---LARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 101 LRLAPEDLAYVVSHSKSDWIFV-----DESLLPVAEALAPKLDVKG-------------WVVMTDKPADEIETTlenvvf 162
Cdd:PRK12583 102 PAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQpgalacerlpelrGVVSLAPAPPPGFLA------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 163 YEDLIKdKPDTYDWPVVDEKTAAYAG-------YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH- 234
Cdd:PRK12583 176 WHELQA-RGETVSREALAERQASLDRddpiniqYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHc 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 235 ---VLSwgfPQNAVAAGAKLVLPGkfaaEEFGAIA--KAFIAEKVTLANGAPAIFAPMLammkDMPQPP--DLSGVR--L 305
Cdd:PRK12583 255 fgmVLA---NLGCMTVGACLVYPN----EAFDPLAtlQAVEEERCTALYGVPTMFIAEL----DHPQRGnfDLSSLRtgI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 306 VSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATtnwhiKPGLDMDEEERwdfkryqgLPVIG-----VEVKVVDPT 380
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSL-----QTTAADDLERR--------VETVGrtqphLEVKVVDPD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 381 GEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEN 458
Cdd:PRK12583 391 GATVPRG--EIGELCTRGYSVMKGYWNNPEATAESIDedGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 459 AILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12583 469 FLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
.
gi 1949187543 539 T 539
Cdd:PRK12583 549 I 549
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
24-545 |
1.01e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 195.12 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 24 AATVFGEQEVVyrnsdgswgrsNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV--PGLAATMLqlNL 101
Cdd:PRK08276 2 AVIMAPSGEVV-----------TYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAArrSGLYYTPI--NW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIETTlenvvfYEDLIKDKPDTydwPVVDE 181
Cdd:PRK08276 69 HLTAAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRS------YEEALAAQPDT---PIADE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 182 KTAAYAGYTTGTTGRPKGVY--YSHRSIYLHTMGGLAALGASF---DDTI--MPiTPMFH--VLSWGfpQNAVAAGAKLV 252
Cdd:PRK08276 140 TAGADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMyggPDSVylSP-APLYHtaPLRFG--MSALALGGTVV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LPGKFAAEEF-GAIAKafiaEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIH 330
Cdd:PRK08276 217 VMEKFDAEEAlALIER----YRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPcPVEVKRAMIDWWGPIIHE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 331 GYGATE---TTPLATTNWHIKPGldmdeeerwdfkrYQGLPVIGvEVKVVDPTGEELPrdGKSMGEVLMRGPWITESYFQ 407
Cdd:PRK08276 293 YYASSEgggVTVITSEDWLAHPG-------------SVGKAVLG-EVRILDEDGNELP--PGEIGTVYFEMDGYPFEYHN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 408 LPDNSE--RFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVA 485
Cdd:PRK08276 357 DPEKTAaaRNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 486 YVVAEDGAEVTRETIVEVLG---DRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR-KTWEDAEA 545
Cdd:PRK08276 437 VVQPADGADAGDALAAELIAwlrGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRdRYWEGRQR 500
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
53-537 |
1.95e-55 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 192.68 E-value: 1.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSdwifvdeSLLpvaea 132
Cdd:cd05919 19 GANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA-------RLV----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 133 lapkldvkgwvvmtdkpadeiettlenvvfyedlikdkpdtydwpVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHT- 211
Cdd:cd05919 87 ---------------------------------------------VTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAd 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 212 MGGLAALGASFDDTIMPITPMFHVLSWG----FPqnaVAAGAKLVL-PGKFAAEEFGAIAKAFiaeKVTLANGAPAIFAP 286
Cdd:cd05919 122 AMAREALGLTPGDRVFSSAKMFFGYGLGnslwFP---LAVGASAVLnPGWPTAERVLATLARF---RPTVLYGVPTFYAN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 287 MLAMmKDMPqPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATETTPLATTNwhiKPGldmdeEERWDfkrYQ 365
Cdd:cd05919 196 LLDS-CAGS-PDALRSLRLCVSAGEAlPRGLGERWMEHFGGPILDGIGATEVGHIFLSN---RPG-----AWRLG---ST 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 366 GLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSE-RFLDGWWRSGDVGVIFPNGYLKLTDRLKDVI 444
Cdd:cd05919 263 GRPVPGYEIRLVDEEGHTIPPG--EEGDLLVRGPSAAVGYWNNPEKSRaTFNGGWYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 445 KSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGA---EVTRETIVEVLGDRFAKWQLPDEIIVTD 521
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAapqESLARDIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*.
gi 1949187543 522 ELPRTSVGKLDKKLLR 537
Cdd:cd05919 421 ELPRTATGKLQRFKLR 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
189-533 |
3.32e-54 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 186.32 E-value: 3.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEfgaIAKA 268
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAE---ALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLAngapAIFAPMLAMMKDM--PQPPDLSGVRLVSGSSEPplSMMRGFKEITGADVIHGYGATETTPLATTnwh 346
Cdd:cd17637 84 IEEEKVTLM----GSFPPILSNLLDAaeKSGVDLSSLRHVLGLDAP--ETIQRFEETTGATFWSLYGQTETSGLVTL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 347 ikpgldMDEEERwdfKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSER-FLDGWWRSGDV 425
Cdd:cd17637 155 ------SPYRER---PGSAGRPGPLVRVRIVDDNDRPVPAG--ETGEIVVRGPLVFQGYWNLPELTAYtFRNGWHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRL--KDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEV 503
Cdd:cd17637 224 GRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 1949187543 504 LGDRFAKWQLPDEIIVTDELPRTSVGKLDK 533
Cdd:cd17637 304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
33-539 |
1.82e-53 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 189.88 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 33 VVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVV 112
Cdd:PRK13295 44 TAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 113 SHSKSDWIFVDESL-----LPVAEALAPKL-DVKGWVVMTDKPADEIETTLENVVFYEDliKDKPDTYDWPVVDEKTAAY 186
Cdd:PRK13295 124 KHAESKVLVVPKTFrgfdhAAMARRLRPELpALRHVVVVGGDGADSFEALLITPAWEQE--PDAPAILARLRPGPDDVTQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 187 AGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLswGFPQNA---VAAGAKLVLPGKFAAEEFG 263
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQT--GFMYGLmmpVMLGATAVLQDIWDPARAA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 264 AIAKAfiaEKVTLANGApaifAPMLAMMKDMPQ--PPDLSGVR--LVSGSSEPPlSMMRGFKEITGADVIHGYGATETTp 339
Cdd:PRK13295 280 ELIRT---EGVTFTMAS----TPFLTDLTRAVKesGRPVSSLRtfLCAGAPIPG-ALVERARAALGAKIVSAWGMTENG- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 340 LATTnwhIKPGldmDEEERWDFKryQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFLDGW 419
Cdd:PRK13295 351 AVTL---TKLD---DPDERASTT--DGCPLPGVEVRVVDADGAPLPAG--QIGRLQVRGCSNFGGYLKRPQLNGTDADGW 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 420 WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET 499
Cdd:PRK13295 421 FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEE 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1949187543 500 IVEVLGD-RFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKT 539
Cdd:PRK13295 501 MVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
8-540 |
1.54e-52 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 187.26 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 8 TLGDSYQlnttsmirHAATVFGEQEVVYRNSDGSWgrsNYADEFKRMAQLAHGLTELGVGAGSMVGvldwnsrrhFEL-- 85
Cdd:PRK06087 24 SLADYWQ--------QTARAMPDKIAVVDNHGASY---TYSALDHAASRLANWLLAKGIEPGDRVA---------FQLpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 86 -------YFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFV---------DESLLPVAEALaPKLDvkgWVVMTDKP 149
Cdd:PRK06087 84 wceftiiYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNQL-PQLQ---QIVGVDKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 150 ADEIETtlenvVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPI 229
Cdd:PRK06087 160 APATSS-----LSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 230 TPMFHvlSWGFPQNAVA---AGAKLVLPGKFAAEEfgaiAKAFIA-EKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRL 305
Cdd:PRK06087 235 APLGH--ATGFLHGVTApflIGARSVLLDIFTPDA----CLALLEqQRCTCMLGATPFIYDLLNLLEK--QPADLSALRF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 306 -VSGSSEPPLSMMRGFKEiTGADVIHGYGATETTPLATTNwhikpgldMDEEERWDFKrYQGLPVIGVEVKVVDPTGEEL 384
Cdd:PRK06087 307 fLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVN--------LDDPLSRFMH-TDGYAAAGVEIKVVDEARKTL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 385 PRDgkSMGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILD 462
Cdd:PRK06087 377 PPG--CEGEEASRGPNVFMGYLDEPELTARALDeeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 463 SPSVKEAAVIGVPDEKWQERPVAYVVAEdgAEVTRETIVEVLG----DRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK06087 455 HPKIHDACVVAMPDERLGERSCAYVVLK--APHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
..
gi 1949187543 539 TW 540
Cdd:PRK06087 533 DI 534
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
57-539 |
1.61e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 187.44 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 57 LAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPK 136
Cdd:PRK07788 87 LARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 137 LD-VKGWVVMTDK--PADEIETTLENVVfyedlikDKPDTYDWPVVdEKTAAYAGYTTGTTGRPKGVYYSHRSIylhtmg 213
Cdd:PRK07788 167 LGrLRAWGGNPDDdePSGSTDETLDDLI-------AGSSTAPLPKP-PKPGGIVILTSGTTGTPKGAPRPEPSP------ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 214 gLAALGASFD-------DTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEfgaiAKAFIAE-KVTLANGAPAIFA 285
Cdd:PRK07788 233 -LAPLAGLLSrvpfragETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEA----TLEDIAKhKATALVVVPVMLS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 286 PMLAMMKDMPQPPDLSGVRLV--SGSSEPPlSMMRGFKEITGaDVIHG-YGATETTpLATT----NWHIKPGLdmdeeer 358
Cdd:PRK07788 308 RILDLGPEVLAKYDTSSLKIIfvSGSALSP-ELATRALEAFG-PVLYNlYGSTEVA-FATIatpeDLAEAPGT------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 359 wdfkryQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQlpDNSERFLDGWWRSGDVGVIFPNGYLKLTD 438
Cdd:PRK07788 378 ------VGRPPKGVTVKILDENGNEVPRG--VVGRIFVGNGFPFEGYTD--GRDKQIIDGLLSSGDVGYFDEDGLLFVDG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 439 RLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEII 518
Cdd:PRK07788 448 RDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVV 527
|
490 500
....*....|....*....|.
gi 1949187543 519 VTDELPRTSVGKLDKKLLRKT 539
Cdd:PRK07788 528 FLDELPRNPTGKVLKRELREM 548
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-537 |
2.13e-51 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 179.40 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSI----YLHTMgglaALGASFDDTIMPITPMFH----VLSWgfpQNAVAAGAKLVLPgkfaAE 260
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIvnngYFIGE----RLGLTEQDRLCIPVPLFHcfgsVLGV---LACLTHGATMVFP----SP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 261 EFGAIA--KAFIAEKVTLANGAPAIFAPMLammkDMPQPP--DLSGVR--LVSGSSEPPLSMMRGFKEITGADVIHGYGA 334
Cdd:cd05917 78 SFDPLAvlEAIEKEKCTALHGVPTMFIAEL----EHPDFDkfDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 335 TETTPLATtnwhikpgldMDEEERWDFKRYQ--GLPVIGVEVKVVDPTGEELPRDGKSmGEVLMRGPWITESYFQLPDNS 412
Cdd:cd05917 154 TETSPVST----------QTRTDDSIEKRVNtvGRIMPHTEAKIVDPEGGIVPPVGVP-GELCIRGYSVMKGYWNDPEKT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 413 ERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAE 490
Cdd:cd05917 223 AEAIdgDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1949187543 491 DGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05917 303 EGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
47-542 |
3.11e-51 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 182.77 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:PRK07514 31 YGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LPVAEALAPKLDVKGwvVMT-DkpADEIETTLEnvvfyedLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHR 205
Cdd:PRK07514 111 FAWLSKIAAAAGAPH--VETlD--ADGTGSLLE-------AAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 SIY-----LHTMGGLAAlgasfDDTIMPITPMFHV--LswgfpqnavaagaklvlpgkfaaeefgaiakaFIAEKVTLAN 278
Cdd:PRK07514 180 NLLsnaltLVDYWRFTP-----DDVLIHALPIFHThgL--------------------------------FVATNVALLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 279 GAPAIFAPML---AMMKDMPQPPDLSGV---------------------RL-VSGSSepPLSM--MRGFKEITGADVIHG 331
Cdd:PRK07514 223 GASMIFLPKFdpdAVLALMPRATVMMGVptfytrllqeprltreaaahmRLfISGSA--PLLAetHREFQERTGHAILER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLaTTNwhikPgldmdeeerWDFKRYQ---GLPVIGVEVKVVDP-TGEELPRDGKSMGEVlmRGPWITESYFQ 407
Cdd:PRK07514 301 YGMTETNMN-TSN----P---------YDGERRAgtvGFPLPGVSLRVTDPeTGAELPPGEIGMIEV--KGPNVFKGYWR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 408 LPDNS-ERF-LDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVA 485
Cdd:PRK07514 365 MPEKTaEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTA 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187543 486 YVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWED 542
Cdd:PRK07514 445 VVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
189-537 |
1.40e-50 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 179.60 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSiYLHTMGGLA--ALGASFDDTIMPITPMFHVLSWG----FPQNAVAAGakLVLPGKFAAEEF 262
Cdd:cd05958 104 FTSGTTGAPKATMHFHRD-PLASADRYAvnVLRLREDDRFVGSPPLAFTFGLGgvllFPFGVGASG--VLLEEATPDLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 GAIAKafiaEKVTLANGAPAIFAPMLAMmKDMPQPpDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGYGATETTP-- 339
Cdd:cd05958 181 SAIAR----YKPTVLFTAPTAYRAMLAH-PDAAGP-DLSSLRKcVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHif 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 340 LATTNWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPrDGkSMGEVLMRGPWItesYFQLPDNSER--FLD 417
Cdd:cd05958 255 ISARPGDARPG-------------ATGKPVPGYEAKVVDDEGNPVP-DG-TIGRLAVRGPTG---CRYLADKRQRtyVQG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG---AE 494
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1949187543 495 VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
47-538 |
1.68e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 183.23 E-value: 1.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRrhfELYFAVPGLAATML--QLNLRLAPEDLAYVVSHSKSDWI---- 120
Cdd:PRK07529 61 YAELLADVTRTANLLHSLGVGPGDVVAFLLPNLP---ETHFALWGGEAAGIanPINPLLEPEQIAELLRAAGAKVLvtlg 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 121 -FVDESLLP-VAEALAPKLDVKGWVVM---------TDKPADEIETTLENVVF-YEDLIKDKPDT---YDWPVVDEKTAA 185
Cdd:PRK07529 138 pFPGTDIWQkVAEVLAALPELRTVVEVdlarylpgpKRLAVPLIRRKAHARILdFDAELARQPGDrlfSGRPIGPDDVAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 186 YAgYTTGTTGRPKGVYYSHRS-IYLHTMGGlAALGASFDDTIMPITPMFHVlswgfpqNAV--------AAGAKLVLP-- 254
Cdd:PRK07529 218 YF-HTGGTTGMPKLAQHTHGNeVANAWLGA-LLLGLGPGDTVFCGLPLFHV-------NALlvtglaplARGAHVVLAtp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 ----GKFAAEEFGAIAKAFiaeKVTLANGAPAIFApmlAMMKDMPQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVI 329
Cdd:PRK07529 289 qgyrGPGVIANFWKIVERY---RINFLSGVPTVYA---ALLQVPVDGHDISSLRYAlCGAAPLPVEVFRRFEAATGVRIV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTPLATTNW---HIKPGldmdeeerwdfkrYQGLPVIGVEVKVV--DPTG---EELPRDgkSMGEVLMRGPWI 401
Cdd:PRK07529 363 EGYGLTEATCVSSVNPpdgERRIG-------------SVGLRLPYQRVRVVilDDAGrylRDCAVD--EVGVLCIAGPNV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 402 TESYFQLPDNSERFLD-GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQ 480
Cdd:PRK07529 428 FSGYLEAAHNKGLWLEdGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAG 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 481 ERPVAYVVAEDGAEVTRETIVEVLGDRFA-KWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK07529 508 ELPVAYVQLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
6-544 |
1.07e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 179.03 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 6 PSTLGDsyqLNTTSMIRHAatvfgeQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLtelGVGAGSMVGVLDWNSRrhfEL 85
Cdd:PRK06188 11 GATYGH---LLVSALKRYP------DRPALVLGDTRLTYGQLADRISRYIQAFEAL---GLGTGDAVALLSLNRP---EV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 86 YFAvpgLAATMLQ------LNLRLAPEDLAYVVSHSKSDWIFVDesllPV-----AEALAPKLD-VKGWVvmtdkpadei 153
Cdd:PRK06188 76 LMA---IGAAQLAglrrtaLHPLGSLDDHAYVLEDAGISTLIVD----PApfverALALLARVPsLKHVL---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 154 etTLENVVFYEDLIkDKPDTYD-WPVVDEKTA---AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPI 229
Cdd:PRK06188 139 --TLGPVPDGVDLL-AAAAKFGpAPLVAAALPpdiAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 230 TPMFHvlswgfpqnavaAGAKLVLPG-----------KFAAEEF-GAIAKafiaEKVTLAngapaIFAP-MLAMMKDMPQ 296
Cdd:PRK06188 216 TPLSH------------AGGAFFLPTllrggtvivlaKFDPAEVlRAIEE----QRITAT-----FLVPtMIYALLDHPD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 297 PP--DLSGVRLVS-GSSepPLSMMR---GFKEItGADVIHGYGATETTPLATTnwhikpgLDMDEEERWDFKRYQ--GLP 368
Cdd:PRK06188 275 LRtrDLSSLETVYyGAS--PMSPVRlaeAIERF-GPIFAQYYGQTEAPMVITY-------LRKRDHDPDDPKRLTscGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 369 VIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSG 447
Cdd:PRK06188 345 TPGLRVALLDEDGREVAQG--EVGEICVRGPLVMDGYWNRPEeTAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 448 GEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTS 527
Cdd:PRK06188 423 GFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTA 502
|
570
....*....|....*...
gi 1949187543 528 VGKLDKKLLR-KTWEDAE 544
Cdd:PRK06188 503 LGKPDKKALRaRYWEGRG 520
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
25-537 |
1.10e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 179.11 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEV-VYRNSDGSWGRSNYA---DEFKRMAQLAHgltELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLN 100
Cdd:PRK08008 17 ADVYGHKTAlIFESSGGVVRRYSYLelnEEINRTANLFY---SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 101 LRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLD--VKGWVVmtdkpADEIETTLENVVFYEDLIKDKPDTYDW-- 176
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtpLRHICL-----TRVALPADDGVSSFTQLKAQQPATLCYap 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAgYTTGTTGRPKGVYYSHRSI-----YLHTMGGLAAlgasfDDTIMPITPMFHV---LSWGFPqnAVAAG 248
Cdd:PRK08008 169 PLSTDDTAEIL-FTSGTTSRPKGVVITHYNLrfagyYSAWQCALRD-----DDVYLTVMPAFHIdcqCTAAMA--AFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 249 AKLVLPGKFAAEEF-GAIAKAfiaeKVTLANGAPAIfapMLAMMKDMPQPPD----LSGVRLVSGSSEpplSMMRGFKEI 323
Cdd:PRK08008 241 ATFVLLEKYSARAFwGQVCKY----RATITECIPMM---IRTLMVQPPSANDrqhcLREVMFYLNLSD---QEKDAFEER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 324 TGADVIHGYGATETTPLATTNwhiKPGldmdEEERWDfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRG---PW 400
Cdd:PRK08008 311 FGVRLLTSYGMTETIVGIIGD---RPG----DKRRWP---SIGRPGFCYEAEIRDDHNRPLPAG--EIGEICIKGvpgKT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 401 ITESYFQLPDNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEK 478
Cdd:PRK08008 379 IFKEYYLDPKATAKVLeaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSI 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 479 WQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK08008 459 RDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
16-489 |
1.54e-48 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 177.60 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 16 NTTSMIRHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAAT 95
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 96 MLQLNLRLAPEDLAYVVSHSKSDWIFV-DESLLPVAEALAPKL-DVKGWVVMTDKPADEIEttleNVVFYEDLIKDKPDT 173
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELpSLRHIVVLDPRGLRDDP----RLLSLDELLALGREV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 174 YDWPVVDEKTAAYAG-------YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVL--SWGFpqNA 244
Cdd:COG1022 168 ADPAELEARRAAVKPddlatiiYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFerTVSY--YA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 245 VAAGAKLVLpgkfaAEEFGAIAKAFIAEKVTLANGAPAIF----APMLAMMKDMP------------------------Q 296
Cdd:COG1022 246 LAAGATVAF-----AESPDTLAEDLREVKPTFMLAVPRVWekvyAGIQAKAEEAGglkrklfrwalavgrryararlagK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 297 PPDL--------------SGVR---------LVSGSSepPLSmmrgfKEIT------GADVIHGYGATETTPLATTN--W 345
Cdd:COG1022 321 SPSLllrlkhaladklvfSKLRealggrlrfAVSGGA--ALG-----PELArffralGIPVLEGYGLTETSPVITVNrpG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 346 HIKPGldmdeeerwdfkrYQGLPVIGVEVKVvdptGEElprdgksmGEVLMRGPWITESYFQLPD-NSERFL-DGWWRSG 423
Cdd:COG1022 394 DNRIG-------------TVGPPLPGVEVKI----AED--------GEILVRGPNVMKGYYKNPEaTAEAFDaDGWLHTG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187543 424 DVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSVKEAAVIGvpdekwQERPvaYVVA 489
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVG------DGRP--FLAA 507
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
46-537 |
1.97e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 175.26 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV--PGLAATMLqlNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAerSGLYYTCV--NSHLTPAEAAYIVDDSGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLPVAEALAPKL-DVKGWVVMtDKPADeiettLENVVFYEDLIKDKPDTydwPVVDEKTAAYAGYTTGTTGRPKGVYy 202
Cdd:PRK13391 104 AAKLDVARALLKQCpGVRHRLVL-DGDGE-----LEGFVGYAEAVAGLPAT---PIADESLGTDMLYSSGTTGRPKGIK- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 203 shrsiylhtmgglAALGASFDDTIMPITPMFHVLsWGF----------------PQNAV----AAGAKLVLPGKFAAEEF 262
Cdd:PRK13391 174 -------------RPLPEQPPDTPLPLTAFLQRL-WGFrsdmvylspaplyhsaPQRAVmlviRLGGTVIVMEHFDAEQY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 GAIAKAFiaeKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGAdVIHG-YGATE---T 337
Cdd:PRK13391 240 LALIEEY---GVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPcPPQVKEQMIDWWGP-IIHEyYAATEglgF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 TPLATTNWHIKPGLdmdeeerwdfkryQGLPVIGVeVKVVDPTGEELPRdgKSMGEVLMRG--PWiteSYFQLPDNSE-- 413
Cdd:PRK13391 316 TACDSEEWLAHPGT-------------VGRAMFGD-LHILDDDGAELPP--GEPGTIWFEGgrPF---EYLNDPAKTAea 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 RFLDG-WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG 492
Cdd:PRK13391 377 RHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1949187543 493 AEVT---RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK13391 457 VDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
189-533 |
2.15e-48 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 170.76 E-value: 2.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRsiylHTMGGLAALGA----SFDDTIMPITPMFHvlSWGFPQNAVAA---GAKLVLPGKFAAEe 261
Cdd:cd17638 7 FTSGTTGRSKGVMCAHR----QTLRAAAAWADcadlTEDDRYLIINPFFH--TFGYKAGIVAClltGATVVPVAVFDVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 262 fgAIAKAFIAEKVTLANGAPAIFAPMLammkDMPQPP--DLSGVRL-VSGSSEPPLSMMRGFKEITGAD-VIHGYGATEt 337
Cdd:cd17638 80 --AILEAIERERITVLPGPPTLFQSLL----DHPGRKkfDLSSLRAaVTGAATVPVELVRRMRSELGFEtVLTAYGLTE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 tplATTNWHIKPGLDMDeeerwDFKRYQGLPVIGVEVKVVDPtgeelprdgksmGEVLMRGPWITESYFQLPDNSERFLD 417
Cdd:cd17638 153 ---AGVATMCRPGDDAE-----TVATTCGRACPGFEVRIADD------------GEVLVRGYNVMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 --GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEV 495
Cdd:cd17638 213 adGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTL 292
|
330 340 350
....*....|....*....|....*....|....*...
gi 1949187543 496 TRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDK 533
Cdd:cd17638 293 TEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
41-544 |
2.31e-48 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 175.27 E-value: 2.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 41 SWGRSNYADEF-KRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDW 119
Cdd:PRK12406 7 SGDRRRSFDELaQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 120 IFVDESLL-PVAEALAPKLDVkgWVVMTdkPAdEIettLENVVFYEDLIKDKPDTYDWPVVDEKTAAYAG---------- 188
Cdd:PRK12406 87 LIAHADLLhGLASALPAGVTV--LSVPT--PP-EI---AAAYRISPALLTPPAGAIDWEGWLAQQEPYDGppvpqpqsmi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGL-AALGASFDDTIMPIT--PMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFGAI 265
Cdd:PRK12406 159 YTSGTTGHPKGVRRAAPTPEQAAAAEQmRALIYGLKPGIRALLtgPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 266 AKafiAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATETTPLATTN 344
Cdd:PRK12406 239 IE---RHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPcPADVKRAMIEWWGPVIYEYYGSTESGAVTFAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 345 ---WHIKPGLdmdeeerwdfkryQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITE-SYFQLPDN---SERflD 417
Cdd:PRK12406 316 sedALSHPGT-------------VGKAAPGAELRFVDEDGRPLPQGEI--GEIYSRIAGNPDfTYHNKPEKraeIDR--G 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTR 497
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1949187543 498 ETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKT-WEDAE 544
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPyWANAG 506
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
23-536 |
9.28e-48 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 171.94 E-value: 9.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDGswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVpgLA-----ATML 97
Cdd:cd05930 3 AVAVVDGDQSLTYAELDA---RAN---------RLARYLRERGVGPGDLVAVL---LERSLEMVVAI--LAvlkagAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 98 QLNLRLAPEDLAYVVSHSKSDwifvdesllpvaealapkldvkgwVVMTDkPADeiettlenvvfyedlikdkpdtydwp 177
Cdd:cd05930 66 PLDPSYPAERLAYILEDSGAK------------------------LVLTD-PDD-------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 vvdektAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMGglAALGASFDDTIMPITPMFHVLSWG--FPqnAVAAGAKLVL 253
Cdd:cd05930 95 ------LAYVIYTSGSTGKPKGVMVEHRGLvnLLLWMQ--EAYPLTPGDRVLQFTSFSFDVSVWeiFG--ALLAGATLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLammkDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEI-TGADVIHG 331
Cdd:cd05930 165 LPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEAlPPDLVRRWRELlPGARLVNL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLATTnWHIKPGLDMDEeerwdfkRYQ-GLPVIGVEVKVVDPTGEELPrDGKsMGEVLMRGPWITESYFQLPD 410
Cdd:cd05930 241 YGPTEATVDATY-YRVPPDDEEDG-------RVPiGRPIPNTRVYVLDENLRPVP-PGV-PGELYIGGAGLARGYLNRPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 NS-ERFLDGWW-------RSGDVGVIFPNGYLKLTDRLKDVIK-SG-----GEwissidMENAILDSPSVKEAAVIGVPD 476
Cdd:cd05930 311 LTaERFVPNPFgpgermyRTGDLVRWLPDGNLEFLGRIDDQVKiRGyrielGE------IEAALLAHPGVREAAVVARED 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 477 EKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05930 385 GDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
53-537 |
1.17e-47 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 173.79 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLP-VAE 131
Cdd:PRK13382 77 RSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSAtVDR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 132 ALAPKLDVKGWVVMTDKPADeieTTLENVVfyedlikDKPDTyDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRsiylht 211
Cdd:PRK13382 157 ALADCPQATRIVAWTDEDHD---LTVEVLI-------AAHAG-QRPEPTGRKGRVILLTSGTTGTPKGARRSGP------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 212 mGGLAALGASFDDTIM----PI---TPMFHvlSWGFPQNAVAA--GAKLVLPGKFAAEEFGAIAKAFIAEKVTLAngaPA 282
Cdd:PRK13382 220 -GGIGTLKAILDRTPWraeePTvivAPMFH--AWGFSQLVLAAslACTIVTRRRFDPEATLDLIDRHRATGLAVV---PV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 283 IFAPMLAMMKDMPQPPDLSGVRLV--SGSSEPPlSMMRGFKEITGaDVIHG-YGATETTPLATTNwhikPGldmdeeerw 359
Cdd:PRK13382 294 MFDRIMDLPAEVRNRYSGRSLRFAaaSGSRMRP-DVVIAFMDQFG-DVIYNnYNATEAGMIATAT----PA--------- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 360 DFKRY---QGLPVIGVEVKVVDPTGEELPrDGKsMGEVLMRGPWITESYfqLPDNSERFLDGWWRSGDVGVIFPNGYLKL 436
Cdd:PRK13382 359 DLRAApdtAGRPAEGTEIRILDQDFREVP-TGE-VGTIFVRNDTQFDGY--TSGSTKDFHDGFMASGDVGYLDENGRLFV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 437 TDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDE 516
Cdd:PRK13382 435 VGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRD 514
|
490 500
....*....|....*....|.
gi 1949187543 517 IIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK13382 515 IVVLDELPRGATGKILRRELQ 535
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
44-537 |
3.73e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 171.53 E-value: 3.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESllpVAEALAPKLDVKGWVVMTDkpADEIETTlenvvfyedlikdkpdtydwPVVDEKTAAYAGYTTGTTGRPKGVYYS 203
Cdd:PRK09088 102 DA---VAAGRTDVEDLAAFIASAD--ALEPADT--------------------PSIPPERVSLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSIY--LHTMGGLAALGASfdDTIMPITPMFHVLswGFPQNA----VAAGAKLVLPGKFAAEEFGAIAKAFIAekVTLA 277
Cdd:PRK09088 157 ERNLQqtAHNFGVLGRVDAH--SSFLCDAPMFHII--GLITSVrpvlAVGGSILVSNGFEPKRTLGRLGDPALG--ITHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 278 NGAPAifapMLAMMKDMPQPpDLSGVR----LVSGSSEPPLSMMRGFKEiTGADVIHGYGATEttplATTNWhikpGLDM 353
Cdd:PRK09088 231 FCVPQ----MAQAFRAQPGF-DAAALRhltaLFTGGAPHAAEDILGWLD-DGIPMVDGFGMSE----AGTVF----GMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 354 DEEERWDFKRYQGLPVIGVEVKVVDPTGEELPrdGKSMGEVLMRGPWITESYFQLPDNSERFL--DGWWRSGDVGVIFPN 431
Cdd:PRK09088 297 DCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCP--AGVPGELLLRGPNLSPGYWRRPQATARAFtgDGWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 432 GYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKW 511
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKY 454
|
490 500
....*....|....*....|....*.
gi 1949187543 512 QLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
53-536 |
1.12e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 171.75 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEA 132
Cdd:PRK06710 58 KVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 133 LAPKLDVKGwvVMTDKPADEI--------------ETTL-------ENVVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTT 191
Cdd:PRK06710 138 VQSATKIEH--VIVTRIADFLpfpknllypfvqkkQSNLvvkvsesETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 192 GTTGRPKGVYYSHRSIYLHTMGGLAAL--GASFDDTIMPITPMFHVLSWGFPQN-AVAAGAKLVLPGKFAAEE-FGAIAK 267
Cdd:PRK06710 216 GTTGFPKGVMLTHKNLVSNTLMGVQWLynCKEGEEVVLGVLPFFHVYGMTAVMNlSIMQGYKMVLIPKFDMKMvFEAIKK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 268 afiaEKVTLANGAPAIFAPML--AMMKDMpqppDLSGVR-LVSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTN 344
Cdd:PRK06710 296 ----HKVTLFPGAPTIYIALLnsPLLKEY----DISSIRaCISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 345 WhikpgldmdeeeRWDfKRYQG---LPVIGVEVKVVD-PTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFL-DGW 419
Cdd:PRK06710 368 F------------LWE-KRVPGsigVPWPDTEAMIMSlETGEALPPG--EIGEIVVKGPQIMKGYWNKPEETAAVLqDGW 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 420 WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET 499
Cdd:PRK06710 433 LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEE 512
|
490 500 510
....*....|....*....|....*....|....*..
gi 1949187543 500 IVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK06710 513 LNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
18-538 |
1.17e-46 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 171.10 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 18 TSMIRHAATVFGEQE-VVyrNSDGSWGrsnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV--PGLAA 94
Cdd:COG1021 28 GDLLRRRAERHPDRIaVV--DGERRLS---YAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALfrAGAIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 95 TMLQLNLRLApeDLAYVVSHSK-SDWIFVDESLL----PVAEALA---PKLDVkgwVVMTDKPADEIEttlenvvfYEDL 166
Cdd:COG1021 103 VFALPAHRRA--EISHFAEQSEaVAYIIPDRHRGfdyrALARELQaevPSLRH---VLVVGDAGEFTS--------LDAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 167 IkDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGV-------YYSHRsiylhTMGGLAALGAsfDDTIMPITPMFH---VL 236
Cdd:COG1021 170 L-AAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIprthddyLYSVR-----ASAEICGLDA--DTVYLAALPAAHnfpLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 237 SWGFpQNAVAAGAKLVLPGKFAAEE-FGAIAKafiaEKVTLAngapAIFAPMLAMMKDMPQ--PPDLSGVRL--VSGSSE 311
Cdd:COG1021 242 SPGV-LGVLYAGGTVVLAPDPSPDTaFPLIER----ERVTVT----ALVPPLALLWLDAAErsRYDLSSLRVlqVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 312 PPlSMMRGFKEITGADVIHGYGATE----TTPLattnwhikpglDMDEEERWdfkRYQGLPV-IGVEVKVVDPTGEELPr 386
Cdd:COG1021 313 SP-ELARRVRPALGCTLQQVFGMAEglvnYTRL-----------DDPEEVIL---TTQGRPIsPDDEVRIVDEDGNPVP- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 387 DGkSMGEVLMRGPWITESYFQLPD-NSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSP 464
Cdd:COG1021 377 PG-EVGELLTRGPYTIRGYYRAPEhNARAFTpDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHP 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187543 465 SVKEAAVIGVPDEKWQERPVAYVVAeDGAEVTRETIVEVLGDR-FAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:COG1021 456 AVHDAAVVAMPDEYLGERSCAFVVP-RGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
22-537 |
1.65e-46 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 171.15 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 22 RHAATVFGEQE-VVYRNSDGSWgrsNYAdEF-KRMAQLAHGLTELGVGAGSMVGVldWNSRRhFE---LYFAVPGLAATM 96
Cdd:PRK08315 23 DRTAARYPDREaLVYRDQGLRW---TYR-EFnEEVDALAKGLLALGIEKGDRVGI--WAPNV-PEwvlTQFATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 97 LQLNLRLAPEDLAYVVSHSKSDWIFVDESL-----LPVAEALAPKLD--VKGWVVMTDKPAdeiettLENVVFYEDliKD 169
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAADGFkdsdyVAMLYELAPELAtcEPGQLQSARLPE------LRRVIFLGD--EK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 170 KPDTYDWP--------VVDEKTAAYAG-----------YTTGTTGRPKGVYYSHRSI----YLHTMgglaALGASFDDTI 226
Cdd:PRK08315 168 HPGMLNFDellalgraVDDAELAARQAtldpddpiniqYTSGTTGFPKGATLTHRNIlnngYFIGE----AMKLTEEDRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 227 -MPItPMFH-------VLswgfpqNAVAAGAKLVLPGkfaaEEF--GAIAKAFIAEKVTLANGAPAIFA-----PMLAMM 291
Cdd:PRK08315 244 cIPV-PLYHcfgmvlgNL------ACVTHGATMVYPG----EGFdpLATLAAVEEERCTALYGVPTMFIaeldhPDFARF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 292 kdmpqppDLSGVR--LVSGSSePPLSMMR------GFKEITGAdvihgYGATETTPLATtnwhiKPGLDMDEEerwdfKR 363
Cdd:PRK08315 313 -------DLSSLRtgIMAGSP-CPIEVMKrvidkmHMSEVTIA-----YGMTETSPVST-----QTRTDDPLE-----KR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 364 YQ--GLPVIGVEVKVVDP-TGEELPRdGKSmGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTD 438
Cdd:PRK08315 370 VTtvGRALPHLEVKIVDPeTGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIDadGWMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 439 RLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEII 518
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIR 527
|
570
....*....|....*....
gi 1949187543 519 VTDELPRTSVGKLDKKLLR 537
Cdd:PRK08315 528 FVDEFPMTVTGKIQKFKMR 546
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
15-541 |
2.59e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 169.84 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 15 LNTTSMIRHAATVFGEQ-EVVYRNSDGSWGrsnyadEFKRMAQ-LAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGL 92
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRiALVWGDRSWTWR------EIDARVDaLAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 93 AATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDKPADEIEttlenvvfYEDLIKDKPD 172
Cdd:PRK07470 81 GAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLD--------YEALVARHLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 173 T-YDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHrsiylHTMG-----GLAAL--GASFDDTIMPITPMFHvlSWGFPQNA 244
Cdd:PRK07470 153 ArVANAAVDHDDPCWFFFTSGTTGRPKAAVLTH-----GQMAfvitnHLADLmpGTTEQDASLVVAPLSH--GAGIHQLC 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 245 -VAAGAKLVLPG--KFAAEEFGAIAKAFiaeKVTLANGAPAIfapmLAMMKDMPQPP--DLSGVRLVSGSSEPplsMMRG 319
Cdd:PRK07470 226 qVARGAATVLLPseRFDPAEVWALVERH---RVTNLFTVPTI----LKMLVEHPAVDryDHSSLRYVIYAGAP---MYRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 320 FKEIT----GADVIHGYGATEttplATTNWHIKPGLDMDEEERWDFKRYQ-GLPVIGVEVKVVDPTGEELPrDGKSmGEV 394
Cdd:PRK07470 296 DQKRAlaklGKVLVQYFGLGE----VTGNITVLPPALHDAEDGPDARIGTcGFERTGMEVQIQDDEGRELP-PGET-GEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 395 LMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIG 473
Cdd:PRK07470 370 CVIGPAVFAGYYNNPEaNAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 474 VPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWE 541
Cdd:PRK07470 450 VPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELE 517
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
23-531 |
4.89e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 169.37 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNsdgswgrsnYADEFKRMAQLAHGltELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLR 102
Cdd:PRK08314 26 KTAIVFYGRAISYRE---------LLEEAERLAGYLQQ--ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 103 LAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKgWVVMT-----------DKPADEIETTLE-------NVVFYE 164
Cdd:PRK08314 95 NREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLR-HVIVAqysdylpaepeIAVPAWLRAEPPlqalapgGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 165 DLIK--DKPDTYDwpvVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLswGFpQ 242
Cdd:PRK08314 174 EALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVT--GM-V 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 243 N----AVAAGAKLVLPGKFAAEefgAIAKAFIAEKVTLANGAPaifapmlAMMKDMPQPP-----DLSGVRLVSGSSEP- 312
Cdd:PRK08314 248 HsmnaPIYAGATVVLMPRWDRE---AAARLIERYRVTHWTNIP-------TMVVDFLASPglaerDLSSLRYIGGGGAAm 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 313 PLSMMRGFKEITGADVIHGYGATETtpLATTnwHIKPGldmdeeerwDFKRYQ--GLPVIGVEVKVVDP-TGEELPrDGK 389
Cdd:PRK08314 318 PEAVAERLKELTGLDYVEGYGLTET--MAQT--HSNPP---------DRPKLQclGIPTFGVDARVIDPeTLEELP-PGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 390 SmGEVLMRGPWITESYFQLPD-NSERF--LDG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSP 464
Cdd:PRK08314 384 V-GEIVVHGPQVFKGYWNRPEaTAEAFieIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 465 SVKEAAVIGVPDEKWQERPVAYVVAEDGAE--VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKL 531
Cdd:PRK08314 463 AIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-545 |
4.99e-46 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 169.55 E-value: 4.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 20 MIRHAATVFGEQEVVYrnSDGSWGRsnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQL 99
Cdd:PRK06155 26 MLARQAERYPDRPLLV--FGGTRWT--YAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMTDK-PADEIETtlenvvfyedlikdKPDTYDWPV 178
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDApASVSVPA--------------GWSTAPLPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAG---------YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGA 249
Cdd:PRK06155 168 LDAPAPAAAVqpgdtaailYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 KLVLPGKFAAEEFGAIAKAFIAeKVTLANGApaifapMLAMMKDMPQPPDLSG--VRLVSGSSEPPlSMMRGFKEITGAD 327
Cdd:PRK06155 248 TYVLEPRFSASGFWPAVRRHGA-TVTYLLGA------MVSILLSQPARESDRAhrVRVALGPGVPA-ALHAAFRERFGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 VIHGYGATETT-PLATTNWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPrDGkSMGEVLMRG--PWITES 404
Cdd:PRK06155 320 LLDGYGSTETNfVIAVTHGSQRPG-------------SMGRLAPGFEARVVDEHDQELP-DG-EPGELLLRAdePFAFAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 405 -YFQLPDNS-ERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQER 482
Cdd:PRK06155 385 gYFGMPEKTvEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDE 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 483 PVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK------TWeDAEA 545
Cdd:PRK06155 465 VMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREqgvtadTW-DREA 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
43-536 |
6.55e-45 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 165.19 E-value: 6.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 43 GRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV--PGLAATMLQLNLRLApeDLAYVVSHSKSdwi 120
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALlrLGAVPVLALPSHRRS--ELSAFCAHAEA--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 121 fvdeSLLPVAEALAPkldvkgwvvmtdkpadeiettLENVVFYEDLIKDKPDTydwpvvdektaAYAGYTTGTTGRPKGV 200
Cdd:cd05920 114 ----VAYIVPDRHAG---------------------FDHRALARELAESIPEV-----------ALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 201 YYSHRSiYLHTMGGLAAL-GASFDDTIMPITPMFHvlswGFPQN------AVAAGAKLVLPGKFAAEE-FGAIAKafiaE 272
Cdd:cd05920 158 PRTHND-YAYNVRASAEVcGLDQDTVYLAVLPAAH----NFPLAcpgvlgTLLAGGRVVLAPDPSPDAaFPLIER----E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 273 KVTLANGAPAIFapMLAMMKDMPQPPDLSGVRL--VSGSSEPPlSMMRGFKEITGADVIHGYGATETTPLATTnwhikpg 350
Cdd:cd05920 229 GVTVTALVPALV--SLWLDAAASRRADLSSLRLlqVGGARLSP-ALARRVPPVLGCTLQQVFGMAEGLLNYTR------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 351 LDmDEEERwdFKRYQGLPVI-GVEVKVVDPTGEELPrDGKsMGEVLMRGPWITESYFQLPDNSERFL--DGWWRSGDVGV 427
Cdd:cd05920 299 LD-DPDEV--IIHTQGRPMSpDDEIRVVDEEGNPVP-PGE-EGELLTRGPYTIRGYYRAPEHNARAFtpDGFYRTGDLVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 428 IFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDgAEVTRETIVEVLGDR 507
Cdd:cd05920 374 RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLRER 452
|
490 500 510
....*....|....*....|....*....|
gi 1949187543 508 -FAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05920 453 gLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
184-538 |
1.45e-44 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 161.11 E-value: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 AAYAgYTTGTTGRPKGVYYSHRS-IYLHTMGGLAALGASfDDTIMPITPMFHVLSwGFPQ--NAVAAGAKLVLPG----- 255
Cdd:cd05944 5 AAYF-HTGGTTGTPKLAQHTHSNeVYNAWMLALNSLFDP-DDVLLCGLPLFHVNG-SVVTllTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 -KFAAEEFGAIAKAFiaeKVTLANGAPAIFAPMLAMmkdmPQPPDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGYG 333
Cdd:cd05944 82 nPGLFDNFWKLVERY---RITSLSTVPTVYAALLQV----PVNADISSLRFaMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 334 ATETTPLATTNW---HIKPGldmdeeerwdfKRYQGLPVIGVEVKVVDPTGEELPRDG-KSMGEVLMRGPWITESYFQLP 409
Cdd:cd05944 155 LTEATCLVAVNPpdgPKRPG-----------SVGLRLPYARVRIKVLDGVGRLLRDCApDEVGEICVAGPGVFGGYLYTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVV 488
Cdd:cd05944 224 GNKNAFVaDGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 489 AEDGAEVTRETIVEVLGDRFA-KWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05944 304 LKPGAVVEEEELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
189-537 |
1.55e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 165.71 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDD---TIMPITPMFHVLSWGFPQNA--VAAGAKLVLPGkfaAEEFG 263
Cdd:PRK05677 214 YTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAmmLIGNHNILISN---PRDLP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 264 AIAKAFIAEKVTLANGAPAIFAPmLAMMKDMpQPPDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLAT 342
Cdd:PRK05677 291 AMVKELGKWKFSGFVGLNTLFVA-LCNNEAF-RKLDFSALKLtLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVS 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 343 TN--WHIKPGLdmdeeerwdfkryQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFLD--G 418
Cdd:PRK05677 369 VNpsQAIQVGT-------------IGIPVPSTLCKVIDDDGNELPLG--EVGELCVKGPQVMKGYWQRPEATDEILDsdG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 419 WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRE 498
Cdd:PRK05677 434 WLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE 513
|
330 340 350
....*....|....*....|....*....|....*....
gi 1949187543 499 TIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK05677 514 QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
189-532 |
7.68e-44 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 158.62 E-value: 7.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHT--MGGLAALGASFddTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEfgaIA 266
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQAlvLAVLQAIDEGT--VFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEE---VL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 267 KAFIAEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRlvSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTNWH 346
Cdd:cd17636 82 ELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLR--SSPAAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATFAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 347 IKPGLDMdeeerwdfkryQGLPVIGVEVKVVDPTGEELPrDGkSMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDV 425
Cdd:cd17636 158 GGGAIGG-----------AGRPSPLVQVRILDEDGREVP-DG-EVGEIVARGPTVMAGYWNRPEvNARRTRGGWHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLG 505
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCR 304
|
330 340
....*....|....*....|....*..
gi 1949187543 506 DRFAKWQLPDEIIVTDELPRTSVGKLD 532
Cdd:cd17636 305 ARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
39-538 |
4.59e-43 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 160.92 E-value: 4.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRS-NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKS 117
Cdd:PLN02246 44 DGATGRVyTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 118 DWIFVDESLLPVAEALAPKLDVKgwVVMTDKPADeiettleNVVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRP 197
Cdd:PLN02246 124 KLIITQSCYVDKLKGLAEDDGVT--VVTIDDPPE-------GCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 198 KGVYYSHRS---------------IYLHTmgglaalgasfDDTIMPITPMFHVLSWgfpqNAVA-----AGAKLVLPGKF 257
Cdd:PLN02246 195 KGVMLTHKGlvtsvaqqvdgenpnLYFHS-----------DDVILCVLPMFHIYSL----NSVLlcglrVGAAILIMPKF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 258 aaeEFGAIAKAFIAEKVTLANGAPAIfapMLAMMK-DMPQPPDLSGVRLV-SGSSepPLSmmrgfKEIT--------GAD 327
Cdd:PLN02246 260 ---EIGALLELIQRHKVTIAPFVPPI---VLAIAKsPVVEKYDLSSIRMVlSGAA--PLG-----KELEdafraklpNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 VIHGYGATETTPL-------ATTNWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDP-TGEELPRDgkSMGEVLMRGP 399
Cdd:PLN02246 327 LGQGYGMTEAGPVlamclafAKEPFPVKSG-------------SCGTVVRNAELKIVDPeTGASLPRN--QPGEICIRGP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 400 WITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDE 477
Cdd:PLN02246 392 QIMKGYLNDPEATANTIDkdGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDE 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 478 KWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PLN02246 472 VAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
25-532 |
2.65e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 158.89 E-value: 2.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRNSDGswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLA 104
Cdd:PRK07798 21 ALVCGDRRLTYAELEE---RAN---------RLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 105 PEDLAYVVSHSKSDWIFVDESLLP-VAEALAPKLDVKGWVVMTDKPADEIETtleNVVFYEDLIKDKPDTYDWPvvdEKT 183
Cdd:PRK07798 89 EDELRYLLDDSDAVALVYEREFAPrVAEVLPRLPKLRTLVVVEDGSGNDLLP---GAVDYEDALAAGSPERDFG---ERS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 A--AYAGYTTGTTGRPKGVYYSHRSIYLHTMGG--------------LAALGASFDDTI-MPITPMFHvlswGFPQNAVA 246
Cdd:PRK07798 163 PddLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGrdfatgepiedeeeLAKRAAAGPGMRrFPAPPLMH----GAGQWAAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 247 A----GAKLVLP--GKFAAEEFGAIAKAfiaEKVTLAN--GaPAIFAPMLAMMkDMPQPPDLSGVRLVSgSSEPPLS--M 316
Cdd:PRK07798 239 AalfsGQTVVLLpdVRFDADEVWRTIER---EKVNVITivG-DAMARPLLDAL-EARGPYDLSSLFAIA-SGGALFSpsV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 317 MRGFKE-ITGADVIHGYGATETTPLATtnwhikpGLDMDEEERWDFKRYQglpvIGVEVKVVDPTGEELPRDGKSMGEVL 395
Cdd:PRK07798 313 KEALLElLPNVVLTDSIGSSETGFGGS-------GTVAKGAVHTGGPRFT----IGPRTVVLDEDGNPVEPGSGEIGWIA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 396 MRGPwITESYFQLPDNSER-F--LDG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAA 470
Cdd:PRK07798 382 RRGH-IPLGYYKDPEKTAEtFptIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADAL 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 471 VIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLD 532
Cdd:PRK07798 461 VVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
178-538 |
2.74e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 156.73 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTimpitpMFHVLSWGFPQNAVAAGAKLVLPG-- 255
Cdd:cd05972 77 VTDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI------HWNIADPGWAKGAWSSFFGPWLLGat 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 -------KFAAEEFGAIAKAfiaEKVTLANGAPAIFApmlAMMKDMPQPPDLSGVRLVSGSSEPPL-SMMRGFKEITGAD 327
Cdd:cd05972 151 vfvyegpRFDAERILELLER---YGVTSFCGPPTAYR---MLIKQDLSSYKFSHLRLVVSAGEPLNpEVIEWWRAATGLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 VIHGYGATETT-PLATTNW-HIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPrDGKSmGEVLMRGPWITES- 404
Cdd:cd05972 225 IRDGYGQTETGlTVGNFPDmPVKPG-------------SMGRPTPGYDVAIIDDDGRELP-PGEE-GDIAIKLPPPGLFl 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 405 -YFQLPDNSE-RFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQER 482
Cdd:cd05972 290 gYVGDPEKTEaSIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEV 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 483 PVAYVVAEDGAEVTRETIVEVLG---DRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05972 370 VKAFVVLTSGYEPSEELAEELQGhvkKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
47-541 |
1.53e-41 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 154.97 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGLA---ATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVL---SPRSPELYFSMLGIGkigAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLlpvaealapkldvkgwvvmtdkpadeiettlenvvfyedliKDKpdtydwpvVDEKTAAYAGYTTGTTGRPKGVYYS 203
Cdd:cd05969 80 EEL-----------------------------------------YER--------TDPEDPTLLHYTSGTTGTPKGVLHV 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSIYLHTMGGLAALGASFDD----TIMP--ITPMFHVLsWGFPQNAVAAgakLVLPGKFAAEE-FGAIAKafiaEKVTL 276
Cdd:cd05969 111 HDAMIFYYFTGKYVLDLHPDDiywcTADPgwVTGTVYGI-WAPWLNGVTN---VVYEGRFDAESwYGIIER----VKVTV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 277 ANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP--PlSMMRGFKEITGADVIHGYGATETTPLATTNW---HIKPGl 351
Cdd:cd05969 183 WYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPlnP-EAIRWGMEVFGVPIHDTWWQTETGSIMIANYpcmPIKPG- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 352 dmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPW--ITESYFQLPDN-SERFLDGWWRSGDVGVI 428
Cdd:cd05969 261 ------------SMGKPLPGVKAAVVDENGNELPPG--TKGILALKPGWpsMFRGIWNDEERyKNSFIDGWYLTGDLAYR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 429 FPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGdrF 508
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIIN--F 404
|
490 500 510
....*....|....*....|....*....|....*...
gi 1949187543 509 AKWQL-----PDEIIVTDELPRTSVGKLDKKLLrKTWE 541
Cdd:cd05969 405 VRQKLgahvaPREIEFVDNLPKTRSGKIMRRVL-KAKE 441
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
47-538 |
5.62e-41 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 155.38 E-value: 5.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:cd17642 47 YAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LPVAEALAPKLD-VKGWVVMTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVD-EKTAAYAGYTTGTTGRPKGVYYSH 204
Cdd:cd17642 127 LQKVLNVQKKLKiIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFDrDEQVALIMNSSGSTGLPKGVQLTH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 205 RSI---YLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFgaiAKAFIAEKVTLANGAP 281
Cdd:cd17642 207 KNIvarFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEELF---LRSLQDYKVQSALLVP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 282 AIFApMLAMmKDMPQPPDLSG-VRLVSGSSepPLSMMRG---FKEITGADVIHGYGATETTP--LATTNWHIKPGldmde 355
Cdd:cd17642 284 TLFA-FFAK-STLVDKYDLSNlHEIASGGA--PLSKEVGeavAKRFKLPGIRQGYGLTETTSaiLITPEGDDKPG----- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 356 eerwdfkrYQGLPVIGVEVKVVDP-TGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFL--DGWWRSGDVGVIFPNG 432
Cdd:cd17642 355 --------AVGKVVPFFYAKVVDLdTGKTLGPNER--GELCVKGPMIMKGYVNNPEATKALIdkDGWLHSGDIAYYDEDG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 433 YLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRF--AK 510
Cdd:cd17642 425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVstAK 504
|
490 500
....*....|....*....|....*...
gi 1949187543 511 WqLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd17642 505 R-LRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-538 |
6.10e-41 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 150.56 E-value: 6.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 190 TTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEefgaiakaf 269
Cdd:cd17630 8 TSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQAL--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 270 iaeKVTLANGAP---AIFAPMLAMMKDMPQ-PPDLSGVRLV-SGSSEPPLSMMRGFKEiTGADVIHGYGATETTPLATTn 344
Cdd:cd17630 79 ---AEDLAPPGVthvSLVPTQLQRLLDSGQgPAALKSLRAVlLGGAPIPPELLERAAD-RGIPLYTTYGMTETASQVAT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 345 whikpgLDMDEEERwdfkRYQGLPVIGVEVKVVDPtgeelprdgksmGEVLMRGPWITESYFQLPDNSERFLDGWWRSGD 424
Cdd:cd17630 154 ------KRPDGFGR----GGVGVLLPGRELRIVED------------GEIWVGGASLAMGYLRGQLVPEFNEDGWFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 425 VGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVtrETIVEVL 504
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADP--AELRAWL 289
|
330 340 350
....*....|....*....|....*....|....
gi 1949187543 505 GDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
41-538 |
1.27e-40 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 154.57 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 41 SWGRSNYADEF-KRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDW 119
Cdd:PLN02860 28 SGNRRRTGHEFvDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 120 IFVDESL----LPVAEALAPKLdvkGWVVMTDKPADEIETTLENVVFYEDL----IKDKPDTYDWPVVDektAAYAGYTT 191
Cdd:PLN02860 108 LVTDETCsswyEELQNDRLPSL---MWQVFLESPSSSVFIFLNSFLTTEMLkqraLGTTELDYAWAPDD---AVLICFTS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 192 GTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVlswGFPQNAVA---AGAKLVLPGKF-AAEEFGAIAK 267
Cdd:PLN02860 182 GTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHI---GGLSSALAmlmVGACHVLLPKFdAKAALQAIKQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 268 AFIAEKVTLangaPAIFAPMLAMMKDMPQPPDLSGVR-LVSGSSEPPLSMMRGFKEI-TGADVIHGYGATETTPLAT--- 342
Cdd:PLN02860 259 HNVTSMITV----PAMMADLISLTRKSMTWKVFPSVRkILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEACSSLTfmt 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 343 ----TNWHIKPGLDMDEEERWD-FKRYQGL----PVIGVEVKVVDPtgeELPRDGKsmgeVLMRGPWITESYFQLP--DN 411
Cdd:PLN02860 335 lhdpTLESPKQTLQTVNQTKSSsVHQPQGVcvgkPAPHVELKIGLD---ESSRVGR----ILTRGPHVMLGYWGQNseTA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 412 SERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAED 491
Cdd:PLN02860 408 SVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRD 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 492 G----------AEVTRETIVEVLGD-----RFAKWQLPDEIIV-TDELPRTSVGKLDKKLLRK 538
Cdd:PLN02860 488 GwiwsdnekenAKKNLTLSSETLRHhcrekNLSRFKIPKLFVQwRKPFPLTTTGKIRRDEVRR 550
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
23-536 |
1.47e-40 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 153.25 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPG-LAATMLQLNL 101
Cdd:cd17655 13 HTAVVFEDQTLTYRELN------------ERANQLARTLREKGVGPDTIVGIM---AERSLEMIVGILGiLKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLA-PED-LAYVVSHSKSDWIFVDEsllpvaeALAPKLDVKGWVVMTDKPADEIE--TTLENVVFYEDLikdkpdtydwp 177
Cdd:cd17655 78 DPDyPEErIQYILEDSGADILLTQS-------HLQPPIAFIGLIDLLDEDTIYHEesENLEPVSKSDDL----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 vvdektaAYAGYTTGTTGRPKGVYYSHRSI--YLH------------TMGGLAALgaSFDDTImpiTPMFHVLswgfpqn 243
Cdd:cd17655 140 -------AYVIYTSGSTGKPKGVMIEHRGVvnLVEwankviyqgehlRVALFASI--SFDASV---TEIFASL------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 244 avAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLANGAPAIfapmLAMMKDMPQPPDLSGVRLVSGSSEPPLSMMRGFKEI 323
Cdd:cd17655 201 --LSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH----LKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIEL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 324 --TGADVIHGYGATETTPLATTnWHIKPGLDMDEeerwdfKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWI 401
Cdd:cd17655 275 fgTNPTITNAYGPTETTVDASI-YQYEPETDQQV------SVPIGKPLGNTRIYILDQYGRPQPVG--VAGELYIGGEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 402 TESYFQLPD-NSERFLDG-------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIG 473
Cdd:cd17655 346 ARGYLNRPElTAEKFVDDpfvpgerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIA 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 474 VPDEKWQERPVAYVVAEdgaevtRETIVEVLGDRFAKwQLPDEIIVT-----DELPRTSVGKLDKKLL 536
Cdd:cd17655 426 RKDEQGQNYLCAYIVSE------KELPVAQLREFLAR-ELPDYMIPSyfiklDEIPLTPNGKVDRKAL 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
52-537 |
1.94e-40 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 152.53 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 52 KRMAQLAHGLTELGVGAGSMvgvlDWNSRRHFELYfAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAE 131
Cdd:cd05929 8 RAQVFHQRRLLLLDVYSIAL----NRNARAAAAEG-VWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 132 ALA-PKLDVKGWVVMTDKPAdeiettLENVVFYEDLIKDKPDTydwPVVDEKTAAYAGYTTGTTGRPKGV--YYSHRSIY 208
Cdd:cd05929 83 AIIeIKAAALVCGLFTGGGA------LDGLEDYEAAEGGSPET---PIEDEAAGWKMLYSGGTTGRPKGIkrGLPGGPPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 209 -LHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFGAIAKAFiaeKVTLANGAPAIFAPM 287
Cdd:cd05929 154 nDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERY---RVTFAQFVPTMFVRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 288 LAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATE---TTPLATTNWHIKPGldmdeeerwdfkr 363
Cdd:cd05929 231 LKLPEAVRNAYDLSSLKRVIHAAAPcPPWVKEQWIDWGGPIIWEYYGGTEgqgLTIINGEEWLTHPG------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 364 YQGLPVIGvEVKVVDPTGEELPRdgKSMGEVLMRGPWITEsYFQLPDNS--ERFLDGWWRSGDVGVIFPNGYLKLTDRLK 441
Cdd:cd05929 298 SVGRAVLG-KVHILDEDGNEVPP--GEIGEVYFANGPGFE-YTNDPEKTaaARNEGGWSTLGDVGYLDEDGYLYLTDRRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 442 DVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGA---EVTRETIVEVLGDRFAKWQLPDEII 518
Cdd:cd05929 374 DMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagTALAEELIAFLRDRLSRYKCPRSIE 453
|
490
....*....|....*....
gi 1949187543 519 VTDELPRTSVGKLDKKLLR 537
Cdd:cd05929 454 FVAELPRDDTGKLYRRLLR 472
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
47-534 |
4.95e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 152.73 E-value: 4.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSrrhfeLYFAVPGLAATmlQLNLRLAPEDLAyvvshsksdwifvdesl 126
Cdd:PRK05852 46 YRDLARLVDDLAGQLTRSGLLPGDRVALRMGSN-----AEFVVALLAAS--RADLVVVPLDPA----------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LPVAEALAPKLDVKGWVVMTDK--PADEIETTLENVVFYEDLIKDKPDTYDWPVVD-----EKTAAYAG----------- 188
Cdd:PRK05852 102 LPIAEQRVRSQAAGARVVLIDAdgPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHldaatEPTPATSTpeglrpddami 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 -YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH-------VLSwgfpqnAVAAGAKLVLP--GKFA 258
Cdd:PRK05852 182 mFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHghgliaaLLA------TLASGGAVLLParGRFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 259 AEEFGAIAKAFIAekvTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATET 337
Cdd:PRK05852 256 AHTFWDDIKAVGA---TWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPlTAETAQALQTEFAAPVVCAFGMTEA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 TPLATTNwHIKpGLDMDEEERWDfkryQGL--PVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPDNS-ER 414
Cdd:PRK05852 333 THQVTTT-QIE-GIGQTENPVVS----TGLvgRSTGAQIRIVGSDGLPLPAG--AVGEVWLRGTTVVRGYLGDPTITaAN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 415 FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAE 494
Cdd:PRK05852 405 FTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1949187543 495 VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKK 534
Cdd:PRK05852 485 PTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
39-537 |
5.73e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 152.69 E-value: 5.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRSNYADEFKRMAQ-LAHGLTE-LGVGAGSMVGVLDWNSRrHFELYF-AVPGLAATMLQLNLRLAPEDLAYVVSHS 115
Cdd:PLN02574 60 DSSTGFSISYSELQPLVKsMAAGLYHvMGVRQGDVVLLLLPNSV-YFPVIFlAVLSLGGIVTTMNPSSSLGEIKKRVVDC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 116 KSDWIFVDeslLPVAEALAPkLDVKgwVVMTDKPADEIETTLENVVFYEdLIKDKPDTYDWPVVDEKTAAYAGYTTGTTG 195
Cdd:PLN02574 139 SVGLAFTS---PENVEKLSP-LGVP--VIGVPENYDFDSKRIEFPKFYE-LIKEDFDFVPKPVIKQDDVAAIMYSSGTTG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 196 RPKGVYYSHRSiYLHTMGGLAALGASF------DDTIMPITPMFHVLSWG-FPQNAVAAGAKLVLPGKFAAEEfgaIAKA 268
Cdd:PLN02574 212 ASKGVVLTHRN-LIAMVELFVRFEASQyeypgsDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASD---MVKV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSepPLS--MMRGF-KEITGADVIHGYGATETTPLATTNW 345
Cdd:PLN02574 288 IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAA--PLSgkFIQDFvQTLPHVDFIQGYGMTESTAVGTRGF 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 346 HIKpgldmdeeerwDFKRYQ--GLPVIGVEVKVVD-PTGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFL--DGWW 420
Cdd:PLN02574 366 NTE-----------KLSKYSsvGLLAPNMQAKVVDwSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATQSTIdkDGWL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 421 RSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETI 500
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAV 512
|
490 500 510
....*....|....*....|....*....|....*..
gi 1949187543 501 VEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PLN02574 513 INYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
44-536 |
7.52e-40 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 151.51 E-value: 7.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd05923 28 RLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLPVAEALAPKLDVkgwVVMTDKPADEIETTlenvvfYEDLIKDKPdtydwPVVDEktAAYAGYTTGTTGRPKGVYYS 203
Cdd:cd05923 108 VDAQVMDAIFQSGVRV---LALSDLVGLGEPES------AGPLIEDPP-----REPEQ--PAFVFYTSGTTGLPKGAVIP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSI-----YLHTMGGLAaLGASfdDTIMPITPMFHVLswGFpqNAVAAGAkLVLPGKF-AAEEF--GAIAKAFIAEKVT 275
Cdd:cd05923 172 QRAAesrvlFMSTQAGLR-HGRH--NVVLGLMPLYHVI--GF--FAVLVAA-LALDGTYvVVEEFdpADALKLIEQERVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 276 LANGAPAIFAPMLAMMKDMPQppDLSGVRLV--SGSSEPPLSMMRGFKEITGADVIHgYGATET-----TPLATTNWHIK 348
Cdd:cd05923 244 SLFATPTHLDALAAAAEFAGL--KLSSLRHVtfAGATMPDAVLERVNQHLPGEKVNI-YGTTEAmnslyMRDARTGTEMR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 349 PGLdmdeeerwdFKRYQGLPvIGVEVKVVDPTGEElprdgksmGE--VLMRGPWITESYFQLPD-NSERFLDGWWRSGDV 425
Cdd:cd05923 321 PGF---------FSEVRIVR-IGGSPDEALANGEE--------GEliVAAAADAAFTGYLNQPEaTAKKLQDGWYRTGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAeVTRETIVEV-L 504
Cdd:cd05923 383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFcR 461
|
490 500 510
....*....|....*....|....*....|..
gi 1949187543 505 GDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05923 462 ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
47-537 |
3.14e-39 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 149.42 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPG---LAATMLQLNLRLAPEDLAYVVSHSksdwifvD 123
Cdd:cd17651 23 YAELDRRANRLAHRLRARGVGPGDLVALC---ARRSAELVVALLAilkAGAAYVPLDPAYPAERLAFMLADA-------G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLPVAEALAPKLDVK-GWVVMTDKPADEIETTLENVvfyedlikdkpdtydwPVVDEKTAAYAGYTTGTTGRPKGVYY 202
Cdd:cd17651 93 PVLVLTHPALAGELAVElVAVTLLDQPGAAAGADAEPD----------------PALDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 203 SHRSIYLHTMGGLAALGASFDDT---IMPITpmFHVLSWG-FPqnAVAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLAN 278
Cdd:cd17651 157 PHRSLANLVAWQARASSLGPGARtlqFAGLG--FDVSVQEiFS--TLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 279 gAPAIFAPMLA--MMKDMPQPPDLSGVrLVSGSSEPPLSMMRGF-KEITGADVIHGYGATETTpLATTnwHIKPGldmdE 355
Cdd:cd17651 233 -LPTVALRALAehGRPLGVRLAALRYL-LTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTETH-VVTA--LSLPG----D 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 356 EERWDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFLDGWW-------RSGDVGV 427
Cdd:cd17651 304 PAAWPAPPPIGRPIDNTRVYVLDAALRPVPPG--VPGELYIGGAGLARGYLNRPElTAERFVPDPFvpgarmyRTGDLAR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 428 IFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDR 507
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATH 461
|
490 500 510
....*....|....*....|....*....|
gi 1949187543 508 FAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
23-536 |
3.40e-39 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 149.35 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQL 99
Cdd:cd17646 14 APAVVDEGRTLTYRELD------------ERANRLAHLLRARGVGPEDRVAVL---LPRSADLVVALLAVlkaGAAYLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWvvmtdkpadeiettlenvvfyedLIKDKPDTYDWPVV 179
Cdd:cd17646 79 DPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDE-----------------------ALAAPPATPPLVPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 DEKTAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGAsfDDTIMPITPM-FHVLSWGFPQnAVAAGAKLVLPGK 256
Cdd:cd17646 136 RPDNLAYVIYTSGSTGRPKGVMVTHAGIvnRLLWMQDEYPLGP--GDRVLQKTPLsFDVSVWELFW-PLVAGARLVVARP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEFGAIAKAFIAEKVTLANgapaiFAP-MLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGA 334
Cdd:cd17646 213 GGHRDPAYLAALIREHGVTTCH-----FVPsMLRVFLAEPAAGSCASLRRVFCSGEAlPPELAARFLALPGAELHNLYGP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 335 TETTpLATTNWHIKPGldmDEEERWDFKRyqglPVIGVEVKVVDPTGEELPrDGkSMGEVLMRGPWITESYFQLPD-NSE 413
Cdd:cd17646 288 TEAA-IDVTHWPVRGP---AETPSVPIGR----PVPNTRLYVLDDALRPVP-VG-VPGELYLGGVQLARGYLGRPAlTAE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 RFLDGW-------WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAY 486
Cdd:cd17646 358 RFVPDPfgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGY 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 487 VVAEDGAE-VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17646 438 VVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
178-536 |
1.13e-38 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 147.07 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAAYAGYTTGTTGRPKGVYYSHRSIylhtMGGLAALGASFDDTIMPITPMFHVLS--------WGfpqnAVAAGA 249
Cdd:cd17643 89 LTDPDDLAYVIYTSGSTGRPKGVVVSHANV----LALFAATQRWFGFNEDDVWTLFHSYAfdfsvweiWG----ALLHGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 KLVLPGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAP-MLAMMKDMPQPPDLsgvRLVSGSSEP-PLSMMRGFKE---IT 324
Cdd:cd17643 161 RLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQlVEAADRDGRDPLAL---RYVIFGGEAlEAAMLRPWAGrfgLD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 325 GADVIHGYGATETTPLATtnWHIkpgLDMDEEERWDfKRYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITES 404
Cdd:cd17643 238 RPQLVNMYGITETTVHVT--FRP---LDAADLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGV--VGELYVSGAGVARG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 405 YFQLPD-NSERFLDG--------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVP 475
Cdd:cd17643 310 YLGRPElTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 476 DEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17643 390 DEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
140-537 |
2.25e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 145.35 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 140 KGWVVMT--DKPADEI-ETTLENVVFYEDLIKDKPDTYDWPV-VDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGL 215
Cdd:PRK12492 161 KGWLVNTvvDKVKKMVpAYHLPQAVPFKQALRQGRGLSLKPVpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVR 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 216 AALGASFDD-----------TIMPItPMFHVlsWGFPQNAVA---AGAKLVLPGKfaAEEFGAIAKAFIAEKVTLANGAP 281
Cdd:PRK12492 241 ACLSQLGPDgqplmkegqevMIAPL-PLYHI--YAFTANCMCmmvSGNHNVLITN--PRDIPGFIKELGKWRFSALLGLN 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 282 AIFapmLAMMkDMPQPPDLS----------GVRLVSGSSEPplsmmrgFKEITGADVIHGYGATETTPLATTNWHikpgl 351
Cdd:PRK12492 316 TLF---VALM-DHPGFKDLDfsalkltnsgGTALVKATAER-------WEQLTGCTIVEGYGLTETSPVASTNPY----- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 352 dmDEEERWDfkrYQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIF 429
Cdd:PRK12492 380 --GELARLG---TVGIPVPGTALKVIDDDGNELPLGER--GELCIKGPQVMKGYWQQPEATAEALDaeGWFKTGDIAVID 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 430 PNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAeVTRETIVEVLGDRFA 509
Cdd:PRK12492 453 PDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFT 531
|
410 420
....*....|....*....|....*...
gi 1949187543 510 KWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK12492 532 GYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
22-541 |
4.03e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 144.65 E-value: 4.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 22 RHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPG---LAATMLQ 98
Cdd:PRK04319 51 RHADGGRKDKVALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIF---MPRIPELYFALLGalkNGAIVGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 99 LNLRLAPEDLAYVVSHSKSDWIFVDESLLP--VAEALaPKLDvkgWVVMTDKPADEIETTLEnvvfYEDLIKDKPDTYDW 176
Cdd:PRK04319 128 LFEAFMEEAVRDRLEDSEAKVLITTPALLErkPADDL-PSLK---HVLLVGEDVEEGPGTLD----FNALMEQASDEFDI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDD----TIMP----------ITPMFHvlswgfpq 242
Cdd:PRK04319 200 EWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDvywcTADPgwvtgtsygiFAPWLN-------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 243 navaaGA-KLVLPGKFAAEE-FGAIAKafiaEKVTLANGAPAIFApMLamMK---DMPQPPDLSGVRLVSGSSEP--PLS 315
Cdd:PRK04319 272 -----GAtNVIDGGRFSPERwYRILED----YKVTVWYTAPTAIR-ML--MGagdDLVKKYDLSSLRHILSVGEPlnPEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 316 MMRGFKEI------------TGADVIHGYGATEttplattnwhIKPGlDMdeeerwdfkryqGLPVIGVEVKVVDPTGEE 383
Cdd:PRK04319 340 VRWGMKVFglpihdnwwmteTGGIMIANYPAMD----------IKPG-SM------------GKPLPGIEAAIVDDQGNE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 384 LPRDGksMGEVLMRGPWitESYF-QLPDNSER----FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEN 458
Cdd:PRK04319 397 LPPNR--MGNLAIKKGW--PSMMrGIWNNPEKyesyFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVES 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 459 AILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGdrFAKWQL-----PDEIIVTDELPRTSVGKLDK 533
Cdd:PRK04319 473 KLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRG--FVKKGLgahaaPREIEFKDKLPKTRSGKIMR 550
|
....*...
gi 1949187543 534 KLLrKTWE 541
Cdd:PRK04319 551 RVL-KAWE 557
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
53-536 |
6.93e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 144.03 E-value: 6.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLahgLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEA 132
Cdd:PRK06178 70 RFAAL---LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 133 LAPkldvkgwvvmtdkpadeiETTLENVVF--YEDLIKDKPDTYDWPVVDEKTAAYAG---------------------- 188
Cdd:PRK06178 147 VRA------------------ETSLRHVIVtsLADVLPAEPTLPLPDSLRAPRLAAAGaidllpalractapvplpppal 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 -------YTTGTTGRPKGVYYSHRS-IYLHTMGGLAALGASFDDTIMPITPMFhvlsWGFPQNA-----VAAGAKLVLPG 255
Cdd:PRK06178 209 dalaalnYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEF----WIAGENFgllfpLFSGATLVLLA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 KFAAEefgAIAKAFIAEKVTlangapaifapMLAMMKD-----MPQPP----DLSGVRLVSGSS-----EPPLSmmRGFK 321
Cdd:PRK06178 285 RWDAV---AFMAAVERYRVT-----------RTVMLVDnavelMDHPRfaeyDLSSLRQVRVVSfvkklNPDYR--QRWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 322 EITGADVIHG-YGATETTPLATtnwhIKPGL---DMDEEERWDFkryQGLPVIGVEVKVVD-PTGEELPRDGKsmGEVLM 396
Cdd:PRK06178 349 ALTGSVLAEAaWGMTETHTCDT----FTAGFqddDFDLLSQPVF---VGLPVPGTEFKICDfETGELLPLGAE--GEIVV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 397 RGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVP 475
Cdd:PRK06178 420 RTPSLLKGYWNKPEaTAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRP 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 476 DEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPdEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK06178 500 DPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
154-538 |
8.35e-37 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 143.58 E-value: 8.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 154 ETTLENVVFYEDLIK--DKP-DTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASF--DDTIMP 228
Cdd:PLN02330 153 EEKIEGAVNWKELLEaaDRAgDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMigQVVTLG 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 229 ITPMFHVLS-WGFPQNAVAAGAKLVLPGKFAAEEFgaiAKAFIAEKVTLANGAPAIfapMLAMMKD-MPQPPDLSGVRLV 306
Cdd:PLN02330 233 LIPFFHIYGiTGICCATLRNKGKVVVMSRFELRTF---LNALITQEVSFAPIVPPI---ILNLVKNpIVEEFDLSKLKLQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 307 S-GSSEPPLS--MMRGF-KEITGADVIHGYGATETTPLATTNWHIKPGLDMDEEERWDFKryqgLPviGVEVKVVDP-TG 381
Cdd:PLN02330 307 AiMTAAAPLApeLLTAFeAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSVGFI----LP--NLEVKFIDPdTG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 382 EELPRDgkSMGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENA 459
Cdd:PLN02330 381 RSLPKN--TPGELCVRSQCVMQGYYNNKEETDRTIDedGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAI 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 460 ILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PLN02330 459 LLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
46-545 |
3.77e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 141.42 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIF---- 121
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVvwpg 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 122 ------------VDESLLPVAEALApkldvkgwVVMTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVDEKTAAYAGY 189
Cdd:PRK06164 117 fkgidfaailaaVPPDALPPLRAIA--------VVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 190 TTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAeefGAIAKAF 269
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDA---ARTARAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 270 IAEKVTLANGAPAIFAPMLammKDMPQPPDLSGVRLV------SGSSE-PPLSMMRGFKeITGAdvihgYGATETTPLAT 342
Cdd:PRK06164 266 RRHRVTHTFGNDEMLRRIL---DTAGERADFPSARLFgfasfaPALGElAALARARGVP-LTGL-----YGSSEVQALVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 343 tnwhIKPgLDMDEEERWDFKryqGLPVIG-VEVKVVDPTGEELPRDGKSmGEVLMRGPWITESYFQLPDNSERFL--DGW 419
Cdd:PRK06164 337 ----LQP-ATDPVSVRIEGG---GRPASPeARVRARDPQDGALLPDGES-GEIEIRAPSLMRGYLDNPDATARALtdDGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 420 WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVpDEKWQERPVAYVVAEDGAEVTRET 499
Cdd:PRK06164 408 FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAG 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 500 IVEVLGDRFAKWQLPDEIIVTDELPRTSVG---KLDKKLLRK---TWEDAEA 545
Cdd:PRK06164 487 LMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREmaqARLAAER 538
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
189-532 |
4.27e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 137.90 E-value: 4.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGG--------------LAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLP 254
Cdd:cd05924 10 YTGGTTGMPKGVMWRQEDIFRMLMGGadfgtgeftpsedaHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 G-KFAAEEfgaIAKAFIAEKVTLAN-GAPAIFAPMLAMMKDmPQPPDLSGVRLVSgSSEPPLS--MMRGFKEIT-GADVI 329
Cdd:cd05924 90 DdRFDPEE---VWRTIEKHKVTSMTiVGDAMARPLIDALRD-AGPYDLSSLFAIS-SGGALLSpeVKQGLLELVpNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTPLATTnwHIKPGLDmdeeERWDFKRYQGLPVigvevkVVDPTGEELPRDGKSMGEVLMRGpWITESYFQLP 409
Cdd:cd05924 165 DAFGSSETGFTGSG--HSAGSGP----ETGPFTRANPDTV------VLDDDGRVVPPGSGGVGWIARRG-HIPLGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSER-F--LDG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPV 484
Cdd:cd05924 232 AKTAEtFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1949187543 485 AYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLD 532
Cdd:cd05924 312 AVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
47-536 |
5.32e-35 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 136.99 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVpgLAATMLqlnlrlapeDLAYVvshsksdwifvdesl 126
Cdd:cd05945 19 YRELKERADALAAALASLGLDAGDPVVVY---GHKSPDAIAAF--LAALKA---------GHAYV--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 lPVAealapkldvkgwvvmTDKPADEIETTLENVvfyedlikdKPDTYdwpVVDEKTAAYAGYTTGTTGRPKGVYYSHRS 206
Cdd:cd05945 70 -PLD---------------ASSPAERIREILDAA---------KPALL---IADGDDNAYIIFTSGSTGRPKGVQISHDN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 I--YLHTMGGLAALGA----------SFDDTIMPITPmfhvlswgfpqnAVAAGAKLVLPGKFAAEEFGAIAkAFIAE-K 273
Cdd:cd05945 122 LvsFTNWMLSDFPLGPgdvflnqapfSFDLSVMDLYP------------ALASGATLVPVPRDATADPKQLF-RFLAEhG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 274 VTLANGAPAiFAPMLAMMKDMpQPPDLSGVRLVSGSSEP-PLSMMRGFKEIT-GADVIHGYGATETTpLATTNWHIKPgL 351
Cdd:cd05945 189 ITVWVSTPS-FAAMCLLSPTF-TPESLPSLRHFLFCGEVlPHKTARALQQRFpDARIYNTYGPTEAT-VAVTYIEVTP-E 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 352 DMDEEERWdfkrYQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFLD-----GWWRSGDVG 426
Cdd:cd05945 265 VLDGYDRL----PIGYAKPGAKLVILDEDGRPVPPGEK--GELVISGPSVSKGYLNNPEKTAAAFFpdegqRAYRTGDLV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 427 VIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET-IVEVLG 505
Cdd:cd05945 339 RLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKaIKAELA 418
|
490 500 510
....*....|....*....|....*....|.
gi 1949187543 506 DRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd05945 419 ERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-537 |
7.24e-35 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 136.42 E-value: 7.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV----PGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLlp 128
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVayagGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 129 vAEALAPKLdvkgwvvmtdkPADEIETTlenVVFYEDLIKDKPDTYDWPVVDEKTAAYAgYTTGTTGRPKGVYYSHRSIY 208
Cdd:cd05922 80 -ADRLRDAL-----------PASPDPGT---VLDADGIRAARASAPAHEVSHEDLALLL-YTSGSTGSPKLVRLSHQNLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 209 LHTMGGLAALGASFDDTIMPITPmfhvLSW--GFPQ--NAVAAGAKLVLPGKFAAEEfgAIAKAFIAEKVTLANGAPAIF 284
Cdd:cd05922 144 ANARSIAEYLGITADDRALTVLP----LSYdyGLSVlnTHLLRGATLVLTNDGVLDD--AFWEDLREHGATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 285 ApMLAMMKDMPQPpdLSGVRLV--SGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTnwhikpgldMDEEERWDFK 362
Cdd:cd05922 218 A-MLTRLGFDPAK--LPSLRYLtqAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTY---------LPPERILEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 363 RYQGLPVIGVEVKVVDPTGEELPRdgKSMGEVLMRGPWITESYFQLP--DNSERFLDGWWRSGDVGVIFPNGYLKLTDRL 440
Cdd:cd05922 286 GSIGLAIPGGEFEILDDDGTPTPP--GEPGEIVHRGPNVMKGYWNDPpyRRKEGRGGGVLHTGDLARRDEDGFLFIVGRR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 441 KDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKwQERPVAYVVAEDGAEVtrETIVEVLGDRFAKWQLPDEIIVT 520
Cdd:cd05922 364 DRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVV 440
|
490
....*....|....*..
gi 1949187543 521 DELPRTSVGKLDKKLLR 537
Cdd:cd05922 441 DELPLTASGKVDYAALR 457
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-538 |
1.59e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.53 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQevvyrnsdgswgRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFEL---YFAVPGLAATMLQLNL 101
Cdd:PRK12467 530 ALVFGEQ------------VLSYAELNRQANRLAHVLIAAGVGPDVLVGIA---VERSIEMvvgLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESL---LPVAEALApkldvkgwVVMTDKPADEIEttlenvvfyedlikDKPDTYDWPV 178
Cdd:PRK12467 595 EYPQDRLAYMLDDSGVRLLLTQSHLlaqLPVPAGLR--------SLCLDEPADLLC--------------GYSGHNPEVA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGASfDDTIMPITPMFHVLSWGFpQNAVAAGAKLVLPGK 256
Cdd:PRK12467 653 LDPDNLAYVIYTSGSTGQPKGVAISHGALanYVCVIAERLQLAAD-DSMLMVSTFAFDLGVTEL-FGALASGATLHLLPP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEFGAIAKAFIAEKVTLANGAPAifapMLAMMKDMPQPPDLSGVR--LVSGSSEPPLSMMRGFKEITGADVIHGYGA 334
Cdd:PRK12467 731 DCARDAEAFAALMADQGVTVLKIVPS----HLQALLQASRVALPRPQRalVCGGEALQVDLLARVRALGPGARLINHYGP 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 335 TETTPLATTnwhikpgLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPrdGKSMGEVLMRGPWITESYFQLPD-NSE 413
Cdd:PRK12467 807 TETTVGVST-------YELSDEERDFGNVPIGQPLANLGLYILDHYLNPVP--VGVVGELYIGGAGLARGYHRRPAlTAE 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 RFL------DG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERpVA 485
Cdd:PRK12467 878 RFVpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQL-VA 956
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 486 YVVAEDGAE-----VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12467 957 YLVPAAVADgaehqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-489 |
1.74e-34 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 135.42 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 40 GSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDW 119
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 120 IFVDesllpvaealapkldvkgwvvmtdKPADeiettLENVVfyedlikdkpdtydwpvvdektaayagYTTGTTGRPKG 199
Cdd:cd05907 81 LFVE------------------------DPDD-----LATII---------------------------YTSGTTGRPKG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 200 VYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNA-VAAGAKLVLpgkfaAEEFGAIAKAFIAEKVTLAN 278
Cdd:cd05907 105 VMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVpLLAGARIYF-----ASSAETLLDDLSEVRPTVFL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 279 GAPAIFAPMLAMMKDMPQPPDL-------SGVRL---VSGSSEPPLSMMRGFKEItGADVIHGYGATETTPLATTNwhik 348
Cdd:cd05907 180 AVPRVWEKVYAAIKVKAVPGLKrklfdlaVGGRLrfaASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTLN---- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 349 pgldmdeeeRWDFKRYQ--GLPVIGVEVKVVDptgeelprDgksmGEVLMRGPWITESYFQLPDNSERFL--DGWWRSGD 424
Cdd:cd05907 255 ---------PPGDNRIGtvGKPLPGVEVRIAD--------D----GEILVRGPNVMLGYYKNPEATAEALdaDGWLHTGD 313
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 425 VGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSVKEAAVIGvpdekwQERPvaYVVA 489
Cdd:cd05907 314 LGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIG------DGRP--FLVA 371
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
189-538 |
3.29e-34 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 135.15 E-value: 3.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHvlSWGF------PQNAvaaGAKLVL-PGKFAAEE 261
Cdd:cd05909 154 FTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFH--SFGLtgclwlPLLS---GIKVVFhPNPLDYKK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 262 FGAIAKAfiaEKVTLANGAPAIFAPMLAMMkdmpQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVIHGYGATETTPL 340
Cdd:cd05909 229 IPELIYD---KKATILLGTPTFLRGYARAA----HPEDFSSLRLVvAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 341 ATTNwhiKPGLDMDEEErwdfkryQGLPVIGVEVKVVDPTGEELPRDGKSmGEVLMRGPWITESYFQLPD-NSERFLDGW 419
Cdd:cd05909 302 ISVN---TPQSPNKEGT-------VGRPLPGMEVKIVSVETHEEVPIGEG-GLLLVRGPNVMLGYLNEPElTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 420 WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILD-SPSVKEAAVIGVPDEKWQERPVAYVVAEDGaevTRE 498
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTTTDT---DPS 447
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1949187543 499 TIVEVLGD-RFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05909 448 SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
185-537 |
4.07e-34 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 135.92 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFD-----DTIMPIT--PMFHV--LSWGFPQNAVAAGAKLVLPG 255
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEkkprpDQLNFVCalPLYHIfaLTVCGLLGMRTGGRNILIPN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 kfaAEEFGAIAKAFIAEKVtlaNGAPAIFAPMLAMMK--DMPQPpDLSGVRLVSGS----SEPplsMMRGFKEITGADVI 329
Cdd:PRK07059 287 ---PRDIPGFIKELKKYQV---HIFPAVNTLYNALLNnpDFDKL-DFSKLIVANGGgmavQRP---VAERWLEMTGCPIT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTPLATTNwhikpGLDMDEeerwdFKRYQGLPVIGVEVKVVDPTGEELPRdGKsMGEVLMRGPWITESYFQLP 409
Cdd:PRK07059 357 EGYGLSETSPVATCN-----PVDATE-----FSGTIGLPLPSTEVSIRDDDGNDLPL-GE-PGEICIRGPQVMAGYWNRP 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYV 487
Cdd:PRK07059 425 DETAKVMtaDGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1949187543 488 VAEDGAeVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK07059 505 VKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
189-538 |
4.41e-34 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 137.75 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIylhtMGGLAA----LGASFDDTIMPITPMFHvlSWGFPqnavaagAKLVLPgkfAAEEFGA 264
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHNI----LSNIEQisdvFNLRNDDVILSSLPFFH--SFGLT-------VTLWLP---LLEGIKV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 265 -----------IAKAFIAEKVTLANGAPAIFapMLAMMKDMPQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVIHGY 332
Cdd:PRK08633 853 vyhpdptdalgIAKLVAKHRATILLGTPTFL--RLYLRNKKLHPLMFASLRLVvAGAEKLKPEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATETTPLATTNwhIKPGLDMDEEERWDFKRYQ-GLPVIGVEVKVVDP-TGEELPrdGKSMGEVLMRGPWITESYFQLPD 410
Cdd:PRK08633 931 GATETSPVASVN--LPDVLAADFKRQTGSKEGSvGMPLPGVAVRIVDPeTFEELP--PGEDGLILIGGPQVMKGYLGDPE 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 NS-----ERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAI---LDSPSVKEAAViGVPDEKWQER 482
Cdd:PRK08633 1007 KTaevikDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakaLGGEEVVFAVT-AVPDEKKGEK 1085
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 483 pVAYVVAEDGAEVtrETIVEVLGDRF--AKWQlPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK08633 1086 -LVVLHTCGAEDV--EELKRAIKESGlpNLWK-PSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
160-537 |
4.62e-34 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 135.95 E-value: 4.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 160 VVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDD-TIMPIT--PMFHVL 236
Cdd:PRK08974 184 ISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPgKELVVTalPLYHIF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 237 swgfpqnAVAAGAKLVLpgkfaaeEFGAIA---------KAFIAE----KVTLANGAPAIFAPMLAMmKDMPQPpDLSGV 303
Cdd:PRK08974 264 -------ALTVNCLLFI-------ELGGQNllitnprdiPGFVKElkkyPFTAITGVNTLFNALLNN-EEFQEL-DFSSL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 304 RLVSGSSEP-PLSMMRGFKEITGADVIHGYGATETTPLATTNwhikpgldmdeeeRWDFKRYQG---LPVIGVEVKVVDP 379
Cdd:PRK08974 328 KLSVGGGMAvQQAVAERWVKLTGQYLLEGYGLTECSPLVSVN-------------PYDLDYYSGsigLPVPSTEIKLVDD 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 380 TGEELPRDgkSMGEVLMRGPWITESYFQLPDNSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEN 458
Cdd:PRK08974 395 DGNEVPPG--EPGELWVKGPQVMLGYWQRPEATDEVIkDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIED 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 459 AILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDgAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK08974 473 VVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-536 |
6.50e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.78 E-value: 6.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 24 AATVFGEQEVVYRNSDGswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRL 103
Cdd:PRK12316 528 PALAFGEETLDYAELNR---RAN---------RLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEY 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 104 APEDLAYVVSHSksdwifvDESLLPVAEALAPKLDVKG--WVVMTDKPADEIETTLENvvfyedlikdKPDTYdwpvVDE 181
Cdd:PRK12316 596 PAERLAYMLEDS-------GVQLLLSQSHLGRKLPLAAgvQVLDLDRPAAWLEGYSEE----------NPGTE----LNP 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 182 KTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVLPGKFAAE 260
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVAAPGDHR 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 261 EFGAIAKAFIAEKVTLANGAPAifapMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMM-RGFKEITGADVIHGYGATETT 338
Cdd:PRK12316 734 DPAKLVELINREGVDTLHFVPS----MLQAFLQDEDVASCTSLRRIVCSGEAlPADAQeQVFAKLPQAGLYNLYGPTEAA 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 339 PLATTNWHIKPGLDMDEeerwdfkryQGLPVIGVEVKVVDPTGEELPRdgKSMGEVLMRGPWITESYFQLPD-NSERFL- 416
Cdd:PRK12316 810 IDVTHWTCVEEGGDSVP---------IGRPIANLACYILDANLEPVPV--GVLGELYLAGRGLARGYHGRPGlTAERFVp 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 ----DG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWqerpVAYVVAE 490
Cdd:PRK12316 879 spfvAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQL----VGYVVLE 954
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1949187543 491 DGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK12316 955 SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-545 |
1.33e-33 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 136.53 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYR--NSdgswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVLdwnSRRHFELyfaVPGLAATM---- 96
Cdd:COG1020 492 AVAVVFGDQSLTYAelNA-----RAN---------RLAHHLRALGVGPGDLVGVC---LERSLEM---VVALLAVLkaga 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 97 --LQLNLRLAPEDLAYVVSHSKSDWIFVDESLlpvAEALaPKLDVKgwVVMTDKPAdeiettlenvvfyedlIKDKPDTY 174
Cdd:COG1020 552 ayVPLDPAYPAERLAYMLEDAGARLVLTQSAL---AARL-PELGVP--VLALDALA----------------LAAEPATN 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 175 DWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGAsfDDTIMPITPMFHVLS----WGfpqnAVAAG 248
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALvnLLAWMQRRYGLGP--GDRVLQFASLSFDASvweiFG----ALLSG 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 249 AKLVLPGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMmkdmpQPPDLSGVRLVSGSSEP-PLSMMRGFKEIT-GA 326
Cdd:COG1020 684 ATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDA-----APEALPSLRLVLVGGEAlPPELVRRWRARLpGA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 327 DVIHGYGATETTpLATTNWHIKPGldmdeEERWDFKRYqGLPVIGVEVKVVDPTGEELPrDGKSmGEVLMRGPWITESYF 406
Cdd:COG1020 759 RLVNLYGPTETT-VDSTYYEVTPP-----DADGGSVPI-GRPIANTRVYVLDAHLQPVP-VGVP-GELYIGGAGLARGYL 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 407 QLPD-NSERFLDG--------WWRSGDVGVIFPNGYLKLTDRLKDVIK-SG-----GEwIssidmENAILDSPSVKEAAV 471
Cdd:COG1020 830 NRPElTAERFVADpfgfpgarLYRTGDLARWLPDGNLEFLGRADDQVKiRGfrielGE-I-----EAALLQHPGVREAVV 903
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 472 IGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWEDAEA 545
Cdd:COG1020 904 VAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA 977
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
50-536 |
2.07e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 133.58 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 50 EFKRMAQ-LAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLApedlayvvshsksdwifvdesllp 128
Cdd:PRK13383 65 ELQRATEsLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFR------------------------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 129 vAEALAPKLDVKGWVVMT--DKPADEIETTLENVVFYEDLIKDKPDTYDWPVVdEKTAAYAGYTTGTTGRPKGVyysHRS 206
Cdd:PRK13383 121 -SDALAAALRAHHISTVVadNEFAERIAGADDAVAVIDPATAGAEESGGRPAV-AAPGRIVLLTSGTTGKPKGV---PRA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 IYLHTMGGLAAlgASFDDT-------IMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLAng 279
Cdd:PRK13383 196 PQLRSAVGVWV--TILDRTrlrtgsrISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAV-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 280 aPAIFAPMLAMMKDMPQPPDLSGVRLV--SGSSEPPlSMMRGFKEITGADVIHGYGATETT--PLATTnwhikpgldmde 355
Cdd:PRK13383 272 -PVVLARILELPPRVRARNPLPQLRVVmsSGDRLDP-TLGQRFMDTYGDILYNGYGSTEVGigALATP------------ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 356 EERWDFKRYQGLPVIGVEVKVVDPTGEelPRDGKSMGEVLMRGPWITESYFQlpDNSERFLDGWWRSGDVGVIFPNGYLK 435
Cdd:PRK13383 338 ADLRDAPETVGKPVAGCPVRILDRNNR--PVGPRVTGRIFVGGELAGTRYTD--GGGKAVVDGMTSTGDMGYLDNAGRLF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 436 LTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPD 515
Cdd:PRK13383 414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPR 493
|
490 500
....*....|....*....|.
gi 1949187543 516 EIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK13383 494 DINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
23-536 |
3.41e-33 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 132.32 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGLA---ATMLQL 99
Cdd:cd12117 13 AVAVVYGDRSLTYAELN------------ERANRLARRLRAAGVGPGDVVGVL---AERSPELVVALLAVLkagAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPkldvkgwVVMTDKPADEIETTLENvvfyedlikdkpdtydwPVV 179
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-------AVVIDEALDAGPAGNPA-----------------VPV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 DEKTAAYAGYTTGTTGRPKGVYYSHRSI--------YLHTMGGLAALGAS---FDdtimpiTPMFHVlsWGfpqnAVAAG 248
Cdd:cd12117 134 SPDDLAYVMYTSGSTGRPKGVAVTHRGVvrlvkntnYVTLGPDDRVLQTSplaFD------ASTFEI--WG----ALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 249 AKLVLPGKFAAEEFGAIAKAFIAEKVTLAngapAIFAPMLAMMKDmpQPPD-LSGVR--LVSGSSEPPLSMMRGFKEITG 325
Cdd:cd12117 202 ARLVLAPKGTLLDPDALGALIAEEGVTVL----WLTAALFNQLAD--EDPEcFAGLRelLTGGEVVSPPHVRRVLAACPG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 326 ADVIHGYGATETTPLATtnWHIKPGLDMDEEErwdfkRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESY 405
Cdd:cd12117 276 LRLVNGYGPTENTTFTT--SHVVTELDEVAGS-----IPIGRPIANTRVYVLDEDGRPVPPG--VPGELYVGGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 406 FQLPD-NSERF-----LDG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDE 477
Cdd:cd12117 347 LNRPAlTAERFvadpfGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 478 KWQERPVAYVVAEdgAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd12117 427 GGDKRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-537 |
4.74e-33 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 131.02 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 49 DEFKRMA-QLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDwifvdesll 127
Cdd:cd05971 10 KELKTASnRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 128 pvaealapkldvkgwVVMTDKPADEiettlenvvfyedlikdkpdtydwpvvdektaAYAGYTTGTTGRPKGVYYSHRSI 207
Cdd:cd05971 81 ---------------ALVTDGSDDP--------------------------------ALIIYTSGTTGPPKGALHAHRVL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 208 YLH-------------------TMGGLAALGASFDDTImpitPMFHvlsWGFPqnavaagaklVLPGKFAAEEFGAIAKA 268
Cdd:cd05971 114 LGHlpgvqfpfnlfprdgdlywTPADWAWIGGLLDVLL----PSLY---FGVP----------VLAHRMTKFDPKAALDL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLAngapaiFAP--MLAMMKDMPQPPDLSGVRLVSGSS--EPPLSMMRGF-KEITGADVIHGYGATETTPLATT 343
Cdd:cd05971 177 MSRYGVTTA------FLPptALKMMRQQGEQLKHAQVKLRAIATggESLGEELLGWaREQFGVEVNEFYGQTECNLVIGN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 344 N---WHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITE--SYFQLPDNSE-RFLD 417
Cdd:cd05971 251 CsalFPIKPG-------------SMGKPIPGHRVAIVDDNGTPLPPG--EVGEIAVELPDPVAflGYWNNPSATEkKMAG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVV---AEDGAE 494
Cdd:cd05971 316 DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpGETPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1949187543 495 VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05971 396 ALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
189-533 |
7.71e-33 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 128.53 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAA-LGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAaeEFGAIAK 267
Cdd:cd17635 8 FTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENT--TYKSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 268 AFIAEKVTLANGAPAIFAPMLAMMKDMPQppDLSGVRLVSGSSEPPLSMMRGFKEITG-ADVIHGYGATETTPLATTNWH 346
Cdd:cd17635 86 ILTTNAVTTTCLVPTLLSKLVSELKSANA--TVPSLRLIGYGGSRAIAADVRFIEATGlTNTAQVYGLSETGTALCLPTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 347 iKPGLDMDEeerwdfkryQGLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDV 425
Cdd:cd17635 164 -DDSIEINA---------VGRPYPGVDVYLAATDGIAGPSASF--GTIWIKSPANMLGYWNNPErTAEVLIDGWVNTGDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 426 GVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVA-----EDGAEVTRETI 500
Cdd:cd17635 232 GERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeldENAIRALKHTI 311
|
330 340 350
....*....|....*....|....*....|...
gi 1949187543 501 VEVLGdrfaKWQLPDEIIVTDELPRTSVGKLDK 533
Cdd:cd17635 312 RRELE----PYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
44-479 |
1.75e-32 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 129.79 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESllpvaealapkldvkgwvvmtdkpADEIETTLenvvfyedlikdkpdtydwpvvdektaayagYTTGTTGRPKGVYYS 203
Cdd:cd17640 85 ND------------------------SDDLATII-------------------------------YTSGTTGNPKGVMLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSIyLHTMGGLAA-LGASFDDTIMPITPMFH---------VLSWGFPQ-----NAVAAGAKLVLPGKFAA--EEFGAIA 266
Cdd:cd17640 110 HANL-LHQIRSLSDiVPPQPGDRFLSILPIWHsyersaeyfIFACGCSQaytsiRTLKDDLKRVKPHYIVSvpRLWESLY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 267 KAFIAEkvtLANGAPaiFAPMLAMMKdmpqppdLSGVRL---VSGSSEPPLSMMRgFKEITGADVIHGYGATETTPLATT 343
Cdd:cd17640 189 SGIQKQ---VSKSSP--IKQFLFLFF-------LSGGIFkfgISGGGALPPHVDT-FFEAIGIEVLNGYGLTETSPVVSA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 344 N--WHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDP-TGEELPRDGKsmGEVLMRGPWITESYFQLPDNSERFL--DG 418
Cdd:cd17640 256 RrlKCNVRG-------------SVGRPLPGTEIKIVDPeGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVLdsDG 320
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 419 WWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSVKEAAVIG----------VPD----EKW 479
Cdd:cd17640 321 WFNTGDLGWLTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlgaliVPNfeelEKW 396
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
46-536 |
2.96e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 129.33 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDEs 125
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 llpvaeALAPKLDVKGWVVMTDKPADEiettlenvvfyedlikdKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHR 205
Cdd:cd12116 93 ------ALPDRLPAGLPVLLLALAAAA-----------------AAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 SI--YLHTMGGLAALGAsfDDTIMPIT-PMF--HVLSWGFPqnaVAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLANGA 280
Cdd:cd12116 150 NLvnFLHSMRERLGLGP--GDRLLAVTtYAFdiSLLELLLP---LLAGARVVIAPRETQRDPEALARLIEAHSITVMQAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 281 PAIFAPMLAmmkdmPQPPDLSGVRLVSGSSEPPLSMMRGFKEiTGADVIHGYGATETTPLATTnwhikpgLDMDEEERwd 360
Cdd:cd12116 225 PATWRMLLD-----AGWQGRAGLTALCGGEALPPDLAARLLS-RVGSLWNLYGPTETTIWSTA-------ARVTAAAG-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 361 fKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFLDG--------WWRSGDVGVIFPN 431
Cdd:cd12116 290 -PIPIGRPLANTQVYVLDAALRPVPPG--VPGELYIGGDGVAQGYLGRPAlTAERFVPDpfagpgsrLYRTGDLVRRRAD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 432 GYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQeRPVAYVVAEDGAEVTRETIVEVLGDRFAKW 511
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDR-RLVAYVVLKAGAAPDAAALRAHLRATLPAY 445
|
490 500
....*....|....*....|....*
gi 1949187543 512 QLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd12116 446 MVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
56-536 |
9.88e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 127.77 E-value: 9.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 56 QLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGLA---ATMLQLNLRLAPEDLAYVVSHSKSDWIFVDEsllPVAEA 132
Cdd:cd12114 24 RVAGALKAAGVRPGDLVAVT---LPKGPEQVVAVLGILaagAAYVPVDIDQPAARREAILADAGARLVLTDG---PDAQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 133 LAPKLDVKGWVVMTDKPADeiettlenvvfyedlikDKPDtydwPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIY--LH 210
Cdd:cd12114 98 DVAVFDVLILDLDALAAPA-----------------PPPP----VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALntIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 211 TMGGLAALGAsfDDTIMPITPMFHVLS----WGfpqnAVAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAP 286
Cdd:cd12114 157 DINRRFAVGP--DDRVLALSSLSFDLSvydiFG----ALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 287 MLAMMKDMPQ-PPDLSGVrLVSGSSePPLSMMRGFKEIT-GADVIHGYGATETTPLAttNWHikpglDMDE-EERWDFKR 363
Cdd:cd12114 231 LLDVLEAAQAlLPSLRLV-LLSGDW-IPLDLPARLRALApDARLISLGGATEASIWS--IYH-----PIDEvPPDWRSIP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 364 YqGLPVIGVEVKVVDPTGEELPrDGkSMGEVLMRGPWITESYFQLPDNS-ERFLD-----GWWRSGDVGVIFPNGYLKLT 437
Cdd:cd12114 302 Y-GRPLANQRYRVLDPRGRDCP-DW-VPGELWIGGRGVALGYLGDPELTaARFVThpdgeRLYRTGDLGRYRPDGTLEFL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 438 DRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVpDEKWQERPVAYVVAE-DGAEVTRETIVEVLGDRFAKWQLPDE 516
Cdd:cd12114 379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDnDGTPIAPDALRAFLAQTLPAYMIPSR 457
|
490 500
....*....|....*....|
gi 1949187543 517 IIVTDELPRTSVGKLDKKLL 536
Cdd:cd12114 458 VIALEALPLTANGKVDRAAL 477
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-538 |
1.01e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.23 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVvyrnsdgswgrsNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLA 104
Cdd:PRK12316 3075 ALAFGEQRL------------SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYP 3142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 105 PEDLAYVVSHSKSDWIFVDESL-LPVAEALApkldvkgwVVMTDKPAdeiettlenvvfyEDLIKDKPDTYdwpvVDEKT 183
Cdd:PRK12316 3143 EERLAYMLEDSGAQLLLSQSHLrLPLAQGVQ--------VLDLDRGD-------------ENYAEANPAIR----TMPEN 3197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 AAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVLPGKfaaEEF 262
Cdd:PRK12316 3198 LAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFsFDVFVEEL-FWPLMSGARVVLAGP---EDW 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 GAIAKAFIAEKVTLANGAPAiFAPMLAMMKDMPQPPDLSGVR--LVSGSSEPPLSMMRGFkeiTGADVIHGYGATETTPL 340
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHA-YPSMLQAFLEEEDAHRCTSLKriVCGGEALPADLQQQVF---AGLPLYNLYGPTEATIT 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 341 ATTNWHIKPGLDmdeeerwdfKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFL--- 416
Cdd:PRK12316 3350 VTHWQCVEEGKD---------AVPIGRPIANRACYILDGSLEPVPVG--ALGELYLGGEGLARGYHNRPGlTAERFVpdp 3418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 ----DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDekwqERPVAYVVAEDG 492
Cdd:PRK12316 3419 fvpgERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVPEDE 3494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1949187543 493 AEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12316 3495 AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
186-533 |
4.10e-31 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 122.90 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 186 YAGYTTGTTGRPKGVYYSHRSiYLHTM-GGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGKFAAEEFGA 264
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERS-WIESFvCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 265 IAKAfiaEKVTLANGAPaifaPMLAMMKDMpQPPDLSGVRLVSGSSEPPLSMMRGFKEIT-GADVIHGYGATETTpLATT 343
Cdd:cd17633 83 KINQ---YNATVIYLVP----TMLQALART-LEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELS-FITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 344 NwhikpgldMDEEERwdfKRYQ-GLPVIGVEVKVVDptgeelpRDGKSMGEVLMRGPWITESYFQLPDNSErflDGWWRS 422
Cdd:cd17633 154 N--------FNQESR---PPNSvGRPFPNVEIEIRN-------ADGGEIGKIFVKSEMVFSGYVRGGFSNP---DGWMSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 423 GDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVaedGAEVTRETIVE 502
Cdd:cd17633 213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKR 289
|
330 340 350
....*....|....*....|....*....|.
gi 1949187543 503 VLGDRFAKWQLPDEIIVTDELPRTSVGKLDK 533
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
24-537 |
1.50e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 124.74 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 24 AATVFGE--QEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNL 101
Cdd:PRK13390 14 PAVIVAEtgEQVSYRQLD------------DDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVK-GWVVMTDKPADeIETTLENVvfyedlikdKPdtydwPVVD 180
Cdd:PRK13390 82 HLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRlSFGGEIDGFGS-FEAALAGA---------GP-----RLTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 181 EKTAAYAGYTTGTTGRPKGVY--YSHRSIYLHTMGGLAALGASFD----DTIMPITPMFHVLSWGFPQNAVAAGAKLVLP 254
Cdd:PRK13390 147 QPCGAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDisesDIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 GKF-AAEEFGAIAKAfiaeKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGY 332
Cdd:PRK13390 227 KRFdAQATLGHVERY----RITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPcPVDVKHAMIDWLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATET---TPLATTNWHIKPGldmdeeerwdfkrYQGLPVIGvEVKVVDPTGEELPrdGKSMGEVLMRGPWITESYFQLP 409
Cdd:PRK13390 303 SSTEAhgmTFIDSPDWLAHPG-------------SVGRSVLG-DLHICDDDGNELP--AGRIGTVYFERDRLPFRYLNDP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNSERFLDG----WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVA 485
Cdd:PRK13390 367 EKTAAAQHPahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 486 YVVAEDGA----EVTREtIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PRK13390 447 VIQLVEGIrgsdELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-538 |
1.75e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.38 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFEL---YFAVPGLAATMLQLNL 101
Cdd:PRK12316 2021 AVVFGDQHLSYAELD------------SRANRLAHRLRARGVGPEVRVAIA---AERSFELvvaLLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESL---LPVAEALaPKLDVkgwvvmtDKPADeiettlenvvfyedlIKDKPDTYDWPV 178
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAALLLTQRHLlerLPLPAGV-ARLPL-------DRDAE---------------WADYPDTAPAVQ 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVLPGK- 256
Cdd:PRK12316 2143 LAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFsFDGAHEQW-FHPLLNGARVLIRDDe 2221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 -FAAEEfgaIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSgVRLVSGSSEPPLSMMRGFKEITGADVIHGYGAT 335
Cdd:PRK12316 2222 lWDPEQ---LYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVR-VYCFGGEAVPAASLRLAWEALRPVYLFNGYGPT 2297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 ET--TPLAttnWHIKPgldmdEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPD-NS 412
Cdd:PRK12316 2298 EAvvTPLL---WKCRP-----QDPCGAAYVPIGRALGNRRAYILDADLNLLAPGM--AGELYLGGEGLARGYLNRPGlTA 2367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 413 ERFL-DGW-------WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVpDEKWQERPV 484
Cdd:PRK12316 2368 ERFVpDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLV 2446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 485 AYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12316 2447 AYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
43-536 |
1.92e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 123.58 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 43 GRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFEL---YFAVPGLAATMLQLNLRLAPEDLAYVVshsksdw 119
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAAGVGPESRVGVC---LERTPDLvvaLLAVLKAGAAYVPLDPAYPPERLRFIL------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 120 ifvdesllpvAEALAPkldvkgwVVMTDkPADeiettlenvvfyedlikdkpdtydwpvvdektAAYAGYTTGTTGRPKG 199
Cdd:cd12115 93 ----------EDAQAR-------LVLTD-PDD--------------------------------LAYVIYTSGSTGRPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 200 VYYSHRSI------YLHTMGG------LAALGASFDdtiMPITPMFHVLswgfpqnavAAGAKLVLpgkfaAEEFGAIAK 267
Cdd:cd12115 123 VAIEHRNAaaflqwAAAAFSAeelagvLASTSICFD---LSVFELFGPL---------ATGGKVVL-----ADNVLALPD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 268 AFIAEKVTLANGAPAIFAPMLAmMKDMPQppdlsGVRLVSGSSEpPLS---MMRGFKEITGADVIHGYGATETTPLATtn 344
Cdd:cd12115 186 LPAAAEVTLINTVPSAAAELLR-HDALPA-----SVRVVNLAGE-PLPrdlVQRLYARLQVERVVNLYGPSEDTTYST-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 345 whikpGLDMDEEERWDFKryQGLPVIGVEVKVVDPTGEELPrDGkSMGEVLMRGPWITESYFQLPDNS-ERFL-DGW--- 419
Cdd:cd12115 257 -----VAPVPPGASGEVS--IGRPLANTQAYVLDRALQPVP-LG-VPGELYIGGAGVARGYLGRPGLTaERFLpDPFgpg 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 420 ---WRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT 496
Cdd:cd12115 328 arlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1949187543 497 RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd12115 408 VEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-531 |
2.00e-30 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 125.38 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 33 VVYRNSDGSWGRS-NYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnsrrhfelYFAVPGLAATMLQLnLRL-------- 103
Cdd:cd17634 72 IIYEGDDTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIY----------MPMIPEAAVAMLAC-ARIgavhsvif 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 104 ---APEDLAYVVSHSKSD-WIFVDESLLP---------VAEALAPKLDVKGWVVMTDKPADEIETTLENVVFYEDLIKDK 170
Cdd:cd17634 141 ggfAPEAVAGRIIDSSSRlLITADGGVRAgrsvplkknVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 171 PDTYDWPVVDEKTAAYAGYTTGTTGRPKGVyyshrsiyLHTMGGLAALGASFDDTIMPITP-----MFHVLSW--GFP-- 241
Cdd:cd17634 221 SPEHQPEAMNAEDPLFILYTSGTTGKPKGV--------LHTTGGYLVYAATTMKYVFDYGPgdiywCTADVGWvtGHSyl 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 242 -QNAVAAGAKLVL-PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP--PLSMM 317
Cdd:cd17634 293 lYGPLACGATTLLyEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPinPEAYE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 318 RGFKEITGAD--VIHGYGATETTPLATTNWHIKPGLDMDEEERwdfkryqglPVIGVEVKVVDPTGEelPRDGKSMGEVL 395
Cdd:cd17634 373 WYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSATR---------PVFGVQPAVVDNEGH--PQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 396 MRGPW--ITESYFQLPDNSE----RFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEA 469
Cdd:cd17634 442 ITDPWpgQTRTLFGDHERFEqtyfSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187543 470 AVIGVPDEKWQERPVAYVVAEDGAE---VTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKL 531
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGVEpspELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
47-536 |
4.74e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 122.94 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDEsl 126
Cdd:cd05914 10 YKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 lpvaealapkldvkgwvvmtdkpadeiettlenvvfyedlikdkpdtydwpvvDEKTAAYAgYTTGTTGRPKGVYYSHRS 206
Cdd:cd05914 88 -----------------------------------------------------EDDVALIN-YTSGTTGNSKGVMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 IYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQ-NAVAAGAKLVLPGKFAAEEFGAIAKA----------------- 268
Cdd:cd05914 114 IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLlLPLLNGAHVVFLDKIPSAKIIALAFAqvtptlgvpvplvieki 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLANGAPAIFApMLAMMKDMP-------QPPDLSGVRL---VSGSSEPPLSMMRGFKEItGADVIHGYGATETT 338
Cdd:cd05914 194 FKMDIIPKLTLKKFKFK-LAKKINNRKirklafkKVHEAFGGNIkefVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 339 PLATTN-WhikpgldmdEEERWDfkrYQGLPVIGVEVKVVDPTGEElprdgkSMGEVLMRGPWITESYFQLPDNSERFL- 416
Cdd:cd05914 272 PIISYSpP---------NRIRLG---SAGKVIDGVEVRIDSPDPAT------GEGEIIVRGPNVMKGYYKNPEATAEAFd 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 -DGWWRSGDVGVIFPNGYLKLTDRLKDVI-KSGGEWISSIDMENAILDSPSVKEaAVIGVPDEKWQERPVAYVVAEDGAE 494
Cdd:cd05914 334 kDGWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLE-SLVVVQEKKLVALAYIDPDFLDVKA 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 495 VTRETIVEVLgdrfaKWQLPDE--------------IIVTDELPRTSVGKLDKKLL 536
Cdd:cd05914 413 LKQRNIIDAI-----KWEVRDKvnqkvpnykkiskvKIVKEEFEKTPKGKIKRFLY 463
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-538 |
1.08e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.89 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVvyrnsdgswgrsNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLA 104
Cdd:PRK12467 3113 ALVFGDQQL------------SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 105 PEDLAYVVSHSKSDWIFVDESLLpvaEALAPKLDVKGWVVMTDKPADEIETTLENVVFYEDLikdkpdtydwpvvdekta 184
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLL---EQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENL------------------ 3239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFPQNAVAAGAKLVLPGKFAAEEfg 263
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFsFDGAQERFLWTLICGGCLVVRDNDLWDPE-- 3317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 264 AIAKAFIAEKVTLANGAPAifapMLAMMKDMPQPPDLSGVR--LVSGSSEPPLSMMRGFKEITGADVIHGYGATETTPLA 341
Cdd:PRK12467 3318 ELWQAIHAHRISIACFPPA----YLQQFAEDAGGADCASLDiyVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTV 3393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 342 TtnwHIKPGLDMDEEERWdfkRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFL---- 416
Cdd:PRK12467 3394 T---LWKCGGDAVCEAPY---APIGRPVAGRSIYVLDGQLNPVPVG--VAGELYIGGVGLARGYHQRPSlTAERFVadpf 3465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 ----DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERpVAYVVAEDG 492
Cdd:PRK12467 3466 sgsgGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQL-VAYVVPADP 3544
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1949187543 493 AEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12467 3545 QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
53-471 |
3.55e-29 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 119.29 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGL-TELGVGAGSMVGVLdwnSRRHFELYFAVpgLA-----ATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:TIGR01733 8 RANRLARHLrAAGGVGPGDRVAVL---LERSAELVVAI--LAvlkagAAYVPLDPAYPAERLAFILEDAGARLLLTDSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LPVAEALAPkldvkgwVVMTDKPADEIETTLENVVFYEDlIKDKPDTydwpvvdektAAYAGYTTGTTGRPKGVYYSHRS 206
Cdd:TIGR01733 83 ASRLAGLVL-------PVILLDPLELAALDDAPAPPPPD-APSGPDD----------LAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 I--YLHTMGGLAALGA----------SFDdtiMPITPMFHVLswgfpqnavAAGAKLVLPGKFAAEEFGAIAKAFIAE-K 273
Cdd:TIGR01733 145 LvnLLAWLARRYGLDPddrvlqfaslSFD---ASVEEIFGAL---------LAGATLVVPPEDEERDDAALLAALIAEhP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 274 VTLANGAPAIFAPMLAMmkdmpQPPDLSGVRLV-SGSSEPPLSMMRGFKE-ITGADVIHGYGATETTpLATTNWHIkpgl 351
Cdd:TIGR01733 213 VTVLNLTPSLLALLAAA-----LPPALASLRLViLGGEALTPALVDRWRArGPGARLINLYGPTETT-VWSTATLV---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 352 dMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPD-NSERFLDG---------WWR 421
Cdd:TIGR01733 283 -DPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGV--VGELYIGGPGVARGYLNRPElTAERFVPDpfaggdgarLYR 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1949187543 422 SGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAV 471
Cdd:TIGR01733 360 TGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
373-538 |
4.24e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 120.87 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 373 EVKVVDPTGEELPRdgksmGEV--LM-RGPWITESYFQLPD-NSERF-LDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSG 447
Cdd:PRK10946 364 EVWVADADGNPLPQ-----GEVgrLMtRGPYTFRGYYKSPQhNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 448 GEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVvaedgaeVTRETIVEVLGDRF------AKWQLPDEIIVTD 521
Cdd:PRK10946 439 GEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFL-------VVKEPLKAVQLRRFlreqgiAEFKLPDRVECVD 511
|
170
....*....|....*..
gi 1949187543 522 ELPRTSVGKLDKKLLRK 538
Cdd:PRK10946 512 SLPLTAVGKVDKKQLRQ 528
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
23-536 |
4.42e-29 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 119.66 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDGswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVldwnsrrhfelyfAVPGLAatmlqlnlr 102
Cdd:cd17652 3 APAVVFGDETLTYAELNA---RAN---------RLARLLAARGVGPERLVAL-------------ALPRSA--------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 103 lapedlayvvshsksDWIFvdeSLLPVAEALAPKLDVKgwvvmTDKPADEIETTLENVVfyEDLIKDKPDTydwpvvdek 182
Cdd:cd17652 49 ---------------ELVV---AILAVLKAGAAYLPLD-----PAYPAERIAYMLADAR--PALLLTTPDN--------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 183 tAAYAGYTTGTTGRPKGVYYSHRsiylhtmgGLAALGASFDDTiMPITPMFHVLSWGFPQ---------NAVAAGAKLVL 253
Cdd:cd17652 95 -LAYVIYTSGSTGRPKGVVVTHR--------GLANLAAAQIAA-FDVGPGSRVLQFASPSfdasvwellMALLAGATLVL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMlammkdmpqPPD--LSGVRLVSGSSEPPLSMMRgfKEITGADVIHG 331
Cdd:cd17652 165 APAEELLPGEPLADLLREHRITHVTLPPAALAAL---------PPDdlPDLRTLVVAGEACPAELVD--RWAPGRRMINA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLATTNwhiKPGLDMDEEErwdfkryQGLPVIGVEVKVVDPTGEELPrDGKSmGEVLMRGPWITESYFQLPD- 410
Cdd:cd17652 234 YGPTETTVCATMA---GPLPGGGVPP-------IGRPVPGTRVYVLDARLRPVP-PGVP-GELYIAGAGLARGYLNRPGl 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 NSERFL--------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQER 482
Cdd:cd17652 302 TAERFVadpfgapgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKR 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 483 PVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17652 382 LVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
25-537 |
5.42e-29 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 119.40 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELyfaVPGLAATMLQlnlrla 104
Cdd:cd17649 5 ALVFGDQSLSYAELD------------ARANRLAHRLRALGVGPEVRVGIA---LERSLEM---VVALLAILKA------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 105 peDLAYVvshsksdwifvdesllpvaeALAPkldvkgwvvmtDKPADEIETTLEnvvfyeD-----LIKDKPDTydwpvv 179
Cdd:cd17649 61 --GGAYV--------------------PLDP-----------EYPAERLRYMLE------DsgaglLLTHHPRQ------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 dektAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVLPGKFA 258
Cdd:cd17649 96 ----LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnFDGAHEQL-LPPLICGACVVLRPDEL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 259 AEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSgVRLVSGSSE--PPLSMMRGFKeiTGADVIHGYGATE 336
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEalSPELLRRWLK--APVRLFNAYGPTE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 337 T--TPLAttnWHIKPGldmdeEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPD-NSE 413
Cdd:cd17649 248 AtvTPLV---WKCEAG-----AARAGASMPIGRPLGGRSAYILDADLNPVPVGV--TGELYIGGEGLARGYLGRPElTAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 RFLDG--------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKwQERPVA 485
Cdd:cd17649 318 RFVPDpfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 486 YVVAEDGAEV--TRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd17649 397 YVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-536 |
3.82e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 120.27 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVldwNSRRHFELyfaVPGLAATM------LQ 98
Cdd:PRK12467 1592 ALVFGEQELTYGELN------------RRANRLAHRLIALGVGPEVLVGI---AVERSLEM---VVGLLAILkaggayVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 99 LNLRLAPEDLAYVVSHSksdwifvDESLLPVAEALAPKLDVKGWV--VMTDKPADEIETtlenvvfyedlikdKPDTYDW 176
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDS-------GIELLLTQSHLQARLPLPDGLrsLVLDQEDDWLEG--------------YSDSNPA 1712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMGglAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVL 253
Cdd:PRK12467 1713 VNLAPQNLAYVIYTSGSTGRPKGAGNRHGALvnRLCATQ--EAYQLSAADVVLQFTSFaFDVSVWEL-FWPLINGARLVI 1789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSgvRLV-SGSSEPPLSMMRGFKEITGADVIHGY 332
Cdd:PRK12467 1790 APPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLR--RVVcGGEALEVEALRPWLERLPDTGLFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATETTpLATTNWHIKPGldmDEEERWDFKryQGLPVIGVEVKVVDPTGEELPRdgKSMGEVLMRGPWITESYFQLPD-N 411
Cdd:PRK12467 1868 GPTETA-VDVTHWTCRRK---DLEGRDSVP--IGQPIANLSTYILDASLNPVPI--GVAGELYLGGVGLARGYLNRPAlT 1939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 412 SERFL---DG-----WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVpDEKWQERP 483
Cdd:PRK12467 1940 AERFVadpFGtvgsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQL 2018
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 484 VAYVV-------AEDGAEVT-RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK12467 2019 VAYVVptdpglvDDDEAQVAlRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
72-538 |
7.78e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.09 E-value: 7.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 72 VGVLDWNSRrHFELYFAVPGLA-ATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVkgwvVMTDKPA 150
Cdd:PRK07867 57 VGVLLDNTP-EFSLLLGAAALSgIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVRV----INVDSPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 151 deiettlenvvfYEDLIKDKPDT-YDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYL--HTMGGLAALGAsfDDTIM 227
Cdd:PRK07867 132 ------------WADELAAHRDAePPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASagVMLAQRFGLGP--DDVCY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 228 PITPMFH----VLSWGFpqnAVAAGAKLVLPGKFAAEEFGAIAKAFiaeKVTLAN--GAPaifapmLAMMKDMPQPPDls 301
Cdd:PRK07867 198 VSMPLFHsnavMAGWAV---ALAAGASIALRRKFSASGFLPDVRRY---GATYANyvGKP------LSYVLATPERPD-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 302 gvrlvsgSSEPPLSMMRG----------FKEITGADVIHGYGATET---------TPlattnwhikPGldmdeeerwdfk 362
Cdd:PRK07867 264 -------DADNPLRIVYGnegapgdiarFARRFGCVVVDGFGSTEGgvaitrtpdTP---------PG------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 363 ryqGLPVIGVEVKVVDP-TGEELPR-----DGK-----SMGE-VLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIF 429
Cdd:PRK07867 316 ---ALGPLPPGVAIVDPdTGTECPPaedadGRLlnadeAIGElVNTAGPGGFEGYYNDPEaDAERMRGGVYWSGDLAYRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 430 PNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDR-- 507
Cdd:PRK07867 393 ADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpd 472
|
490 500 510
....*....|....*....|....*....|.
gi 1949187543 508 FAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK07867 473 LGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
33-537 |
1.23e-27 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 116.44 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 33 VVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQLNLRLAPEDLA 109
Cdd:cd05970 36 LVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLALhklGAIAIPATHQLTAKDIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 110 YVVSHSKSDWIF-VDESLLP--VAEALA--PKLDVKGWVvmtdkpADEIettLENVVFYEDLIKD------KPDTYDWPV 178
Cdd:cd05970 113 YRIESADIKMIVaIAEDNIPeeIEKAAPecPSKPKLVWV------GDPV---PEGWIDFRKLIKNaspdfeRPTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYagYTTGTTGRPKGVyySHRSIYlhtmgglaalgasfddtimpitPMFHVLSWGFPQNAVAAGAKLVLP---- 254
Cdd:cd05970 184 GEDILLVY--FSSGTTGMPKMV--EHDFTY----------------------PLGHIVTAKYWQNVREGGLHLTVAdtgw 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 -----GKFAAEEFGAIA------KAFIAEK---------VTLANGAPAIFApmlAMMKDMPQPPDLSGVRLVSGSSEPpL 314
Cdd:cd05970 238 gkavwGKIYGQWIAGAAvfvydyDKFDPKAlleklskygVTTFCAPPTIYR---FLIREDLSRYDLSSLRYCTTAGEA-L 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 315 SM--MRGFKEITGADVIHGYGATETT-PLATTNW-HIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELP----- 385
Cdd:cd05970 314 NPevFNTFKEKTGIKLMEGFGQTETTlTIATFPWmEPKPG-------------SMGKPAPGYEIDLIDREGRSCEageeg 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 386 ------RDGKSMGevLMRGpwitesYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEN 458
Cdd:cd05970 381 eivirtSKGKPVG--LFGG------YYKDAEkTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVES 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 459 AILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEvLGDRFAK----WQLPDEIIVTDELPRTSVGKLDKK 534
Cdd:cd05970 453 ALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKE-LQDHVKKvtapYKYPRIVEFVDELPKTISGKIRRV 531
|
...
gi 1949187543 535 LLR 537
Cdd:cd05970 532 EIR 534
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-538 |
2.89e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.37 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVvyrnsdgswgrsNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLA 104
Cdd:PRK12316 4569 AVVFDEEKL------------TYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 105 PEDLAYVVSHSKSDWIFVDESL---LPVAEALApKLDVKgwvvmtdkPADEIEttlenvvfyedlikDKPDTYDWPVVDE 181
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQSHLlqrLPIPDGLA-SLALD--------RDEDWE--------------GFPAHDPAVRLHP 4693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 182 KTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpQNAVAAGAKLVLPGkfAAE 260
Cdd:PRK12316 4694 DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFsFDGSHEGL-YHPLINGASVVIRD--DSL 4770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 261 EFGAIAKAFIAE-KVTLANGAPAIFAPMLammKDMPQPPDLSGVR--LVSGSSEPPLSMMRGFKEITGADVIHGYGATET 337
Cdd:PRK12316 4771 WDPERLYAEIHEhRVTVLVFPPVYLQQLA---EHAERDGEPPSLRvyCFGGEAVAQASYDLAWRALKPVYLFNGYGPTET 4847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 TpLATTNWHIKPGlDMDEEERWDFkryqGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLPD-NSERFL 416
Cdd:PRK12316 4848 T-VTVLLWKARDG-DACGAAYMPI----GTPLGNRSGYVLDGQLNPLPVGV--AGELYLGGEGVARGYLERPAlTAERFV 4919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 DG--------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERpVAYVV 488
Cdd:PRK12316 4920 PDpfgapggrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQL-VGYVV 4998
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 489 AEDGAEVT--------RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK12316 4999 PQDPALADadeaqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
189-538 |
5.93e-27 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 113.38 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVyyshrsiyLHTMGGLAALGASFDDTImPITP--MFHVLS---WGFP-----QNAVAAG-AKLVLPGKF 257
Cdd:cd05973 95 FTSGTTGLPKGV--------PVPLRALAAFGAYLRDAV-DLRPedSFWNAAdpgWAYGlyyaiTGPLALGhPTILLEGGF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 258 AAEEFGAIAKAFiaeKVTLANGAPAIFAPMLAMMKDMPQPPDLSgVRLVSGSSEP--PlSMMRGFKEITGADVIHGYGAT 335
Cdd:cd05973 166 SVESTWRVIERL---GVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPltP-EVIRWFDAALGVPIHDHYGQT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 ETTPLATTNWHIKPGLDMDEeerwdfkryQGLPVIGVEVKVVDPTGEELPRdgKSMGEVLM---RGPWITESYFQLPDNS 412
Cdd:cd05973 241 ELGMVLANHHALEHPVHAGS---------AGRAMPGWRVAVLDDDGDELGP--GEPGRLAIdiaNSPLMWFRGYQLPDTP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 413 ErFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDG 492
Cdd:cd05973 310 A-IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1949187543 493 AEVTRETIVEV---LGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05973 389 HEGTPALADELqlhVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
185-539 |
1.78e-26 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 113.43 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFD-----DTIMPITPMFHVLSW---GFPQNAVAAGAKLV---- 252
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALtanGLVFMKIGGCNHLIsnpr 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 -LPGkFAAEEFGAIAKAFIAEKvTLANGApaIFAPMLAMMkdmpqppDLSGVRL-VSGSSEPPLSMMRGFKEITGADVIH 330
Cdd:PRK08751 291 dMPG-FVKELKKTRFTAFTGVN-TLFNGL--LNTPGFDQI-------DFSSLKMtLGGGMAVQRSVAERWKQVTGLTLVE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 331 GYGATETTPLATTNwhikpGLDMDeeerwDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD 410
Cdd:PRK08751 360 AYGLTETSPAACIN-----PLTLK-----EYNGSIGLPIPSTDACIKDDAGTVLAIG--EIGELCIKGPQVMKGYWKRPE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 NSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVV 488
Cdd:PRK08751 428 ETAKVMDadGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 489 AEDGAeVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKT 539
Cdd:PRK08751 508 KKDPA-LTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
364-540 |
1.93e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 110.52 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 364 YQGLPVIGVEVKVVDptgeelprdgksmGEVLMRGPWITESYFQLPDNSERFLDGWWRSGDVGVIfPNGYLKLTDRLKDV 443
Cdd:PRK07824 193 YDGVPLDGVRVRVED-------------GRIALGGPTLAKGYRNPVDPDPFAEPGWFRTDDLGAL-DDGVLTVLGRADDA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 444 IKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDEL 523
Cdd:PRK07824 259 ISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDEL 338
|
170
....*....|....*..
gi 1949187543 524 PRTSVGKLDKKLLRKTW 540
Cdd:PRK07824 339 PRRGIGKVDRRALVRRF 355
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-538 |
3.70e-26 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 110.86 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRSNYAdEFKRMA-QLAHGLTELGVGAGSMVGVLdwnSRRHFELyfavpgLAATMLQLNLRLApedlaYVvshsks 117
Cdd:cd17653 17 ESLGGSLTYG-ELDAASnALANRLLQLGVVPGDVVPLL---SDRSLEM------LVAILAILKAGAA-----YV------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 118 dwifvdesllPVAEALapkldvkgwvvmtdkPADEIETTLENVVFYEDLIKDKPDTYdwpvvdektaAYAGYTTGTTGRP 197
Cdd:cd17653 76 ----------PLDAKL---------------PSARIQAILRTSGATLLLTTDSPDDL----------AYIIFTSGSTGIP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 198 KGVYYSHRSI--YLHTMGGLAALGasfddtimPITPMFHVLSWGFPQNA------VAAGAKLVLPGkfAAEEFGAIAKaf 269
Cdd:cd17653 121 KGVMVPHRGVlnYVSQPPARLDVG--------PGSRVAQVLSIAFDACIgeifstLCNGGTLVLAD--PSDPFAHVAR-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 270 iaeKVTLANGAPAIfapmLAMMKdmpqPPDLSGVRLVS-GSSEPPLSMMRGFKEitGADVIHGYGATETTpLATTNWHIK 348
Cdd:cd17653 189 ---TVDALMSTPSI----LSTLS----PQDFPNLKTIFlGGEAVPPSLLDRWSP--GRRLYNAYGPTECT-ISSTMTELL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 349 PGldmdeeerwdfKRYQ-GLPVIGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLP-DNSERFL-DGWW----- 420
Cdd:cd17653 255 PG-----------QPVTiGKPIPNSTCYILDADLQPVPEGVV--GEICISGVQVARGYLGNPaLTASKFVpDPFWpgsrm 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 421 -RSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDS-PSVKEAAVIGVpdekwQERPVAYVVAEDgaeVTRE 498
Cdd:cd17653 322 yRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSqPEVTQAAAIVV-----NGRLVAFVTPET---VDVD 393
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1949187543 499 TIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd17653 394 GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
46-536 |
7.92e-26 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 112.45 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQLNLRLAPEDLAYVVSHSKSdwifv 122
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVA---LPRSVFLTLALHAIveaGAAWLPLDTGYPDDRLKMMLEDARP----- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 123 deSLLPVAEALAPKLDvkgwvvmtDKPADEIET--TLENVVFYEDLIKDKPDTydwpvvdektAAYAGYTTGTTGRPKGV 200
Cdd:PRK10252 557 --SLLITTADQLPRFA--------DVPDLTSLCynAPLAPQGAAPLQLSQPHH----------TAYIIFTSGSTGRPKGV 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 201 YYSHRSI-----YLHTMGGLAAlgasfDDTIMPITPM-FHVLSWGF--PqnaVAAGAKLVLPGKFAAEEFGAIAKAFIAE 272
Cdd:PRK10252 617 MVGQTAIvnrllWMQNHYPLTA-----DDVVLQKTPCsFDVSVWEFfwP---FIAGAKLVMAEPEAHRDPLAMQQFFAEY 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 273 KVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP-PLSMMRGFKEITGADVIHGYGATETTplATTNWHIKPGL 351
Cdd:PRK10252 689 GVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEAlPADLCREWQQLTGAPLHNLYGPTEAA--VDVSWYPAFGE 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 352 DMDEEErwdfkryqGLPV-IGVEV-----KVVDPTGEELPrDGKSmGEVLMRGPWITESYFQLPD-NSERFLDG------ 418
Cdd:PRK10252 767 ELAAVR--------GSSVpIGYPVwntglRILDARMRPVP-PGVA-GDLYLTGIQLAQGYLGRPDlTASRFIADpfapge 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 419 -WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGV-----PDEKWQERP-VAYVVAED 491
Cdd:PRK10252 837 rMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDARQlVGYLVSQS 916
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1949187543 492 GAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK10252 917 GLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
47-538 |
1.12e-25 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 111.11 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGvldwnsrrhfeLYFA-VPGLAATMLQLNlRL-----------APEDLAYVVSH 114
Cdd:cd05966 87 YRELLREVCRFANVLKSLGVKKGDRVA-----------IYMPmIPELVIAMLACA-RIgavhsvvfagfSAESLADRIND 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 115 SKSDW-IFVDES--------LLPVA-EALAPKLDVKGwVVMTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVDEKTA 184
Cdd:cd05966 155 AQCKLvITADGGyrggkvipLKEIVdEALEKCPSVEK-VLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVyyshrsiyLHTMGGLAaLGAS------FD----DT------IMPIT--------PMfhvlswgf 240
Cdd:cd05966 234 LFILYTSGSTGKPKGV--------VHTTGGYL-LYAAttfkyvFDyhpdDIywctadIGWITghsyivygPL-------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 241 pqnavAAGAKLVL---------PGKFaaeeFGAIAKafiaEKVTLANGAP-AIfapmLAMMKDMPQPP---DLSGVRLVS 307
Cdd:cd05966 297 -----ANGATTVMfegtptypdPGRY----WDIVEK----HKVTIFYTAPtAI----RALMKFGDEWVkkhDLSSLRVLG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 308 GSSEP--PLSMMRGFKEITG--ADVIHGYGATET-----TPLATTnWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVD 378
Cdd:cd05966 360 SVGEPinPEAWMWYYEVIGKerCPIVDTWWQTETggimiTPLPGA-TPLKPG-------------SATRPFFGIEPAILD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 379 PTGEELPRDGKsmGEVLMRGPWitesyfqlPD-------NSERFLDGWWR-------SGDVGVIFPNGYLKLTDRLKDVI 444
Cdd:cd05966 426 EEGNEVEGEVE--GYLVIKRPW--------PGmartiygDHERYEDTYFSkfpgyyfTGDGARRDEDGYYWITGRVDDVI 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 445 KSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVE-------VLGdRFAKwqlPDEI 517
Cdd:cd05966 496 NVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKElrkhvrkEIG-PIAT---PDKI 571
|
570 580
....*....|....*....|.
gi 1949187543 518 IVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILRK 592
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
33-545 |
2.62e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 109.73 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 33 VVYRNSDGSWgrsnyaDEFKRMAQL-AHGLTELGVGAGSM-VGVLDWNSRrHFELYFAVPGLA-ATMLQLNLRLAPEDLA 109
Cdd:PRK13388 20 VRYGDRTWTW------REVLAEAAArAAALIALADPDRPLhVGVLLGNTP-EMLFWLAAAALGgYVLVGLNTTRRGAALA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 110 YVVSHSKSDWIFVDESLLPVAEALapklDVKG-WVVMTDKPAdeiettlenvvfYEDLIKDKPDTYDWPVVDEKTAAYAG 188
Cdd:PRK13388 93 ADIRRADCQLLVTDAEHRPLLDGL----DLPGvRVLDVDTPA------------YAELVAAAGALTPHREVDAMDPFMLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHrsiylhtmGGLAALGASF--------DDTIMPITPMFH---VLS-WGfPqnAVAAGAKLVLPGK 256
Cdd:PRK13388 157 FTSGTTGAPKAVRCSH--------GRLAFAGRALterfgltrDDVCYVSMPLFHsnaVMAgWA-P--AVASGAAVALPAK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEFGAIAKAFIAekvTLAN--GAPaifapmLAMMKDMPQPPDLSGVRLVSG-SSEPPLSMMRGFKEITGADVIHGYG 333
Cdd:PRK13388 226 FSASGFLDDVRRYGA---TYFNyvGKP------LAYILATPERPDDADNPLRVAfGNEASPRDIAEFSRRFGCQVEDGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 334 ATETTPLATTNWHIKPGLdmdeeerwdfkryQGLPVIGVEVkvVDP-TGEELPR-----DGK------SMGE-VLMRGPW 400
Cdd:PRK13388 297 SSEGAVIVVREPGTPPGS-------------IGRGAPGVAI--YNPeTLTECAVarfdaHGAllnadeAIGElVNTAGAG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 401 ITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKW 479
Cdd:PRK13388 362 FFEGYYNNPEaTAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 480 QERPVAYVVAEDGAEVTRETIVEVLG---DRFAKWQlPDEIIVTDELPRTSVGKLDKKLLRKT-WEDAEA 545
Cdd:PRK13388 442 GDQVMAALVLRDGATFDPDAFAAFLAaqpDLGTKAW-PRYVRIAADLPSTATNKVLKRELIAQgWATGDP 510
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
46-488 |
4.02e-25 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 109.23 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 46 NYADEFKRMAQLAHGLTELGV--GAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 esllpvaealapkldvKGWVVMTdkpadeiettLENVvfyEDLIKDKPdtYDWPVVDEKTAAYAGYTTGTTGRPKGVYYS 203
Cdd:cd05927 87 ----------------AGVKVYS----------LEEF---EKLGKKNK--VPPPPPKPEDLATICYTSGTTGNPKGVMLT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 204 HRSIylhtMGGLAALGASFDDTIMPIT--------PMFHVLSWGFPQNAVAAGAKL--------------------VLPG 255
Cdd:cd05927 136 HGNI----VSNVAGVFKILEILNKINPtdvyisylPLAHIFERVVEALFLYHGAKIgfysgdirlllddikalkptVFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 ------KFAAEEFGAI-AKAFIAEKvtLANGAPAIFAPMLAMMKDMPQP----------PDLSG--VRL-VSGSSEPPLS 315
Cdd:cd05927 212 vprvlnRIYDKIFNKVqAKGPLKRK--LFNFALNYKLAELRSGVVRASPfwdklvfnkiKQALGgnVRLmLTGSAPLSPE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 316 MMRGFKEITGADVIHGYGATETTPLATTNWHikpgldmdeeerWDF-KRYQGLPVIGVEVKVVD-PTGEELPRDGKSMGE 393
Cdd:cd05927 290 VLEFLRVALGCPVLEGYGQTECTAGATLTLP------------GDTsVGHVGGPLPCAEVKLVDvPEMNYDAKDPNPRGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 394 VLMRGPWITESYFQLPDNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSVKEAA 470
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALdeDGWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIF 437
|
490
....*....|....*...
gi 1949187543 471 VIGVPDEKWqerPVAYVV 488
Cdd:cd05927 438 VYGDSLKSF---LVAIVV 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
189-488 |
4.99e-25 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 108.46 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIY--LHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKL------VLPGKFAAE 260
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNLVagIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIgygsprTLTDKSKRG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 261 EFGAIAkAFiaeKVTLANGAPAIF-----------APM---------------LAMMKDMPQPP-----------DLSGV 303
Cdd:cd17639 175 CKGDLT-EF---KPTLMVGVPAIWdtirkgvlaklNPMgglkrtlfwtayqskLKALKEGPGTPlldelvfkkvrAALGG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 304 RL---VSGSSepPLSM-MRGFKEITGADVIHGYGATETTPLATTNwhikpgldmdEEERWDFKRYqGLPVIGVEVKVVDP 379
Cdd:cd17639 251 RLrymLSGGA--PLSAdTQEFLNIVLCPVIQGYGLTETCAGGTVQ----------DPGDLETGRV-GPPLPCCEIKLVDW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 380 tgEEL--------PRdgksmGEVLMRGPWITESYFQLPD-NSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKS-GG 448
Cdd:cd17639 318 --EEGgystdkppPR-----GEILIRGPNVFKGYYKNPEkTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNG 390
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1949187543 449 EWISSIDMENAILDSPSVKEAAVIGVPDekwQERPVAYVV 488
Cdd:cd17639 391 EYIALEKLESIYRSNPLVNNICVYADPD---KSYPVAIVV 427
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
23-536 |
9.90e-25 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 106.78 E-value: 9.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDGswgRSNyadefkrmaQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQL 99
Cdd:cd17650 3 AIAVSDATRQLTYRELNE---RAN---------QLARTLRGLGVAPGSVVGVC---ADRSLDAIVGLLAVlkaGGAYVPI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDwifvdesllpvaealapkldvkgwVVMTDkPADeiettlenvvfyedlikdkpdtydwpvv 179
Cdd:cd17650 68 DPDYPAERLQYMLEDSGAK------------------------LLLTQ-PED---------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 dektAAYAGYTTGTTGRPKGVYYSHRSIY--LHTMGGLAALgASFDDTIMPITPM-FHVLSWGFPQNAVAAGAKLVLPGK 256
Cdd:cd17650 95 ----LAYVIYTSGTTGKPKGVMVEHRNVAhaAHAWRREYEL-DSFPVRLLQMASFsFDVFAGDFARSLLNGGTLVICPDE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEfGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVR-LVSGSSEPPlsmMRGFKEIT-----GADVIH 330
Cdd:cd17650 170 VKLDP-AALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRlLIVGSDGCK---AQDFKTLAarfgqGMRIIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 331 GYGATETTpLATTNWHikpgLDMDEEERWDFKRYqGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD 410
Cdd:cd17650 244 SYGVTEAT-IDSTYYE----EGRDPLGDSANVPI-GRPLPNTAMYVLDERLQPQPVG--VAGELYIGGAGVARGYLNRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 411 -NSERFLDG-------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQER 482
Cdd:cd17650 316 lTAERFVENpfapgerMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEAR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 483 PVAYVVAEDGAEvTREtIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17650 396 LCAYVVAAATLN-TAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
39-493 |
4.44e-24 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 105.63 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRSnyADEFKRMAqlAHgLTELGVGAGSMVGVLDWNSRRHFelyfaVPGLAATM-----LQLNLRLAPEDLAYVVS 113
Cdd:cd05932 6 EFTWGEV--ADKARRLA--AA-LRALGLEPGSKIALISKNCAEWF-----ITDLAIWMaghisVPLYPTLNPDTIRYVLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 114 HSKSDWIFVDesllpvaealapKLDvkGWVVMTDKPADEIET-------TLENVVFYEDLIKDKPDTYDWPVVDEKTAAY 186
Cdd:cd05932 76 HSESKALFVG------------KLD--DWKAMAPGVPEGLISislpppsAANCQYQWDDLIAQHPPLEERPTRFPEQLAT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 187 AGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVlpgkFAAEEFGAIA 266
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLV----AFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 267 KAFIAEKVTLANGAPAIFAPMLAMMKD-MPQPP----------------------DLSGVRLVSGSSEP-PLSMMRGFKE 322
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWTKFQQGVQDkIPQQKlnlllkipvvnslvkrkvlkglGLDQCRLAGCGSAPvPPALLEWYRS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 323 ItGADVIHGYGATETTPLATTNwhiKPGldmDEEERWdfkryQGLPVIGVEVKVVDPtgeelprdgksmGEVLMRGPWIT 402
Cdd:cd05932 298 L-GLNILEAYGMTENFAYSHLN---YPG---RDKIGT-----VGNAGPGVEVRISED------------GEILVRSPALM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 403 ESYFQLPDNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSVKEAAVIGvpdeKW 479
Cdd:cd05932 354 MGYYKDPEATAEAFtaDGFLRTGDKGELDADGNLTITGRVKDIFKtSKGKYVAPAPIENKLAEHDRVEMVCVIG----SG 429
|
490
....*....|....
gi 1949187543 480 QERPVAYVVAEDGA 493
Cdd:cd05932 430 LPAPLALVVLSEEA 443
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
47-544 |
4.71e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 105.25 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGvGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:PRK07638 29 YKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LpvaealAPKLDVKGWVVMTDKPADEIETTLENVVFYEDLikdkpdtydwpvvdEKTAAYAGYTTGTTGRPKGVYYSHRS 206
Cdd:PRK07638 108 L------NDLPDEEGRVIEIDEWKRMIEKYLPTYAPIENV--------------QNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 207 iYLHtmgglaalgaSFDDTIMPitpmFHVLSwgfpQNAVaagaklVLPGKFAAEEF--GAIAKAFIAEKVTLANGapaiF 284
Cdd:PRK07638 168 -WLH----------SFDCNVHD----FHMKR----EDSV------LIAGTLVHSLFlyGAISTLYVGQTVHLMRK----F 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 285 APmlAMMKDMPQPPDLSGVRLVSGSSEPPLSMMRgFKE------ITGADvihgYGATETTPLATTNWHIKpgldmdeeeR 358
Cdd:PRK07638 219 IP--NQVLDKLETENISVMYTVPTMLESLYKENR-VIEnkmkiiSSGAK----WEAEAKEKIKNIFPYAK---------L 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 359 WDF-----------------KRYQ---GLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYF-QLPDNSERFLD 417
Cdd:PRK07638 283 YEFygaselsfvtalvdeesERRPnsvGRPFHNVQVRICNEAGEEVQKG--EIGTVYVKSPQFFMGYIiGGVLARELNAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 418 GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVvaeDGAEvTR 497
Cdd:PRK07638 361 GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSA-TK 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1949187543 498 ETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRKTWEDAE 544
Cdd:PRK07638 437 QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQE 483
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
4-542 |
9.45e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 104.67 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 4 GIPSTLGDsyqlnttsMIRHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVgVLDWNSRRHF 83
Cdd:cd05906 7 GAPRTLLE--------LLLRAAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 84 ELYF---------AVPgLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVmtdkpadeie 154
Cdd:cd05906 78 IPAFwacvlagfvPAP-LTVPPTYDEPNARLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRV---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 155 TTLENVvfyedliKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH 234
Cdd:cd05906 147 LSIEEL-------LDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 235 VlswgfpqnavaagAKLVLPGKFA----AEEFGAIAKAFIAE-----------KVTLAngapaiFAP--MLAMMKDM--- 294
Cdd:cd05906 220 V-------------GGLVELHLRAvylgCQQVHVPTEEILADplrwldlidryRVTIT------WAPnfAFALLNDLlee 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 295 --PQPPDLSGVR-LVSGSSEPPLSMMRGFKEITG-----ADVIH-GYGATETTPLATTNwHIKPGLDMDEEERwdFKRYq 365
Cdd:cd05906 281 ieDGTWDLSSLRyLVNAGEAVVAKTIRRLLRLLEpyglpPDAIRpAFGMTETCSGVIYS-RSFPTYDHSQALE--FVSL- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 366 GLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFL-DGWWRSGDVGVIfPNGYLKLTDRLKDV 443
Cdd:cd05906 357 GRPIPGVSMRIVDDEGQLLPEG--EVGRLQVRGPVVTKGYYNNPEaNAEAFTeDGWFRTGDLGFL-DNGNLTITGRTKDT 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 444 IKSGGEWISSIDMENAILDSPSVK-----------------EAAVIGVPDEKWQERPVAYVvaedgaEVTRETIVEVLGD 506
Cdd:cd05906 434 IIVNGVNYYSHEIEAAVEEVPGVEpsftaafavrdpgaeteELAIFFVPEYDLQDALSETL------RAIRSVVSREVGV 507
|
570 580 590
....*....|....*....|....*....|....*...
gi 1949187543 507 RfakwqlPDEII--VTDELPRTSVGKLDKKLLRKTWED 542
Cdd:cd05906 508 S------PAYLIplPKEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-537 |
2.09e-23 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 104.11 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 22 RHAATVFGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNL 101
Cdd:cd05968 69 KWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 102 RLAPEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKgwvvmtdkPADEIETTLENVVFYEDLIKDKPDT---YDWPV 178
Cdd:cd05968 149 GFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEAD--------KACAQCPTVEKVVVVRHLGNDFTPAkgrDLSYD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 vDEKTAAYAG-------------YTTGTTGRPKGVYYSHRSIYLHtmgGLAALGASFD----DTIMPITPMFHVLSWGFP 241
Cdd:cd05968 221 -EEKETAGDGaertesedplmiiYTSGTTGKPKGTVHVHAGFPLK---AAQDMYFQFDlkpgDLLTWFTDLGWMMGPWLI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 242 QNAVAAGAKLVL----PGKFAAEEFGAIAKAFiaeKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEP--PLS 315
Cdd:cd05968 297 FGGLILGATMVLydgaPDHPKADRLWRMVEDH---EITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPwnPEP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 316 MMRGFKEITGADV-IHGY-GATETTPLATTNWHIKPGLDMDeeerwdfkrYQGlPVIGVEVKVVDPTGEELPrdgKSMGE 393
Cdd:cd05968 374 WNWLFETVGKGRNpIINYsGGTEISGGILGNVLIKPIKPSS---------FNG-PVPGMKADVLDESGKPAR---PEVGE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 394 VLMRGPWI--TESYFQLPDnseRFLDGWWRS-------GDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSP 464
Cdd:cd05968 441 LVLLAPWPgmTRGFWRDED---RYLETYWSRfdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 465 SVKEAAVIGVPDEKWQERPVAYVVAEDG---AEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05968 518 AVLESAAIGVPHPVKGEAIVCFVVLKPGvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
43-536 |
4.31e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.48 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 43 GRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFV 122
Cdd:PRK05691 1155 GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 123 DESL---LPVAEALAPKldvkgwvvmtdkPADEIEttLENvvfyedlikdkpdtydWPV------VDEKTAAYAGYTTGT 193
Cdd:PRK05691 1235 QSHLlerLPQAEGVSAI------------ALDSLH--LDS----------------WPSqapglhLHGDNLAYVIYTSGS 1284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 194 TGRPKGVYYSHRSI--YLHTMGGLAALGASfdDTIMPITPM-FHVLSWG--FPqnaVAAGAKLVLPGKFAAEEFGAIAKA 268
Cdd:PRK05691 1285 TGQPKGVGNTHAALaeRLQWMQATYALDDS--DVLMQKAPIsFDVSVWEcfWP---LITGCRLVLAGPGEHRDPQRIAEL 1359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 269 FIAEKVTLANGAPaifaPMLAMMKDMPQPPDLSGVRLV-SGSSEPPLSMMRGFKEITGADVIHG-YGATETTpLATTNWH 346
Cdd:PRK05691 1360 VQQYGVTTLHFVP----PLLQLFIDEPLAAACTSLRRLfSGGEALPAELRNRVLQRLPQVQLHNrYGPTETA-INVTHWQ 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 347 IKpgldMDEEERWDFKRyqglPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESYFQLPD-NSERFL------DG- 418
Cdd:PRK05691 1435 CQ----AEDGERSPIGR----PLGNVLCRVLDAELNLLPPG--VAGELCIGGAGLARGYLGRPAlTAERFVpdplgeDGa 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 419 -WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIgVPDEKWQERPVAYVVAEDGAEVTR 497
Cdd:PRK05691 1505 rLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEA 1583
|
490 500 510
....*....|....*....|....*....|....*....
gi 1949187543 498 ETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK05691 1584 ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
185-536 |
4.79e-23 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 102.13 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGA------------SFDDTIMPITPMFHvlswgfpqnavaAGAKLV 252
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGItssdrvlqfasiAFDVAAEEIYVTLL------------SGATLV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 L-PGK--FAAEEFgaiaKAFIAE-KVTLANGAPAIFAPM-LAMMKDMPQPPDLSGVRLVSGSSEPPlSMMRGFKEITGAD 327
Cdd:cd17644 177 LrPEEmrSSLEDF----VQYIQQwQLTVLSLPPAYWHLLvLELLLSTIDLPSSLRLVIVGGEAVQP-ELVRQWQKNVGNF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 V--IHGYGATETTpLATTNWHIKpgldmDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESY 405
Cdd:cd17644 252 IqlINVYGPTEAT-IAATVCRLT-----QLTERNITSVPIGRPIANTQVYILDENLQPVPVG--VPGELHIGGVGLARGY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 406 FQLPD-NSERFL---------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVP 475
Cdd:cd17644 324 LNRPElTAEKFIshpfnssesERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRE 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 476 DEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17644 404 DQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
47-542 |
1.44e-22 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 101.16 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGvGAGSMVGVLDWNSRRHFELYFAV--PGLAATMLQL-NLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:cd05931 27 YAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGClyAGAIAVPLPPpTPGRHAERLAAILADAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLP--VAEALAPKLDVKGWVVMTDKPADEIettlenvvfyedlikdkPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVY 201
Cdd:cd05931 106 AAALAavRAFAASRPAAGTPRLLVVDLLPDTS-----------------AADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 202 YSHRSIYLHTMGGLAALGASFDDTIMPITPMFH----VLSWGFPqnaVAAGAKLVL--PGKFAAEEFG---AIAKAfiae 272
Cdd:cd05931 169 VTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHdmglIGGLLTP---LYSGGPSVLmsPAAFLRRPLRwlrLISRY---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 273 KVTLAnGAPAiFAPMLAMMKDMPQ---PPDLSGVR-LVSGsSEP--PLSMMR--------GFKeitgADVIH-GYGATET 337
Cdd:cd05931 242 RATIS-AAPN-FAYDLCVRRVRDEdleGLDLSSWRvALNG-AEPvrPATLRRfaeafapfGFR----PEAFRpSYGLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 TPLATTNWH-IKPGLDMDEEERWDFKRYQ--------------GLPVIGVEVKVVDP-TGEELPRDGksMGEVLMRGPWI 401
Cdd:cd05931 315 TLFVSGGPPgTGPVVLRVDRDALAGRAVAvaaddpaarelvscGRPLPDQEVRIVDPeTGRELPDGE--VGEIWVRGPSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 402 TESYFQLPDNSERFL--------DGWWRSGDVGVIFpNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKE---AA 470
Cdd:cd05931 393 ASGYWGRPEATAETFgalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 471 VIGVPDEkwQERPVAyVVAEDGAEVTRET-------IVEVLGDRFakwQL-PDEIIV--TDELPRTSVGKLDKKLLRKTW 540
Cdd:cd05931 472 AFSVPDD--GEERLV-VVAEVERGADPADlaaiaaaIRAAVAREH---GVaPADVVLvrPGSIPRTSSGKIQRRACRAAY 545
|
..
gi 1949187543 541 ED 542
Cdd:cd05931 546 LD 547
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
455-530 |
3.28e-22 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 90.30 E-value: 3.28e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 455 DMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGK 530
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
178-536 |
1.49e-21 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 97.47 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAAYAGYTTGTTGRPKGVYYSHRSIyLHTMGGLAAL-GASFDDTIMPITPMFHVLSWGFPQ--NAVAAGAKLVLP 254
Cdd:cd17648 90 ITNSTDLAYAIYTSGTTGKPKGVLVEHGSV-VNLRTSLSERyFGRDNGDEAVLFFSNYVFDFFVEQmtLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 ---GKFAAEEFGAIAKAfiaEKVTLANGAPAIFApmlamMKDMPQPPDLSGVRLVSGS-SEPPLSMMRG-FKeitgADVI 329
Cdd:cd17648 169 pdeMRFDPDRFYAYINR---EKVTYLSGTPSVLQ-----QYDLARLPHLKRVDAAGEEfTAPVFEKLRSrFA----GLII 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 HGYGATETTplATTNWHIKPGldmdeEERWDfkRYQGLPVIGVEVKVVDPTGEELPRDGksMGEVLMRGPWITESYFQLP 409
Cdd:cd17648 237 NAYGPTETT--VTNHKRFFPG-----DQRFD--KSLGRPVRNTKCYVLNDAMKRVPVGA--VGELYLGGDGVARGYLNRP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 D-NSERFL-----------DG----WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVI- 472
Cdd:cd17648 306 ElTAERFLpnpfqteqeraRGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVa 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 473 ----GVPDEKWQERPVAYVVAEDGAeVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17648 386 kedaSQAQSRIQKYLVGYYLPEPGH-VPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
186-538 |
1.89e-21 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 98.16 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 186 YAGYTTGTTGRPKGV-----------YYSHRSIYlhtmgGLAAlgasfDDTIMPITPMFHVLSWGF----PqnaVAAGAK 250
Cdd:cd05967 234 YILYTSGTTGKPKGVvrdngghavalNWSMRNIY-----GIKP-----GDVWWAASDVGWVVGHSYivygP---LLHGAT 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 251 LVL----------PGKFaaeeFGAIAKafiaEKVTLANGAPAIFApmlAMMKDMPQPP-----DLSGVRLVSGSSEP-PL 314
Cdd:cd05967 301 TVLyegkpvgtpdPGAF----WRVIEK----YQVNALFTAPTAIR---AIRKEDPDGKyikkyDLSSLRTLFLAGERlDP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 315 SMMRGFKEITGADVIHGYGATET------TPLATTNWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDg 388
Cdd:cd05967 370 PTLEWAENTLGVPVIDHWWQTETgwpitaNPVGLEPLPIKAG-------------SPGKPVPGYQVQVLDEDGEPVGPN- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 389 kSMGEVLMRGPWITESYFQLPDNSERFLDGWW-------RSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAIL 461
Cdd:cd05967 436 -ELGNIVIKLPLPPGCLLTLWKNDERFKKLYLskfpgyyDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 462 DSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET----IVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLR 537
Cdd:cd05967 515 SHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEElekeLVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
.
gi 1949187543 538 K 538
Cdd:cd05967 595 K 595
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
35-473 |
2.68e-21 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 97.49 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 35 YRNSD-GSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVS 113
Cdd:cd17641 1 LREKDfGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 114 HSKSDWIFV-DESLLPVAEALAPKLDVKGWVVMTD-----KPADEIETTLENVVFYEDLIKDK-PDTYDWPVVDEK--TA 184
Cdd:cd17641 81 YTGARVVIAeDEEQVDKLLEIADRIPSVRYVIYCDprgmrKYDDPRLISFEDVVALGRALDRRdPGLYEREVAAGKgeDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPmfhvLSWGFPQnAVAAGAKLVLPGKFAAEEFGA 264
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLP----LPWIGEQ-MYSVGQALVCGFIVNFPEEPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 265 IAKAFIAE---KVTLAngAPAIFAPMLA-----MMKDMP-----------------------QPPDLsGVRLVSGSSEP- 312
Cdd:cd17641 236 TMMEDLREigpTFVLL--PPRVWEGIAAdvrarMMDATPfkrfmfelgmklglraldrgkrgRPVSL-WLRLASWLADAl 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 313 ---PLSMMRGFKEIT--------------------GADVIHGYGATETTPLATtnwhIKPGLDMDEEErwdfkryQGLPV 369
Cdd:cd17641 313 lfrPLRDRLGFSRLRsaatggaalgpdtfrffhaiGVPLKQLYGQTELAGAYT----VHRDGDVDPDT-------VGVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 370 IGVEVKVVDptgeelprdgksMGEVLMRGPWITESYFQLPDNS-ERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIK-S 446
Cdd:cd17641 382 PGTEVRIDE------------VGEILVRSPGVFVGYYKNPEATaEDFDeDGWLHTGDAGYFKENGHLVVIDRAKDVGTtS 449
|
490 500
....*....|....*....|....*..
gi 1949187543 447 GGEWISSIDMENAILDSPSVKEAAVIG 473
Cdd:cd17641 450 DGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
103-538 |
3.30e-21 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 97.15 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 103 LAPEDLAYVVSHSKSDWIFVDESLLPVAEALA---PKLDVKgwVVMTDKPADeiettleNVVFYEDLIKDKPDTYDwpVV 179
Cdd:cd05928 101 LTAKDILYRLQASKAKCIVTSDELAPEVDSVAsecPSLKTK--LLVSEKSRD-------GWLNFKELLNEASTEHH--CV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 DEKT----AAYagYTTGTTGRPKGVYYSHRSIYL-HTMGGLAALGASFDDTIMPITPMFHVLS-WGFPQNAVAAGAkLVL 253
Cdd:cd05928 170 ETGSqepmAIY--FTSGTTGSPKMAEHSHSSLGLgLKVNGRYWLDLTASDIMWNTSDTGWIKSaWSSLFEPWIQGA-CVF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFApMLAMMkdmpqppDLSGVR-------LVSGSSEPPlSMMRGFKEITGA 326
Cdd:cd05928 247 VHHLPRFDPLVILKTLSSYPITTFCGAPTVYR-MLVQQ-------DLSSYKfpslqhcVTGGEPLNP-EVLEKWKAQTGL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 327 DVIHGYGATETTPLATTNW--HIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRdGKSmGEVLMR-GPWITE 403
Cdd:cd05928 318 DIYEGYGQTETGLICANFKgmKIKPG-------------SMGKASPPYDVQIIDDNGNVLPP-GTE-GDIGIRvKPIRPF 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 404 SYF-QLPDNSER----FLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEK 478
Cdd:cd05928 383 GLFsGYVDNPEKtaatIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPI 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 479 WQERPVAYVV------AEDGAEVTREtIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05928 463 RGEVVKAFVVlapqflSHDPEQLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
135-537 |
5.72e-21 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 97.02 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 135 PKLDVKGWVVMTDKP-ADEIETTleNVVFYEDLIKD--KPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHT 211
Cdd:PRK06060 97 AARNTEPALVVTSDAlRDRFQPS--RVAEAAELMSEaaRVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 212 MGGLA-ALGASFDDTIMPITPMFHVLSWG----FPqnAVAAGAKLVLPGKFAAEEFGAIAKAFiaeKVTLANGAPAIFAP 286
Cdd:PRK06060 175 DAMCRkALRLTPEDTGLCSARMYFAYGLGnsvwFP--LATGGSAVINSAPVTPEAAAILSARF---GPSVLYGVPNFFAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 287 MLammkDMPQPPDLSGVRLV--SGSSEPPLSMMRGFKEITGADVIHGYGATETTPLATTNwhikpglDMDEEERWDFKRY 364
Cdd:PRK06060 250 VI----DSCSPDSFRSLRCVvsAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSN-------RVDEWRLGTLGRV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 365 qgLPviGVEVKVVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPDnSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVI 444
Cdd:PRK06060 319 --LP--PYEIRVVAPDGTTAGPGVE--GDLWVRGPAIAKGYWNRPD-SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 445 KSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEV---LGDRFAKWQLPDEIIVTD 521
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLhrgLLNRLSAFKVPHRFAVVD 471
|
410
....*....|....*.
gi 1949187543 522 ELPRTSVGKLDKKLLR 537
Cdd:PRK06060 472 RLPRTPNGKLVRGALR 487
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
23-536 |
1.34e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 94.85 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 23 HAATVFGEQEVVYRNSDgswgrsnyadefKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQL 99
Cdd:cd17656 4 AVAVVFENQKLTYRELN------------ERSNQLARFLREKGVKKDSIVAIM---MERSAEMIVGILGIlkaGGAFVPI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 100 NLRLAPEDLAYVVSHSKSDWIFVDESLlpvaealapkldvkgwvvmTDKPADEIETTLenvvFYEDLIKDKPDTYDWPVV 179
Cdd:cd17656 69 DPEYPEERRIYIMLDSGVRVVLTQRHL-------------------KSKLSFNKSTIL----LEDPSISQEDTSNIDYIN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 180 DEKTAAYAGYTTGTTGRPKGVYYSHRSI-------YLHTmgglaaLGASFDDTIMPITPMFHVlSWGFPQNAVAAGAKLV 252
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQLEHKNMvnllhfeREKT------NINFSDKVLQFATCSFDV-CYQEIFSTLLSGGTLY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LPGKFAAEE----FGAIAKAFIaEKVTLangaPAIFAPMLAMMKDMpQPPDLSGVRLVSGSSEPpLSMMRGFKEITGADV 328
Cdd:cd17656 199 IIREETKRDveqlFDLVKRHNI-EVVFL----PVAFLKFIFSEREF-INRFPTCVKHIITAGEQ-LVITNEFKEMLHEHN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IH---GYGATETtplattnwHIKPGLDMDEEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGPWITESY 405
Cdd:cd17656 272 VHlhnHYGPSET--------HVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQG--IVGELYISGASVARGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 406 FQLPD-NSERFLDG-------WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDE 477
Cdd:cd17656 342 LNRQElTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADD 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 478 KWQERPVAYVVAEdgAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17656 422 KGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
37-473 |
1.91e-20 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 95.12 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 37 NSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRrhfELYFA------VPGLAATMLQLNlrlAPEDLAY 110
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSP---EWFIAavgaifAGGIAVGIYTTN---SPEACQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 111 VVSHSKSDWIFVD-----ESLLPVAEALaPKLDVkgwVVMTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVDEKTA- 184
Cdd:cd05933 75 VAETSEANILVVEnqkqlQKILQIQDKL-PHLKA---IIQYKEPLKEKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 --AYAGYTTGTTGRPKGVYYSHRSIYLHTmgglAALGASFDDTIMPITPMfHVLSWgFPQNAVAAGA-KLVLPGKFAAEE 261
Cdd:cd05933 151 qcCTLIYTSGTTGMPKGVMLSHDNITWTA----KAASQHMDLRPATVGQE-SVVSY-LPLSHIAAQIlDIWLPIKVGGQV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 262 FGAIAKAFiaeKVTLAN-----------GAPAIFAPMLAMMKDMPQppDLSGVR-----------------LVSGSSEPP 313
Cdd:cd05933 225 YFAQPDAL---KGTLVKtlrevrptafmGVPRVWEKIQEKMKAVGA--KSGTLKrkiaswakgvgletnlkLMGGESPSP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 314 LSM-------------MRGF----KEITGA----------------DVIHGYGATETTPLATTNWHIKPGLDMdeeerwd 360
Cdd:cd05933 300 LFYrlakklvfkkvrkALGLdrcqKFFTGAapisretlefflslniPIMELYGMSETSGPHTISNPQAYRLLS------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 361 fkryQGLPVIGVEVKVVDPtgeelprDGKSMGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTD 438
Cdd:cd05933 373 ----CGKALPGCKTKIHNP-------DADGIGEICFWGRHVFMGYLNMEDKTEEAIDedGWLHSGDLGKLDEDGFLYITG 441
|
490 500 510
....*....|....*....|....*....|....*..
gi 1949187543 439 RLKDVIK-SGGEWISSIDMENAILDS-PSVKEAAVIG 473
Cdd:cd05933 442 RIKELIItAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-538 |
2.65e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 94.56 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 25 ATVFGEQEVVYRnsdgswgrsnyadEFKRMA-QLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGLA-----ATMLQ 98
Cdd:PRK08279 55 ALLFEDQSISYA-------------ELNARAnRYAHWAAARGVGKGDVVALL---MENRPEYLAAWLGLAklgavVALLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 99 LNLRLAPedLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKG--WVVMTDkpadeietTLENVVFYEDLI-------KD 169
Cdd:PRK08279 119 TQQRGAV--LAHSLNLVDAKHLIVGEELVEAFEEARADLARPPrlWVAGGD--------TLDDPEGYEDLAaaaagapTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 170 KPDTYDwPVVDEKTAAYAgYTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGAsfDDTIMPITPMFH----VLSWGfpqN 243
Cdd:PRK08279 189 NPASRS-GVTAKDTAFYI-YTSGTTGLPKAAVMSHMRWlkAMGGFGGLLRLTP--DDVLYCCLPLYHntggTVAWS---S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 244 AVAAGAKLVLPGKFAAEEFGAIAkafIAEKVT-----------LANgapaifapmlammkdmpQPPDLS----GVRLVSG 308
Cdd:PRK08279 262 VLAAGATLALRRKFSASRFWDDV---RRYRATafqyigelcryLLN-----------------QPPKPTdrdhRLRLMIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 309 SSepplsmMRG-----FKEITG-ADVIHGYGATETTpLATTNWHIKPG----LDMDEEERWDFKRY---QGLPVIGVE-- 373
Cdd:PRK08279 322 NG------LRPdiwdeFQQRFGiPRILEFYAASEGN-VGFINVFNFDGtvgrVPLWLAHPYAIVKYdvdTGEPVRDADgr 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 374 -VKVvdPTGEElprdGKSMGEVLMRGPWitESYFQlPDNSER------FLDG--WWRSGDVGVIFPNGYLKLTDRLKDVI 444
Cdd:PRK08279 395 cIKV--KPGEV----GLLIGRITDRGPF--DGYTD-PEASEKkilrdvFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 445 KSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERP-VAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDEL 523
Cdd:PRK08279 466 RWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAgMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPEL 545
|
570
....*....|....*
gi 1949187543 524 PRTSVGKLDKKLLRK 538
Cdd:PRK08279 546 ETTGTFKYRKVDLRK 560
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
332-538 |
5.24e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 92.75 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 332 YGATETTPLATTnwhIKPgldmdeEERWDFKRYQGLPVIGVEVKVVDPTGEELPRDGKSmgevLMRGpwiteSYFQLPDN 411
Cdd:PRK07445 261 YGMTETASQIAT---LKP------DDFLAGNNSSGQVLPHAQITIPANQTGNITIQAQS----LALG-----YYPQILDS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 412 SERFLdgwwrSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAED 491
Cdd:PRK07445 323 QGIFE-----TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKD 397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1949187543 492 GaEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK07445 398 P-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
189-538 |
9.97e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 92.90 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVyyshrsiyLHTMGGLAaLGAS------FD----DT------IMPIT--------PMfhvlswgfpqna 244
Cdd:PRK00174 252 YTSGSTGKPKGV--------LHTTGGYL-VYAAmtmkyvFDykdgDVywctadVGWVTghsyivygPL------------ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 245 vAAGAKLVL---------PGKFAAeefgAIAKafiaEKVTlangapaIF--APML--AMMKDMPQPP---DLSGVRLVSG 308
Cdd:PRK00174 311 -ANGATTLMfegvpnypdPGRFWE----VIDK----HKVT-------IFytAPTAirALMKEGDEHPkkyDLSSLRLLGS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 309 SSEP--PLSMMRGFKEItGAD---VIHGYGATET-----TPL--ATtnwHIKPGLDMdeeerwdfkryqgLPVIGVEVKV 376
Cdd:PRK00174 375 VGEPinPEAWEWYYKVV-GGErcpIVDTWWQTETggimiTPLpgAT---PLKPGSAT-------------RPLPGIQPAV 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 377 VDPTGEELPRDGK----------SMgevlMRGPWitesyfqlpDNSERFLDGWWR-------SGDVGVIFPNGYLKLTDR 439
Cdd:PRK00174 438 VDEEGNPLEGGEGgnlvikdpwpGM----MRTIY---------GDHERFVKTYFStfkgmyfTGDGARRDEDGYYWITGR 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 440 LKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRETIVEV-------LGDrFAKwq 512
Cdd:PRK00174 505 VDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELrnwvrkeIGP-IAK-- 581
|
410 420
....*....|....*....|....*.
gi 1949187543 513 lPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PRK00174 582 -PDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
178-538 |
1.76e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 88.01 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAA----YAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPIT-PMFHVLSWGFPQNAVAAGAKLV 252
Cdd:cd05974 77 AVDENTHAddpmLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISsPGWAKHAWSCFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LpgkFAAEEFGAiaKAFIAEKVTLanGAPAIFAP--MLAMMKDMPQPPDLSGVRLVSGSSEP--PlSMMRGFKEITGADV 328
Cdd:cd05974 157 L---FNYARFDA--KRVLAALVRY--GVTTLCAPptVWRMLIQQDLASFDVKLREVVGAGEPlnP-EVIEQVRRAWGLTI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLA--TTNWHIKPGldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPR--------DGKSMGevLMRG 398
Cdd:cd05974 229 RDGYGQTETTALVgnSPGQPVKAG-------------SMGRPLPGYRVALLDPDGAPATEgevaldlgDTRPVG--LMKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 399 pwitesYFQLPDN-SERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDE 477
Cdd:cd05974 294 ------YAGDPDKtAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDP 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 478 KWQERPVAYVVAEDGAEVTRET---IVEVLGDRFAKWQLPDEIIVTdELPRTSVGKLDKKLLRK 538
Cdd:cd05974 368 VRLSVPKAFIVLRAGYEPSPETaleIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
161-538 |
2.38e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 88.42 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 161 VFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVyyshrsiyLHTMGGLAALGAS-----FDDTIMPITPMFHV 235
Cdd:PLN02654 254 VWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGV--------LHTTGGYMVYTATtfkyaFDYKPTDVYWCTAD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 236 LSWGFPQNAVAAGAKL------VLPGKFAAEEFGAIAKAFIAEKVTLANGAPAIfapMLAMMKDMPQPP---DLSGVRLV 306
Cdd:PLN02654 326 CGWITGHSYVTYGPMLngatvlVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTL---VRSLMRDGDEYVtrhSRKSLRVL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 307 SGSSEP--PlSMMRGFKEITG---ADVIHGYGATET-----TPLATTnWHIKPGldmdeeerwdfkrYQGLPVIGVEVKV 376
Cdd:PLN02654 403 GSVGEPinP-SAWRWFFNVVGdsrCPISDTWWQTETggfmiTPLPGA-WPQKPG-------------SATFPFFGVQPVI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 377 VDPTGEELprDGKSMGEVLMRGPWiTESYFQLPDNSERF-------LDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGE 449
Cdd:PLN02654 468 VDEKGKEI--EGECSGYLCVKKSW-PGAFRTLYGDHERYettyfkpFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 450 WISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT---RETIVEVLGDRFAKWQLPDEIIVTDELPRT 526
Cdd:PLN02654 545 RIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeelRKSLILTVRNQIGAFAAPDKIHWAPGLPKT 624
|
410
....*....|..
gi 1949187543 527 SVGKLDKKLLRK 538
Cdd:PLN02654 625 RSGKIMRRILRK 636
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
27-473 |
7.85e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 87.00 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 27 VFGEQEVvyrnSDGSWGR---SNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRL 103
Cdd:PLN02614 63 MLGRREI----VDGKPGKyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 104 APEDLAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKGWVVMT---DKPADEIETTLENVVFY---EDLIKDKPDTYDWP 177
Cdd:PLN02614 139 GAGAVEFIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSfggVSREQKEEAETFGLVIYawdEFLKLGEGKQYDLP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGA-----SFDDTIMPITPMFHVLSWGFPQNAVAAGA--- 249
Cdd:PLN02614 219 IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanaalTVKDVYLSYLPLAHIFDRVIEECFIQHGAaig 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 ------KLVLP--GKFAAEEFGAIAK----------------AFIAEKV----------TLANGAPAIFA-PMLAMMKDM 294
Cdd:PLN02614 299 fwrgdvKLLIEdlGELKPTIFCAVPRvldrvysglqkklsdgGFLKKFVfdsafsykfgNMKKGQSHVEAsPLCDKLVFN 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 295 PQPPDLSG-VRLVSGSSEPPLSMMRGFKEITGA-DVIHGYGATETTplATTNWHIKPGLDMdeeerwdfkryqgLPVIGV 372
Cdd:PLN02614 379 KVKQGLGGnVRIILSGAAPLASHVESFLRVVACcHVLQGYGLTESC--AGTFVSLPDELDM-------------LGTVGP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 373 EVKVVDPTGEELPR------DGKSMGEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIK 445
Cdd:PLN02614 444 PVPNVDIRLESVPEmeydalASTPRGEICIRGKTLFSGYYKREDlTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
490 500
....*....|....*....|....*....
gi 1949187543 446 -SGGEWISSIDMENAILDSPSVKEAAVIG 473
Cdd:PLN02614 524 lSQGEYVAVENIENIYGEVQAVDSVWVYG 552
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
47-473 |
1.36e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 86.31 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVL-----DW---NSRRHFELYFAVPgLAATmlqlnlrLAPEDLAYVVSHSKSD 118
Cdd:PLN02736 81 YGEAGTARTAIGSGLVQHGIPKGACVGLYfinrpEWlivDHACSAYSYVSVP-LYDT-------LGPDAVKFIVNHAEVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 119 WIFVDESLLPVAEALAPKL-DVKGWVVM--TDKPADEIETTLE-NVVFYEDLI---KDKPDTYDWPVVDEktAAYAGYTT 191
Cdd:PLN02736 153 AIFCVPQTLNTLLSCLSEIpSVRLIVVVggADEPLPSLPSGTGvEIVTYSKLLaqgRSSPQPFRPPKPED--VATICYTS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 192 GTTGRPKGVYYSHRSIYLHTMGglAALGASF--DDTIMPITPMFHV-------------LSWGFPQ-------------- 242
Cdd:PLN02736 231 GTTGTPKGVVLTHGNLIANVAG--SSLSTKFypSDVHISYLPLAHIyervnqivmlhygVAVGFYQgdnlklmddlaalr 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 243 -----------NAVAAGAKL-VLPGKFAAEEFGAIAkaFIAEKVTLANGAPAifAPM-----LAMMKDmpqppDLSG-VR 304
Cdd:PLN02736 309 ptifcsvprlyNRIYDGITNaVKESGGLKERLFNAA--YNAKKQALENGKNP--SPMwdrlvFNKIKA-----KLGGrVR 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 305 L-VSGSSepPLS--MMRGFKEITGADVIHGYGATETTPLATTnwhikpgldMDEEERwdFKRYQGLPVIGVEVKVVD-P- 379
Cdd:PLN02736 380 FmSSGAS--PLSpdVMEFLRICFGGRVLEGYGMTETSCVISG---------MDEGDN--LSGHVGSPNPACEVKLVDvPe 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 380 ---TGEE--LPRdgksmGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWI 451
Cdd:PLN02736 447 mnyTSEDqpYPR-----GEICVRGPIIFKGYYKDEVQTREVIDedGWLHTGDIGLWLPGGRLKIIDRKKNIFKlAQGEYI 521
|
490 500
....*....|....*....|..
gi 1949187543 452 SSIDMENAILDSPSVKEAAVIG 473
Cdd:PLN02736 522 APEKIENVYAKCKFVAQCFVYG 543
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
189-504 |
1.51e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 85.72 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSiyLHTMggLAALGASF----DDTIMPITPMFHVLSwgfpqnaVAAGAKLVLP----GKFA-- 258
Cdd:PRK09274 181 FTSGSTGTPKGVVYTHGM--FEAQ--IEALREDYgiepGEIDLPTFPLFALFG-------PALGMTSVIPdmdpTRPAtv 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 259 --AEEFGAIAKafiaEKVTLANGAPAIFAPMLAMMKDMPQPpdLSGVRLV-SGSSEPPLSMMRGFKEI--TGADVIHGYG 333
Cdd:PRK09274 250 dpAKLFAAIER----YGVTNLFGSPALLERLGRYGEANGIK--LPSLRRViSAGAPVPIAVIERFRAMlpPDAEILTPYG 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 334 ATETTPLATtnwhikpgLDMDEE-----ERWDfkryQ------GLPVIGVEVKVVDPTGE---------ELPRDGksMGE 393
Cdd:PRK09274 324 ATEALPISS--------IESREIlfatrAATD----NgagicvGRPVDGVEVRIIAISDApipewddalRLATGE--IGE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 394 VLMRGPWITESYFQLPDNSE--RFLDG----WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEnAILDS-PSV 466
Cdd:PRK09274 390 IVVAGPMVTRSYYNRPEATRlaKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNThPGV 468
|
330 340 350
....*....|....*....|....*....|....*...
gi 1949187543 467 KEAAVIGVPdEKWQERPVAYVVAEDGAEVTRETIVEVL 504
Cdd:PRK09274 469 KRSALVGVG-VPGAQRPVLCVELEPGVACSKSALYQEL 505
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
47-473 |
2.30e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 85.64 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESl 126
Cdd:PLN02430 79 YKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 lPVAEALAPKLD----VKGWVVMTDKPADEIETTLE---NVVFYEDLI---KDKP-DTYDWPVVDEKTAAYagyTTGTTG 195
Cdd:PLN02430 158 -KIKELLEPDCKsakrLKAIVSFTSVTEEESDKASQigvKTYSWIDFLhmgKENPsETNPPKPLDICTIMY---TSGTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 196 RPKGVYYSHRSIYLHTMGGLAAL-----GASFDDTIMPITPMFHVL-------------SWGFPQ---NAVA-------- 246
Cdd:PLN02430 234 DPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHILdrmieeyffrkgaSVGYYHgdlNALRddlmelkp 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 247 ---AGAKLVLPG-----KFAAEE--------FGAIAK---AFIAEKVTLANGAPaiFAPMLAMMKDMPQppdLSG-VRL- 305
Cdd:PLN02430 314 tllAGVPRVFERihegiQKALQElnprrrliFNALYKyklAWMNRGYSHKKASP--MADFLAFRKVKAK---LGGrLRLl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 306 VSGSSepPLSM-MRGFKEITG-ADVIHGYGATETTPLATTNWhikPgldmDEEERwdfkryqgLPVIGVEVKVVDPTGEE 383
Cdd:PLN02430 389 ISGGA--PLSTeIEEFLRVTScAFVVQGYGLTETLGPTTLGF---P----DEMCM--------LGTVGAPAVYNELRLEE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 384 LPRDG------KSMGEVLMRGPWITESYFQLPDNSERFL-DGWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSID 455
Cdd:PLN02430 452 VPEMGydplgePPRGEICVRGKCLFSGYYKNPELTEEVMkDGWFHTGDIGEILPNGVLKIIDRKKNLIKlSQGEYVALEY 531
|
490
....*....|....*...
gi 1949187543 456 MENAILDSPSVKEAAVIG 473
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYG 549
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
156-536 |
2.32e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 84.95 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 156 TLENVVfyEDLIKDKPDTYDWPVVDEKTAaYAGYTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGA----------SFD 223
Cdd:PRK04813 120 TLDELK--DIFATGNPYDFDHAVKGDDNY-YIIFTSGTTGKPKGVQISHDNLvsFTNWMLEDFALPEgpqflnqapySFD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 224 DTIMPITPmfhvlswgfpqnAVAAGAKLVLPGKFAAEEFGAIAKAFIAEKVTLANGAPAiFAPMLAMMKDMPQP--PDLS 301
Cdd:PRK04813 197 LSVMDLYP------------TLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPS-FADMCLLDPSFNEEhlPNLT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 302 gVRLVSGSsEPPLSMMRGFKE-ITGADVIHGYGATETTpLATTNWHIKPglDMdeeerwdFKRYQGLPvIGV-----EVK 375
Cdd:PRK04813 264 -HFLFCGE-ELPHKTAKKLLErFPSATIYNTYGPTEAT-VAVTSIEITD--EM-------LDQYKRLP-IGYakpdsPLL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 376 VVDPTGEELPRDGKsmGEVLMRGPWITESYFQLPDNSER---FLDGWW--RSGDVGViFPNGYLKLTDRLKDVIKSGGEW 450
Cdd:PRK04813 331 IIDEEGTKLPDGEQ--GEIVISGPSVSKGYLNNPEKTAEaffTFDGQPayHTGDAGY-LEDGLLFYQGRIDFQIKLNGYR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 451 ISSIDMENAILDSPSVKEAAVIGV-PDEKWQERpVAYVVAEDGaEVTRE-----TIVEVLGDRFAKWQLPDEIIVTDELP 524
Cdd:PRK04813 408 IELEEIEQNLRQSSYVESAVVVPYnKDHKVQYL-IAYVVPKEE-DFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLP 485
|
410
....*....|..
gi 1949187543 525 RTSVGKLDKKLL 536
Cdd:PRK04813 486 LTPNGKIDRKAL 497
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
185-544 |
2.47e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.85 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHVLSW-GFPQNAVAAGAK-LVLPGKFAAEEF 262
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLiAFHLAPLIAGMNqYLMPTRLFIRRP 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 GAIAKAFIAEKVTLANGAPAIFAPMLAMMKD-MPQPPDLSGVRLVSGSSEPPLSMMrgFKEITGADVIHG---------Y 332
Cdd:cd05908 189 ILWLKKASEHKATIVSSPNFGYKYFLKTLKPeKANDWDLSSIRMILNGAEPIDYEL--CHEFLDHMSKYGlkrnailpvY 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATE-------------TTPLATTNWHIKPGLDMDEEERWDFKRYQ----GLPVIGVEVKVVDPTGEELPRDgkSMGEVL 395
Cdd:cd05908 267 GLAEasvgaslpkaqspFKTITLGRRHVTHGEPEPEVDKKDSECLTfvevGKPIDETDIRICDEDNKILPDG--YIGHIQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 396 MRGPWITESYFQLPDNSERFL--DGWWRSGDVGVIFpNGYLKLTDRLKDVIKSGGEWISSIDMENAI--LDSPSVKEAAV 471
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFtdDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAeeLEGVELGRVVA 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 472 IGVPDEKW-QERPVAYVV----AEDGAEVTREtiVEVLGDRFAKWQLpDEIIVTDELPRTSVGKLDKKLLRKTWEDAE 544
Cdd:cd05908 424 CGVNNSNTrNEEIFCFIEhrksEDDFYPLGKK--IKKHLNKRGGWQI-NEVLPIRRIPKTTSGKVKRYELAQRYQSGE 498
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
39-473 |
6.64e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 83.94 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 39 DGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHfelyfAVPGLAAtmLQLNLRLAPEDLAY-VVSHS-- 115
Cdd:PRK12582 75 HGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEH-----ALMTLAA--MQAGVPAAPVSPAYsLMSHDha 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 116 ---------KSDWIFVDeSLLPVAEAL-APKLDVKGWVVMTDKPADEIETTLENVVFYedlikdkpdtydwPVVDEKTAA 185
Cdd:PRK12582 148 klkhlfdlvKPRVVFAQ-SGAPFARALaALDLLDVTVVHVTGPGEGIASIAFADLAAT-------------PPTAAVAAA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 186 YAG----------YTTGTTGRPKGVYYSHRSiylhtMGGLAALGAS-FDDTimPITPMFHVLSW-----------GFPQN 243
Cdd:PRK12582 214 IAAitpdtvakylFTSGSTGMPKAVINTQRM-----MCANIAMQEQlRPRE--PDPPPPVSLDWmpwnhtmggnaNFNGL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 244 AVAAGAKLVLPGKFAAEEFGAIAKAF--IAeKVTLANgAPAIFApMLAmmKDMPQPPDL-------------SGVRLVSG 308
Cdd:PRK12582 287 LWGGGTLYIDDGKPLPGMFEETIRNLreIS-PTVYGN-VPAGYA-MLA--EAMEKDDALrrsffknlrlmayGGATLSDD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 309 SSEpplSMMRGFKEITGADV--IHGYGATETTPLaTTNWHikpgldmdeeerWDFKRYQ--GLPVIGVEVKVVdPTGEEL 384
Cdd:PRK12582 362 LYE---RMQALAVRTTGHRIpfYTGYGATETAPT-TTGTH------------WDTERVGliGLPLPGVELKLA-PVGDKY 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 385 prdgksmgEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIF----PNGYLKLTDRLKDVIK-SGGEWISSIDME 457
Cdd:PRK12582 425 --------EVRVKGPNVTPGYHKDPELTAAAFDeeGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKlSTGTWVSVGTLR 496
|
490
....*....|....*...
gi 1949187543 458 NAILD--SPSVKEAAVIG 473
Cdd:PRK12582 497 PDAVAacSPVIHDAVVAG 514
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
44-531 |
7.36e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.51 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 44 RSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRrhfELYFAVPGL-----AATMLQ-----LNLRLAPEDLAYVVS 113
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPV---EIAPTAQGLwmrgaSLTMLHqptprTDLAVWAEDTLRVIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 114 HSKSDWIFVDESLlpvaEALAPKLDVKGWVVMT------DKPADEIETTlenvvfyEDLIkdkpdtydwpvvdektaAYA 187
Cdd:PRK07768 106 MIGAKAVVVGEPF----LAAAPVLEEKGIRVLTvadllaADPIDPVETG-------EDDL-----------------ALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 188 GYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIM-PITPMFHVLSW-GFPQNAVAAGAKLVL--PGKFAAeefG 263
Cdd:PRK07768 158 QLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMvSWLPLFHDMGMvGFLTVPMYFGAELVKvtPMDFLR---D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 264 AIAKAFIAEK----VTLA-NGAPAIFAPMLAMmKDMPQPPDLSGVRLVSGSSEP--PLSMMR--------GFKEitgADV 328
Cdd:PRK07768 235 PLLWAELISKyrgtMTAApNFAYALLARRLRR-QAKPGAFDLSSLRFALNGAEPidPADVEDlldagarfGLRP---EAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTpLATTNWHIKPGLDMDE--------------EERWDFKRYQ--GLPVIGVEVKVVDPTGEELPRdgKSMG 392
Cdd:PRK07768 311 LPAYGMAEAT-LAVSFSPCGAGLVVDEvdadllaalrravpATKGNTRRLAtlGPPLPGLEVRVVDEDGQVLPP--RGVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 393 EVLMRGPWITESYFQ----LPDNSErflDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKE 468
Cdd:PRK07768 388 VIELRGESVTPGYLTmdgfIPAQDA---DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRP 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949187543 469 AAVIGVPDEKWQERPVAYVVAE-----DGAEVTR------ETIVEVLGDRfakwqlPDEIIVTD--ELPRTSVGKL 531
Cdd:PRK07768 465 GNAVAVRLDAGHSREGFAVAVEsnafeDPAEVRRirhqvaHEVVAEVGVR------PRNVVVLGpgSIPKTPSGKL 534
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-527 |
9.90e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 79.43 E-value: 9.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEkTAAYAgYTTGTTGRPKGVYYSHRsiylHTMGGLAALGASFD----DTIMPITPMFHVLSWGFPQNAVAAGAKLV 252
Cdd:cd05910 82 PKADE-PAAIL-FTSGSTGTPKGVVYRHG----TFAAQIDALRQLYGirpgEVDLATFPLFALFGPALGLTSVIPDMDPT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LPGKFAAEE-FGAIAKafiaEKVTLANGAPAIFAPMLAMMKDMPQPpdLSGVRLVSGSSEP-PLSMMRGFKEIT--GADV 328
Cdd:cd05910 156 RPARADPQKlVGAIRQ----YGVSIVFGSPALLERVARYCAQHGIT--LPSLRRVLSAGAPvPIALAARLRKMLsdEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLATTNWHikpglDMDEEERWDFKRYQ----GLPVIGVEVKVVDPTGE---------ELPRDGksMGEVL 395
Cdd:cd05910 230 LTPYGATEALPVSSIGSR-----ELLATTTAATSGGAgtcvGRPIPGVRVRIIEIDDEpiaewddtlELPRGE--IGEIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 396 MRGPWITESYF---------QLPDNSERFldgWWRSGDVgvifpnGYLKLTDRL-------KDVIKSGGEwISSIDMENA 459
Cdd:cd05910 303 VTGPTVTPTYVnrpvatalaKIDDNSEGF---WHRMGDL------GYLDDEGRLwfcgrkaHRVITTGGT-LYTEPVERV 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949187543 460 ILDSPSVKEAAVIGVpDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWqlPDEIIVTDELPRTS 527
Cdd:cd05910 373 FNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY--PHTQRIGRFLIHPS 437
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
185-536 |
2.02e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 78.37 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSI-----YLHTMGGLAA-------LGASFDDTIMPITPmfhvlswgfpqnAVAAGAKLV 252
Cdd:cd17645 107 AYVIYTSGSTGLPKGVMIEHHNLvnlceWHRPYFGVTPadkslvyASFSFDASAWEIFP------------HLTAGAALH 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 LPGKFAAEEFGAIAKAFIAEKVTLAngapaiFAPMLAMMKDMpQPPDLSGVRLVSGSSEPPLSMMRGFKeitgadVIHGY 332
Cdd:cd17645 175 VVPSERRLDLDALNDYFNQEGITIS------FLPTGAAEQFM-QLDNQSLRVLLTGGDKLKKIERKGYK------LVNNY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 333 GATETTPLATTnwhikpgLDMDEEERwdfKRYQGLPVIGVEVKVVDpTGEELPRDGKSmGEVLMRGPWITESYFQLPD-N 411
Cdd:cd17645 242 GPTENTVVATS-------FEIDKPYA---NIPIGKPIDNTRVYILD-EALQLQPIGVA-GELCIAGEGLARGYLNRPElT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 412 SERFL-------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPV 484
Cdd:cd17645 310 AEKFIvhpfvpgERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 485 AYVVAEDgaEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17645 390 AYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
366-540 |
2.20e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 78.89 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 366 GLPVIGVEVKVVDPTGEELPRdgKSMGEVLMRGPWITESYFQLPDnSERFL--DGWWRSGDVGVIFpNGYLKLTDRLKDV 443
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPE--RVVGHICVRGPSLMSGYFRDEE-SQDVLaaDGWLDTGDLGYLL-DGYLYITGRAKDL 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 444 IKSGGEWISSIDMENAILDSPSVK--EAAVIGVPDEKwQERPVAYVVAEDGAEVTRETIVEVLGDRF-AKWQLPDEIIVT 520
Cdd:PRK09192 464 IIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELV 542
|
170 180
....*....|....*....|..
gi 1949187543 521 --DELPRTSVGKLDKKLLRKTW 540
Cdd:PRK09192 543 ppHSLPRTSSGKLSRAKAKKRY 564
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
53-514 |
2.92e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 77.99 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 53 RMAQLAHGLTELGVGAGSMVGVLDWNsrrHFELYFAVpgLAAtmLQLNLRLAPedlayvvshsksdwifvdesllpvaea 132
Cdd:PRK09029 37 RIDQLAAGFAQQGVVEGSGVALRGKN---SPETLLAY--LAL--LQCGARVLP--------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 133 LAPKLdvkgwvvmtdkPADEIETTLE--NVVFYEDLIKDK-PDTYDWPVVDEKTAAYAG-----------YTTGTTGRPK 198
Cdd:PRK09029 83 LNPQL-----------PQPLLEELLPslTLDFALVLEGENtFSALTSLHLQLVEGAHAVawqpqrlatmtLTSGSTGLPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 199 GVYYSHRSiYLHTMGGLAALgasfddtiMPIT---------PMFHVlS-------WgfpqnaVAAGAKLVLPGKFAAEEf 262
Cdd:PRK09029 152 AAVHTAQA-HLASAEGVLSL--------MPFTaqdswllslPLFHV-SgqgivwrW------LYAGATLVVRDKQPLEQ- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 gAIAKafiaekVTLANGAPAifapMLAMMKDMPQPP-DLSGVrLVSGSSEPPlsmmrgfkEITGADV---IH---GYGAT 335
Cdd:PRK09029 215 -ALAG------CTHASLVPT----QLWRLLDNRSEPlSLKAV-LLGGAAIPV--------ELTEQAEqqgIRcwcGYGLT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 336 EttpLATTNWhIKpgldmdeeeRWDFKRYQGLPVIGVEVKVVDptgeelprdgksmGEVLMRGPWITESYFQ------LP 409
Cdd:PRK09029 275 E---MASTVC-AK---------RADGLAGVGSPLPGREVKLVD-------------GEIWLRGASLALGYWRqgqlvpLV 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 410 DNserflDGWWRSGDVGvIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVA 489
Cdd:PRK09029 329 ND-----EGWFATRDRG-EWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVES 402
|
490 500
....*....|....*....|....*
gi 1949187543 490 EDGAEVtrETIVEVLGDRFAKWQLP 514
Cdd:PRK09029 403 DSEAAV--VNLAEWLQDKLARFQQP 425
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
179-478 |
1.23e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 179 VDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHvlSWGFpqNAVAAGAKLV-LPGKF 257
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFH--AYGF--NSCTLFPLLSgVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 258 AAEEFGA--IAKAFIAEKVTLANGAPAIFAPMLAMMKDmpQPPDLSGVRLVSGSSEPPLSMMRGFKEITGADVI--HGYG 333
Cdd:PRK06334 256 AYNPLYPkkIVEMIDEAKVTFLGSTPVFFDYILKTAKK--QESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQlrQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 334 ATETTPLATTNwhikpgldmdEEERWDFKRYQGLPVIGVEVKVVDptgEE--LPRDGKSMGEVLMRGPWITESYFQlPDN 411
Cdd:PRK06334 334 TTECSPVITIN----------TVNSPKHESCVGMPIRGMDVLIVS---EEtkVPVSSGETGLVLTRGTSLFSGYLG-EDF 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187543 412 SERFL----DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAIL------DSPSVKEAAVIGVPDEK 478
Cdd:PRK06334 400 GQGFVelggETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfgqnAADHAGPLVVCGLPGEK 476
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
189-543 |
1.46e-14 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.93 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFHvlSWGFPQNAV---AAGAKLVL---PGKFAaeef 262
Cdd:PRK06814 800 FTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFH--SFGLTGGLVlplLSGVKVFLypsPLHYR---- 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 263 gaiakafIAEKVTLANGAPAIFAP--MLAMMKDMPQPPDLSGVRLVSGSSEPPLSMMRGF-KEITGADVIHGYGATETTP 339
Cdd:PRK06814 874 -------IIPELIYDTNATILFGTdtFLNGYARYAHPYDFRSLRYVFAGAEKVKEETRQTwMEKFGIRILEGYGVTETAP 946
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 340 L--ATTNWHIKPG----LdmdeeerwdfkryqgLPviGVEVKVVDPTGEElprDGksmGEVLMRGPWITESYFqLPDNS- 412
Cdd:PRK06814 947 ViaLNTPMHNKAGtvgrL---------------LP--GIEYRLEPVPGID---EG---GRLFVRGPNVMLGYL-RAENPg 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 413 --ERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAIL----DSPSvkeaAVIGVPDEKWQERPVAY 486
Cdd:PRK06814 1003 vlEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAelwpDALH----AAVSIPDARKGERIILL 1078
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 487 VVAEDGaevTRETIVevlgdRFAKWQ------LPDEIIVTDELPRTSVGKLDKKLLRKTWEDA 543
Cdd:PRK06814 1079 TTASDA---TRAAFL-----AHAKAAgaselmVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
36-512 |
2.45e-14 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 75.55 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 36 RNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAV--PGLAATMLQLNLRLAPED---LAY 110
Cdd:cd05921 17 REGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAmyAGVPAAPVSPAYSLMSQDlakLKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 111 VVSHSKSDWIFVDESLlPVAEAL-APKLDVKGWVVMTDKPADEIETTLENVVFYEDLIKDKPDtydWPVVDEKTAAYAGY 189
Cdd:cd05921 97 LFELLKPGLVFAQDAA-PFARALaAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAA---FAAVGPDTVAKFLF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 190 TTGTTGRPKGVYYSHRSIYLHTMGgLAALGASFDDTImPItpmfhVLSWgFPQNAVAAGAK---LVL---------PGKF 257
Cdd:cd05921 173 TSGSTGLPKAVINTQRMLCANQAM-LEQTYPFFGEEP-PV-----LVDW-LPWNHTFGGNHnfnLVLynggtlyidDGKP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 258 AAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMP--QPPDLSGVRLV--SGSSEPPlSMMRGFKEITGADVIH--- 330
Cdd:cd05921 245 MPGGFEETLRNLREISPTVYFNVPAGWEMLVAALEKDEalRRRFFKRLKLMfyAGAGLSQ-DVWDRLQALAVATVGErip 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 331 ---GYGATETTPLAT-TNWHI-KPGldmdeeerwdfkrYQGLPVIGVEVKVVdptgeelPRDGKSmgEVLMRGPWITESY 405
Cdd:cd05921 324 mmaGLGATETAPTATfTHWPTeRSG-------------LIGLPAPGTELKLV-------PSGGKY--EVRVKGPNVTPGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 406 FQLPDNSERFLD--GWWRSGDvGVIF-----PNGYLKLTDRLKDVIK-SGGEWISSIDMENAILD--SPSVKEAAVIG-- 473
Cdd:cd05921 382 WRQPELTAQAFDeeGFYCLGD-AAKLadpddPAKGLVFDGRVAEDFKlASGTWVSVGPLRARAVAacAPLVHDAVVAGed 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1949187543 474 --------VPDEKWQERPVAYVVAEDGAEVTRETIVEVLGDRFAKWQ 512
Cdd:cd05921 461 raevgalvFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAALN 507
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
178-538 |
2.88e-14 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 75.08 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 178 VVDekTAAYAgYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH----VLSWGfpqNAVAAGAKLVL 253
Cdd:cd05940 80 VVD--AALYI-YTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHstalIVGWS---ACLASGATLVI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 254 PGKFAAEEFGaiaKAFIAEKVTlangapaIF---APMLAMMKDMPQPPDLSG--VRLVSGSSEPPlSMMRGFKEITG-AD 327
Cdd:cd05940 154 RKKFSASNFW---DDIRKYQAT-------IFqyiGELCRYLLNQPPKPTERKhkVRMIFGNGLRP-DIWEEFKERFGvPR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 VIHGYGATETTpLATTNWHIKPGLdmdeeerWDFKRYQGLPVIGVEVKVVDPTGEELPRD-------------GKSMGEV 394
Cdd:cd05940 223 IAEFYAATEGN-SGFINFFGKPGA-------IGRNPSLLRKVAPLALVKYDLESGEPIRDaegrcikvprgepGLLISRI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 395 LMRGPWitESYFQLPDNSERFL-------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVK 467
Cdd:cd05940 295 NPLEPF--DGYTDPAATEKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 468 EAAVIGVPDEKWQERP-VAYVVAEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05940 373 EANVYGVQVPGTDGRAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-536 |
6.37e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.20 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELyfaVPGLAATM------LQLNLRLAPEDLAYVVSHSKSDWI 120
Cdd:PRK05691 2216 YAELDARANRLARALRERGVGPQVRVGLA---LERSLEM---VVGLLAILkaggayVPLDPEYPLERLHYMIEDSGIGLL 2289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 121 FVDESLLpvaEALAPKLD-VKGWVVMTDKPAdeiettlenVVFYEDlikDKPDTYDWPvvdeKTAAYAGYTTGTTGRPKG 199
Cdd:PRK05691 2290 LSDRALF---EALGELPAgVARWCLEDDAAA---------LAAYSD---APLPFLSLP----QHQAYLIYTSGSTGKPKG 2350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 200 VYYSHRSIYLHTMGGLAALGASFDDTIMpitpmfHVLSWGFPQN------AVAAGAKLVL--PGKFAAEEfgaIAKAFIA 271
Cdd:PRK05691 2351 VVVSHGEIAMHCQAVIERFGMRADDCEL------HFYSINFDAAserllvPLLCGARVVLraQGQWGAEE---ICQLIRE 2421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 272 EKVTLANGAPAiFAPMLA--MMKDMPQPPdlsgVRLV--SGSSEPPLSMMRGFKEITGADVIHGYGATETT--PLATtnw 345
Cdd:PRK05691 2422 QQVSILGFTPS-YGSQLAqwLAGQGEQLP----VRMCitGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVvmPLAC--- 2493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 346 hikPGLDMDEEERwdfkryQGLP---VIGVEVK-VVDPTGEELPRDGksMGEVLMRGPWITESYFQLPDNS-ERFL---- 416
Cdd:PRK05691 2494 ---LAPEQLEEGA------ASVPigrVVGARVAyILDADLALVPQGA--TGELYVGGAGLAQGYHDRPGLTaERFVadpf 2562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 417 --DG--WWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVpDEKWQERPVAYVVAE-- 490
Cdd:PRK05691 2563 aaDGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAva 2641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 491 DGAEVTRETIVEVLGDRfAKWQLPD-----EIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK05691 2642 GQDDEAQAALREALKAH-LKQQLPDymvpaHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
31-536 |
1.42e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.12 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 31 QEVVYRNSDGSWGRSnYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAY 110
Cdd:PRK05857 29 EAIALRRCDGTSALR-YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 111 VVSHSKSDWIFVDESLLPVAEALAPKLdvkgwvvmTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVDEKTAAYagYT 190
Cdd:PRK05857 108 FCQITDPAAALVAPGSKMASSAVPEAL--------HSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMI--FT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 191 TGTTGRPKGVYYSHRSIY----LHTMGGLAALGASFDDTIMPITPMFHVLSWGFPQNAVAAGAKLVLPGkfaaEEFGAIA 266
Cdd:PRK05857 178 SGTTGEPKAVLLANRTFFavpdILQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGG----ENTTSLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 267 KAFIAEKVTLANGAPAIFAPMLAMMK--DMPQPPdlsgVRLVS-GSSEPPLSMMRgFKEITGADVIHGYGATETTPLATT 343
Cdd:PRK05857 254 EILTTNAVATTCLVPTLLSKLVSELKsaNATVPS----LRLVGyGGSRAIAADVR-FIEATGVRTAQVYGLSETGCTALC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 344 nwhikpgLDMDEEErwdFKRYQ----GLPVIGVEVKVVDPTGEELPRDG----KSMGEVLMRGPWITESYFQLPDNSERF 415
Cdd:PRK05857 329 -------LPTDDGS---IVKIEagavGRPYPGVDVYLAATDGIGPTAPGagpsASFGTLWIKSPANMLGYWNNPERTAEV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 416 L-DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVA----- 489
Cdd:PRK05857 399 LiDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVAsaeld 478
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1949187543 490 EDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK05857 479 ESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
50-538 |
1.61e-13 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 72.85 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 50 EFKRMA-QLAHGL-TELGVGAGSMVGVLDWNSRRHFELYFAVP--GLAATMLQLNLRLAPedLAYVVSHSKSDWIFVDEs 125
Cdd:cd05937 10 ETYDLVlRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWsiGAAPAFINYNLSGDP--LIHCLKLSGSRFVIVDP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 llpvaealapkldvkgwvvmtDKPADEIettlenvvfyedlikdkpdtydwpvvdektaayagYTTGTTGRPKGVYYSHR 205
Cdd:cd05937 87 ---------------------DDPAILI-----------------------------------YTSGTTGLPKAAAISWR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 206 SIYLHTMGGLAALGASFDDTIMPITPMFH--VLSWGFpQNAVAAGAKLVLPGKFAAEEF-------GAIAKAFIAEKVTL 276
Cdd:cd05937 111 RTLVTSNLLSHDLNLKNGDRTYTCMPLYHgtAAFLGA-CNCLMSGGTLALSRKFSASQFwkdvrdsGATIIQYVGELCRY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 277 ANGAPaifapmlammkdmPQPPD-LSGVRLVSGSSEPPlSMMRGFKEITGADVIHG-YGATETtPLATTNWHIKP----- 349
Cdd:cd05937 190 LLSTP-------------PSPYDrDHKVRVAWGNGLRP-DIWERFRERFNVPEIGEfYAATEG-VFALTNHNVGDfgaga 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 350 ----GLDMdeeeRWDFkRYQGLPVigvevkVVDPTGEELPRDGKS----------MGEVLMRGPWITESYFQLPDNSE-- 413
Cdd:cd05937 255 ighhGLIR----RWKF-ENQVVLV------KMDPETDDPIRDPKTgfcvrapvgePGEMLGRVPFKNREAFQGYLHNEda 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 414 ---RFL-------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERP 483
Cdd:cd05937 324 tesKLVrdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRA 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 484 VAYVV-----AEDGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05937 404 GCAAItleesSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
186-539 |
7.14e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 71.13 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 186 YAGYTTGTTGRPKGVyysHRSIylhtmGGLA-ALGASFDdTIMPITP---MFHV--LSW--GFPQNAVA---AGAKLV-- 252
Cdd:PRK10524 237 YILYTSGTTGKPKGV---QRDT-----GGYAvALATSMD-TIFGGKAgetFFCAsdIGWvvGHSYIVYApllAGMATImy 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 253 --LPGKFAAEEFGAIAKAFiaeKVTLANGAP-AIfapmlAMMKDmpQPP------DLSGVRLVSGSSEP---PLSmmRGF 320
Cdd:PRK10524 308 egLPTRPDAGIWWRIVEKY---KVNRMFSAPtAI-----RVLKK--QDPallrkhDLSSLRALFLAGEPldePTA--SWI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 321 KEITGADVIHGYGATETT-PLATtnwhIKPGLDMDEEerwdfkRY--QGLPVIGVEVKVVD-PTGEELPRDGKsmGEVLM 396
Cdd:PRK10524 376 SEALGVPVIDNYWQTETGwPILA----IARGVEDRPT------RLgsPGVPMYGYNVKLLNeVTGEPCGPNEK--GVLVI 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 397 RGPwitesyfqLP--------DNSERFLDGWWRS--------GDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAI 460
Cdd:PRK10524 444 EGP--------LPpgcmqtvwGDDDRFVKTYWSLfgrqvystFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESI 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 461 LDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVTRET--------IVEVLGDRFAKWQLPDEIIVTDELPRTSVGkld 532
Cdd:PRK10524 516 SSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlalekeIMALVDSQLGAVARPARVWFVSALPKTRSG--- 592
|
....*..
gi 1949187543 533 kKLLRKT 539
Cdd:PRK10524 593 -KLLRRA 598
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
189-458 |
1.59e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 70.01 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYlhtmGGLAALGASFDDTIMPIT---------PMFHVLS---------------WGFPQN- 243
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLT----AGILALEDRLNDLIGPPEedetycsylPLAHIMEfgvtniflargaligFGSPRTl 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 244 --------------------AV---------AAGAKLVLPGKFAAEEFGaiaKAFIAEKVTLANG--AP----AIFAPML 288
Cdd:PTZ00216 347 tdtfarphgdltefrpvfliGVprifdtikkAVEAKLPPVGSLKRRVFD---HAYQSRLRALKEGkdTPywneKVFSAPR 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 289 AMMKdmpqppdlSGVR-LVSGSSepPLS-MMRGFKEITGADVIHGYGATETTPLATTNwhiKPGlDMDEEErwdfkryQG 366
Cdd:PTZ00216 424 AVLG--------GRVRaMLSGGG--PLSaATQEFVNVVFGMVIQGWGLTETVCCGGIQ---RTG-DLEPNA-------VG 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 367 LPVIGVEVKVVDP-----TGEELPRdgksmGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDR 439
Cdd:PTZ00216 483 QLLKGVEMKLLDTeeykhTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLDedGWFHTGDVGSIAANGTLRIIGR 557
|
330 340
....*....|....*....|
gi 1949187543 440 LKDVIK-SGGEWISsidMEN 458
Cdd:PTZ00216 558 VKALAKnCLGEYIA---LEA 574
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
47-542 |
1.80e-12 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 70.15 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPGL---AATMLQLNLRLAPEDLAYVVSHSKSDWIFVD 123
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNKEERVAIF---ADTRAEWLIALQGCfrqNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 124 ESLLPVAEALAPKLD-VKGWVVMTDKPADEIET-------TLENVVFYEDLIKDKPDTYDWPVVDEktAAYAGYTTGTTG 195
Cdd:PLN02387 186 SKQLKKLIDISSQLEtVKRVIYMDDEGVDSDSSlsgssnwTVSSFSEVEKLGKENPVDPDLPSPND--IAVIMYTSGSTG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 196 RPKGVYYSHRSIyLHTMGGLAAL--GASFDDTIMPITPMFHVLS---------------WGFP------QNAVAAGAK-- 250
Cdd:PLN02387 264 LPKGVMMTHGNI-VATVAGVMTVvpKLGKNDVYLAYLPLAHILElaaesvmaavgaaigYGSPltltdtSNKIKKGTKgd 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 251 --LVLPGKFAA----------------EEFGAIAKAF--IAEKVTL---------ANGAPAIFAPMLAMMKdmpqppdls 301
Cdd:PLN02387 343 asALKPTLMTAvpaildrvrdgvrkkvDAKGGLAKKLfdIAYKRRLaaiegswfgAWGLEKLLWDALVFKK--------- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 302 gVRLVSG-------SSEPPLSM-MRGFKEIT-GADVIHGYGATETTPLAT-TNWhikpglDMDEEERwdfkryQGLPVIG 371
Cdd:PLN02387 414 -IRAVLGgrirfmlSGGAPLSGdTQRFINIClGAPIGQGYGLTETCAGATfSEW------DDTSVGR------VGPPLPC 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 372 VEVKVVD-PTGEELPRDgKSM--GEVLMRGPWITESYFQLPDNS-------ERFLDgWWRSGDVGVIFPNGYLKLTDRLK 441
Cdd:PLN02387 481 CYVKLVSwEEGGYLISD-KPMprGEIVIGGPSVTLGYFKNQEKTdevykvdERGMR-WFYTGDIGQFHPDGCLEIIDRKK 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 442 DVIK-SGGEWISSIDMENAILDSPSVKEAAV-----------IGVPD----EKW-QERPVAYvvaEDGAEVTR--ETIVE 502
Cdd:PLN02387 559 DIVKlQHGEYVSLGKVEAALSVSPYVDNIMVhadpfhsycvaLVVPSqqalEKWaKKAGIDY---SNFAELCEkeEAVKE 635
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1949187543 503 VLGD--------RFAKWQLPDEIIVTDEL--PR----TSVGKLDKKLLRKTWED 542
Cdd:PLN02387 636 VQQSlskaakaaRLEKFEIPAKIKLLPEPwtPEsglvTAALKLKREQIRKKFKD 689
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
184-538 |
7.19e-12 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 67.57 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 AAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGA------------SFDdtiMPITPMFHVLswgfpqnavAAGAKL 251
Cdd:cd05918 108 AAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLtsesrvlqfasyTFD---VSILEIFTTL---------AAGGCL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 252 VLPgkfaAEE--FGAIAKAFIAEKVTLAngapaIFAPMLAMMKDMPQPPDLSgvRLVSGSsEPpLSMmrgfKEIT----G 325
Cdd:cd05918 176 CIP----SEEdrLNDLAGFINRLRVTWA-----FLTPSVARLLDPEDVPSLR--TLVLGG-EA-LTQ----SDVDtwadR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 326 ADVIHGYGATETTPLATTNwHIKPGLDMdeeerwdfkRYQGLPViGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESY 405
Cdd:cd05918 239 VRLINAYGPAECTIAATVS-PVVPSTDP---------RNIGRPL-GATCWVVDPDNHDRLVPIGAVGELLIEGPILARGY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 406 FQLPD-NSERFLDG--WW------------RSGDVGVIFPNGYLKLTDRLKDVIKSGG---EwISSIdmENAILDSPSVK 467
Cdd:cd05918 308 LNDPEkTAAAFIEDpaWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGqrvE-LGEI--EHHLRQSLPGA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 468 EAAVIGV---PDEKWQERPVAYVVAEDG--------------AEVTRETIVEV---LGDRFAKWQLPDEIIVTDELPRTS 527
Cdd:cd05918 385 KEVVVEVvkpKDGSSSPQLVAFVVLDGSssgsgdgdslflepSDEFRALVAELrskLRQRLPSYMVPSVFLPLSHLPLTA 464
|
410
....*....|.
gi 1949187543 528 VGKLDKKLLRK 538
Cdd:cd05918 465 SGKIDRRALRE 475
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
185-536 |
7.39e-12 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 67.50 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIyLHTMGGLAALGASFDDTIMPITPMFHvlswgFPQN------AVAAGAKL------- 251
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLT-----FDPSvveiflSLSSGATLlivptsv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 252 -VLPGKFAAeefgAIAKAFiaeKVTLANGAPAIFAPMLAmmkDMPQPPDLSG-----VRLVSGSSEPPLSMMRGF-KEIT 324
Cdd:cd17654 195 kVLPSKLAD----ILFKRH---RITVLQATPTLFRRFGS---QSIKSTVLSAtsslrVLALGGEPFPSLVILSSWrGKGN 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 325 GADVIHGYGATETTPLATtnWHIKPGLDMDEEerwdfkryQGLPVIGVEVKVVDPTGEElpRDGKSMGEVLMRGpwites 404
Cdd:cd17654 265 RTRIFNIYGITEVSCWAL--AYKVPEEDSPVQ--------LGSPLLGTVIEVRDQNGSE--GTGQVFLGGLNRV------ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 405 YFqLPDNSERFLDGWWRSGDVgVIFPNGYLKLTDRLKDVIKSGGEWIsSIDMENAILDSPSVKEAAVIGVPDekwQERPV 484
Cdd:cd17654 327 CI-LDDEVTVPKGTMRATGDF-VTVKDGELFFLGRKDSQIKRRGKRI-NLDLIQQVIESCLGVESCAVTLSD---QQRLI 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 485 AYVVaedGAEVTRETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17654 401 AFIV---GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
31-536 |
2.45e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 31 QEVVYRNSDGSWgrsNYADEFKRMAQLAHGLTELGVGAGSMVGVLdwnSRRHFELYFAVPG---LAATMLQLNLRLAPED 107
Cdd:PRK05691 3735 QRIAASCLDQQW---SYAELNRAANRLGHALRAAGVGVDQPVALL---AERGLDLLGMIVGsfkAGAGYLPLDPGLPAQR 3808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 108 LAYVVSHSKSDWIFVDESLLPVAEALAPKLDVKG---WVVMTDKPADEIETtlenvvfyedlikDKPDTYDWPvvdeKTA 184
Cdd:PRK05691 3809 LQRIIELSRTPVLVCSAACREQARALLDELGCANrprLLVWEEVQAGEVAS-------------HNPGIYSGP----DNL 3871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 185 AYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPM-FHVLSWGFpqnaVAA---GAKL-VLPGKFAA 259
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQsFDISVWQF----LAAplfGARVeIVPNAIAH 3947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 260 EEFGAIAKAfIAEKVTLANGAPAIFAPMLAMMKDmpqppDLSGVR--LVSGSSEPPLSMMRGFKEITGADVIHGYGATET 337
Cdd:PRK05691 3948 DPQGLLAHV-QAQGITVLESVPSLIQGMLAEDRQ-----ALDGLRwmLPTGEAMPPELARQWLQRYPQIGLVNAYGPAEC 4021
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 338 T--------PLATTNWHIKP-GLDMDEEERWDFKRYQGLPVIGVevkvvdpTGEeLPRDGKSMGEVLMRGPWITESYFqL 408
Cdd:PRK05691 4022 SddvaffrvDLASTRGSYLPiGSPTDNNRLYLLDEALELVPLGA-------VGE-LCVAGTGVGRGYVGDPLRTALAF-V 4092
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 409 PD----NSERFldgwWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAViGVpdekwQERP- 483
Cdd:PRK05691 4093 PHpfgaPGERL----YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AV-----QEGVn 4162
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949187543 484 ----VAYVVAEDGAEVTRETIvevlgDRFAKW---QLPDEII-----VTDELPRTSVGKLDKKLL 536
Cdd:PRK05691 4163 gkhlVGYLVPHQTVLAQGALL-----ERIKQRlraELPDYMVplhwlWLDRLPLNANGKLDRKAL 4222
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
6-424 |
4.39e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 65.29 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 6 PSTLGDsYQLNTTSMIRHAATVFGEQE-VVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFE 84
Cdd:PRK08180 31 AEPLGD-YPRRLTDRLVHWAQEAPDRVfLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 85 LYFA-----VP--------GLAATmlqlnlrlAPEDLAYVVSHSKSDWIFVDESLlPVAEAL-APKLDVKGWVVMTDKPA 150
Cdd:PRK08180 110 LALAamyagVPyapvspaySLVSQ--------DFGKLRHVLELLTPGLVFADDGA-AFARALaAVVPADVEVVAVRGAVP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 151 DEIETTLEnvvfyeDLIkdkpDTYDWPVVDEKTAAYAG-------YTTGTTGRPKGVYYSHRSIYLHtmggLAALGASFD 223
Cdd:PRK08180 181 GRAATPFA------ALL----ATPPTAAVDAAHAAVGPdtiakflFTSGSTGLPKAVINTHRMLCAN----QQMLAQTFP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 224 DtiMPITP--MFHVLSW--GFPQN-----AVAAGAKLVL-PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKd 293
Cdd:PRK08180 247 F--LAEEPpvLVDWLPWnhTFGGNhnlgiVLYNGGTLYIdDGKPTPGGFDETLRNLREISPTVYFNVPKGWEMLVPALE- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 294 mpQPPDL-----SGVRLV--SGSSEPPL---SMMRGFKEITGADV--IHGYGATETTPLAT-TNWHI-KPGldmdeeerw 359
Cdd:PRK08180 324 --RDAALrrrffSRLKLLfyAGAALSQDvwdRLDRVAEATCGERIrmMTGLGMTETAPSATfTTGPLsRAG--------- 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949187543 360 dfkrYQGLPVIGVEVKVVdptgeelPRDGKSmgEVLMRGPWITESYFQLPD-NSERFLD-GWWRSGD 424
Cdd:PRK08180 393 ----NIGLPAPGCEVKLV-------PVGGKL--EVRVKGPNVTPGYWRAPElTAEAFDEeGYYRSGD 446
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
28-262 |
5.06e-11 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 65.01 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 28 FGEQEVVYRNSDGswgRSNyadefkrmaQLAHGL-TELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPE 106
Cdd:cd05938 1 FEGETYTYRDVDR---RSN---------QAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 107 DLAYVVSHSKSDWIFVDESLLPVAEALAPKL---DVKGWVVMTDKPADEIETTLENVvfyeDLIKDKPDTYDWPV-VDEK 182
Cdd:cd05938 69 SLLHCFRCCGAKVLVVAPELQEAVEEVLPALradGVSVWYLSHTSNTEGVISLLDKV----DAASDEPVPASLRAhVTIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 183 TAAYAGYTTGTTGRPKGVYYSHRSIyLHTMGGLAALGASFDDTIMPITPMFHV--LSWGFpQNAVAAGAKLVLPGKFAAE 260
Cdd:cd05938 145 SPALYIYTSGTTGLPKAARISHLRV-LQCSGFLSLCGVTADDVIYITLPLYHSsgFLLGI-GGCIELGATCVLKPKFSAS 222
|
..
gi 1949187543 261 EF 262
Cdd:cd05938 223 QF 224
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
177-545 |
5.12e-11 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 65.17 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 177 PVVDEKTAAYAGyTTGTTGRPKGVYYShRSIYLHTMGGLAA-LGASFD-DTIMPITPMFHVLSWGFPQNAVAAGAKLVLP 254
Cdd:PRK05851 148 PPDSGGPAVLQG-TAGSTGTPRTAILS-PGAVLSNLRGLNArVGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 255 --GKFAAEEFGAIAkaFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEPP--------LSMMRGFKEIT 324
Cdd:PRK05851 226 ptTAFSASPFRWLS--WLSDSRATLTAAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVdcdgferfATAMAPFGFDA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 325 GAdVIHGYGATETTpLATTNWHIKPGLDMDEEERWD---FKRYQ--GLPVIGVEVKVvDPTGEELPRDGKSMGEVLMRGP 399
Cdd:PRK05851 304 GA-AAPSYGLAEST-CAVTVPVPGIGLRVDEVTTDDgsgARRHAvlGNPIPGMEVRI-SPGDGAAGVAGREIGEIEIRGA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 400 WITESYF-QLPDNSerflDGWWRSGDVGViFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEK 478
Cdd:PRK05851 381 SMMSGYLgQAPIDP----DDWFPTGDLGY-LVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGE 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949187543 479 WQERPVAYVVAE----DGAEVTRETIVEVLGDRFAkwqLPDEIIVTD--ELPRTSVGKLDKKLLRKTWEDAEA 545
Cdd:PRK05851 456 GSARPGLVIAAEfrgpDEAGARSEVVQRVASECGV---VPSDVVFVApgSLPRTSSGKLRRLAVKRSLEAADG 525
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-493 |
7.97e-11 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 64.86 E-value: 7.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDESL 126
Cdd:PLN02861 80 YKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 127 LPVAEALAPKL--DVKGWVV---MTDKPADEIETTLENVVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVY 201
Cdd:PLN02861 160 ISSILSCLPKCssNLKTIVSfgdVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 202 YSHRSIYLHTMGGLAAL-----GASFDDTIMPITPMFHVL-------------SWGFPQNAV---AAGAKLVLPGKFAA- 259
Cdd:PLN02861 240 LTNRAIIAEVLSTDHLLkvtdrVATEEDSYFSYLPLAHVYdqvietyciskgaSIGFWQGDIrylMEDVQALKPTIFCGv 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 260 ---------------EEFGAIAKAFI--AEKVTLAN---GAP-AIFAPMLAMMKDMPQPPDLSG-VRLVSGSSEPPLSMM 317
Cdd:PLN02861 320 prvydriytgimqkiSSGGMLRKKLFdfAYNYKLGNlrkGLKqEEASPRLDRLVFDKIKEGLGGrVRLLLSGAAPLPRHV 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 318 RGFKEITGADVI-HGYGATET-----TPLATTnwhikpgldmdeeerwdfkrYQGLPVIGVEVKVVDPTGEELPRDGKSM 391
Cdd:PLN02861 400 EEFLRVTSCSVLsQGYGLTEScggcfTSIANV--------------------FSMVGTVGVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 392 ------GEVLMRGPWITESYFQLPD-NSERFLDGWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDS 463
Cdd:PLN02861 460 lsdvprGEICLRGNTLFSGYHKRQDlTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKlSQGEYVAVENLENTYSRC 539
|
490 500 510
....*....|....*....|....*....|
gi 1949187543 464 PSVKEAAVIGVPDEKWQerpVAYVVAEDGA 493
Cdd:PLN02861 540 PLIASIWVYGNSFESFL---VAVVVPDRQA 566
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
329-538 |
8.36e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 64.76 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 329 IHGYGATETTPLATTNWHIKPgldmdeeerwdfKRYQ--GLPVIGVEVKVVDPTGEELPRDgkSMGEVLMRGP----WIT 402
Cdd:PTZ00237 409 SRGYGQTEIGITYLYCYGHIN------------IPYNatGVPSIFIKPSILSEDGKELNVN--EIGEVAFKLPmppsFAT 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 403 ESYfqlpDNSERF------LDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPD 476
Cdd:PTZ00237 475 TFY----KNDEKFkqlfskFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYD 550
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949187543 477 EKWQERPVAYVVAEDGAEVT-------RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PTZ00237 551 PDCYNVPIGLLVLKQDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
20-530 |
5.75e-10 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 61.90 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 20 MIRHAATvfGEQEVVYRNSDGSWGRSNYADEFKRMAQLAHGLTELGVGAGSMVGVLDWNSRRHFELYFA----------- 88
Cdd:cd05943 76 LLRHADA--DDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLAtasigaiwssc 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 89 -----VPGLAATMLQLNLRLAPEDLAYVVSHSKSDwifVDESLLPVAEALAPKLDVKgwVVMTDKPADEIE-TTLENVVF 162
Cdd:cd05943 154 spdfgVPGVLDRFGQIEPKVLFAVDAYTYNGKRHD---VREKVAELVKGLPSLLAVV--VVPYTVAAGQPDlSKIAKALT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 163 YEDLI---KDKPDTYDWPVVDEKTaaYAGYTTGTTGRPKGVYYSHRSIYL-HtmggLAALGASFD----DTIMPITP--- 231
Cdd:cd05943 229 LEDFLatgAAGELEFEPLPFDHPL--YILYSSGTTGLPKCIVHGAGGTLLqH----LKEHILHCDlrpgDRLFYYTTcgw 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 232 -MfhvlsWGFPQNAVAAGAKLVL-PGKFAAEEFGAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLV--S 307
Cdd:cd05943 303 mM-----WNWLVSGLAVGATIVLyDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTIlsT 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 308 GSSEPPLSMMRGFKEIT----------GADVIHGYGATETTpLATTNWHIK-PGLDMDEEErWDfkrYQGLPVIGVEVKV 376
Cdd:cd05943 378 GSPLKPESFDYVYDHIKpdvllasisgGTDIISCFVGGNPL-LPVYRGEIQcRGLGMAVEA-FD---EEGKPVWGEKGEL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 377 V-------DPTGEELPRDGKSMgevlmrgpwiTESYFqlpdnsERFlDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGE 449
Cdd:cd05943 453 VctkpfpsMPVGFWNDPDGSRY----------RAAYF------AKY-PGVWAHGDWIEITPRGGVVILGRSDGTLNPGGV 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 450 WISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT-------RETIVEVLGDRFakwqLPDEIIVTDE 522
Cdd:cd05943 516 RIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDdelrkriRSTIRSALSPRH----VPAKIIAVPD 591
|
....*...
gi 1949187543 523 LPRTSVGK 530
Cdd:cd05943 592 IPRTLSGK 599
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
172-544 |
7.37e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.11 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 172 DTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHrsiylhtmGGLAA----------LGASFDDTIMPITPMFHV--LSWG 239
Cdd:PRK05691 156 EAWQEPALQPDDIAFLQYTSGSTALPKGVQVSH--------GNLVAneqlirhgfgIDLNPDDVIVSWLPLYHDmgLIGG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 240 FPQnAVAAGAKLVL--PGKFAAEEFGAIAKafIAEKVTLANGAPAiFAPMLA---MMKDMPQPPDLSGVRLVSGSSEP-P 313
Cdd:PRK05691 228 LLQ-PIFSGVPCVLmsPAYFLERPLRWLEA--ISEYGGTISGGPD-FAYRLCserVSESALERLDLSRWRVAYSGSEPiR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 314 LSMMRGFKE------ITGADVIHGYGATETTPLAT--TNWHIKPGLDMDEE--ERWDFKRYQGLPVI-------GVEVKV 376
Cdd:PRK05691 304 QDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSggRRGQGIPALELDAEalARNRAEPGTGSVLMscgrsqpGHAVLI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 377 VDP-TGEELPrDGKsMGEVLMRGPWITESYFQLPDNSERF---LDG--WWRSGDVGVIfPNGYLKLTDRLKDVIKSGGEW 450
Cdd:PRK05691 384 VDPqSLEVLG-DNR-VGEIWASGPSIAHGYWRNPEASAKTfveHDGrtWLRTGDLGFL-RDGELFVTGRLKDMLIVRGHN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 451 ISSIDMENAIldspsvkEAAVigvpDEKWQERPVAYVVAEDG-------AEVTR------------ETIVEVLGDRFAkw 511
Cdd:PRK05691 461 LYPQDIEKTV-------EREV----EVVRKGRVAAFAVNHQGeegigiaAEISRsvqkilppqaliKSIRQAVAEACQ-- 527
|
410 420 430
....*....|....*....|....*....|....*
gi 1949187543 512 QLPDEIIVTD--ELPRTSVGKLDKKLLRKTWEDAE 544
Cdd:PRK05691 528 EAPSVVLLLNpgALPKTSSGKLQRSACRLRLADGS 562
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
173-444 |
1.03e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 61.28 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 173 TYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH---VLSWGFPqnAVAAGA 249
Cdd:PRK07769 171 TWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHdmgLITVLLP--ALLGHY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 250 -KLVLPGKFAAEEFGAIAKafIAEKVTLANG----APAiFAPMLAMMKDMPQ----PPDLSGVRLVSGSSEP-PLSMMRG 319
Cdd:PRK07769 249 iTFMSPAAFVRRPGRWIRE--LARKPGGTGGtfsaAPN-FAFEHAAARGLPKdgepPLDLSNVKGLLNGSEPvSPASMRK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 320 FKEITG-----ADVIH-GYGATETTP-LATTNWHIKPG---LDMDEEERWDFKRY-QGLP---------VIGVE--VKVV 377
Cdd:PRK07769 326 FNEAFApyglpPTAIKpSYGMAEATLfVSTTPMDEEPTviyVDRDELNAGRFVEVpADAPnavaqvsagKVGVSewAVIV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 378 DP-TGEELPrDGkSMGEVLMRGPWITESYFQLPDNSERFL-------------------DGWWRSGDVGVIFpNGYLKLT 437
Cdd:PRK07769 406 DPeTASELP-DG-QIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapddALWVRTGDYGVYF-DGELYIT 482
|
....*..
gi 1949187543 438 DRLKDVI 444
Cdd:PRK07769 483 GRVKDLV 489
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
167-537 |
8.85e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.21 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 167 IKDKPDT----YDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYLHTMGGLAALGAsFDDTIMPIT--PMFH---VLS 237
Cdd:PRK12476 174 IDAIPDSagesFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDL-LDRNTHGVSwlPLYHdmgLSM 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 238 WGFPqnAVAAG-AKLVLPGKFAAEEFGAIaKAFIAEKVT--LANGAPAiFAPMLAMMKDMPQPP---DLSGVRLVSGSSe 311
Cdd:PRK12476 253 IGFP--AVYGGhSTLMSPTAFVRRPQRWI-KALSEGSRTgrVVTAAPN-FAYEWAAQRGLPAEGddiDLSNVVLIIGSE- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 312 pPLSM--MRGFKE------ITGADVIHGYGATETTPLATTnwhIKPGLD-----MDEEErwdFKRYQGLPVIG------V 372
Cdd:PRK12476 328 -PVSIdaVTTFNKafapygLPRTAFKPSYGIAEATLFVAT---IAPDAEpsvvyLDREQ---LGAGRAVRVAAdapnavA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 373 EVK-----------VVDP-TGEELPrDGKsMGEVLMRGPWITESYFQLPDNSE---------RFLDG-----------WW 420
Cdd:PRK12476 401 HVScgqvarsqwavIVDPdTGAELP-DGE-VGEIWLHGDNIGRGYWGRPEETErtfgaklqsRLAEGshadgaaddgtWL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 421 RSGDVGViFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILD-SPSVKE--AAVIGVPDEkwqERPVAYVVAEDGAEVTR 497
Cdd:PRK12476 479 RTGDLGV-YLDGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRgyVTAFTVPAE---DNERLVIVAERAAGTSR 554
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1949187543 498 ---ETIVEVLGDRFAKWQlpdEIIVTD-------ELPRTSVGKLDKKLLR 537
Cdd:PRK12476 555 adpAPAIDAIRAAVSRRH---GLAVADvrlvpagAIPRTTSGKLARRACR 601
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
421-536 |
2.07e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 56.58 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 421 RSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDgaEVTRETI 500
Cdd:PRK08308 294 FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHE--EIDPVQL 371
|
90 100 110
....*....|....*....|....*....|....*.
gi 1949187543 501 VEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK08308 372 REWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
47-499 |
8.27e-08 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 55.15 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 47 YADEFKRMAQLAHGL-TELGVGAGSMVGVLDWNSRRHFELYFAVPGLAATMLQLNLRLAPEDLAYVVSHSKSDWIFVDES 125
Cdd:cd17632 70 YAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 126 LLPVA-EALAPKLDVKGWVVMTDKPADEIETT-LEN----------VVFYEDLIKDK-----PDTYDWPVVDEKTAAYAG 188
Cdd:cd17632 150 HLDLAvEAVLEGGTPPRLVVFDHRPEVDAHRAaLESarerlaavgiPVTTLTLIAVRgrdlpPAPLFRPEPDDDPLALLI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTI-MPITPMFHVLSWGFPQNAVAAGAKlvlpGKFAAE------- 260
Cdd:cd17632 230 YTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASItLNFMPMSHIAGRISLYGTLARGGT----AYFAAAsdmstlf 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 261 ---------EFGAIAKA-------FIAE---KVTLANGAPAIFAPMLAMMKDmpqppDLSGVRL---VSGSSepPLSM-M 317
Cdd:cd17632 306 ddlalvrptELFLVPRVcdmlfqrYQAEldrRSVAGADAETLAERVKAELRE-----RVLGGRLlaaVCGSA--PLSAeM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 318 RGFKEIT-GADVIHGYGATETTPLATTNWHIKPgldmdeeerwdfkryqglPVIgvEVKVVD-P------TGEELPRdgk 389
Cdd:cd17632 379 KAFMESLlDLDLHDGYGSTEAGAVILDGVIVRP------------------PVL--DYKLVDvPelgyfrTDRPHPR--- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 390 smGEVLMRGPWITESYFQLPDNSERFLD--GWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSIDMENAILDSPSV 466
Cdd:cd17632 436 --GELLVKTDTLFPGYYKRPEVTAEVFDedGFYRTGDVMAELGPDRLVYVDRRNNVLKlSQGEFVTVARLEAVFAASPLV 513
|
490 500 510
....*....|....*....|....*....|....*
gi 1949187543 467 KEAAVIGVpdekwQER--PVAYVVAEDGAEVTRET 499
Cdd:cd17632 514 RQIFVYGN-----SERayLLAVVVPTQDALAGEDT 543
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
189-531 |
2.13e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 53.65 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYL-HtmggLAALGASFD----DTIMPITP----MfhvlsWGFPQNAVAAGAKLVL----PG 255
Cdd:PRK03584 270 YSSGTTGLPKCIVHGHGGILLeH----LKELGLHCDlgpgDRFFWYTTcgwmM-----WNWLVSGLLVGATLVLydgsPF 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 --------KFAAEE----FGAIAKaFIAekvtlangapaifapmlAMMKDMPQPP---DLSGVRLVsGSSEPPLS----- 315
Cdd:PRK03584 341 ypdpnvlwDLAAEEgvtvFGTSAK-YLD-----------------ACEKAGLVPGethDLSALRTI-GSTGSPLPpegfd 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 316 -MMRGFKE------ITGA-DVIHGY-GATETTPLattnwhikpgldmdeeerwdfkrYQG---LPVIGVEVKVVDPTGEE 383
Cdd:PRK03584 402 wVYEHVKAdvwlasISGGtDICSCFvGGNPLLPV-----------------------YRGeiqCRGLGMAVEAWDEDGRP 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 384 LpRDGKsmGEVLMRGP--------W-------ITESYFqlpdnsERFlDGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGG 448
Cdd:PRK03584 459 V-VGEV--GELVCTKPfpsmplgfWndpdgsrYRDAYF------DTF-PGVWRHGDWIEITEHGGVVIYGRSDATLNRGG 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 449 EWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT-------RETIVEVLGDRFakwqLPDEIIVTD 521
Cdd:PRK03584 529 VRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDdalrariRTTIRTNLSPRH----VPDKIIAVP 604
|
410
....*....|
gi 1949187543 522 ELPRTSVGKL 531
Cdd:PRK03584 605 DIPRTLSGKK 614
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
189-538 |
6.36e-07 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 52.04 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSIYLHTMGGLAALGASFDDTIMPITPMFH----VLSWGfpqNAVAAGAKLVLPGKFAAEEFga 264
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVG---QALLHGSTVVIRKKFSASNF-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 265 iAKAFIAEKVTLANGAPAIFAPMLAmmkdmpQPPDLS----GVRLVSGSSepplsmMRG--FKEITG----ADVIHGYGA 334
Cdd:cd05939 186 -WDDCVKYNCTIVQYIGEICRYLLA------QPPSEEeqkhNVRLAVGNG------LRPqiWEQFVRrfgiPQIGEFYGA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 335 TE-TTPLATTNWHIKPgldmdeeerWDFKRYQGLPVIGVEVKVVDPTGEELPRD-------------GKSMGEVLMRGPW 400
Cdd:cd05939 253 TEgNSSLVNIDNHVGA---------CGFNSRILPSVYPIRLIKVDEDTGELIRDsdglcipcqpgepGLLVGKIIQNDPL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 401 IT-ESYFQLPDNSERFL-------DGWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVI 472
Cdd:cd05939 324 RRfDGYVNEGATNKKIArdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949187543 473 GVPDEKWQERP-VAYVVaedgaEVTRETIVEVLGDRFAK----WQLPDEIIVTDELPRTSVGKLDKKLLRK 538
Cdd:cd05939 404 GVEVPGVEGRAgMAAIV-----DPERKVDLDRFSAVLAKslppYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
189-536 |
8.59e-07 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 51.75 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 189 YTTGTTGRPKGVYYSHRSI--YLHTMGGLAALGASFDDTIM------PI-----TPMFhvlswgfpqnavaAGAKLVLPg 255
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLayYFPWMAKRFNLSENDKFTMLsgiahdPIqrdmfTPLF-------------LGAQLLVP- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 256 kfAAEEFGAIAKafIAE-----KVTLANGAPAIfapmlammkdmpqppdlsGVRLVSGSSEPPLSMMRGF---KEITGAD 327
Cdd:cd17647 182 --TQDDIGTPGR--LAEwmakyGATVTHLTPAM------------------GQLLTAQATTPFPKLHHAFfvgDILTKRD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 328 ------------VIHGYGATETTplATTNWHIKPGLDMDEEERWDFKRY--QGLPVIGVEVKVV---DPT-----GEelp 385
Cdd:cd17647 240 clrlqtlaenvrIVNMYGTTETQ--RAVSYFEVPSRSSDPTFLKNLKDVmpAGRGMLNVQLLVVnrnDRTqicgiGE--- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 386 rdgksMGEVLMRGPWITESYFQLPD-NSERFLDGW-----------------------------WRSGDVGVIFPNGYLK 435
Cdd:cd17647 315 -----VGEIYVRAGGLAEGYRGLPElNKEKFVNNWfvepdhwnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCE 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 436 LTDRLKDVIKSGGEWISSIDMENAILDSPSVKEAAVIGVPDEKWQERPVAYVVAEDGAEVT------------------- 496
Cdd:cd17647 390 CCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaqedvpkevstdpivk 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1949187543 497 --------RETIVEVLGDRFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:cd17647 470 gligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
184-545 |
9.12e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 184 AAYAGYTTGTTGRPKGVYYSHRSIylhtmggLAALG-----ASF--DDTIMPITPMFHvlSWGFPqnavaagAKLVLPGK 256
Cdd:PRK08043 367 AALILFTSGSEGHPKGVVHSHKSL-------LANVEqiktiADFtpNDRFMSALPLFH--SFGLT-------VGLFTPLL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 257 FAAEEF---GAIAKAFIAEKVTLAN-----------GAPAIFApmlammkdmpQPPDLSGVR-LVSGSSEPPLSMMRGFK 321
Cdd:PRK08043 431 TGAEVFlypSPLHYRIVPELVYDRNctvlfgtstflGNYARFA----------NPYDFARLRyVVAGAEKLQESTKQLWQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 322 EITGADVIHGYGATETTPLATTN----------WHIKPGLDMdeeerwdfkryQGLPVIGVEvkvvdptgeelprDGksm 391
Cdd:PRK08043 501 DKFGLRILEGYGVTECAPVVSINvpmaakpgtvGRILPGMDA-----------RLLSVPGIE-------------QG--- 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 392 GEVLMRGPWITESYFQL----------PDNSERFLD-GWWRSGDVGVIFPNGYLKLTDRLKDVIKSGGEWISSIDMEN-A 459
Cdd:PRK08043 554 GRLQLKGPNIMNGYLRVekpgvlevptAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlA 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 460 ILDSPSVKEAAVIgVPDEKWQErpvAYVVAEDGAEVTRETIVEV---LGdrFAKWQLPDEIIVTDELPRTSVGKLDKKLL 536
Cdd:PRK08043 634 LGVSPDKQHATAI-KSDASKGE---ALVLFTTDSELTREKLQQYareHG--VPELAVPRDIRYLKQLPLLGSGKPDFVTL 707
|
....*....
gi 1949187543 537 RKTWEDAEA 545
Cdd:PRK08043 708 KSMVDEPEQ 716
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
164-396 |
3.23e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 49.54 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 164 EDLIKDKPdtYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSI--YLHTMG-GLAALGASFDDTIMpITPMFHVLS--W 238
Cdd:cd05913 62 EDLRDNYP--FGLFAVPREKVVRIHASSGTTGKPTVVGYTKNDLdvWAELVArCLDAAGVTPGDRVQ-NAYGYGLFTggL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 239 GFPQNAVAAGAkLVLPGKFAAEEfgAIAKAFIAEKVTLANGAPAIFAPMLAMMKDMPQPPDLSGVRLVSGSSEPPLSMMR 318
Cdd:cd05913 139 GFHYGAERLGA-LVIPAGGGNTE--RQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 319 G-FKEITGADVIHGYGATETtplattnwhIKPGLDMDEEERwdfkryQGLPVI--GVEVKVVDP-TGEELPrDGKSmGEV 394
Cdd:cd05913 216 KrIERRLGIKAYDIYGLTEI---------IGPGVAFECEEK------DGLHIWedHFIPEIIDPeTGEPVP-PGEV-GEL 278
|
..
gi 1949187543 395 LM 396
Cdd:cd05913 279 VF 280
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
152-458 |
4.23e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 49.72 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 152 EIETTLENVVFYEDLIKDKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSIYlhtmgglaalgasfdDTIMPIT- 230
Cdd:PTZ00342 274 KAKKLGISIILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLY---------------NTVVPLCk 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 231 ----------------PMFHVLSWGFPQNAVAAGAKLVLPGKfaaeEFGAIAKAFIAEKVTLANGAPAIFAPMLA-MMKD 293
Cdd:PTZ00342 339 hsifkkynpkthlsylPISHIYERVIAYLSFMLGGTINIWSK----DINYFSKDIYNSKGNILAGVPKVFNRIYTnIMTE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 294 MPQPPDLSGvRLVSGSseppLSMMRGFKE---------ITGA------------DVI----------------------- 329
Cdd:PTZ00342 415 INNLPPLKR-FLVKKI----LSLRKSNNNggfskflegITHIsskikdkvnpnlEVIlngggklspkiaeelsvllnvny 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 330 -HGYGATETT-PLattnwHIKPGLDMDEEerwdfkrYQGLPVI-GVEVKVV-----DPTGeELPRdgksmGEVLMRGPWI 401
Cdd:PTZ00342 490 yQGYGLTETTgPI-----FVQHADDNNTE-------SIGGPISpNTKYKVRtwetyKATD-TLPK-----GELLIKSDSI 551
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 402 TESYFQLPDNSERFL--DGWWRSGDVGVIFPNGYLKLTDRLKDVIK-SGGEWISSiDMEN 458
Cdd:PTZ00342 552 FSGYFLEKEQTKNAFteDGYFKTGDIVQINKNGSLTFLDRSKGLVKlSQGEYIET-DMLN 610
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
169-477 |
8.06e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 45.32 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 169 DKPDTYDWPVVDEKTAAYAGYTTGTTGRPKGVYYSHRSI----------YLHTMGGLAALgasfDDTIMPITPMFH---- 234
Cdd:PRK05850 147 DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVianfeqlmsdYFGDTGGVPPP----DTTVVSWLPFYHdmgl 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 235 VLSWGFPqnaVAAG--AKLVLPGKF---AAEEFGAIAK---AFIAekvtlangAPAiFAPMLAMMK----DMpQPPDLSG 302
Cdd:PRK05850 223 VLGVCAP---ILGGcpAVLTSPVAFlqrPARWMQLLASnphAFSA--------APN-FAFELAVRKtsddDM-AGLDLGG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 303 VR-LVSGSSEPPLSMMRGFKE------ITGADVIHGYGATETTP-LATTNWHIKPgldmdEEERWDfkrYQGLPVIGVE- 373
Cdd:PRK05850 290 VLgIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEATVyVATREPGQPP-----ESVRFD---YEKLSAGHAKr 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 374 -------------------VKVVDP-TGEELPrDGKsMGEVLMRGPWITESYFQLPDNSERFLDG-------------WW 420
Cdd:PRK05850 362 cetgggtplvsygsprsptVRIVDPdTCIECP-AGT-VGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgtpegpWL 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949187543 421 RSGDVGVIFpNGYLKLTDRLKDVIKSGGEWISSIDMENaildspSVKE-----AAVIGVPDE 477
Cdd:PRK05850 440 RTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEA------TIQEitggrVAAISVPDD 494
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
368-537 |
4.54e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 39.80 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 368 PVIGVEVKVVDPTGEELPRDGKSMGEVLMRGPWITESYFQL-PDNSERFLDGW----------WRSGDVGVIFPNGYLKL 436
Cdd:PLN03051 296 ASLGTRFVLLNDNGVPYPDDQPCVGEVALAPPMLGASDRLLnADHDKVYYKGMpmygskgmplRRHGDIMKRTPGGYFCV 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 437 TDRLKDVIKSGGEWISSIDMENAILDS-PSVKEAAVIGV------PDEKWQerPVAYVVAEDGAEVTRETIVEVLGDRFA 509
Cdd:PLN03051 376 QGRADDTMNLGGIKTSSVEIERACDRAvAGIAETAAVGVappdggPELLVI--FLVLGEEKKGFDQARPEALQKKFQEAI 453
|
170 180 190
....*....|....*....|....*....|...
gi 1949187543 510 KWQL-P----DEIIVTDELPRTSVGKLDKKLLR 537
Cdd:PLN03051 454 QTNLnPlfkvSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
368-538 |
8.61e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 38.91 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 368 PVIGVEVKVVDPTGEELPRDGKSMGEV----LMRGPWIT-------ESYFQ-LPDNSERFLDgwwRSGDVGVIFPNGYLK 435
Cdd:PLN03052 530 PAMGCKLFILDDSGNPYPDDAPCTGELalfpLMFGASSTllnadhyKVYFKgMPVFNGKILR---RHGDIFERTSGGYYR 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949187543 436 LTDRLKDVIKSGGEWISSIDME---NAILDspSVKEAAVIGV-PDEKWQERPVAYVVAEDGAEVTRETivEVLGDRFAKW 511
Cdd:PLN03052 607 AHGRADDTMNLGGIKVSSVEIErvcNAADE--SVLETAAIGVpPPGGGPEQLVIAAVLKDPPGSNPDL--NELKKIFNSA 682
|
170 180 190
....*....|....*....|....*....|....*
gi 1949187543 512 QLPD--------EIIVTDELPRTSVGKLDKKLLRK 538
Cdd:PLN03052 683 IQKKlnplfkvsAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| |
