|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1-451 |
0e+00 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 804.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 1 MIFSDWPWRHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVL 80
Cdd:PRK09029 2 MIFSDWPWRHWAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 81 PVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHL 160
Cdd:PRK09029 82 PLNPQLPQPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 161 ASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLAGCTHASLVPTQLWRLLVNRS-SVS 239
Cdd:PRK09029 162 ASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGATLVVRDKQPLEQALAGCTHASLVPTQLWRLLDNRSePLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 240 LKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADVGSPLPGREVKIVNDEVWLRAASMAEGYWRN 319
Cdd:PRK09029 242 LKAVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMASTVCAKRADGLAGVGSPLPGREVKLVDGEIWLRGASLALGYWRQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 320 GQLVPLVNDEGWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE 399
Cdd:PRK09029 322 GQLVPLVNDEGWFATRDRGEWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446499693 400 YDQQTV--DLGEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALKEWVQRQQ 451
Cdd:PRK09029 402 SDSEAAvvNLAEWLQDKLARFQQPVAYYLLPPELKNGGIKISRQALKEWVAQQL 455
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
135-447 |
3.92e-142 |
|
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: 409.41 E-value: 3.92e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK-QPLDQ 213
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERnQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 214 MLA--GCTHASLVPTQLWRLLVNR----SSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADG-- 285
Cdd:cd17630 81 DLAppGVTHVSLVPTQLQRLLDSGqgpaALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGfg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LADVGSPLPGREVKIVND-EVWLRAASMAEGYWRnGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:cd17630 161 RGGVGVLLPGRELRIVEDgEIWVGGASLAMGYLR-GQLVPEFNEDGWFTTKDLGELHaDGRLTVLGRADNMIISGGENIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 364 PEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQ--TVDLGEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQ 441
Cdd:cd17630 240 PEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPadPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
....*.
gi 446499693 442 ALKEWV 447
Cdd:cd17630 320 ALRAWL 325
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
30-443 |
7.03e-122 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 362.15 E-value: 7.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 30 WRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPD-- 107
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 108 GENTFPALtSLHIQLVEGAHA----AAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:TIGR01923 82 EEKDFQAD-SLDRIEAAGRYEtslsASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 184 LFHVSGQGIMWRWLYAGARMTVRDKQP-LDQMLAG--CTHASLVPTQLWRLLVNRSS-VSLKAVLLGGAAIPVELTEQAR 259
Cdd:TIGR01923 161 LYHISGLSILFRWLIEGATLRIVDKFNqLLEMIANerVTHISLVPTQLNRLLDEGGHnENLRKILLGGSAIPAPLIEEAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 260 EQGIRCFCGYGLTEFASTVCAKEADGLA---DVGSPLPGREVKIVND------EVWLRAASMAEGYWRNGQLVPLVNDEG 330
Cdd:TIGR01923 241 QYGLPIYLSYGMTETCSQVTTATPEMLHarpDVGRPLAGREIKIKVDnkeghgEIMVKGANLMKGYLYQGELTPAFEQQG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 331 WCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV--EYDQQTVDL 407
Cdd:TIGR01923 321 WFNTGDIGELdGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIvsESDISQAKL 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 446499693 408 GEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQAL 443
Cdd:TIGR01923 401 IAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-451 |
8.77e-93 |
|
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: 287.86 E-value: 8.77e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpq 88
Cdd:COG0318 6 RRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 89 plleellpnltlqfalvpdgentfPALTSLHIQ-LVEGAHAAAwqptrLCSMTL--TSGSTGLPKAAVHTYQAHLASAEG 165
Cdd:COG0318 81 ------------------------PRLTAEELAyILEDSGARA-----LVTALIlyTSGTTGRPKGVMLTHRNLLANAAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 166 VLSLIPFGDHDDWLLSLPLFHVSGQGI-MWRWLYAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL--VNRSS 237
Cdd:COG0318 132 IAAALGLTPGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLLPRFDPERVLEliereRVTVLFGVPTMLARLLrhPEFAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 238 V---SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD----VGSPLPGREVKIVND------ 303
Cdd:COG0318 212 YdlsSLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGERrpgsVGRPLPGVEVRIVDEdgrelp 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -----EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAV 377
Cdd:COG0318 292 pgevgEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLdEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 378 LQVFIVPVADKEFGHRPVAVVEY-DQQTVD---LGEWVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKEWVQRQ 450
Cdd:COG0318 372 AEAAVVGVPDEKWGERVVAFVVLrPGAELDaeeLRAFLRERLARYKVPRRVEfvdELP---RTASGKIDRRALRERYAAG 448
|
.
gi 446499693 451 Q 451
Cdd:COG0318 449 A 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
135-438 |
5.32e-87 |
|
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: 269.15 E-value: 5.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQM 214
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 215 LA-----GCTHASLVPTQLWRLLVNRSSV-----SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEA 283
Cdd:cd04433 81 LEliereKVTILLGVPTLLARLLKAPESAgydlsSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 284 DGLA----DVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTI 347
Cdd:cd04433 161 DDDArkpgSVGRPVPGVEVRIVDPdggelppgeigELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDeDGYLYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQT----VDLGEWVKDKLARFQQPVR 423
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdldaEELRAHVRERLAPYKVPRR 320
|
330
....*....|....*
gi 446499693 424 WLTLPPELKNGGIKI 438
Cdd:cd04433 321 VVFVDALPRTASGKI 335
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
32-445 |
5.43e-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: 209.51 E-value: 5.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfalvpdgent 111
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR-------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 112 fpaLTS--LHIQLVEgahaAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEG-VLSLiPFGDHDDWLLSLPLFHVS 188
Cdd:cd05912 60 ---LTPneLAFQLKD----SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGsALNL-GLTEDDNWLCALPLFHIS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 189 GQGIMWRWLYAGARMTVRDK---QPLDQML--AGCTHASLVPTQLWRLLV---NRSSVSLKAVLLGGAAIPVELTEQARE 260
Cdd:cd05912 132 GLSILMRSVIYGMTVYLVDKfdaEQVLHLInsGKVTIISVVPTMLQRLLEilgEGYPNNLRCILLGGGPAPKPLLEQCKE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 261 QGIRCFCGYGLTEFASTVCA-KEADGLADVGS---PLPGREVKIVND--------EVWLRAASMAEGYWRNGQLVPLVND 328
Cdd:cd05912 212 KGIPVYQSYGMTETCSQIVTlSPEDALNKIGSagkPLFPVELKIEDDgqppyevgEILLKGPNVTKGYLNRPDATEESFE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 329 EGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVeYDQQTVDL 407
Cdd:cd05912 292 NGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFV-VSERPISE 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446499693 408 GE---WVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKE 445
Cdd:cd05912 371 EEliaYCSEKLAKYKVPKKIYfvdELP---RTASGKLLRHELKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
13-450 |
1.80e-58 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 199.42 E-value: 1.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:PRK03640 13 FLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 93 ELLPNLTLQF---------ALVPDGENTFPALTSL---HIQLVEgahaaAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHL 160
Cdd:PRK03640 93 WQLDDAEVKClitdddfeaKLIPGISVKFAELMNGpkeEAEIQE-----EFDLDEVATIMYTSGTTGKPKGVIQTYGNHW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 161 ASAEG-VLSLipfG--DHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK---QPLDQML--AGCTHASLVPTQLWRLL 232
Cdd:PRK03640 168 WSAVGsALNL---GltEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEKfdaEKINKLLqtGGVTIISVVSTMLQRLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 V----NRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCA-KEADGLADVGS---PLPGREVKIVND- 303
Cdd:PRK03640 245 ErlgeGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASQIVTlSPEDALTKLGSagkPLFPCELKIEKDg 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ---------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAA 373
Cdd:PRK03640 325 vvvppfeegEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 374 HPAVLQVFIVPVADKEFGHRPVAVVEYDqQTVDLGE---WVKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKEWV 447
Cdd:PRK03640 405 HPGVAEAGVVGVPDDKWGQVPVAFVVKS-GEVTEEElrhFCEEKLAKYKVPKRFYfveELP---RNASGKLLRHELKQLV 480
|
...
gi 446499693 448 QRQ 450
Cdd:PRK03640 481 EEM 483
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
9-438 |
1.85e-58 |
|
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: 198.22 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpq 88
Cdd:cd17631 2 RRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 89 plleellpnltlqFALVPDgENTFPALTSlhiqlveGAHAAAWQPTRLCsmtLTSGSTGLPKAAVHTYQAHLASAEGVLS 168
Cdd:cd17631 77 -------------FRLTPP-EVAYILADS-------GAKVLFDDLALLM---YTSGTTGRPKGAMLTHRNLLWNAVNALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 169 LIPFGDHDDWLLSLPLFHVSGQGIMW-RWLYAGARMTVRDKQPLDQMLAGC-----THASLVPTQLWRLL--VNRSSV-- 238
Cdd:cd17631 133 ALDLGPDDVLLVVAPLFHIGGLGVFTlPTLLRGGTVVILRKFDPETVLDLIerhrvTSFFLVPTMIQALLqhPRFATTdl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 -SLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADG----LADVGSPLPGREVKIVND---------- 303
Cdd:cd17631 213 sSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDhrrkLGSAGRPVFFVEVRIVDPdgrevppgev 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVF 381
Cdd:cd17631 293 gEIVVRGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLdEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446499693 382 IVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQPVR---WLTLPpelKNGGIKI 438
Cdd:cd17631 373 VIGVPDEKWGEAVVAVVVPRPGAEldedELIAHCRERLARYKIPKSvefVDALP---RNATGKI 433
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-445 |
1.18e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 195.41 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQ 88
Cdd:PRK06187 13 RHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 89 PlleellpnltlQFA----------------LVPDGENTFPALTSLHIQLVEGAHAAAWQPTR----------------- 135
Cdd:PRK06187 93 E-----------EIAyilndaedrvvlvdseFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEvgeyeellaaasdtfdf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 136 -------LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK 208
Cdd:PRK06187 162 pdidendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPRR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 209 -QP---LDQMLA-GCTHASLVPTqLWRLLVNRSSV------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:PRK06187 242 fDPenlLDLIETeRVTFFFAVPT-IWQMLLKAPRAyfvdfsSLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 277 TV-CAKEADGLAD-------VGSPLPGREVKIVND-------------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATR 335
Cdd:PRK06187 321 VVsVLPPEDQLPGqwtkrrsAGRPLPGVEARIVDDdgdelppdggevgEIIVRGPWLMQGYWNRPEATAETIDGGWLHTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 336 DRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY-DQQTVD---LGEW 410
Cdd:PRK06187 401 DVGYIDeDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLkPGATLDakeLRAF 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 446499693 411 VKDKLARFQQPVRWL---TLPpelKNGGIKISRQALKE 445
Cdd:PRK06187 481 LRGRLAKFKLPKRIAfvdELP---RTSVGKILKRVLRE 515
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
8-355 |
1.39e-51 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 179.43 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 8 WRHWRQVRGEAIALRLND-EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN--- 83
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNprl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 ---------------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAH---AAAWQPTRLCSM 139
Cdd:pfam00501 81 paeelayiledsgakvlitddALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPpppPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 140 TLTSGSTGLPKAAVHTYQAHLASAEGVLSLIP----FGDHDDWLLSLPLFHVSGQG-IMWRWLYAGARMTVRDKQPLDQM 214
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 215 LA--------GCTHASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPVELTEQAREQGIRCF-CGYGLTEfASTVC 279
Cdd:pfam00501 241 AAllelieryKVTVLYGVPT-LLNMLLEagapkrALLSSLRLVLSGGAPLPPELARRFRELFGGALvNGYGLTE-TTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 280 AKEADGLAD------VGSPLPGREVKIVND------------EVWLRAASMAEGYWRNGQL-VPLVNDEGWCATRDRGEM 340
Cdd:pfam00501 319 TTPLPLDEDlrslgsVGRPLPGTEVKIVDDetgepvppgepgELCVRGPGVMKGYLNDPELtAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*.
gi 446499693 341 H-NGKLTIVGRLDNLF 355
Cdd:pfam00501 399 DeDGYLEIVGRKKDQI 414
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
15-444 |
1.69e-50 |
|
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: 177.76 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 15 RGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEEL 94
Cdd:cd05936 12 FPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 95 LPNLTLQFALVPDGENTfpaltslhiqLVEGAHAAAWQPTR----LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLI 170
Cdd:cd05936 92 LNDSGAKALIVAVSFTD----------LLAAGAPLGERVALtpedVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 171 PF-GDHDDWLL-SLPLFHVSGQGI-MWRWLYAGARM----TVRDKQPLDQMLA-GCTHASLVPTqLWRLLVNRSSV---- 238
Cdd:cd05936 162 EDlLEGDDVVLaALPLFHVFGLTVaLLLPLALGATIvlipRFRPIGVLKEIRKhRVTIFPGVPT-MYIALLNAPEFkkrd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 --SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLADVGS---PLPGREVKIVND--------- 303
Cdd:cd05936 241 fsSLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSigiPLPGTEVKIVDDdgeelppge 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:cd05936 321 vgELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 381 FIVPVADKEFGHRPVA-VVEYDQQTV---DLGEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05936 401 AVVGVPDPYSGEAVKAfVVLKEGASLteeEIIAFCREQLAGYKVP-RQVEFRDELpKSAVGKILRRELR 468
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
142-443 |
8.20e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 173.31 E-value: 8.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIpfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD----------KQPL 211
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRL--GGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVELDvsagfdptalPRAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQMLAGCTHASLVPTQLWRLLVNRSSV----SLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEfastvcakEADGLA 287
Cdd:PRK07824 121 AELGGGRRYTSLVPMQLAKALDDPAATaalaELDAVLVGGGPAPAPVLDAAAAAGINVVRTYGMSE--------TSGGCV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 288 DVGSPLPGREVKIVNDEVWLRAASMAEGYwRNGQLVPLVNDEGWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:PRK07824 193 YDGVPLDGVRVRVEDGRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQPvRWLTLPPELKNGGI-KISRQA 442
Cdd:PRK07824 272 EAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAptleALRAHVARTLDRTAAP-RELHVVDELPRRGIgKVDRRA 350
|
.
gi 446499693 443 L 443
Cdd:PRK07824 351 L 351
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
27-431 |
2.86e-46 |
|
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: 165.85 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 27 QLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVnpqlpqplleellpnltlqFAlvp 106
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI-------------------YP--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 107 dgenTFPALTSLHI--------QLVEGahaaawqPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDW 178
Cdd:cd05907 63 ----TSSAEQIAYIlndseakaLFVED-------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 179 LLSLPLFHVSGQgIMWRWLYAGARMTVRDKQPLDQMLAGCTHASlvPTQL------WRLLVNRSSV-------------- 238
Cdd:cd05907 132 LSFLPLAHVFER-RAGLYVPLLAGARIYFASSAETLLDDLSEVR--PTVFlavprvWEKVYAAIKVkavpglkrklfdla 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 ---SLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVND-EVWLRAASM 312
Cdd:cd05907 209 vggRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDnrIGTVGKPLPGVEVRIADDgEILVRGPNV 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 313 AEGYWRNGQLVPLVNDE-GWCATRDRGEMH-NGKLTIVGRLDNLFF-SGGEGIQPEEVERVIAAHPAVLQvfIVPVADKe 389
Cdd:cd05907 289 MLGYYKNPEATAEALDAdGWLHTGDLGEIDeDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQ--AVVIGDG- 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446499693 390 fghRP--VAVVEYDQQTV-------------------------DLGEWVKD---KLARFQQPVRWLTLPPEL 431
Cdd:cd05907 366 ---RPflVALIVPDPEALeawaeehgiaytdvaelaanpavraEIEAAVEAanaRLSRYEQIKKFLLLPEPF 434
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
142-451 |
1.46e-45 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 164.01 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGvlslipFGDHDDW-----LLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQ--- 213
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQG------FQRYFQLqqvnsFCVLPLYHVSGLMQFMRSFLTGGKLVILPYKRLKSgqe 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 214 MLAGCTHA--SLVPTQLWRLLVNRSS--VSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCA-KEADGLA- 287
Cdd:PRK07445 202 LPPNPSDFflSLVPTQLQRLLQLRPQwlAQFRTILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATlKPDDFLAg 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 288 --DVGSPLPGREVKIVND---EVWLRAASMAEGYWRNgqlvpLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEG 361
Cdd:PRK07445 282 nnSSGQVLPHAQITIPANqtgNITIQAQSLALGYYPQ-----ILDSQGIFETDDLGYLdAQGYLHILGRNSQKIITGGEN 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 362 IQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGE---WVKDKLARFQQPVRWLTLPPELKNGGIKI 438
Cdd:PRK07445 357 VYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEElktAIKDQLSPFKQPKHWIPVPQLPRNPQGKI 436
|
330
....*....|...
gi 446499693 439 SRQALKEWVQRQQ 451
Cdd:PRK07445 437 NRQQLQQIAVQRL 449
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-444 |
6.63e-41 |
|
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: 150.90 E-value: 6.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleellpnltlqfAL 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT------------------AL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 105 VPDGentfpaltsLHIQLvegAHA-AAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:cd05934 63 RGDE---------LAYII---DHSgAQLVVVDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 184 LFHVSGQGIMW-RWLYAGARMTVRDK----QPLDQML-AGCTHASLVPTQLWRLLVNRSSVSLKAVLL---GGAAIPVEL 254
Cdd:cd05934 131 LFHINAQAVSVlAALSVGATLVLLPRfsasRFWSDVRrYGATVTNYLGAMLSYLLAQPPSPDDRAHRLraaYGAPNPPEL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 255 TEQAREQ-GIRCFCGYGLTE----FASTVCAKEADGLAdvGSPLPGREVKIVND-----------EVWLRAA---SMAEG 315
Cdd:cd05934 211 HEEFEERfGVRLLEGYGMTEtivgVIGPRDEPRRPGSI--GRPAPGYEVRIVDDdgqelpagepgELVIRGLrgwGFFKG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 316 YWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR- 393
Cdd:cd05934 289 YYNMPEATAEAMRNGWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEv 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 394 PVAVVEYDQQTVD---LGEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05934 369 KAVVVLRPGETLDpeeLFAFCEGQLAYFKVP-RYIRFVDDLpKTPTEKVAKAQLR 422
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
17-445 |
1.83e-39 |
|
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: 147.44 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVV-EGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleell 95
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 96 pnltlqfalvpdgenTFPALTSLHIqlVEGAHAAAWqpTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDH 175
Cdd:cd05941 70 ---------------SYPLAELEYV--ITDSEPSLV--LDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 176 DDWLLSLPLFHVSG--QGIMWRwLYAGARMTVRDKQPLDQMLAGCTHASL-----VPTQLWRLL----------VNRSSV 238
Cdd:cd05941 131 DVLLHVLPLHHVHGlvNALLCP-LFAGASVEFLPKFDPKEVAISRLMPSItvfmgVPTIYTRLLqyyeahftdpQFARAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLL---GGAAIPVELTEQARE-QGIRCFCGYGLTEFA-STVCAKEADGLA-DVGSPLPGREVKIVND--------- 303
Cdd:cd05941 210 AAERLRLmvsGSAALPVPTLEEWEAiTGHTLLERYGMTEIGmALSNPLDGERRPgTVGMPLPGVQARIVDEetgeplprg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ---EVWLRAASMAEGYWRNgqlvPLVNDE-----GWCATRDRGEM-HNGKLTIVGRL-DNLFFSGGEGIQPEEVERVIAA 373
Cdd:cd05941 290 evgEIQVRGPSVFKEYWNK----PEATKEeftddGWFKTGDLGVVdEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446499693 374 HPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV-----DLGEWVKDKLARFQQPVRwLTLPPEL-KNGGIKISRQALKE 445
Cdd:cd05941 366 HPGVSECAVIGVPDPDWGERVVAVVVLRAGAAalsleELKEWAKQRLAPYKRPRR-LILVDELpRNAMGKVNKKELRK 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
17-443 |
1.21e-38 |
|
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: 144.98 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpvnpqlpqplleellp 96
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfALVP-DgentfPALTSLHIQ-LVEGAHAAAW--QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPF 172
Cdd:cd05930 63 ------AYVPlD-----PSYPAERLAyILEDSGAKLVltDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 173 GDHDDWL-LSLPLFHVSGQGIMWrWLYAGA------RMTVRDKQPLDQMLA--GCTHASLVPTqLWRLLVN----RSSVS 239
Cdd:cd05930 132 TPGDRVLqFTSFSFDVSVWEIFG-ALLAGAtlvvlpEEVRKDPEALADLLAeeGITVLHLTPS-LLRLLLQelelAALPS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 240 LKAVLLGGAAIPVELTEQAREQGIRC--FCGYGLTE--FAST--VCAKEADGLADV--GSPLPGREVKIVND-------- 303
Cdd:cd05930 210 LRLVLVGGEALPPDLVRRWRELLPGArlVNLYGPTEatVDATyyRVPPDDEEDGRVpiGRPIPNTRVYVLDEnlrpvppg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ---EVWLRAASMAEGYWRNGQL-----VPLVNDEG--WCATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIA 372
Cdd:cd05930 290 vpgELYIGGAGLARGYLNRPELtaerfVPNPFGPGerMYRTGDLVrWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446499693 373 AHPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05930 370 AHPGVREAAVVAREDGDGEKRLVAYVvpdeGGELDEEELRAHLAERLPDYMVPSAFVVLDalPLTPNG--KVDRKAL 444
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
26-445 |
2.56e-38 |
|
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: 145.47 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGA-----------------------RVLPV 82
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvlhtinprlfpeqiayiinhaedRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 83 NPQLPQPLLEELLPNLTLQ--FALVPDGENTFPALTSLHI--QLVEGAHAAAWQP----TRLCSMTLTSGSTGLPKAAV- 153
Cdd:cd12119 104 DRDFLPLLEAIAPRLPTVEhvVVMTDDAAMPEPAGVGVLAyeELLAAESPEYDWPdfdeNTAAAICYTSGTTGNPKGVVy 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 154 -------HTYQAHLASAegvlslIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTV--RDKQP--LDQMLA--GCTH 220
Cdd:cd12119 184 shrslvlHAMAALLTDG------LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLpgPYLDPasLAELIEreGVTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 221 ASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEF-----ASTVCAKEADGLADV 289
Cdd:cd12119 258 AAGVPT-VWQGLLDhleangRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETsplgtVARPPSEHSNLSEDE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 290 --------GSPLPGREVKIVND-------------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTI 347
Cdd:cd12119 337 qlalrakqGRPVPGVELRIVDDdgrelpwdgkavgELQVRGPWVTKSYYKNDEESEALTEDGWLRTGDVATIDeDGYLTI 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE-YDQQTVD---LGEWVKDKLARFQQPVR 423
Cdd:cd12119 417 TDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVlKEGATVTaeeLLEFLADKVAKWWLPDD 496
|
490 500
....*....|....*....|....*
gi 446499693 424 WL---TLPpelKNGGIKISRQALKE 445
Cdd:cd12119 497 VVfvdEIP---KTSTGKIDKKALRE 518
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
24-420 |
1.44e-36 |
|
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: 140.04 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 24 NDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFA 103
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 104 LV-PDG-ENTFPALTSL----HIQLVEGAHAAA------WQPT---------------------RLCSmtltSGSTGLPK 150
Cdd:cd05911 87 FTdPDGlEKVKEAAKELgpkdKIIVLDDKPDGVlsiedlLSPTlgeededlppplkdgkddtaaILYS----SGTTGLPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 151 AAVHTYQAHLASAEGVLSLIP--FGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLAGC-----THASL 223
Cdd:cd05911 163 GVCLSHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLIekykiTFLYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 224 VPTQLwRLLVNRSSV------SLKAVLLGGAAIPVELTEQAREQGIRCFC--GYGLTE--FASTVCAKEADGLADVGSPL 293
Cdd:cd05911 243 VPPIA-AALAKSPLLdkydlsSLRVILSGGAPLSKELQELLAKRFPNATIkqGYGMTEtgGILTVNPDGDDKPGSVGRLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 294 PGREVKIVND------------EVWLRAASMAEGYWRNgqlvP-----LVNDEGWCATRDRGEM-HNGKLTIVGRLDNLF 355
Cdd:cd05911 322 PNVEAKIVDDdgkdslgpnepgEICVRGPQVMKGYYNN----PeatkeTFDEDGWLHTGDIGYFdEDGYLYIVDRKKELI 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 356 FSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTV---DLGEWVKDKLARFQQ 420
Cdd:cd05911 398 KYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAyVVRKPGEKLtekEVKDYVAKKVASYKQ 466
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
28-398 |
2.59e-36 |
|
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: 138.67 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPD 107
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 108 gentfpaltslhiqlVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV 187
Cdd:cd05903 82 ---------------RFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 188 SGQ-GIMWRWLYAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL-----VNRSSVSLKAVLLGGAAIPVELTE 256
Cdd:cd05903 147 TGFvYGFTLPLLLGAPVVLQDIWDPDKALAlmrehGVTFMMGATPFLTDLLnaveeAGEPLSRLRTFVCGGATVPRSLAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 257 QAREQGIRCFCG-YGLTEFASTVCAKEaDGLADV-----GSPLPGREVKIVND-----------EVWLRAASMAEGYWRN 319
Cdd:cd05903 227 RAAELLGAKVCSaYGSTECPGAVTSIT-PAPEDRrlytdGRPLPGVEIKVVDDtgatlapgvegELLSRGPSVFLGYLDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 320 GQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:cd05903 306 PDLTADAAPEGWFRTGDLARLdEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVV 385
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
16-445 |
3.69e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 139.27 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 16 GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELL 95
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 96 PNLTLQFALVPDG--ENTFPALTSL----HIQLVEGAH-----------------------AAAWQPTRLCSMTLTSGST 146
Cdd:PRK07656 99 ARGDAKALFVLGLflGVDYSATTRLpaleHVVICETEEddphtekmktftdflaagdpaerAPEVDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 147 GLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRW-LYAGARM-------------TVRDKQPld 212
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNApLMRGATIlplpvfdpdevfrLIETERI-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 213 QMLAGcthaslVPTQLWRLL--VNRSSV---SLKAVLLGGAAIPVELTEQAREQ-GIRCFC-GYGLTEFASTVCAKEADG 285
Cdd:PRK07656 257 TVLPG------PPTMYNSLLqhPDRSAEdlsSLRLAVTGAASMPVALLERFESElGVDIVLtGYGLSEASGVTTFNRLDD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LAD-----VGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNgqlvP-----LVNDEGWCATRDRGEM-HNG 343
Cdd:PRK07656 331 DRKtvagtIGTAIAGVENKIVNElgeevpvgevgELLVRGPNVMKGYYDD----PeataaAIDADGWLHTGDLGRLdEEG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 344 KLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGH--------RPVAVVEYDqqtvDLGEWVKDKL 415
Cdd:PRK07656 407 YLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEvgkayvvlKPGAELTEE----ELIAYCREHL 482
|
490 500 510
....*....|....*....|....*....|...
gi 446499693 416 ARFQQP--VRWL-TLPpelKNGGIKISRQALKE 445
Cdd:PRK07656 483 AKYKVPrsIEFLdELP---KNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
27-421 |
9.27e-34 |
|
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: 131.45 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 27 QLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLeellpnltlQFALVP 106
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKEREL---------EYILND 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 107 DGENTFPALTSLHiqlvegahaaawqptRLCSMTLTSGSTGLPKAAVHTYQAHLASAegVLSLIPFG-DHDDWLL-SLPL 184
Cdd:cd05935 72 SGAKVAVVGSELD---------------DLALIPYTSGTTGLPKGCMHTHFSAAANA--LQSAVWTGlTPSDVILaCLPL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 185 FHVSG-QGIMWRWLYAGAR---MTVRDKQPLDQMLA--GCTHASLVPTQLWRLLVN-----RSSVSLKAVLLGGAAIPVE 253
Cdd:cd05935 135 FHVTGfVGSLNTAVYVGGTyvlMARWDRETALELIEkyKVTFWTNIPTMLVDLLATpefktRDLSSLKVLTGGGAPMPPA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 254 LTEQAREQ-GIRCFCGYGLTEFAS--TVCAKEADGLADVGSPLPGREVKIVN------------DEVWLRAASMAEGYWR 318
Cdd:cd05935 215 VAEKLLKLtGLRFVEGYGLTETMSqtHTNPPLRPKLQCLGIP*FGVDARVIDietgrelppnevGEIVVRGPQIFKGYWN 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 319 NgqlvPLVNDEGWCA--------TRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKE 389
Cdd:cd05935 295 R----PEETEESFIEikgrrffrTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDER 370
|
410 420 430
....*....|....*....|....*....|....*...
gi 446499693 390 FGHRPVAVV----EYDQQTV--DLGEWVKDKLARFQQP 421
Cdd:cd05935 371 VGEEVKAFIvlrpEYRGKVTeeDIIEWAREQMAAYKYP 408
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
14-445 |
1.17e-33 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 132.29 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 14 VRGEAIALRLNDEQLNWRELCARVDELASGFAAQ-GVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:PRK06839 14 LHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 93 ELLPNLTLQFALVpdgENTFPAlTSLHIQLVEGAHAAAW---------------------QPTRLCsmtLTSGSTGLPKA 151
Cdd:PRK06839 94 FQLKDSGTTVLFV---EKTFQN-MALSMQKVSYVQRVISitslkeiedrkidnfveknesASFIIC---YTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 152 AVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIM-WRWLYAGARMTVRDKQPLDQMLA-----GCTHASLVP 225
Cdd:PRK06839 167 AVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVIIVPRKFEPTKALSmiekhKVTVVMGVP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 226 TQLWRLL--VNRSSVSLKAVLL---GGAAIPVELTEQAREQGIRCFCGYGLTEFASTV--CAKE--ADGLADVGSPLPGR 296
Cdd:PRK06839 247 TIHQALIncSKFETTNLQSVRWfynGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVfmLSEEdaRRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 297 EVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQP 364
Cdd:PRK06839 327 DYELIDEnknkvevgevgELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVdEDGFVYIVGRKKEMIISGGENIYP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 365 EEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQPVRWLTLPPELKNGGIKISR 440
Cdd:PRK06839 407 LEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVliekDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
....*
gi 446499693 441 QALKE 445
Cdd:PRK06839 487 AQLVN 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
13-421 |
6.97e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 130.43 E-value: 6.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 93 ELLPNLTLQfALVPDGENTfPALTSLHIQLV-----------EGAHAAAWQ----------------PTRLCSMT-LTSG 144
Cdd:PRK07788 140 EVAAREGVK-ALVYDDEFT-DLLSALPPDLGrlrawggnpddDEPSGSTDEtlddliagsstaplpkPPKPGGIViLTSG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 145 STGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLAG-----CT 219
Cdd:PRK07788 218 TTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRRFDPEATLEDiakhkAT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 220 HASLVPTQLWRLL-------VNRSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD--- 288
Cdd:PRK07788 298 ALVVVPVMLSRILdlgpevlAKYDTSSLKIIFVSGSALSPELATRALEAfGPVLYNLYGSTEVAFATIATPEDLAEApgt 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 289 VGSPLPGREVKIVNDE-----------VWLRAASMAEGYW--RNGQLVplvndEGWCATRDRGEM-HNGKLTIVGRLDNL 354
Cdd:PRK07788 378 VGRPPKGVTVKILDENgnevprgvvgrIFVGNGFPFEGYTdgRDKQII-----DGLLSSGDVGYFdEDGLLFVDGRDDDM 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446499693 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR-PVAVVEYDQQTVD---LGEWVKDKLARFQQP 421
Cdd:PRK07788 453 IVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRlRAFVVKAPGAALDedaIKDYVRDNLARYKVP 523
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
17-445 |
1.95e-32 |
|
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: 128.58 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd05926 4 PALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALVPDGENT--FPALTSLHIQLVEGAHAAAWQPTRLCSMTL--------------------------TSGSTGL 148
Cdd:cd05926 84 DLGSKLVLTPKGELGpaSRAASKLGLAILELALDVGVLIRAPSAESLsnlladkknaksegvplpddlalilhTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 149 PKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-GIMWRWLYAGARMTVRDK-QPL---DQMLA-GCTHAS 222
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLvASLLSTLAAGGSVVLPPRfSAStfwPDVRDyNATWYT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 223 LVPTqLWRLLVNRSS-------VSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD----VG 290
Cdd:cd05926 244 AVPT-IHQILLNRPEpnpesppPKLRFIRSCSASLPPAVLEALEATfGAPVLEAYGMTEAAHQMTSNPLPPGPRkpgsVG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 291 SPLpGREVKIVND-----------EVWLRAASMAEGYWRNgqlvPLVNDE-----GWCATRDRGEM-HNGKLTIVGRLDN 353
Cdd:cd05926 323 KPV-GVEVRILDEdgeilppgvvgEICLRGPNVTRGYLNN----PEANAEaafkdGWFRTGDLGYLdADGYLFLTGRIKE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 354 LFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQPVR-WLT-- 426
Cdd:cd05926 398 LINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAaVVLREGASVTeeeLRAFCRKHLAAFKVPKKvYFVde 477
|
490
....*....|....*....
gi 446499693 427 LPpelKNGGIKISRQALKE 445
Cdd:cd05926 478 LP---KTATGKIQRRKVAE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3-444 |
9.74e-32 |
|
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: 126.71 E-value: 9.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 3 FSDWPWRHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV 82
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 83 NPQ------------------------LPQPLLEELLPNLTLQFALVPDG---ENTFPALTSLHIQLVEGAHAAAWQPTR 135
Cdd:cd05959 85 NTLltpddyayyledsrarvvvvsgelAPVLAAALTKSEHTLVVLIVSGGagpEAGALLLAELVAAEAEQLKPAATHADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 136 LCSMTLTSGSTGLPKAAVHTYQAHLASAE----GVLSLIPfgdhDDWLLSLP-LFHVSGQG-IMWRWLYAGARMTVRDKQ 209
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAElyarNVLGIRE----DDVCFSAAkLFFAYGLGnSLTFPLSVGATTVLMPER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 210 P-----LDQMLAGctHASL---VPTQLWRLLVN-----RSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFA 275
Cdd:cd05959 241 PtpaavFKRIRRY--RPTVffgVPTLYAAMLAApnlpsRDLSSLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEML 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 276 STVCAKEADGL--ADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDR-GEMH 341
Cdd:cd05959 319 HIFLSNRPGRVryGTTGKPVPGYEVELRDEdggdvadgepgELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKyVRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 342 NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTV---DLGEWVKDK 414
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVvlrpGYEDSEAleeELKEFVKDR 478
|
490 500 510
....*....|....*....|....*....|.
gi 446499693 415 LARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05959 479 LAPYKYP-RWIVFVDELpKTATGKIQRFKLR 508
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
13-421 |
6.98e-31 |
|
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: 124.33 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLE 92
Cdd:cd12118 15 AVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 93 ELLPNLTLQFALVpDGENTFPALtslhiqLVEGAHAAAWQPTR----LCSMTLTSGSTGLPKAAVHTYQ-AHLASAEGVL 167
Cdd:cd12118 95 FILRHSEAKVLFV-DREFEYEDL------LAEGDPDFEWIPPAdewdPIALNYTSGTTGRPKGVVYHHRgAYLNALANIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 168 SLiPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGA-----RmTVRDKQPLDQM-LAGCTHASLVPTQLWRLLVNRSSVSLK 241
Cdd:cd12118 168 EW-EMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGtnvclR-KVDAKAIYDLIeKHKVTHFCGAPTVLNMLANAPPSDARP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 242 A-----VLLGGAAIPVELTEQAREQGIRCFCGYGLTEFA--STVCAK--EADGLA---------------------DVGS 291
Cdd:cd12118 246 LphrvhVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYgpATVCAWkpEWDELPteerarlkarqgvryvgleevDVLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 292 PLPGREV----KIVNdEVWLRAASMAEGYWRNgqlvPLVNDE----GWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGI 362
Cdd:cd12118 326 PETMKPVprdgKTIG-EIVFRGNIVMKGYLKN----PEATAEafrgGWFHSGDLAVIHpDGYIEIKDRSKDIIISGGENI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 363 QPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY-DQQTV---DLGEWVKDKLARFQQP 421
Cdd:cd12118 401 SSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELkEGAKVteeEIIAFCREHLAGFMVP 463
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-437 |
1.47e-30 |
|
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: 120.85 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ--GIMWRWLYaGARMTVRDKQ- 209
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSvlGVLACLTH-GATMVFPSPSf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 210 -PLDQMLA----GCTHASLVPTQLWRLL-----VNRSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCF-CGYGLTEfAST 277
Cdd:cd05917 80 dPLAVLEAiekeKCTALHGVPTMFIAELehpdfDKFDLSSLRTGIMAGAPCPPELMKRVIEVmNMKDVtIAYGMTE-TSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 278 VC-AKEADGLAD-----VGSPLPGREVKIVND------------EVWLRAASMAEGYWRNGQLVPLVND-EGWCATRDRG 338
Cdd:cd05917 159 VStQTRTDDSIEkrvntVGRIMPHTEAKIVDPeggivppvgvpgELCIRGYSVMKGYWNDPEKTAEAIDgDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 339 EMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV---EYDQQTV-DLGEWVKD 413
Cdd:cd05917 239 VMDeDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrlkEGAELTEeDIKAYCKG 318
|
330 340
....*....|....*....|....*.
gi 446499693 414 KLARFQQP--VRWLTLPPELKNGGIK 437
Cdd:cd05917 319 KIAHYKVPryVFFVDEFPLTVSGKIQ 344
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
8-383 |
1.91e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.06 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 8 WRHWRQVRGEAIALRLND----EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV- 82
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 83 -----------------------NPQLPQPLLEELLPNLTLQFALV--PDGENTFPALTSLHiQLVE-GAHA-------- 128
Cdd:COG1022 97 ptssaeevayilndsgakvlfveDQEQLDKLLEVRDELPSLRHIVVldPRGLRDDPRLLSLD-ELLAlGREVadpaelea 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 129 --AAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV----SGQGIMWR------- 195
Cdd:COG1022 176 rrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVfertVSYYALAAgatvafa 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 196 ------------------------W--LYAGARMTVRDKQPLDQML----------------AGCTHASL--VPTQLWRL 231
Cdd:COG1022 256 espdtlaedlrevkptfmlavprvWekVYAGIQAKAEEAGGLKRKLfrwalavgrryararlAGKSPSLLlrLKHALADK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 232 LVnRSSV------SLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVND 303
Cdd:COG1022 336 LV-FSKLrealggRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDnrIGTVGPPLPGVEVKIAED 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -EVWLRAASMAEGYWRNgqlvP-----LVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFF-SGGEGIQPEEVERVIAAHP 375
Cdd:COG1022 415 gEILVRGPNVMKGYYKN----PeataeAFDADGWLHTGDIGELdEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASP 490
|
....*...
gi 446499693 376 AVLQVFIV 383
Cdd:COG1022 491 LIEQAVVV 498
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
9-421 |
5.35e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 122.19 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHwRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN----- 83
Cdd:PRK07786 25 RH-ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNfrltp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEG-------------------AHAAAWQPTRLCSMTL-TS 143
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGgssddsvlgyedllaeagpAHAPVDIPNDSPALIMyTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 144 GSTGLPKAAVHTyqaHLASAEGVLSLI----PFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLD--QML-- 215
Cdd:PRK07786 184 GTTGRPKGAVLT---HANLTGQAMTCLrtngADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDpgQLLdv 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 216 ---AGCTHASLVPTQlWRLL-----VNRSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFASTVCAKEADG 285
Cdd:PRK07786 261 leaEKVTGIFLVPAQ-WQAVcaeqqARPRDLALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMSPVTCMLLGED 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 ----LADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVG 349
Cdd:PRK07786 340 airkLGSVGKVIPTVAARVVDEnmndvpvgevgEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQdEEGYVWVVD 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446499693 350 RLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV-----DLGEWVKDKLARFQQP 421
Cdd:PRK07786 420 RKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAaltleDLAEFLTDRLARYKHP 496
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
32-398 |
9.57e-30 |
|
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: 121.19 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVpDGENt 111
Cdd:cd05904 37 ELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT-TAEL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 112 FPALTSLHIQ--LVEGAHAAAWQPTRLCSMT-------------------LTSGSTGLPKAAVHTYQAHLASAEGVLSLI 170
Cdd:cd05904 115 AEKLASLALPvvLLDSAEFDSLSFSDLLFEAdeaeppvvvikqddvaallYSSGTTGRSKGVMLTHRNLIAMVAQFVAGE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 171 PFGDHDD--WLLSLPLFHVSG-QGIMWRWLYAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLlVNRSSV---- 238
Cdd:cd05904 195 GSNSDSEdvFLCVLPMFHIYGlSSFALGLLRLGATVVVMPRFDLEELLAaieryKVTHLPVVPPIVLAL-VKSPIVdkyd 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 --SLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEF--ASTVCAKEADGLADVGSP---LPGREVKIVN------- 302
Cdd:cd05904 274 lsSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTEStgVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDpetgesl 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 -----DEVWLRAASMAEGYWRNGQLVPL-VNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHP 375
Cdd:cd05904 354 ppnqtGELWIRGPSIMKGYLNNPEATAAtIDKEGWLHTGDLCYIdEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHP 433
|
410 420
....*....|....*....|...
gi 446499693 376 AVLQVFIVPVADKEFGHRPVAVV 398
Cdd:cd05904 434 EILDAAVIPYPDEEAGEVPMAFV 456
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
25-444 |
6.26e-29 |
|
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: 117.95 E-value: 6.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfaL 104
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPL------------------L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 105 VPDgeNTFPALTSLHIQLVEgAHAAAwqptrLCSMTLTSGSTGLPKAAVHTYQAHLASAEG----VLSLIPfgdhDDWLL 180
Cdd:cd05919 70 HPD--DYAYIARDCEARLVV-TSADD-----IAYLLYSSGTTGPPKGVMHAHRDPLLFADAmareALGLTP----GDRVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 181 SLP-LFHVSGQG-IMWRWLYAGARMTVRDKQPL-DQMLAgcTHASLVPTQLW-------RLLVN-----RSSVSLKAVLL 245
Cdd:cd05919 138 SSAkMFFGYGLGnSLWFPLAVGASAVLNPGWPTaERVLA--TLARFRPTVLYgvptfyaNLLDScagspDALRSLRLCVS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 246 GGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVNDE-----------VWLRAAS 311
Cdd:cd05919 216 AGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRPGAwrLGSTGRPVPGYEIRLVDEEghtippgeegdLLVRGPS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 312 MAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEF 390
Cdd:cd05919 296 AAVGYWNNPEKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446499693 391 GHRPVA-VVEYDQQTVD------LGEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05919 376 LSRLTAfVVLKSPAAPQeslardIHRHLLERLSAHKVP-RRIAFVDELpRTATGKLQRFKLR 436
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
9-443 |
1.15e-28 |
|
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: 117.81 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARvlPVNPQLPQ 88
Cdd:cd05920 22 ARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 89 PLLEELLPNLTLQ-FALVPDGENTFPALTSLHIQLVEGAHAAAWqptrlcsMTLTSGSTGLPKAAVHTYQAHLASAEGVL 167
Cdd:cd05920 100 RRSELSAFCAHAEaVAYIVPDRHAGFDHRALARELAESIPEVAL-------FLLSGGTTGTPKLIPRTHNDYAYNVRASA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 168 SLIPFGDHDDWLLSLPLFH---VSGQGIMWRwLYAGARMTV-RDKQPLDQMLA----GCTHASLVPT--QLWRLLVNRSS 237
Cdd:cd05920 173 EVCGLDQDTVYLAVLPAAHnfpLACPGVLGT-LLAGGRVVLaPDPSPDAAFPLiereGVTVTALVPAlvSLWLDAAASRR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 238 V---SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEfaSTVCAKEADGLADV-----GSPL-PGREVKIVND---- 303
Cdd:cd05920 252 AdlsSLRLLQVGGARLSPALARRVPPVlGCTLQQVFGMAE--GLLNYTRLDDPDEViihtqGRPMsPDDEIRVVDEegnp 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -------EVWLRAASMAEGYWR----NGQLVplvNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVI 371
Cdd:cd05920 330 vppgeegELLTRGPYTIRGYYRapehNARAF---TPDGFYRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 372 AAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEwVKDKL-----ARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05920 407 LRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQ-LRRFLrerglAAYKLPDRIEFVDslPLTAVG--KIDKKAL 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
18-443 |
1.39e-28 |
|
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: 117.61 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 18 AIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPN 97
Cdd:cd05923 19 AIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 98 LTLQFALVPDGENTFPALTSLHIQ-LVEGA--------------HAAAWQPTRLCSMTLTSGSTGLPKAAVhtyQAHLAS 162
Cdd:cd05923 99 GEMTAAVIAVDAQVMDAIFQSGVRvLALSDlvglgepesagpliEDPPREPEQPAFVFYTSGTTGLPKGAV---IPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 163 AEGVLSLIP-----FGDHDDWLLSLPLFHVSGqgimWRWLYAGAR------MTVRDKQPLDQML----AGCTHASLVPTQ 227
Cdd:cd05923 176 ESRVLFMSTqaglrHGRHNVVLGLMPLYHVIG----FFAVLVAALaldgtyVVVEEFDPADALKlieqERVTSLFATPTH 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 228 LWRLL-----VNRSSVSLKAVLLGGAAIPVELTEQAREqgirCFCG-----YGLTEFASTVCAKEADgladVGSPL-PG- 295
Cdd:cd05923 252 LDALAaaaefAGLKLSSLRHVTFAGATMPDAVLERVNQ----HLPGekvniYGTTEAMNSLYMRDAR----TGTEMrPGf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 296 -REVKIVN------------DE----VWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFS 357
Cdd:cd05923 324 fSEVRIVRiggspdealangEEgeliVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDpSGDVRILGRVDDMIIS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 358 GGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV---DLGEWVKD-KLARFQQPVRWLTLPPELKN 433
Cdd:cd05923 404 GGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLsadELDQFCRAsELADFKRPRRYFFLDELPKN 483
|
490
....*....|
gi 446499693 434 GGIKISRQAL 443
Cdd:cd05923 484 AMNKVLRRQL 493
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
135-440 |
2.28e-28 |
|
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: 114.04 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 135 RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH-VSGQGIMWRwLYAGARMTVRDK-QPLD 212
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISA-LYLGGTFIGQRKfNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 213 QMLAGCTHAS----LVPTQLWRLL-VNRSSVSLKAVLLGGAAIPVELTEQAREQ----GIRCFCGYGLTEFASTVCAKEA 283
Cdd:cd17633 80 WIRKINQYNAtviyLVPTMLQALArTLEPESKIKSIFSSGQKLFESTKKKLKNIfpkaNLIEFYGTSELSFITYNFNQES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 284 DGLADVGSPLPGREVKIVNDE------VWLRAASMAEGYWRNGQlvplVNDEGWCATRDRG-EMHNGKLTIVGRLDNLFF 356
Cdd:cd17633 160 RPPNSVGRPFPNVEIEIRNADggeigkIFVKSEMVFSGYVRGGF----SNPDGWMSVGDIGyVDEEGYLYLVGRESDMII 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 357 SGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV-DLGEWVKDKLARFQQPVRWLTLP--PELKN 433
Cdd:cd17633 236 IGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYkQLKRFLKQKLSRYEIPKKIIFVDslPYTSS 315
|
....*..
gi 446499693 434 GgiKISR 440
Cdd:cd17633 316 G--KIAR 320
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3-449 |
3.44e-28 |
|
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: 116.78 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 3 FSDWpWRHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvLPV 82
Cdd:COG1021 27 LGDL-LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 83 NP------------------------------QLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAwQ 132
Cdd:COG1021 104 FAlpahrraeishfaeqseavayiipdrhrgfDYRALARELQAEVPSLRHVLVVGDAGEFTSLDALLAAPADLSEPRP-D 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTLTSGSTGLPKAAVHT-----YQAhLASAE--GVlslipfgDHDD-WLLSLPLFH---VSGQGIMWRwLYAGA 201
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIPRThddylYSV-RASAEicGL-------DADTvYLAALPAAHnfpLSSPGVLGV-LYAGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 202 RMTV-RDKQPlDQMLA-----GCTHASLVPTQLWRLL--VNRSSV---SLKAVLLGGAAIPVELTEQAREQ-GircfCG- 268
Cdd:COG1021 254 TVVLaPDPSP-DTAFPliereRVTVTALVPPLALLWLdaAERSRYdlsSLRVLQVGGAKLSPELARRVRPAlG----CTl 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 269 ---YGLtefastvcakeADGL---------ADV-----GSPL-PGREVKIVND-----------EVWLRAASMAEGYWRN 319
Cdd:COG1021 329 qqvFGM-----------AEGLvnytrlddpEEVilttqGRPIsPDDEVRIVDEdgnpvppgevgELLTRGPYTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 320 gqlvPLVN-----DEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR 393
Cdd:COG1021 398 ----PEHNaraftPDGFYRTGDLVRRTpDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGER 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446499693 394 PVAVVEYDQQTVDLGE---WVKDK-LARFQQPVRwLTLPPELKNGGI-KISRQALKEWVQR 449
Cdd:COG1021 474 SCAFVVPRGEPLTLAElrrFLRERgLAAFKLPDR-LEFVDALPLTAVgKIDKKALRAALAA 533
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
16-445 |
5.52e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 116.29 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 16 GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTL------------------------LAWLA 71
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFesmfaafrlgavwvptnfrqtpdeVAYLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 72 LlQCGARVLPVNPQLPQPLLEELLPNLTLQFALV---PDGENTFPALTSLHI-QLVEGAHAAAWQPtrlCSMTLTSGSTG 147
Cdd:PRK07470 101 E-ASGARAMICHADFPEHAAAVRAASPDLTHVVAiggARAGLDYEALVARHLgARVANAAVDHDDP---CWFFFTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 148 LPKAAVHTY-------QAHLASaegvlsLIP-FGDHDDWLLSLPLFHvsGQGIMWRWLYAGARMTV---RDKQPLDQMLA 216
Cdd:PRK07470 177 RPKAAVLTHgqmafviTNHLAD------LMPgTTEQDASLVVAPLSH--GAGIHQLCQVARGAATVllpSERFDPAEVWA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 -----GCTHASLVPTQLwRLLVNRSSV------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTV-----C 279
Cdd:PRK07470 249 lverhRVTNLFTVPTIL-KMLVEHPAVdrydhsSLRYVIYAGAPMYRADQKRALAKlGKVLVQYFGLGEVTGNItvlppA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 280 AKEADGLADV-----GSPLPGREVKIVND-----------EVWLRAASMAEGYWRNgqlvPLVNDE----GWCATRDRGE 339
Cdd:PRK07470 328 LHDAEDGPDArigtcGFERTGMEVQIQDDegrelppgetgEICVIGPAVFAGYYNN----PEANAKafrdGWFRTGDLGH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 340 MH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAV-VEYDQQTVD---LGEWVKDK 414
Cdd:PRK07470 404 LDaRGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVcVARDGAPVDeaeLLAWLDGK 483
|
490 500 510
....*....|....*....|....*....|....
gi 446499693 415 LARFQQPVR---WLTLPpelKNGGIKISRQALKE 445
Cdd:PRK07470 484 VARYKLPKRfffWDALP---KSGYGKITKKMVRE 514
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
17-421 |
4.29e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 113.71 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12583 35 EALVVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQF-----------------ALVP------------------------DGENTfPALTSLHIQLVEG---------A 126
Cdd:PRK12583 115 QSGVRWvicadafktsdyhamlqELLPglaegqpgalacerlpelrgvvslAPAPP-PGFLAWHELQARGetvsrealaE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 127 HAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-----GIMwrwlYAGA 201
Cdd:PRK12583 194 RQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMvlanlGCM----TVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 202 RMTVRDK--QPLDQMLA----GCTHASLVPTQLWRLLVN--RSSV---SLKAVLLGGAAIPVELTEQAREQgIRC---FC 267
Cdd:PRK12583 270 CLVYPNEafDPLATLQAveeeRCTALYGVPTMFIAELDHpqRGNFdlsSLRTGIMAGAPCPIEVMRRVMDE-MHMaevQI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 268 GYGLTEfASTVCAKE--ADGL----ADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDE- 329
Cdd:PRK12583 349 AYGMTE-TSPVSLQTtaADDLerrvETVGRTQPHLEVKVVDPdgatvprgeigELCTRGYSVMKGYWNNPEATAESIDEd 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 330 GWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV--EYDQQT-- 404
Cdd:PRK12583 428 GWMHTGDLATMdEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVrlHPGHAAse 507
|
490
....*....|....*..
gi 446499693 405 VDLGEWVKDKLARFQQP 421
Cdd:PRK12583 508 EELREFCKARIAHFKVP 524
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
32-446 |
4.79e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 112.98 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 32 ELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQF--------A 103
Cdd:PRK09088 27 ELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLllgddavaA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 104 LVPDGENtFPALTSlHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLP 183
Cdd:PRK09088 107 GRTDVED-LAAFIA-SADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 184 LFHVSGQGIMWR-WLYAGARMTVRD----KQPL----DQMLaGCTHASLVPtQLWRLLVNRSSV------SLKAVLLGGA 248
Cdd:PRK09088 185 MFHIIGLITSVRpVLAVGGSILVSNgfepKRTLgrlgDPAL-GITHYFCVP-QMAQAFRAQPGFdaaalrHLTALFTGGA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 249 AIPVELTEQAREQGIRCFCGYGLTEfASTV------CAKEADGLADVGSPLPGREVKIVND-----------EVWLRAAS 311
Cdd:PRK09088 263 PHAAEDILGWLDDGIPMVDGFGMSE-AGTVfgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDqgndcpagvpgELLLRGPN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 312 MAEGYWRNGQLVPLVND-EGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADK- 388
Cdd:PRK09088 342 LSPGYWRRPQATARAFTgDGWFRTGDIARRDaDGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAq 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446499693 389 --EFGHrpVAVVEYDQQTVDLGE---WVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALKEW 446
Cdd:PRK09088 422 wgEVGY--LAIVPADGAPLDLERirsHLSTRLAKYKVP-KHLRLVDALpRTASGKLQKARLRDA 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
141-445 |
1.46e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 112.16 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 141 LTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQG-IMWRWLYAGARMTVRDKQP------LDQ 213
Cdd:PRK13382 203 LTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSqLVLAASLACTIVTRRRFDPeatldlIDR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 214 MLAgcTHASLVPTQLWRLL------VNR-SSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADG 285
Cdd:PRK13382 283 HRA--TGLAVVPVMFDRIMdlpaevRNRySGRSLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATEAGMIATATPADL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LA---DVGSPLPGREVKIVNDE-----------VWLRAASMAEGYwRNGQLVPLVndEGWCATRDRGEMH-NGKLTIVGR 350
Cdd:PRK13382 361 RAapdTAGRPAEGTEIRILDQDfrevptgevgtIFVRNDTQFDGY-TSGSTKDFH--DGFMASGDVGYLDeNGRLFVVGR 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 351 LDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTV--DLGEWVKDKLARFQQPvRWLT 426
Cdd:PRK13382 438 DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAfvVLKPGASATpeTLKQHVRDNLANYKVP-RDIV 516
|
330 340
....*....|....*....|
gi 446499693 427 LPPELKNGGI-KISRQALKE 445
Cdd:PRK13382 517 VLDELPRGATgKILRRELQA 536
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
139-450 |
2.89e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 111.02 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 139 MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH-------VSGqgimwrwLYAGARMTVRDKQPL 211
Cdd:PRK07638 148 MGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHslflygaIST-------LYVGQTVHLMRKFIP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQMLAGCTHASL-----VPTQLWRLL-VNRSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTE--FASTVCAK 281
Cdd:PRK07638 221 NQVLDKLETENIsvmytVPTMLESLYkENRVIENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASElsFVTALVDE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 282 EADGLAD-VGSPLPGREVKIVN--------DE---VWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRG-EMHNGKLTIV 348
Cdd:PRK07638 301 ESERRPNsVGRPFHNVQVRICNeageevqkGEigtVYVKSPQFFMGYIIGGVLARELNADGWMTVRDVGyEDEEGFIYIV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLARFQQPVRWLTLP 428
Cdd:PRK07638 381 GREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVD 460
|
330 340
....*....|....*....|....
gi 446499693 429 --PELKNGgiKISRQALKEWVQRQ 450
Cdd:PRK07638 461 eiPYTNSG--KIARMEAKSWIENQ 482
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
17-443 |
4.52e-26 |
|
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: 109.70 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPqlpqplleellp 96
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfalvpdgenTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd17643 70 --------------AYPVERIAFILADSGPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 177 DWLLslplFHVSGQGI----MWRWLYAGARMTV------RDKQPLDQML--AGCTHASLVPTQLWRLL-----VNRSSVS 239
Cdd:cd17643 136 VWTL----FHSYAFDFsvweIWGALLHGGRLVVvpyevaRSPEDFARLLrdEGVTVLNQTPSAFYQLVeaadrDGRDPLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 240 LKAVLLGGAAIPVELTEQARE----QGIRCFCGYGLTEfaSTV-------CAKEADGLAD--VGSPLPGREVKIVND--- 303
Cdd:cd17643 212 LRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITE--TTVhvtfrplDAADLPAAAAspIGRPLPGLRVYVLDAdgr 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --------EVWLRAASMAEGY-----------------------WRNGQLVPLVNDegwcatrdrgemhnGKLTIVGRLD 352
Cdd:cd17643 290 pvppgvvgELYVSGAGVARGYlgrpeltaerfvanpfggpgsrmYRTGDLARRLPD--------------GELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQPVRWLTLP 428
Cdd:cd17643 356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAyVVADDGAAADiaeLRALLKELLPDYMVPARYVPLD 435
|
490
....*....|....*..
gi 446499693 429 --PELKNGgiKISRQAL 443
Cdd:cd17643 436 alPLTVNG--KLDRAAL 450
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-443 |
6.16e-26 |
|
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: 110.06 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQVR--GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:cd17646 6 EQAArtPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 90 LLEELLPNLTLQF-----ALVPDGENTFPALTSLHIQLVEGAHAAAWQPTR---LCSMTLTSGSTGLPKAAVHTyqaHLA 161
Cdd:cd17646 86 RLAYMLADAGPAVvlttaDLAARLPAGGDVALLGDEALAAPPATPPLVPPRpdnLAYVIYTSGSTGRPKGVMVT---HAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 162 SAEGVLSL---IPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLDQMLA--GCTHASLVPTQLw 229
Cdd:cd17646 163 IVNRLLWMqdeYPLGPGDRVLQKTPLsFDVSVWELFWP-LVAGARLVVarpgghRDPAYLAALIRehGVTTCHFVPSML- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 230 RLLVN----RSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLAD-----VGSPLPGREVK 299
Cdd:cd17646 241 RVFLAepaaGSCASLRRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPVRGPAEtpsvpIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 300 IVND-----------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGE 360
Cdd:cd17646 321 VLDDalrpvpvgvpgELYLGGVQLARGYLGRPALTaerfvpdPFGPGSRMYRTGDLARWrPDGALEFLGRSDDQVKIRGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 361 GIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTVD---LGEWVKDKLARFQQPVRWLTLP--PELKN 433
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGyvVPAAGAAGPDtaaLRAHLAERLPEYMVPAAFVVLDalPLTAN 480
|
490
....*....|
gi 446499693 434 GgiKISRQAL 443
Cdd:cd17646 481 G--KLDRAAL 488
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
11-448 |
7.59e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 110.20 E-value: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 11 WRQVRGEAIALR-----LNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALL------------ 73
Cdd:COG0365 18 HAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACArigavhspvfpg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 74 -----------QCGARVLPVNPQLPQPLLEELLPNLTLQ-FALVPDGENTF-----------PALTSLHiQLVEGAhAAA 130
Cdd:COG0365 98 fgaealadrieDAEAKVLITADGGLRGGKVIDLKEKVDEaLEELPSLEHVIvvgrtgadvpmEGDLDWD-ELLAAA-SAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 131 WQPTRLCS-----MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIpFGDHDD----------WllslplfhvsgqgIMWR 195
Cdd:COG0365 176 FEPEPTDAddplfILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV-LDLKPGdvfwctadigW-------------ATGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 196 W------LYAGARMTVRDKQPL----DQMLA-----GCTHASLVPTqLWRLLVN--------RSSVSLKAVLLGGAAIPV 252
Cdd:COG0365 242 SyivygpLLNGATVVLYEGRPDfpdpGRLWEliekyGVTVFFTAPT-AIRALMKagdeplkkYDLSSLRLLGSAGEPLNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 253 ELTEQAREQ-GIRCFCGYGLTEFASTVCAkeADGLADV--GS---PLPGREVKIVND-----------EVWLRAA--SMA 313
Cdd:COG0365 321 EVWEWWYEAvGVPIVDGWGQTETGGIFIS--NLPGLPVkpGSmgkPVPGYDVAVVDEdgnpvppgeegELVIKGPwpGMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 314 EGYWRNgqlvplvnDE-----------GWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVF 381
Cdd:COG0365 399 RGYWND--------PEryretyfgrfpGWYRTGDGARRDeDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 382 IVPVADKEFGHRPVAVV------EYDQQTV-DLGEWVKDKLARFQQP--VRWLtlpPEL---KNGgiKISRQALKEWVQ 448
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVvlkpgvEPSDELAkELQAHVREELGPYAYPreIEFV---DELpktRSG--KIMRRLLRKIAE 544
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
133-444 |
8.95e-26 |
|
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: 107.57 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG---QGIMwrWLYAGARMTV---- 205
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGsvvTLLT--PLASGAHVVLagpa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 206 --RDKQPLDQMLA-----GCTHASLVPTQLWRLL---VNRSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEF 274
Cdd:cd05944 79 gyRNPGLFDNFWKlveryRITSLSTVPTVYAALLqvpVNADISSLRFAMSGAAPLPVELRARFEDAtGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 275 ASTVCAKEADG---LADVGSPLPGREVKIVND----------------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATR 335
Cdd:cd05944 159 TCLVAVNPPDGpkrPGSVGLRLPYARVRIKVLdgvgrllrdcapdevgEICVAGPGVFGGYLYTEGNKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 336 DRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEW 410
Cdd:cd05944 239 DLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVveeeELLAW 318
|
330 340 350
....*....|....*....|....*....|....*
gi 446499693 411 VKDKLA-RFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:cd05944 319 ARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
13-391 |
1.30e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 109.33 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLND--EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPL 90
Cdd:PRK05857 25 RQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 91 LEELLPNLTLQFALV-----------PDGENTFPALTslhIQLVEGAHAAAWQPTR-------------LCSMTLTSGST 146
Cdd:PRK05857 105 IERFCQITDPAAALVapgskmassavPEALHSIPVIA---VDIAAVTRESEHSLDAaslagnadqgsedPLAMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 147 GLPKAAVHTYQAHLA-----SAEGvLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQ--PLDQMLAG-- 217
Cdd:PRK05857 182 GEPKAVLLANRTFFAvpdilQKEG-LNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENttSLLEILTTna 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 CTHASLVPTQLWRLLVNRSSV-----SLKAVLLGGA---AIPVELTEQAreqGIRCFCGYGLTEFAST-VCAKEADG--- 285
Cdd:PRK05857 261 VATTCLVPTLLSKLVSELKSAnatvpSLRLVGYGGSraiAADVRFIEAT---GVRTAQVYGLSETGCTaLCLPTDDGsiv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 ---LADVGSPLPGREVKIVNDE-----------------VWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGK 344
Cdd:PRK05857 338 kieAGAVGRPYPGVDVYLAATDgigptapgagpsasfgtLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERReDGF 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446499693 345 LTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFG 391
Cdd:PRK05857 418 FYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
26-399 |
1.62e-25 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 109.66 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLA--------------WL-------ALLQ-CGARVL--- 80
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFAlwggeaagianpinPLlepeqiaELLRaAGAKVLvtl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 81 ---PvNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAA---------------------AWQPTRL 136
Cdd:PRK07529 137 gpfP-GTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHArildfdaelarqpgdrlfsgrPIGPDDV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 137 CSMTLTSGSTGLPKAAVHTYQAHLASAeGVLSLIPFGDHDDWLLS-LPLFHV------------SGQGIMWrwlyaGARM 203
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNEVANA-WLGALLLGLGPGDTVFCgLPLFHVnallvtglaplaRGAHVVL-----ATPQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 204 TVRDKQPLDQMLA-----GCTHASLVPTQLWRLL---VNRSSV-SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTE 273
Cdd:PRK07529 290 GYRGPGVIANFWKiveryRINFLSGVPTVYAALLqvpVDGHDIsSLRYALCGAAPLPVEVFRRFEAAtGVRIVEGYGLTE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 274 FASTVCAKEADGLADVGS---PLPGREVKIV---NDEVWLRAASMAE-------------GYWRNGQLVPLVNDEGWCAT 334
Cdd:PRK07529 370 ATCVSSVNPPDGERRIGSvglRLPYQRVRVVildDAGRYLRDCAVDEvgvlciagpnvfsGYLEAAHNKGLWLEDGWLNT 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 335 RDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE 399
Cdd:PRK07529 450 GDLGRIdADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQ 515
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
26-451 |
1.77e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.99 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALV 105
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 106 PD----------GENTFPALTSL-HIQLVEGAHA---------AAWQ---------------PTRLCSMTLTSGSTGLPK 150
Cdd:PRK13295 134 PKtfrgfdhaamARRLRPELPALrHVVVVGGDGAdsfeallitPAWEqepdapailarlrpgPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 151 AAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG--QGIMWRwLYAGARMTVRDKQPLDQMLA-----GCTHaSL 223
Cdd:PRK13295 214 GVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfmYGLMMP-VMLGATAVLQDIWDPARAAElirteGVTF-TM 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 224 VPTQLWRLLVN------RSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTE--FASTVCAKEADGLADV--GSP 292
Cdd:PRK13295 292 ASTPFLTDLTRavkesgRPVSSLRTFLCAGAPIPGALVERARAAlGAKIVSAWGMTEngAVTLTKLDDPDERASTtdGCP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 293 LPGREVKIVNDE-----------VWLRAASMAEGYWRNGQLVpLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGE 360
Cdd:PRK13295 372 LPGVEVRVVDADgaplpagqigrLQVRGCSNFGGYLKRPQLN-GTDADGWFDTGDLARIDaDGYIRISGRSKDVIIRGGE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 361 GIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQ-QTVDLGEWVK----DKLARFQQPVRWLTLP--PELKN 433
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgQSLDFEEMVEflkaQKVAKQYIPERLVVRDalPRTPS 530
|
490
....*....|....*...
gi 446499693 434 GgiKISRQALKEWVQRQQ 451
Cdd:PRK13295 531 G--KIQKFRLREMLRGED 546
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-443 |
2.01e-25 |
|
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: 108.15 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 16 GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELL 95
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 96 PNLTLQFALV-PDGENTFPA---LTSLHIQLVEGAHAAAW---QPTRLCSMTLTSGSTGLPKAAVHTYQA---HLASAEG 165
Cdd:cd12116 81 EDAEPALVLTdDALPDRLPAglpVLLLALAAAAAAPAAPRtpvSPDDLAYVIYTSGSTGRPKGVVVSHRNlvnFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 166 VLSLIPfgdhDDWLLSL--PLFHVSGQGIMWRwLYAGARM------TVRDKQPLDQMLA--GCTHASLVPTqLWRLLV-- 233
Cdd:cd12116 161 RLGLGP----GDRLLAVttYAFDISLLELLLP-LLAGARVviapreTQRDPEALARLIEahSITVMQATPA-TWRMLLda 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 234 ---NRSSVSLkavLLGGAAIPVELTEQAREQGIRCFCGYGLTEFA--STVCA-KEADGLADVGSPLPGREVKIVND---- 303
Cdd:cd12116 235 gwqGRAGLTA---LCGGEALPPDLAARLLSRVGSLWNLYGPTETTiwSTAARvTAAAGPIPIGRPLANTQVYVLDAalrp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -------EVWLRAASMAEGYWRNGQL-----VPLVNDEG---WCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd12116 312 vppgvpgELYIGGDGVAQGYLGRPALtaerfVPDPFAGPgsrLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHRIELGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVfIVPVADKEFGHRPVA-VVEYDQQTVDLGEW---VKDKLARFQQPVRWLTLP--PELKNGgiKISRQ 441
Cdd:cd12116 392 EAALAAHPGVAQA-AVVVREDGGDRRLVAyVVLKAGAAPDAAALrahLRATLPAYMVPSAFVRLDalPLTANG--KLDRK 468
|
..
gi 446499693 442 AL 443
Cdd:cd12116 469 AL 470
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-443 |
2.23e-25 |
|
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: 107.72 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLD------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfalvpdgeNTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd05945 73 -------------ASSPAERIREILDAAKPALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 177 DWLLSLPL-FHVSGQGIMWRWLYAGA-----RMTVRDKQPLDQMLA--GCTHASLVPTqLWRLLV-----NRSSV-SLKA 242
Cdd:cd05945 140 VFLNQAPFsFDLSVMDLYPALASGATlvpvpRDATADPKQLFRFLAehGITVWVSTPS-FAAMCLlsptfTPESLpSLRH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 243 VLLGGAAIPVELTE--QAREQGIRCFCGYGLTE--FASTVCAKEADGLAD-----VGSPLPGREVKIVND---------- 303
Cdd:cd05945 219 FLFCGEVLPHKTARalQQRFPDARIYNTYGPTEatVAVTYIEVTPEVLDGydrlpIGYAKPGAKLVILDEdgrpvppgek 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -EVWLRAASMAEGYWRNGQLVP--LVNDEG--WCATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAV 377
Cdd:cd05945 299 gELVISGPSVSKGYLNNPEKTAaaFFPDEGqrAYRTGDLVRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGV 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 378 LQVFIVPVADKEFGHRPVAVVE-----YDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd05945 379 KEAVVVPKYKGEKVTELIAFVVpkpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDelPLNANG--KIDRKAL 449
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
17-443 |
2.77e-25 |
|
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: 107.34 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfalvPDgentFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAV--HTYQAHLASAEGvlSLIPFGD 174
Cdd:cd17652 69 ---------PA----YPAERIAYMLADARPALLLTTPDNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQI--AAFDVGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 175 HDDWL-LSLPLFHVSgqgiMWRW---LYAGARMTVRDK------QPLDQMLA--GCTHASLVPTQLwRLLVNRSSVSLKA 242
Cdd:cd17652 134 GSRVLqFASPSFDAS----VWELlmaLLAGATLVLAPAeellpgEPLADLLRehRITHVTLPPAAL-AALPPDDLPDLRT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 243 VLLGGAAIPVELTEQ-AReqGIRCFCGYGLTEfaSTVCAKEADGLAD-----VGSPLPGREVKIVND-----------EV 305
Cdd:cd17652 209 LVVAGEACPAELVDRwAP--GRRMINAYGPTE--TTVCATMAGPLPGggvppIGRPVPGTRVYVLDArlrpvppgvpgEL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 306 WLRAASMAEGYW-----------------------RNGQLVPLVNDegwcatrdrgemhnGKLTIVGRLDNLFFSGGEGI 362
Cdd:cd17652 285 YIAGAGLARGYLnrpgltaerfvadpfgapgsrmyRTGDLARWRAD--------------GQLEFLGRADDQVKIRGFRI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 363 QPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQPVRWLTLP--PELKNGgi 436
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAyVVPAPGAAPTaaeLRAHLAERLPGYMVPAAFVVLDalPLTPNG-- 428
|
....*..
gi 446499693 437 KISRQAL 443
Cdd:cd17652 429 KLDRRAL 435
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
142-428 |
2.85e-25 |
|
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: 105.66 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMW-RWLYAGArmTVRDKQPLD-------- 212
Cdd:cd17638 8 TSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIvACLLTGA--TVVPVAVFDvdaileai 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 213 -----QMLAGcthaslVPTQLWRLLV-----NRSSVSLKAVLLGGAAIPVELTEQAREQ-GIR-CFCGYGLTEFASTVCA 280
Cdd:cd17638 86 ereriTVLPG------PPTLFQSLLDhpgrkKFDLSSLRAAVTGAATVPVELVRRMRSElGFEtVLTAYGLTEAGVATMC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 281 KEADGLADV----GSPLPGREVKIVND-EVWLRAASMAEGYWRNGQLVPLVNDE-GWCATRDRGEM-HNGKLTIVGRLDN 353
Cdd:cd17638 160 RPGDDAETVattcGRACPGFEVRIADDgEVLVRGYNVMQGYLDDPEATAEAIDAdGWLHTGDVGELdERGYLRITDRLKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 354 LFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTV---DLGEWVKDKLARFQQP--VRWL-T 426
Cdd:cd17638 240 MYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAfVVARPGVTLteeDVIAWCRERLANYKVPrfVRFLdE 319
|
..
gi 446499693 427 LP 428
Cdd:cd17638 320 LP 321
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
20-421 |
2.96e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 108.51 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 20 ALRLNDEQLNWRELCARVDELAsGFAAQ--GVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN-------------- 83
Cdd:PRK08314 28 AIVFYGRAISYRELLEEAERLA-GYLQQecGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNpmnreeelahyvtd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 --------------PQLPQPLLEELLPNLTLQF--ALVPDGENTFPAL--TSLHIQLVEGAHAAAWQ------------- 132
Cdd:PRK08314 107 sgarvaivgselapKVAPAVGNLRLRHVIVAQYsdYLPAEPEIAVPAWlrAEPPLQALAPGGVVAWKealaaglapppht 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 --PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAegVLSLIPFGDHDD--WLLSLPLFHVSG-QGIMWRWLYAGAR---MT 204
Cdd:PRK08314 187 agPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPEsvVLAVLPLFHVTGmVHSMNAPIYAGATvvlMP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 205 VRDKQPLDQMLA--GCTHASLVPTQLWRLLVN-----RSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:PRK08314 265 RWDREAAARLIEryRVTHWTNIPTMVVDFLASpglaeRDLSSLRYIGGGGAAMPEAVAERLKELtGLDYVEGYGLTETMA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 277 TVCAKEAD-------GLA-----------DVGSPLPGREVkivnDEVWLRAASMAEGYWRNgqlvPLVNDEGWCA----- 333
Cdd:PRK08314 345 QTHSNPPDrpklqclGIPtfgvdarvidpETLEELPPGEV----GEIVVHGPQVFKGYWNR----PEATAEAFIEidgkr 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 334 ---TRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTV 405
Cdd:PRK08314 417 ffrTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVvlrpEARGKTT 496
|
490
....*....|....*...
gi 446499693 406 --DLGEWVKDKLARFQQP 421
Cdd:PRK08314 497 eeEIIAWAREHMAAYKYP 514
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
6-421 |
4.33e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 107.77 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 6 WPWRhwrqvrgeaIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCGARVLPVN 83
Cdd:PRK13383 48 WPGR---------TAIIDDDGALSYRELQRATESLARRLTRDGVAPGRavGVMCR--NGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVE---------GAHAAAWQPTRLcsMTLTSGSTGLPKAAVH 154
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDpatagaeesGGRPAVAAPGRI--VLLTSGTTGKPKGVPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 155 TYQahLASAEGV----LSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLAGCT-HA----SLVP 225
Cdd:PRK13383 195 APQ--LRSAVGVwvtiLDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASlHRadafTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 226 TQLWRLLVNRSSV-------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADgLAD----VGSPL 293
Cdd:PRK13383 273 VVLARILELPPRVrarnplpQLRVVMSSGDRLDPTLGQRFMDTyGDILYNGYGSTEVGIGALATPAD-LRDapetVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 294 PGREVKI-----------VNDEVWLRAASMAEGYWRNGQLVPLvndEGWCATRDRGEMHN-GKLTIVGRLDNLFFSGGEG 361
Cdd:PRK13383 352 AGCPVRIldrnnrpvgprVTGRIFVGGELAGTRYTDGGGKAVV---DGMTSTGDMGYLDNaGRLFIVGREDDMIISGGEN 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446499693 362 IQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQP 421
Cdd:PRK13383 429 VYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAfVVLHPGSGVDaaqLRDYLKDRVSRFEQP 492
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
142-438 |
1.21e-24 |
|
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: 104.26 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLplFHVSGQGIMWRWL----YAGARMTVRDKQPLDQMLA- 216
Cdd:cd17635 9 TSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLP--LPATHIGGLWWILtcliHGGLCVTGGENTTYKSLFKi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 ----GCTHASLVPTqLWRLLVN------RSSVSLKAVLLGGAaIPVELTEQARE--QGIRCFCGYGLTEFASTVCAKEAD 284
Cdd:cd17635 87 lttnAVTTTCLVPT-LLSKLVSelksanATVPSLRLIGYGGS-RAIAADVRFIEatGLTNTAQVYGLSETGTALCLPTDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLAD---VGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVG 349
Cdd:cd17635 165 DSIEinaVGRPYPGVDVYLAATdgiagpsasfgTIWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLGERrEDGFLFITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 350 RLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGhrpvavvEYDQQTVDLGEWVKDKLARFQQPVRWLTLPP 429
Cdd:cd17635 245 RSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFG-------ELVGLAVVASAELDENAIRALKHTIRRELEP 317
|
....*....
gi 446499693 430 ELKNGGIKI 438
Cdd:cd17635 318 YARPSTIVI 326
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
11-445 |
1.23e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 106.12 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 11 WRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPL 90
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 91 LEELLPNLTLQFALVPDGENTFPALTslHIQLVEGAHA-----------------AAWQPTRLCSMTLTSGSTGLPKAAV 153
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAIVALE--TPKIVIDAAAqadsrrlaqggleippqAAVAPTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 154 HTY-QAHLASAEGVLSLIPFGDhDDWLLSLPLFHVS-----GQGIMWrwlYAGARMTVRDKQPlDQMLAGC-----THAS 222
Cdd:PRK06145 169 HSYgNLHWKSIDHVIALGLTAS-ERLLVVGPLYHVGafdlpGIAVLW---VGGTLRIHREFDP-EAVLAAIerhrlTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 223 LVPTQLWRLLV----NRSSVSLKAVLLGGAaipveltEQAREQGIRCFC----------GYGLTEFAS----TVCAKEAD 284
Cdd:PRK06145 244 MAPVMLSRVLTvpdrDRFDLDSLAWCIGGG-------EKTPESRIRDFTrvftraryidAYGLTETCSgdtlMEAGREIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLADVGSPLPGREVKI-----------VNDEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLD 352
Cdd:PRK06145 317 KIGSTGRALAHVEIRIadgagrwlppnMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLdEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQ-QTVDLGEW---VKDKLARFQQPvRWLTLP 428
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLEALdrhCRQRLASFKVP-RQLKVR 475
|
490
....*....|....*...
gi 446499693 429 PEL-KNGGIKISRQALKE 445
Cdd:PRK06145 476 DELpRNPSGKVLKRVLRD 493
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
142-436 |
2.35e-24 |
|
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: 103.12 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK----QPLDQMLAg 217
Cdd:cd17637 8 TAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKfdpaEALELIEE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 cTHASLV---PTQLWRLL--VNRSSV---SLKAVLlgGAAIPVELTEQAREQGIRCFCGYGLTE---FASTVCAKEADGL 286
Cdd:cd17637 87 -EKVTLMgsfPPILSNLLdaAEKSGVdlsSLRHVL--GLDAPETIQRFEETTGATFWSLYGQTEtsgLVTLSPYRERPGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 287 AdvGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRL--D 352
Cdd:cd17637 164 A--GRPGPLVRVRIVDDndrpvpagetgEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFdEDGYLWYAGRKpeK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQP--VRWLT 426
Cdd:cd17637 242 ELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATltadELIEFVGSRIARYKKPryVVFVE 321
|
330
....*....|
gi 446499693 427 LPPELKNGGI 436
Cdd:cd17637 322 ALPKTADGSI 331
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
142-389 |
4.33e-24 |
|
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: 104.06 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-QGIMWRWLYAGARMTVRDKQPLDQMLA---- 216
Cdd:cd05914 97 TSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFLDKIPSAKIIAlafa 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 --GCTHASLVPTQL------------------WRL---LVNRSSVSL-------------KAVLLGGAAIPVELTEQARE 260
Cdd:cd05914 177 qvTPTLGVPVPLVIekifkmdiipkltlkkfkFKLakkINNRKIRKLafkkvheafggniKEFVIGGAKINPDVEEFLRT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 261 QGIrCFC-GYGLTEFASTVC--AKEADGLADVGSPLPGREVKIVND-------EVWLRAASMAEGYWRNGQL-VPLVNDE 329
Cdd:cd05914 257 IGF-PYTiGYGMTETAPIISysPPNRIRLGSAGKVIDGVEVRIDSPdpatgegEIIVRGPNVMKGYYKNPEAtAEAFDKD 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446499693 330 GWCATRDRGEM-HNGKLTIVGRLDNLFFSG-GEGIQPEEVERVIAAHPAVLQVFIVPVADKE 389
Cdd:cd05914 336 GWFHTGDLGKIdAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKKL 397
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
12-443 |
4.54e-24 |
|
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: 104.21 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQVR--GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:cd12117 5 EQAArtPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 90 LLEELLPNLTLQfALVPDGENTF----PALTSLHIQLVEGAHAAAW----QPTRLCSMTLTSGSTGLPKAAVHTYQAHLA 161
Cdd:cd12117 85 RLAFMLADAGAK-VLLTDRSLAGraggLEVAVVIDEALDAGPAGNPavpvSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 162 SAEGVlSLIPFGDHDDWLLSLPL-FHVSGQGImWRWLYAGARMTVRDKQPLDQMLA--------GCThASLVPTQLWRLL 232
Cdd:cd12117 164 LVKNT-NYVTLGPDDRVLQTSPLaFDASTFEI-WGALLNGARLVLAPKGTLLDPDAlgaliaeeGVT-VLWLTAALFNQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 VN---RSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTE---FASTVCAKEADGLAD---VGSPLPGREVKIV 301
Cdd:cd12117 241 ADedpECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTEnttFTTSHVVTELDEVAGsipIGRPIANTRVYVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 302 ND-----------EVWLRAASMAEGYWRNGQL-------VPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGI 362
Cdd:cd12117 321 DEdgrpvppgvpgELYVGGDGLALGYLNRPALtaerfvaDPFGPGERLYRTGDLARWLpDGRLEFLGRIDDQVKIRGFRI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 363 QPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKI 438
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAyvVAEGALDAAELRAFLRERLPAYMVPAAFVVLDelPLTANG--KV 478
|
....*
gi 446499693 439 SRQAL 443
Cdd:cd12117 479 DRRAL 483
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
13-445 |
6.50e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 104.20 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLNDEQ--LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPL 90
Cdd:PRK05852 27 TRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 91 LEELLPNLTLQFALVPD--------------------GENTFPALTSLHIQLVEGA--HAAAWQPTRL----CSMTLTSG 144
Cdd:PRK05852 107 QRVRSQAAGARVVLIDAdgphdraepttrwwpltvnvGGDSGPSGGTLSVHLDAATepTPATSTPEGLrpddAMIMFTGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 145 STGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHvsGQGIMWRWLY-----------AGARMTVRDKQPlDQ 213
Cdd:PRK05852 187 TTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYH--GHGLIAALLAtlasggavllpARGRFSAHTFWD-DI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 214 MLAGCTHASLVPTqLWRLLVNRSSV--------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEAD 284
Cdd:PRK05852 264 KAVGATWYTAVPT-IHQILLERAATepsgrkpaALRFIRSCSAPLTAETAQALQTEfAAPVVCAFGMTEATHQVTTTQIE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLADVGSP-----LPGR----EVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NG 343
Cdd:PRK05852 343 GIGQTENPvvstgLVGRstgaQIRIVGSdglplpagavgEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSaAG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 344 KLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV---EYDQQTVD-LGEWVKDKLARFQ 419
Cdd:PRK05852 423 DLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIvprESAPPTAEeLVQFCRERLAAFE 502
|
490 500
....*....|....*....|....*....
gi 446499693 420 QPVRW---LTLPPELKNGgikISRQALKE 445
Cdd:PRK05852 503 IPASFqeaSGLPHTAKGS---LDRRAVAE 528
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
15-398 |
1.37e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 103.14 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 15 RGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEEL 94
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 95 LPNLTLQfALVPDGeNTF-----------PALTS-LHIQLVEG-----AHAAAWQPTRL---------CSMTLTSGSTGL 148
Cdd:PRK06188 105 LEDAGIS-TLIVDP-APFveralallarvPSLKHvLTLGPVPDgvdllAAAAKFGPAPLvaaalppdiAGLAYTGGTTGK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 149 PKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGI---MWRwlyaGARMTVRDKQPLDQMLA-----GCTH 220
Cdd:PRK06188 183 PKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFlptLLR----GGTVIVLAKFDPAEVLRaieeqRITA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 221 ASLVPTQLWRLL-----VNRSSVSLKAVLLGGAAI-PVELTEQAREQGIRCFCGYGLTEFASTVC--------AKEADGL 286
Cdd:PRK06188 259 TFLVPTMIYALLdhpdlRTRDLSSLETVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEAPMVITylrkrdhdPDDPKRL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 287 ADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNL 354
Cdd:PRK06188 339 TSCGRPTPGLRVALLDEdgrevaqgevgEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREdEDGFYYIVDRKKDM 418
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446499693 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:PRK06188 419 IVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVV 462
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-445 |
2.08e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 102.70 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN--------------- 83
Cdd:PRK08316 28 TALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNfmltgeelayildhs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 ----------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAwqpTRLCSMTLTSGSTG 147
Cdd:PRK08316 108 garaflvdpalaptaeAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELAD---DDLAQILYTSGTES 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 148 LPKAAVHTYQAHLAsaEGVLSLIP--FGDHDDWLLSLPLFHvSGQ--GIMWRWLYAGARMTVRDKQPLDQMLA-----GC 218
Cdd:PRK08316 185 LPKGAMLTHRALIA--EYVSCIVAgdMSADDIPLHALPLYH-CAQldVFLGPYLYVGATNVILDAPDPELILRtieaeRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 219 THASLVPTqLWRLLVN------RSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFA--STVC-AKEADGLA 287
Cdd:PRK08316 262 TSFFAPPT-VWISLLRhpdfdtRDLSSLRKGYYGASIMPVEVLKELRERlpGLRFYNCYGQTEIAplATVLgPEEHLRRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 288 D-VGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNL 354
Cdd:PRK08316 341 GsAGRPVLNVETRVVDDdgndvapgevgEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMdEEGYITVVDRKKDM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQPVRWL---TL 427
Cdd:PRK08316 421 IKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAvVVPKAGATVTedeLIAHCRARLAGFKVPKRVIfvdEL 500
|
490
....*....|....*...
gi 446499693 428 PpelKNGGIKISRQALKE 445
Cdd:PRK08316 501 P---RNPSGKILKRELRE 515
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
130-450 |
2.69e-23 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 102.57 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 130 AWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDK- 208
Cdd:PLN02860 168 AWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKf 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 209 ------QPLDQMlaGCTHASLVPTQLWRLL-VNRSSV------SLKAVLLGGAAIPVELTEQARE--QGIRCFCGYGLTE 273
Cdd:PLN02860 248 dakaalQAIKQH--NVTSMITVPAMMADLIsLTRKSMtwkvfpSVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 274 FASTV---------CAKEADGLAD----------------VGSPLPGREVKIVNDE------VWLRAASMAEGYWRNGQL 322
Cdd:PLN02860 326 ACSSLtfmtlhdptLESPKQTLQTvnqtksssvhqpqgvcVGKPAPHVELKIGLDEssrvgrILTRGPHVMLGYWGQNSE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 323 VPLV-NDEGWCATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVey 400
Cdd:PLN02860 406 TASVlSNDGWLDTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACV-- 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446499693 401 dqqtvdlgewvkdklaRFQQPVRWLTLPPELKNGGIKISRQALKEWVQRQ 450
Cdd:PLN02860 484 ----------------RLRDGWIWSDNEKENAKKNLTLSSETLRHHCREK 517
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
13-448 |
4.57e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 101.95 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 13 QVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLA--------------------- 71
Cdd:PRK08162 29 EVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGvpmagavlntlntrldaasia 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 72 --LLQCGARVLPVNPQLPQPLLEELLPNLTLQFALV-----PDGENTFPALTSLHIQLVEGAHAAAWQPTR----LCSMT 140
Cdd:PRK08162 109 fmLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIdvddpEYPGGRFIGALDYEAFLASGDPDFAWTLPAdewdAIALN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 141 LTSGSTGLPKAAV-HTYQAHLASAEGVLSLiPFGDHDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVRDKQP---LDQML 215
Cdd:PRK08162 189 YTSGTTGNPKGVVyHHRGAYLNALSNILAW-GMPKHPVYLWTLPMFHCNGWCFPWTVaARAGTNVCLRKVDPkliFDLIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 216 A-GCTHASLVPTQLwRLLVN-----RSSVSLK-AVLLGGAAIPVELTEQAREQGIRCFCGYGLTEF--ASTVCAKEA--D 284
Cdd:PRK08162 268 EhGVTHYCGAPIVL-SALINapaewRAGIDHPvHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETygPATVCAWQPewD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLAD---------------------VGSPLPGREVKivND-----EVWLRAASMAEGYWRNgqlvPLVNDE----GWCAT 334
Cdd:PRK08162 347 ALPLderaqlkarqgvryplqegvtVLDPDTMQPVP--ADgetigEIMFRGNIVMKGYLKN----PKATEEafagGWFHT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 335 RDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY-DQQTV---DLGE 409
Cdd:PRK08162 421 GDLAVLHpDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELkDGASAteeEIIA 500
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446499693 410 WVKDKLARFQQP--VRWLTLPpelKNGGIKISRQALKEWVQ 448
Cdd:PRK08162 501 HCREHLAGFKVPkaVVFGELP---KTSTGKIQKFVLREQAK 538
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
26-444 |
8.65e-23 |
|
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: 100.20 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfALV 105
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS-ALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 106 PDGENTfPALtslhiqlvegahaaawqptrlcsMTLTSGSTGLPKAAVHTYQ---AHLASAEGVLSLIP-----FGDHDD 177
Cdd:cd05971 84 TDGSDD-PAL-----------------------IIYTSGTTGPPKGALHAHRvllGHLPGVQFPFNLFPrdgdlYWTPAD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 178 WLLSLPLFhvsgqGIMWRWLYAGA-----RMTVRDKQPLDQMLA--GCTHASLVPTQLwRLL------VNRSSVSLKAVL 244
Cdd:cd05971 140 WAWIGGLL-----DVLLPSLYFGVpvlahRMTKFDPKAALDLMSryGVTTAFLPPTAL-KMMrqqgeqLKHAQVKLRAIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 245 LGGAAIPVELTEQAREQ-GIRCFCGYGLTE--FASTVCAKEADGL-ADVGSPLPGREVKIVNDE-------------VWL 307
Cdd:cd05971 214 TGGESLGEELLGWAREQfGVEVNEFYGQTEcnLVIGNCSALFPIKpGSMGKPIPGHRVAIVDDNgtplppgevgeiaVEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 308 RAASMAEGYWRN--GQLVPLVNDegWCATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVP 384
Cdd:cd05971 294 PDPVAFLGYWNNpsATEKKMAGD--WLLTGDLGrKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVG 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 385 VAD-------KEFGHRPVAVVEYDQQTVDLGEWVKDKLARFQQPvRWLTLPPEL---KNGgiKISRQALK 444
Cdd:cd05971 372 IPDpirgeivKAFVVLNPGETPSDALAREIQELVKTRLAAHEYP-REIEFVNELprtATG--KIRRRELR 438
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
31-377 |
9.85e-23 |
|
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: 99.65 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 31 RELCARVDELASGFAAQGVVE-GSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQ-------------LPQPLLEELLP 96
Cdd:TIGR01733 3 RELDERANRLARHLRAAGGVGpGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAypaerlafiledaGARLLLTDSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:TIGR01733 83 ASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 177 DWLLSLPL-FHVSGQGImWRWLYAGARMTVRDKQPLDQMLA---------GCTHASLVPT--QLWRLLVNRSSVSLKAVL 244
Cdd:TIGR01733 163 RVLQFASLsFDASVEEI-FGALLAGATLVVPPEDEERDDAAllaaliaehPVTVLNLTPSllALLAAALPPALASLRLVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 245 LGGAAIPVELTEQAREQ--GIRCFCGYGLTEFASTVCAKEADG-------LADVGSPLPGREVKIVND-----------E 304
Cdd:TIGR01733 242 LGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPddapresPVPIGRPLANTRLYVLDDdlrpvpvgvvgE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 305 VWLRAASMAEGYWRNGQLVP--LVNDEGWCATRDR--------GEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:TIGR01733 322 LYIGGPGVARGYLNRPELTAerFVPDPFAGGDGARlyrtgdlvRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRH 401
|
...
gi 446499693 375 PAV 377
Cdd:TIGR01733 402 PGV 404
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
18-444 |
1.34e-22 |
|
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: 99.47 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 18 AIALRLNDEQLNWRELCARVDELASGFAAQGV-VEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGiVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATM------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfALVPDGENTFPaLTSLHIQLVEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEG----VLSLIPf 172
Cdd:cd05958 68 ------PLLRPKELAYI-LDKARITVALCAHALT-ASDDICILAFTSGTTGAPKATMHFHRDPLASADRyavnVLRLRE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 173 gdhDDWLLSLP-LFHVSGQGIMWRW-LYAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL-----VNRSSVSL 240
Cdd:cd05958 139 ---DDRFVGSPpLAFTFGLGGVLLFpFGVGASGVLLEEATPDLLLSaiaryKPTVLFTAPTAYRAMLahpdaAGPDLSSL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 241 KAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTE-FASTVCAKEADG-LADVGSPLPGREVKIVND--------EVWLRA 309
Cdd:cd05958 216 RKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEmFHIFISARPGDArPGATGKPVPGYEAKVVDDegnpvpdgTIGRLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 310 ASMAEGYWRNGQLVPLVN-DEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAD 387
Cdd:cd05958 296 VRGPTGCRYLADKRQRTYvQGGWNITGDTYSRDpDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 388 KEFGHRPVA-VVEYDQQTVD------LGEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05958 376 ESRGVVVKAfVVLRPGVIPGpvlareLQDHAKAHIAPYKYP-RAIEFVTELpRTATGKLQRFALR 439
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
17-444 |
1.41e-22 |
|
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: 99.75 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfalvPDgentFPAlTSLHIQLVEGAHAA--AWQPTRLCSMTLTSGSTGLPKAAVHTYQA---HLASAEGVLSLIP 171
Cdd:cd17649 69 ---------PE----YPA-ERLRYMLEDSGAGLllTHHPRQLAYVIYTSGSTGTPKGVAVSHGPlaaHCQATAERYGLTP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 172 fGDHDdwllsLPLFHVSGQGIMWRW---LYAGARMTVRDKQPLD--QMLA------GCTHASLvPTQLWRLLV------- 233
Cdd:cd17649 135 -GDRE-----LQFASFNFDGAHEQLlppLICGACVVLRPDELWAsaDELAemvrelGVTVLDL-PPAYLQQLAeeadrtg 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 234 NRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTE--FASTVCAKEAD-----GLADVGSPLPGREVKI------ 300
Cdd:cd17649 208 DGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEatVTPLVWKCEAGaaragASMPIGRPLGGRSAYIldadln 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 -----VNDEVWLRAASMAEGY-----------------------WRNGQLVPlvndegWCAtrdrgemhNGKLTIVGRLD 352
Cdd:cd17649 288 pvpvgVTGELYIGGEGLARGYlgrpeltaerfvpdpfgapgsrlYRTGDLAR------WRD--------DGVIEYLGRVD 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVAVV---EYDQQTVDLGE---WVKDKLARFQQPVRWLT 426
Cdd:cd17649 354 HQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVvlrAAAAQPELRAQlrtALRASLPDYMVPAHLVF 432
|
490 500
....*....|....*....|
gi 446499693 427 LP--PELKNGgiKISRQALK 444
Cdd:cd17649 433 LArlPLTPNG--KLDRKALP 450
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
138-445 |
1.42e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 100.48 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 138 SMTLTSGSTGLPKAAVHTYQAHLASAegvLSLI---PFGDHDDWLLSLPLFHVSGQGIMWRWLYAGA-----RMTVRDKQ 209
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYLST---LSAIigwEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGtsvcmRHVTAPEI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 210 PLDQMLAGCTHASLVPTqLWRLLV--NRSSVSLKA----VLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTV--CAK 281
Cdd:PLN03102 267 YKNIEMHNVTHMCCVPT-VFNILLkgNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlfCEW 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 282 EAD---------------------GLADV---------GSPLPGREVkivnDEVWLRAASMAEGYWRNGQLVPLVNDEGW 331
Cdd:PLN03102 346 QDEwnrlpenqqmelkarqgvsilGLADVdvknketqeSVPRDGKTM----GEIVIKGSSIMKGYLKNPKATSEAFKHGW 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 332 CATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTV--- 405
Cdd:PLN03102 422 LNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAfvVLEKGETTKedr 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446499693 406 ---------DLGEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALKE 445
Cdd:PLN03102 502 vdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
15-423 |
1.72e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 99.95 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 15 RGEAIALRLNDEQ-LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN---------- 83
Cdd:PRK07514 15 DRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNtaytlaeldy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 --------------PQLPQPLLEELLPNLTLQFALVPDGENTFPALTSlhiQLVEGAHAAAWQPTRLCSMTLTSGSTGLP 149
Cdd:PRK07514 95 figdaepalvvcdpANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAA---AAPDDFETVPRGADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 150 KAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-----QGImwrwLYAGARMTVRDKQPLDQMLAGCTHASL- 223
Cdd:PRK07514 172 KGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGlfvatNVA----LLAGASMIFLPKFDPDAVLALMPRATVm 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 224 --VPTQLWRLL----VNRSSVSLKAVLLGGAAiPVeLTEQARE----QGIRCFCGYGLTE---FASTVCAKEADGlADVG 290
Cdd:PRK07514 248 mgVPTFYTRLLqeprLTREAAAHMRLFISGSA-PL-LAETHREfqerTGHAILERYGMTEtnmNTSNPYDGERRA-GTVG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 291 SPLPGREVKIVNDE------------VWLRAASMAEGYWRNgqlvP------LVNDeGWCATRDRGEM-HNGKLTIVGRL 351
Cdd:PRK07514 325 FPLPGVSLRVTDPEtgaelppgeigmIEVKGPNVFKGYWRM----PektaeeFRAD-GFFITGDLGKIdERGYVHIVGRG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 352 DNLFFSGGEGIQPEEVERVIAAHPAVLQ--VFIVPVADkeFGHRPVAVV------EYDQQTVdLGEwVKDKLARFQQPVR 423
Cdd:PRK07514 400 KDLIISGGYNVYPKEVEGEIDELPGVVEsaVIGVPHPD--FGEGVTAVVvpkpgaALDEAAI-LAA-LKGRLARFKQPKR 475
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
140-444 |
4.68e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 99.34 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 140 TLTSGSTGLPKAAVHTYQAHLASAEGV----LSLIPfgdHDDWLLSLPLFHVSGQG-IMWRWLYAGARMTVrDKQPLDQM 214
Cdd:PRK06060 151 TYTSGTTGPPKAAIHRHADPLTFVDAMcrkaLRLTP---EDTGLCSARMYFAYGLGnSVWFPLATGGSAVI-NSAPVTPE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 215 LAGCTHASLVPTQLWRL------LVNRSSV----SLKAVLLGGAAIPVELTEQARE--QGIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK06060 227 AAAILSARFGPSVLYGVpnffarVIDSCSPdsfrSLRCVVSAGEALELGLAERLMEffGGIPILDGIGSTEVGQTFVSNR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 283 ADG--LADVGSPLPGREVKIV-----------NDEVWLRAASMAEGYWRNGQlvPLVNDEGWCATRDRGEMH-NGKLTIV 348
Cdd:PRK06060 307 VDEwrLGTLGRVLPPYEIRVVapdgttagpgvEGDLWVRGPAIAKGYWNRPD--SPVANEGWLDTRDRVCIDsDGWVTYR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVadKEFGHRPV-------AVVEYDQQTV--DLGEWVKDKLARFQ 419
Cdd:PRK06060 385 CRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTlqaflvaTSGATIDGSVmrDLHRGLLNRLSAFK 462
|
330 340
....*....|....*....|....*..
gi 446499693 420 QPVRWLTLP--PELKNGgiKISRQALK 444
Cdd:PRK06060 463 VPHRFAVVDrlPRTPNG--KLVRGALR 487
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
44-445 |
6.47e-22 |
|
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: 97.83 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 44 FAAQGVVEGSGVMLRAWN---TPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLqfALVPDGENTFPALTSLhi 120
Cdd:cd05929 34 AAAEGVWIADGVYIYLINsilTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALV--CGLFTGGGALDGLEDY-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 121 qlvegAHAAAWQPTRLCS-------MTLTSGSTGLPKA------AVHTYQAHLASAEGvlsLIPFGDHDDWLLSLPLFHV 187
Cdd:cd05929 110 -----EAAEGGSPETPIEdeaagwkMLYSGGTTGRPKGikrglpGGPPDNDTLMAAAL---GFGPGADSVYLSPAPLYHA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 188 SGQGIMWRWLYAGARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLL------VNRSSV-SLKAVLLGGAAIPVELT 255
Cdd:cd05929 182 APFRWSMTALFMGGTLVLMEKFDPEEFLRlieryRVTFAQFVPTMFVRLLklpeavRNAYDLsSLKRVIHAAAPCPPWVK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 256 EQARE-QGIRCFCGYGLTE-FASTVCAKEaDGLA---DVGSPLPGrEVKIVND-----------EVWLRAASMAEGYWRN 319
Cdd:cd05929 262 EQWIDwGGPIIWEYYGGTEgQGLTIINGE-EWLThpgSVGRAVLG-KVHILDEdgnevppgeigEVYFANGPGFEYTNDP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 320 GQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:cd05929 340 EKTAAARNEGGWSTLGDVGYLdEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 399 E----YDQQTV---DLGEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQALKE 445
Cdd:cd05929 420 QpapgADAGTAlaeELIAFLRDRLSRYKCPrsIEFVAELPRDDTG--KLYRRLLRD 473
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
133-383 |
1.39e-21 |
|
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: 97.15 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQ-GIMWRWLYAGarMTVRDKQPL 211
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERvFVEGGSLYGG--VLVAFAESL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQMLAGCTHASlvPT------QLW-----------------RLL----VNR-------SSVSLKAV--LLGGAA-IPVEL 254
Cdd:cd05932 214 DTFVEDVQRAR--PTlffsvpRLWtkfqqgvqdkipqqklnLLLkipvVNSlvkrkvlKGLGLDQCrlAGCGSApVPPAL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 255 TEQAREQGIRCFCGYGLTE-FA-STVCAKEADGLADVGSPLPGREVKIVND-EVWLRAASMAEGYWRNG-QLVPLVNDEG 330
Cdd:cd05932 292 LEWYRSLGLNILEAYGMTEnFAySHLNYPGRDKIGTVGNAGPGVEVRISEDgEILVRSPALMMGYYKDPeATAEAFTADG 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 331 WCATRDRGEM-HNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAHPAVLQVFIV 383
Cdd:cd05932 372 FLRTGDKGELdADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
134-445 |
4.13e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 95.82 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 134 TRLCSMTLTSGSTGLPKAAVHTYQ---AHLASA------EGVLSLIPFGdhddwllSLPLFHVSG-QGIMWRWLYAGARM 203
Cdd:PLN02330 184 TDLCALPFSSGTTGISKGVMLTHRnlvANLCSSlfsvgpEMIGQVVTLG-------LIPFFHIYGiTGICCATLRNKGKV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 204 TVRDKQPLDQMLAG-----CTHASLVPTQLWRLLVNR-------SSVSLKAVLLGGAAIPVELTE--QAREQGIRCFCGY 269
Cdd:PLN02330 257 VVMSRFELRTFLNAlitqeVSFAPIVPPIILNLVKNPiveefdlSKLKLQAIMTAAAPLAPELLTafEAKFPGVQVQEAY 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 270 GLTEFaSTVCAKEAD-----GLA---DVGSPLPGREVKIVN------------DEVWLRAASMAEGYWRNGQLVP-LVND 328
Cdd:PLN02330 337 GLTEH-SCITLTHGDpekghGIAkknSVGFILPNLEVKFIDpdtgrslpkntpGELCVRSQCVMQGYYNNKEETDrTIDE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 329 EGWCATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV-- 405
Cdd:PLN02330 416 DGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKes 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446499693 406 --DLGEWVKDKLARFQQ--PVRWLTLPPELKNGgiKISRQALKE 445
Cdd:PLN02330 496 eeDILNFVAANVAHYKKvrVVQFVDSIPKSLSG--KIMRRLLKE 537
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
17-443 |
2.29e-20 |
|
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: 93.15 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpvnpqlpqplleellp 96
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfALVPDGENTFPALTSLHIQLVEGAHAAAwQPTRLCSMTLTSGSTGLPK---------AAVHTYQAHLASAE--- 164
Cdd:cd12115 75 ------AYVPLDPAYPPERLRFILEDAQARLVLT-DPDDLAYVIYTSGSTGRPKgvaiehrnaAAFLQWAAAAFSAEela 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 165 GVLSLIPFGdhddwlLSLPLFHVSGQgimwrwLYAGARMTVRDK--QPLDqmLAGCTHASL---VPTQLWRLL-VNRSSV 238
Cdd:cd12115 148 GVLASTSIC------FDLSVFELFGP------LATGGKVVLADNvlALPD--LPAAAEVTLintVPSAAAELLrHDALPA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTE--QAREQGIRCFCGYGLTEFA--STVCA--KEADGLADVGSPLPGREVKIVND--------- 303
Cdd:cd12115 214 SVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTtySTVAPvpPGASGEVSIGRPLANTQAYVLDRalqpvplgv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAA 373
Cdd:cd12115 294 pgELYIGGAGVARGYLGRPGLTaerflpdPFGPGARLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRS 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 374 HPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd12115 374 IPGVREAVVVAIGDAAGERRLVAYIvaepGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDalPLTPNG--KIDRSAL 447
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
133-414 |
2.68e-20 |
|
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: 93.43 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTLTSGSTGLPKAAVHTyQAHLASAEGVLSLIPFG----DHDDWLLS-LPLFHVSGQGIMWRWLYAGARM---- 203
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLT-HGNIVSNVAGVFKILEIlnkiNPTDVYISyLPLAHIFERVVEALFLYHGAKIgfys 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 204 ----------------------------------TVRDKQPLDQML---------AGCTHASLVPTQLWRLLV-NRSSVS 239
Cdd:cd05927 192 gdirlllddikalkptvfpgvprvlnriydkifnKVQAKGPLKRKLfnfalnyklAELRSGVVRASPFWDKLVfNKIKQA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 240 L----KAVLLGGAAIPVELTEQAREqgirCFC-----GYGLTE-FASTVCAKEADGLA-DVGSPLPGREVKIVN------ 302
Cdd:cd05927 272 LggnvRLMLTGSAPLSPEVLEFLRV----ALGcpvleGYGQTEcTAGATLTLPGDTSVgHVGGPLPCAEVKLVDvpemny 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 --------DEVWLRAASMAEGYWRNGQLVPLVNDE-GWCATRDRGE-MHNGKLTIVGRLDNLF-FSGGEGIQPEEVERVI 371
Cdd:cd05927 348 dakdpnprGEVCIRGPNVFSGYYKDPEKTAEALDEdGWLHTGDIGEwLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIY 427
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446499693 372 AAHPAVLQVFIVPVADKEFghrPVAVVEYDQQTVDlgEWVKDK 414
Cdd:cd05927 428 ARSPFVAQIFVYGDSLKSF---LVAIVVPDPDVLK--EWAASK 465
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
26-383 |
2.94e-20 |
|
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: 92.81 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 26 EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpVNpqlpqplleellpnltlqfalV 105
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGA----VD---------------------V 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 106 PDGeNTFPALTSLHI--------QLVEGAhaaawqPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDD 177
Cdd:cd17640 59 VRG-SDSSVEELLYIlnhsesvaLVVEND------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 178 WLLSLPLFH---------VSGQGI---------------------------MWRWLYAGARMTVRDKQPLDQMLAGCTha 221
Cdd:cd17640 132 FLSILPIWHsyersaeyfIFACGCsqaytsirtlkddlkrvkphyivsvprLWESLYSGIQKQVSKSSPIKQFLFLFF-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 222 slvptqlwrLLVNRssvsLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVK 299
Cdd:cd17640 210 ---------LSGGI----FKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCnvRGSVGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 300 IVNDE------------VWLRAASMAEGYWRNGQLVPLV-NDEGWCATRDRGEM-HNGKLTIVGRL-DNLFFSGGEGIQP 364
Cdd:cd17640 277 IVDPEgnvvlppgekgiVWVRGPQVMKGYYKNPEATSKVlDSDGWFNTGDLGWLtCGGELVLTGRAkDTIVLSNGENVEP 356
|
410
....*....|....*....
gi 446499693 365 EEVERVIAAHPAVLQVFIV 383
Cdd:cd17640 357 QPIEEALMRSPFIEQIMVV 375
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
12-445 |
2.95e-20 |
|
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: 94.15 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQVR--GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqp 89
Cdd:COG1020 484 AQAArtPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLD------ 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 90 lleellpnltlqfalvPD--------------------GENTFPALTSLHIQLVE------GAHAAAWQPTRLCSMTL-- 141
Cdd:COG1020 558 ----------------PAypaerlaymledagarlvltQSALAARLPELGVPVLAldalalAAEPATNPPVPVTPDDLay 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 ---TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGImWRWLYAGARM------TVRDKQPL 211
Cdd:COG1020 622 viyTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLsFDASVWEI-FGALLSGATLvlappeARRDPAAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQMLA--GCTHASLVPTqLWRLLVN---RSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFASTVCAKEAD 284
Cdd:COG1020 701 AELLArhRVTVLNLTPS-LLRALLDaapEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETTVDSTYYEVT 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLAD------VGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQL-----VPlvNDEGWCATR-----DR 337
Cdd:COG1020 780 PPDAdggsvpIGRPIANTRVYVLDAhlqpvpvgvpgELYIGGAGLARGYLNRPELtaerfVA--DPFGFPGARlyrtgDL 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 338 GEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLA 416
Cdd:COG1020 858 ARWLpDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALA 937
|
490 500 510
....*....|....*....|....*....|...
gi 446499693 417 R----FQQPVRWLTLPPELKNGGIKISRQALKE 445
Cdd:COG1020 938 LllppYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
142-423 |
3.85e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 93.14 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLS-LPLFHVSGQGI-MWRWLYAGARM----TVRDKQPLDQM 214
Cdd:PRK05605 227 TSGTTGKPKGAQLTHRNLFANAAQGKAWVPgLGDGPERVLAaLPMFHAYGLTLcLTLAVSIGGELvllpAPDIDLILDAM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 215 -------LAGcthaslVPTQLWRLLV--NRSSVSLKAV---LLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAK 281
Cdd:PRK05605 307 kkhpptwLPG------VPPLYEKIAEaaEERGVDLSGVrnaFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGN 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 282 ---EADGLADVGSPLPGREVKIVN-------------DEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGK 344
Cdd:PRK05605 381 pmsDDRRPGYVGVPFPDTEVRIVDpedpdetmpdgeeGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEeDGF 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 345 LTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA-VVEYDQQTVD---LGEWVKDKLARFQQ 420
Cdd:PRK05605 461 IRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAaVVLEPGAALDpegLRAYCREHLTRYKV 540
|
...
gi 446499693 421 PVR 423
Cdd:PRK05605 541 PRR 543
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-443 |
4.85e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 8 WRHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLP 87
Cdd:PRK12316 517 FEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYP 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 88 QPLLEELLPNLTLQFALVPDGENTFPALtSLHIQLVEGAHAAAWQP--------TRLCSMTL-----TSGSTGLPKAAVH 154
Cdd:PRK12316 597 AERLAYMLEDSGVQLLLSQSHLGRKLPL-AAGVQVLDLDRPAAWLEgyseenpgTELNPENLayviyTSGSTGKPKGAGN 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 155 TYQA---HLASAEGVLSLipfGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLDQMLA--GCTHAS 222
Cdd:PRK12316 676 RHRAlsnRLCWMQQAYGL---GVGDTVLQKTPFsFDVSVWEFFWP-LMSGARLVVaapgdhRDPAKLVELINreGVDTLH 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 223 LVPTQLWRLLVN---RSSVSLKAVLLGGAAIPVELTEQ--AREQGIRCFCGYGLTEFASTV----CAKEADGLADVGSPL 293
Cdd:PRK12316 752 FVPSMLQAFLQDedvASCTSLRRIVCSGEALPADAQEQvfAKLPQAGLYNLYGPTEAAIDVthwtCVEEGGDSVPIGRPI 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 294 PGREVKI-----------VNDEVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGEMH-NGKLTIVGRLDNL 354
Cdd:PRK12316 832 ANLACYIldanlepvpvgVLGELYLAGRGLARGYHGRPGLTaerfvpsPFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 355 FFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELK 432
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALErlPLTP 991
|
490
....*....|.
gi 446499693 433 NGgiKISRQAL 443
Cdd:PRK12316 992 NG--KLDRKAL 1000
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-444 |
6.87e-20 |
|
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: 91.24 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVnpqlpqplleellpnltlqfalvpd 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPL------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 108 gentFPALTSLHIQL---VEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQ---AHLASAEGVLSLIPFGDHddWLLS 181
Cdd:cd05972 56 ----TTLLGPKDIEYrleAAGAKAIVTDAEDPALIYFTSGTTGLPKGVLHTHSyplGHIPTAAYWLGLRPDDIH--WNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 182 LP--LFHVSGqGIMWRWLyAGARMTVRDKQPLDQMLA-------GCTHASLVPTqLWRLLV-----NRSSVSLKAVLLGG 247
Cdd:cd05972 130 DPgwAKGAWS-SFFGPWL-LGATVFVYEGPRFDAERIlelleryGVTSFCGPPT-AYRMLIkqdlsSYKFSHLRLVVSAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 248 AAIPVELTEQAREQ-GIRCFCGYGLTEFASTV----CAKEADGlaDVGSPLPGREVKIVNDE-------------VWLRA 309
Cdd:cd05972 207 EPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVgnfpDMPVKPG--SMGRPTPGYDVAIIDDDgrelppgeegdiaIKLPP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 310 ASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADK 388
Cdd:cd05972 285 PGLFLGYVGDPEKTEASIRGDYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446499693 389 EFGHRPVAVV-------EYDQQTVDLGEWVKDKLARFQQPvRWLTLPPEL-KNGGIKISRQALK 444
Cdd:cd05972 365 VRGEVVKAFVvltsgyePSEELAEELQGHVKKVLAPYKYP-REIEFVEELpKTISGKIRRVELR 427
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
142-449 |
1.00e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 91.73 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG--QGIMWRWLyAGARMTVRDKQPLDQMLA--- 216
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGflHGVTAPFL-IGARSVLLDIFTPDACLAlle 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 --GCTHASLVPTQLWRLLVNRSS-----VSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADGL--- 286
Cdd:PRK06087 274 qqRCTCMLGATPFIYDLLNLLEKqpadlSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLsrf 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 287 -ADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNGQLVPLV-NDEGWCATRDRGEM-HNGKLTIVGRLD 352
Cdd:PRK06087 354 mHTDGYAAAGVEIKVVDEarktlppgcegEEASRGPNVFMGYLDEPELTARAlDEEGWYYSGDLCRMdEAGYIKITGRKK 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTV-DLGEWV-KDKLARFQQPVRWLT 426
Cdd:PRK06087 434 DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVvlkaPHHSLTLeEVVAFFsRKRVAKYKYPEHIVV 513
|
330 340
....*....|....*....|....*
gi 446499693 427 LP--PELKNGGIKISRQAlKEWVQR 449
Cdd:PRK06087 514 IDklPRTASGKIQKFLLR-KDIMRR 537
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
12-445 |
1.83e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 90.97 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQVR--GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:PRK06155 29 RQAEryPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 90 LLE-----ELLPNLTLQFALVPDGENTFPALTSL-HIQLVEGAHAAAW---------------------QPTRLCSMTLT 142
Cdd:PRK06155 109 QLEhilrnSGARLLVVEAALLAALEAADPGDLPLpAVWLLDAPASVSVpagwstaplppldapapaaavQPGDTAAILYT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 143 SGSTGL------PKAAVHTYQAHLASAEGVlslipfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLA 216
Cdd:PRK06155 189 SGTTGPskgvccPHAQFYWWGRNSAEDLEI------GADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGFWP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 -----GCTHASLVPTQLWRLLVNRSSVSLKA----VLLGGaAIPVELTEQAREQ-GIRCFCGYGLTEfASTVCA--KEAD 284
Cdd:PRK06155 263 avrrhGATVTYLLGAMVSILLSQPARESDRAhrvrVALGP-GVPAALHAAFRERfGVDLLDGYGSTE-TNFVIAvtHGSQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 GLADVGSPLPGREVKIVND-----------EVWLRAA---SMAEGY----------WRNgqlvplvndeGWCATRDRGEM 340
Cdd:PRK06155 341 RPGSMGRLAPGFEARVVDEhdqelpdgepgELLLRADepfAFATGYfgmpektveaWRN----------LWFHTGDRVVR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAdKEFGHRPV--AVVEYDQQT---VDLGEWVKDK 414
Cdd:PRK06155 411 dADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVmaAVVLRDGTAlepVALVRHCEPR 489
|
490 500 510
....*....|....*....|....*....|...
gi 446499693 415 LARFQQP--VRWLTLPPELKNGgiKISRQALKE 445
Cdd:PRK06155 490 LAYFAVPryVEFVAALPKTENG--KVQKFVLRE 520
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
9-422 |
1.19e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 88.56 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQ 88
Cdd:PRK06178 40 RAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFRE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 89 PLLE-----ELLPNLTLQFALVPDGENTFPAL-------TSLHIQL------------------VEGAH------AAAWQ 132
Cdd:PRK06178 120 HELSyelndAGAEVLLALDQLAPVVEQVRAETslrhvivTSLADVLpaeptlplpdslraprlaAAGAIdllpalRACTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTL--------TSGSTGLPKAAVHTyQAHL---ASAEGVLSLIpfGDHDDWLLS-LPLFHVSGQ--GIMWRwLY 198
Cdd:PRK06178 200 PVPLPPPALdalaalnyTGGTTGMPKGCEHT-QRDMvytAAAAYAVAVV--GGEDSVFLSfLPEFWIAGEnfGLLFP-LF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 199 AGARMTVRDK-QPLDQMLA----GCTHASLVPTQLWRLLvNRSSV------SLKAVllGGAAIPVELTEQAREQ------ 261
Cdd:PRK06178 276 SGATLVLLARwDAVAFMAAveryRVTRTVMLVDNAVELM-DHPRFaeydlsSLRQV--RVVSFVKKLNPDYRQRwraltg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 262 GIRCFCGYGLTEF--ASTVCAKEADGLAD-------VGSPLPGREVKIVN------------DEVWLRAASMAEGYWRNG 320
Cdd:PRK06178 353 SVLAEAAWGMTEThtCDTFTAGFQDDDFDllsqpvfVGLPVPGTEFKICDfetgellplgaeGEIVVRTPSLLKGYWNKP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 321 QLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV- 398
Cdd:PRK06178 433 EATAEALRDGWLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVq 512
|
490 500
....*....|....*....|....*..
gi 446499693 399 ---EYDQQTVDLGEWVKDKLARFQQPV 422
Cdd:PRK06178 513 lkpGADLTAAALQAWCRENMAVYKVPE 539
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
111-406 |
2.18e-18 |
|
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: 87.39 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 111 TFPALTSLHIQLVEGAhaaawQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG- 189
Cdd:cd05909 129 KFPPKWLLRIFGVAPV-----QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGl 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 190 QGIMWRWLYAGARMtVRDKQPLD-----QML--AGCTHASLVPTQLwRLLVNRSS----VSLKAVLLGGAAIPVELTEQA 258
Cdd:cd05909 204 TGCLWLPLLSGIKV-VFHPNPLDykkipELIydKKATILLGTPTFL-RGYARAAHpedfSSLRLVVAGAEKLKDTLRQEF 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 259 RE-QGIRCFCGYGLTEfASTVCA---KEADGLAD-VGSPLPGREVKIVNDE------------VWLRAASMAEGYWRNGQ 321
Cdd:cd05909 282 QEkFGIRILEGYGTTE-CSPVISvntPQSPNKEGtVGRPLPGMEVKIVSVEtheevpigegglLLVRGPNVMLGYLNEPE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 322 LVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH-PAVLQVFIVPVADKEFGHRPVAVVE 399
Cdd:cd05909 361 LTSFAFGDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT 440
|
....*..
gi 446499693 400 YDQQTVD 406
Cdd:cd05909 441 TTDTDPS 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
17-443 |
2.34e-18 |
|
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: 87.40 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN---------PQLP 87
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDpaypaerlaFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 88 QPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAV--HTYQAHLASAEG 165
Cdd:cd17651 90 DAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 166 VLSLIPFGDHDDwLLSLPLFHVSGQGImWRWLYAGARMTVRD---KQPLDQMLAGC----THASLVPTQLWRLLVN---- 234
Cdd:cd17651 170 RASSLGPGARTL-QFAGLGFDVSVQEI-FSTLCAGATLVLPPeevRTDPPALAAWLdeqrISRVFLPTVALRALAEhgrp 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 235 --RSSVSLKAVLLGGAAIPVELTEQ---AREQGIRCFCGYGLTEfASTVCAKEADGLAD-------VGSPLPGREVKIVN 302
Cdd:cd17651 248 lgVRLAALRYLLTGGEQLVLTEDLRefcAGLPGLRLHNHYGPTE-THVVTALSLPGDPAawpapppIGRPIDNTRVYVLD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 D-----------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:cd17651 327 AalrpvppgvpgELYIGGAGLARGYLNRPELTaerfvpdPFVPGARMYRTGDLARwLPDGELEFLGRADDQVKIRGFRIE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 364 PEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLAR----FQQPVRWLTLP--PELKNGgiK 437
Cdd:cd17651 407 LGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALAThlpeYMVPSAFVLLDalPLTPNG--K 484
|
....*.
gi 446499693 438 ISRQAL 443
Cdd:cd17651 485 LDRRAL 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-443 |
3.44e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.09 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFAL----------VPDGENTFPALTSLHIQ-LVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQA---HLAS 162
Cdd:PRK12316 2098 DSGAALLLtqrhllerlpLPAGVARLPLDRDAEWAdYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGAlvaHCQA 2177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 163 AEGVLSLIPfGDHDDWLLSLPlFHVSGQGIMWRwLYAGARMTVRD------KQPLDQMLA-GCTHASLVPTQLWRLL--- 232
Cdd:PRK12316 2178 AGERYELSP-ADCELQFMSFS-FDGAHEQWFHP-LLNGARVLIRDdelwdpEQLYDEMERhGVTILDFPPVYLQQLAeha 2254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 -VNRSSVSLKAVLLGGAAIPVELTEQARE--QGIRCFCGYGLTEFASTV-----CAKEADGLADV--GSPLPGREVKIVN 302
Cdd:PRK12316 2255 eRDGRPPAVRVYCFGGEAVPAASLRLAWEalRPVYLFNGYGPTEAVVTPllwkcRPQDPCGAAYVpiGRALGNRRAYILD 2334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 D-----------EVWLRAASMAEGY-----------------------WRNGQLvplvndegwcaTRDRGEmhnGKLTIV 348
Cdd:PRK12316 2335 AdlnllapgmagELYLGGEGLARGYlnrpgltaerfvpdpfsasgerlYRTGDL-----------ARYRAD---GVVEYL 2400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVA-VVEYDQQTVDLGE---WVKDKLARFQQPVRW 424
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAyVVPDDAAEDLLAElraWLAARLPAYMVPAHW 2479
|
490
....*....|....*....
gi 446499693 425 LTLPPELKNGGIKISRQAL 443
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
17-443 |
4.76e-18 |
|
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: 85.95 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPvnpqlpqplleellp 96
Cdd:cd17644 15 DAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfaLVPDgentFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD 176
Cdd:cd17644 80 -------LDPN----YPQERLTYILEDAQISVLLTQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 177 DWLLSLPL-FHVSGQGIMWRWlYAGARMTVRDKQ---PLDQMLAGCTHASL----VPTQLWRLLVNRSSVS-------LK 241
Cdd:cd17644 149 RVLQFASIaFDVAAEEIYVTL-LSGATLVLRPEEmrsSLEDFVQYIQQWQLtvlsLPPAYWHLLVLELLLStidlpssLR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 242 AVLLGGAAIPVELTEQARE---QGIRCFCGYGLTE--FASTVCAKEADGLAD-----VGSPLPGREVKI----------- 300
Cdd:cd17644 228 LVIVGGEAVQPELVRQWQKnvgNFIQLINVYGPTEatIAATVCRLTQLTERNitsvpIGRPIANTQVYIldenlqpvpvg 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 VNDEVWLRAASMAEGYWRNGQLV-------PLVNDEG--WCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVERV 370
Cdd:cd17644 308 VPGELHIGGVGLARGYLNRPELTaekfishPFNSSESerLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 371 IAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQ--TVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17644 388 LSQHNDVKTAVVIVREDQPGNKRLVAyiVPHYEESpsTVELRQFLKAKLPDYMIPSAFVVLEelPLTPNG--KIDRRAL 464
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
132-450 |
7.02e-18 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 86.31 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHV-------------------SG--Q 190
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIyervnqivmlhygvavgfyQGdnL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 191 GIM-----------------WRWLYAGARMTVRDKQPLDQMLAGCTHAS--------LVPTQLW-RLLVNRSSVSL---- 240
Cdd:PLN02736 299 KLMddlaalrptifcsvprlYNRIYDGITNAVKESGGLKERLFNAAYNAkkqalengKNPSPMWdRLVFNKIKAKLggrv 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 241 KAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCA-KEADGL-ADVGSPLPGREVKIVN--------------- 302
Cdd:PLN02736 379 RFMSSGASPLSPDVMEFLRICfGGRVLEGYGMTETSCVISGmDEGDNLsGHVGSPNPACEVKLVDvpemnytsedqpypr 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 DEVWLRAASMAEGYWRNG-QLVPLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:PLN02736 459 GEICVRGPIIFKGYYKDEvQTREVIDEDGWLHTGDIGLwLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 380 VFIvpvADKEFGHRPVAVVEYDQQTV------------DLGEWVKDKLAR------------------FQQpVRWLTLPP 429
Cdd:PLN02736 539 CFV---YGDSLNSSLVAVVVVDPEVLkawaasegikyeDLKQLCNDPRVRaavladmdavgreaqlrgFEF-AKAVTLVP 614
|
410 420
....*....|....*....|....*...
gi 446499693 430 E---LKNG----GIKISRQALKEWVQRQ 450
Cdd:PLN02736 615 EpftVENGlltpTFKVKRPQAKAYFAKA 642
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
110-399 |
9.67e-18 |
|
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: 85.37 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 110 NTFPALTSLHIQLVEGAHAAAWQPTRLCSMTL-----TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL 184
Cdd:cd05931 120 PAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIaylqyTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 185 FH----VSGQGIMwrwLYAGAR---MTVRD--KQPLD--QMLA--GCTHaSLVPTQLWRLLVNRSSV---------SLKA 242
Cdd:cd05931 200 YHdmglIGGLLTP---LYSGGPsvlMSPAAflRRPLRwlRLISryRATI-SAAPNFAYDLCVRRVRDedlegldlsSWRV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 243 VLLGGaaipveltEQAREQGIRCF---------------CGYGLTE-----------------------FASTVCAKEAD 284
Cdd:cd05931 276 ALNGA--------EPVRPATLRRFaeafapfgfrpeafrPSYGLAEatlfvsggppgtgpvvlrvdrdaLAGRAVAVAAD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 285 G-----LADVGSPLPGREVKIVND------------EVWLRAASMAEGYWRNGQLVPLVN-------DEGWCATRDRGEM 340
Cdd:cd05931 348 DpaareLVSCGRPLPDQEVRIVDPetgrelpdgevgEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWLRTGDLGFL 427
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446499693 341 HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ-----VFIVPVADKEfghRPVAVVE 399
Cdd:cd05931 428 HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcvaAFSVPDDGEE---RLVVVAE 488
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
142-398 |
1.06e-17 |
|
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: 85.34 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLS-LPLFHV---SGQGIMwrwLYAGARMTVRDKQPL-DQML 215
Cdd:cd17639 96 TSGSTGNPKGVMLTHGNLVAGIAGLGDRVPeLLGPDDRYLAyLPLAHIfelAAENVC---LYRGGTIGYGSPRTLtDKSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 216 AGC---------THASLVP-----------------------------------------TQLWRLLV---------NRs 236
Cdd:cd17639 173 RGCkgdltefkpTLMVGVPaiwdtirkgvlaklnpmgglkrtlfwtayqsklkalkegpgTPLLDELVfkkvraalgGR- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 237 svsLKAVLLGGAAipveLTEQAREQGIRCFC----GYGLTEfasTVCAKEADGLAD-----VGSPLPGREVKIVN----- 302
Cdd:cd17639 252 ---LRYMLSGGAP----LSADTQEFLNIVLCpviqGYGLTE---TCAGGTVQDPGDletgrVGPPLPCCEIKLVDweegg 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 303 ---------DEVWLRAASMAEGYWRNGQLVPLV-NDEGWCATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQPEEVERV 370
Cdd:cd17639 322 ystdkppprGEILIRGPNVFKGYYKNPEKTKEAfDGDGWFHTGDIGEFHpDGTLKIIDRKKDLVkLQNGEYIALEKLESI 401
|
330 340
....*....|....*....|....*...
gi 446499693 371 IAAHPAVLQVFIVPVADKEFghrPVAVV 398
Cdd:cd17639 402 YRSNPLVNNICVYADPDKSY---PVAIV 426
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
17-447 |
3.15e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 83.50 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCArvdelASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAG-----AATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALV--PDGENTFPALT-SLHiqlVEGAHAAAWQPTRLCSMTL-TSGSTGLPKAAVHTYQA------HLASAEGV 166
Cdd:PRK07787 90 DSGAQAWLGpaPDDPAGLPHVPvRLH---ARSWHRYPEPDPDAPALIVyTSGTTGPPKGVVLSRRAiaadldALAEAWQW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 167 LSlipfgdhDDWLL-SLPLFHVSG--QGIMWRwLYAGARM--TVRDKqPLDQMLAGCTHASL---VPTQLWRLLVNRSSV 238
Cdd:PRK07787 167 TA-------DDVLVhGLPLFHVHGlvLGVLGP-LRIGNRFvhTGRPT-PEAYAQALSEGGTLyfgVPTVWSRIAADPEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 -SLK-AVLL--GGAAIPVELTEQ-AREQGIRCFCGYGLTEFASTVCAKeADG---LADVGSPLPGREVKIVND------- 303
Cdd:PRK07787 238 rALRgARLLvsGSAALPVPVFDRlAALTGHRPVERYGMTETLITLSTR-ADGerrPGWVGLPLAGVETRLVDEdggpvph 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ------EVWLRAASMAEGYW-RNGQLVPLVNDEGW-----CATRDRGEMHNgkltIVGRLD-NLFFSGGEGIQPEEVERV 370
Cdd:PRK07787 317 dgetvgELQVRGPTLFDGYLnRPDATAAAFTADGWfrtgdVAVVDPDGMHR----IVGREStDLIKSGGYRIGAGEIETA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 371 IAAHPAVLQVFIVPVADKEFGHRPVAVV--EYDQQTVDLGEWVKDKLARFQQP--VRWL-TLPpelKNGGIKISRQALKE 445
Cdd:PRK07787 393 LLGHPGVREAAVVGVPDDDLGQRIVAYVvgADDVAADELIDFVAQQLSVHKRPreVRFVdALP---RNAMGKVLKKQLLS 469
|
..
gi 446499693 446 WV 447
Cdd:PRK07787 470 EG 471
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-399 |
4.61e-17 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 83.26 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 29 NWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGA-------RVLPVNPQLPQPLLEELLPNLTLQ 101
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAichtvnpRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 102 FalVPDGENTFPALTSL----------HI------------QLVEGAHA-AAWQ---PTRLCSMTLTSGSTGLPKAAVHT 155
Cdd:PRK06018 121 F--VPILEKIADKLPSVeryvvltdaaHMpqttlknavayeEWIAEADGdFAWKtfdENTAAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 156 Y-----QAHLASAEGVLSLipfGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTV----RDKQPLDQMLAG--CTHASLV 224
Cdd:PRK06018 199 HrsnvlHALMANNGDALGT---SAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMpgakLDGASVYELLDTekVTFTAGV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 225 PTqLWRLLV------NRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFA--STVCA-----------KEADG 285
Cdd:PRK06018 276 PT-VWLMLLqymekeGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSplGTLAAlkppfsklpgdARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LADVGSPLPGREVKIVNDE-------------VWLRAASMAEGYWRNGQLVplVNDEGWCATRDRGEM-HNGKLTIVGRL 351
Cdd:PRK06018 355 LQKQGYPPFGVEMKITDDAgkelpwdgktfgrLKVRGPAVAAAYYRVDGEI--LDDDGFFDTGDVATIdAYGYMRITDRS 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446499693 352 DNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE 399
Cdd:PRK06018 433 KDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQ 480
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
142-444 |
1.08e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 82.10 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQML------ 215
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFwedlre 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 216 AGCTHASLVPT---QLWRLLVNRSSV-SLKAVLLGGAAIPVELTEQARE--QGIRCFCGYGLTE-FA--STVCA-KEADG 285
Cdd:cd05922 205 HGATGLAGVPStyaMLTRLGFDPAKLpSLRYLTQAGGRLPQETIARLREllPGAQVYVMYGQTEaTRrmTYLPPeRILEK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LADVGSPLPGREVKIVNDEVWL-----------RAASMAEGYWRNGQLVP-LVNDEGWCATRDRG-EMHNGKLTIVGRLD 352
Cdd:cd05922 285 PGSIGLAIPGGEFEILDDDGTPtppgepgeivhRGPNVMKGYWNDPPYRRkEGRGGGVLHTGDLArRDEDGFLFIVGRRD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 353 NLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADkEFGHRPVAVVEYDQQTV--DLGEWVKDKLARFQQP--VRWLTLP 428
Cdd:cd05922 365 RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDpkDVLRSLAERLPPYKVPatVRVVDEL 443
|
330
....*....|....*.
gi 446499693 429 PELKNGgiKISRQALK 444
Cdd:cd05922 444 PLTASG--KVDYAALR 457
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
17-443 |
2.24e-16 |
|
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: 81.16 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEEL 94
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDlvAVTLP--KGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 95 LPNLTLQFALVpDGENTFPALTSLHIQLVEGAHAAAW--------QPTRLCSMTLTSGSTGLPKAAVHTYQA-------- 158
Cdd:cd12114 80 LADAGARLVLT-DGPDAQLDVAVFDVLILDLDALAAPappppvdvAPDDLAYVIFTSGSTGTPKGVMISHRAalntildi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 159 ----HLASAEGVLSLIPFgDHDdwllsLPLFHVSGQgimwrwLYAGARMTV----RDKQPLDQMLAGCTHA----SLVPT 226
Cdd:cd12114 159 nrrfAVGPDDRVLALSSL-SFD-----LSVYDIFGA------LSAGATLVLpdeaRRRDPAHWAELIERHGvtlwNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 227 QLWRLL-----VNRSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFA--STVC--AKEADGLADV--GSPL 293
Cdd:cd12114 227 LLEMLLdvleaAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASiwSIYHpiDEVPPDWRSIpyGRPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 294 PGREVKIVND-----------EVWLRAASMAEGYWRNGQL-----VPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFF 356
Cdd:cd12114 307 ANQRYRVLDPrgrdcpdwvpgELWIGGRGVALGYLGDPELtaarfVTHPDGERLYRTGDLGRYrPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 357 SGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLA----RFQQPVRWLTLP--PE 430
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAqtlpAYMIPSRVIALEalPL 466
|
490
....*....|...
gi 446499693 431 LKNGgiKISRQAL 443
Cdd:cd12114 467 TANG--KVDRAAL 477
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
126-445 |
2.40e-16 |
|
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: 81.17 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 126 AHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIM-WRWLYAGARMT 204
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 205 vrdKQPLDQMLAGcthaslvPTQLWRL-----------------LVNRSS----------VSLKAVLLGG----AAIPVE 253
Cdd:cd05906 239 ---HVPTEEILAD-------PLRWLDLidryrvtitwapnfafaLLNDLLeeiedgtwdlSSLRYLVNAGeavvAKTIRR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 254 LTEQAREQGIRCFC---GYGLTEFAS-----TVCAKE----ADGLADVGSPLPGREVKIVNDE-----------VWLRAA 310
Cdd:cd05906 309 LLRLLEPYGLPPDAirpAFGMTETCSgviysRSFPTYdhsqALEFVSLGRPIPGVSMRIVDDEgqllpegevgrLQVRGP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 311 SMAEGYWRNgqlvPLVNDE-----GWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPV 385
Cdd:cd05906 389 VVTKGYYNN----PEANAEaftedGWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAF 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 386 AdkefgHRP-------VAVV---EYDQQ--TVDLGEWVKDKLARFQ--QPVRWLTLPPEL--KNGGIKISRQALKE 445
Cdd:cd05906 465 A-----VRDpgaeteeLAIFfvpEYDLQdaLSETLRAIRSVVSREVgvSPAYLIPLPKEEipKTSLGKIQRSKLKA 535
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
132-432 |
2.97e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 81.01 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGV-LSLIPFGD---HDDWLLS-LPLFHVSGQGIMWRWLYAGARM--- 203
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdLFMEQFEDkmtHDDVYLSfLPLAHILDRMIEEYFFRKGASVgyy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 204 -----TVRD-------------------------------------------KQPLDQMLAGCTHASLVPTQ---LWRLL 232
Cdd:PLN02430 298 hgdlnALRDdlmelkptllagvprvferihegiqkalqelnprrrlifnalyKYKLAWMNRGYSHKKASPMAdflAFRKV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 VNRSSVSLKAVLLGGAAIPVELTEQAReqgIRCFC----GYGLTE--------FASTVCAKEADGLADVGSPLPGREVKI 300
Cdd:PLN02430 378 KAKLGGRLRLLISGGAPLSTEIEEFLR---VTSCAfvvqGYGLTEtlgpttlgFPDEMCMLGTVGAPAVYNELRLEEVPE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 VN---------DEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQPEEVER 369
Cdd:PLN02430 455 MGydplgepprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILpNGVLKIIDRKKNLIkLSQGEYVALEYLEN 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 370 VIAAHPAVLQVFivpVADKEFGHRPVAVVEYDQQTVDlgEWVKDKlaRFQQPVRWLTLPPELK 432
Cdd:PLN02430 535 VYGQNPIVEDIW---VYGDSFKSMLVAVVVPNEENTN--KWAKDN--GFTGSFEELCSLPELK 590
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
122-398 |
4.26e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 80.66 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 122 LVEGAHAAAWQPT----RLCSMTLTSGSTGLPKAAV-HTYQAHLASAEGVLsLIPFGDHDDWLLSLPLFHVSGQGIMWRW 196
Cdd:PLN02479 179 LETGDPEFAWKPPadewQSIALGYTSGTTASPKGVVlHHRGAYLMALSNAL-IWGMNEGAVYLWTLPMFHCNGWCFTWTL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 197 -LYAGARMTVRD--KQPLDQMLA--GCTHASLVPTQLwRLLVNrSSVSLKA--------VLLGGAAIPVELTEQAREQGI 263
Cdd:PLN02479 258 aALCGTNICLRQvtAKAIYSAIAnyGVTHFCAAPVVL-NTIVN-APKSETIlplprvvhVMTAGAAPPPSVLFAMSEKGF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 264 RCFCGYGLTEF--ASTVCA--KEADGLA---------------------DV-----GSPLPGREVKIvnDEVWLRAASMA 313
Cdd:PLN02479 336 RVTHTYGLSETygPSTVCAwkPEWDSLPpeeqarlnarqgvryigleglDVvdtktMKPVPADGKTM--GEIVMRGNMVM 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 314 EGYWRNgqlvPLVNDE----GWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADK 388
Cdd:PLN02479 414 KGYLKN----PKANEEafanGWFHSGDLGVKHpDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE 489
|
330
....*....|
gi 446499693 389 EFGHRPVAVV 398
Cdd:PLN02479 490 RWGESPCAFV 499
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
137-398 |
4.80e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.14 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 137 CSMTLTSGSTGLPKAAV--------HTYQAHLASAEGVLSLipfgdhDDWLLSLPLFHVSGQGIMWRWLYAGARMTV--- 205
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALyshrstvlHAYGAALPDAMGLSAR------DAVLPVVPMFHVNAWGLPYSAPLTGAKLVLpgp 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 206 -RDKQPLDQMLA--GCTHASLVPTqLWRLLVN-------RSSvSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEF 274
Cdd:PRK07008 253 dLDGKSLYELIEaeRVTFSAGVPT-VWLGLLNhmreaglRFS-TLRRTVIGGSACPPAMIRTFEDEyGVEVIHAWGMTEM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 275 A--STVCAKEADGLADV-----------GSPLPGREVKIVND-------------EVWLRAASMAEGYWRNGQlVPLVNd 328
Cdd:PRK07008 331 SplGTLCKLKWKHSQLPldeqrkllekqGRVIYGVDMKIVGDdgrelpwdgkafgDLQVRGPWVIDRYFRGDA-SPLVD- 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446499693 329 eGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:PRK07008 409 -GWFPTGDVATIdADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVV 478
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
142-444 |
7.80e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.50 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVL----SLIPFGDHDD-WLLSLPLFHVSGQGIMWRWLYA-GARMTVRDKQPLDQML 215
Cdd:PLN02574 206 SSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNvYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASDMV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 216 A-----GCTHASLVPTQLWRLLVNRSSV------SLKAVLLGGAAipveLTEQAREQGIRCFC------GYGLTEFAST- 277
Cdd:PLN02574 286 KvidrfKVTHFPVVPPILMALTKKAKGVcgevlkSLKQVSCGAAP----LSGKFIQDFVQTLPhvdfiqGYGMTESTAVg 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 278 ---VCAKEADGLADVGSPLPGREVKIVN------------DEVWLRAASMAEGYWRNGQLVPL-VNDEGWCATRDRGEM- 340
Cdd:PLN02574 362 trgFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgncGELWIQGPGVMKGYLNNPKATQStIDKDGWLRTGDIAYFd 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 341 HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLA 416
Cdd:PLN02574 442 EDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTlsqeAVINYVAKQVA 521
|
330 340
....*....|....*....|....*...
gi 446499693 417 RFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:PLN02574 522 PYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
17-443 |
8.77e-16 |
|
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: 79.05 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellp 96
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPID------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 nltlqfalvPDgentFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQ--AHLASA---EGVLSLIP 171
Cdd:cd17650 69 ---------PD----YPAERLQYMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRnvAHAAHAwrrEYELDSFP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 172 FGdhddwLLSLPLFHVS-GQGIMWRWLYAGARM------TVRDKQPLDQML--AGCTHASLVPTQLWRLL--VNRSSV-- 238
Cdd:cd17650 136 VR-----LLQMASFSFDvFAGDFARSLLNGGTLvicpdeVKLDPAALYDLIlkSRITLMESTPALIRPVMayVYRNGLdl 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 -SLKAVLLGG----AAIPVELTEQAReQGIRCFCGYGLTEFA--STVCAKEADGLAD-----VGSPLPGREVKIVND--- 303
Cdd:cd17650 211 sAMRLLIVGSdgckAQDFKTLAARFG-QGMRIINSYGVTEATidSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDErlq 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd17650 290 pqpvgvagELYIGGAGVARGYLNRPELTaerfvenPFAPGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQ--TVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17650 370 ESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATlnTAELRAFLAKELPSYMIPSYYVQLDalPLTPNG--KVDRRAL 447
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-451 |
1.13e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 79.31 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 136 LCSMTLTSGSTGLPKAAVHTYQAHLASA-EGVLSLIPFGDHDDWLLS-LPLFHVSGQ-GIMWRWLYAGARMTVRDKQPLD 212
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNLVSNTlMGVQWLYNCKEGEEVVLGvLPFFHVYGMtAVMNLSIMQGYKMVLIPKFDMK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 213 QMLAGCTH--ASLVP--TQLWRLLVNRSSV------SLKAVLLGGAAIPVELTEQ-AREQGIRCFCGYGLTEFASTVCAK 281
Cdd:PRK06710 288 MVFEAIKKhkVTLFPgaPTIYIALLNSPLLkeydisSIRACISGSAPLPVEVQEKfETVTGGKLVEGYGLTESSPVTHSN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 282 ---EADGLADVGSPLPGREVKIVN------------DEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKL 345
Cdd:PRK06710 368 flwEKRVPGSIGVPWPDTEAMIMSletgealppgeiGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMdEDGFF 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 346 TIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQP 421
Cdd:PRK06710 448 YVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTEcseeELNQFARKYLAAYKVP 527
|
330 340 350
....*....|....*....|....*....|.
gi 446499693 422 vRWLTLPPELKNGGI-KISRQALKEWVQRQQ 451
Cdd:PRK06710 528 -KVYEFRDELPKTTVgKILRRVLIEEEKRKN 557
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
239-421 |
1.41e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTEQARE-QGIRCFCGYGLTEFASTVCAKEADG--LADVGSPLPGREVKIVND-----------E 304
Cdd:PRK05677 327 ALKLTLSGGMALQLATAERWKEvTGCAICEGYGMTETSPVVSVNPSQAiqVGTIGIPVPSTLCKVIDDdgnelplgevgE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 305 VWLRAASMAEGYW-RNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFI 382
Cdd:PRK05677 407 LCVKGPQVMKGYWqRPEATDEILDSDGWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446499693 383 VPVADKEFG-HRPVAVVEYDQQTVD---LGEWVKDKLARFQQP 421
Cdd:PRK05677 487 IGVPDEKSGeAIKVFVVVKPGETLTkeqVMEHMRANLTGYKVP 529
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-445 |
1.84e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 79.43 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 8 WRHWRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLP 87
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 88 QPLLEELLPNLTLQFAL----------VPDGentfpaLTSLHIQ----LVEGAHAA----AWQPTRLCSMTLTSGSTGLP 149
Cdd:PRK12467 598 QDRLAYMLDDSGVRLLLtqshllaqlpVPAG------LRSLCLDepadLLCGYSGHnpevALDPDNLAYVIYTSGSTGQP 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 150 KAAVHTYQAHLASAEGVLSLIPFGDHDDWLL-SLPLFHVSGQGIMWRwLYAGARMTVRDKQPL---DQMLA-----GCTH 220
Cdd:PRK12467 672 KGVAISHGALANYVCVIAERLQLAADDSMLMvSTFAFDLGVTELFGA-LASGATLHLLPPDCArdaEAFAAlmadqGVTV 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 221 ASLVPTQlWRLLVNRSSV----SLKAVLLGGAAIPVELTEQARE--QGIRCFCGYGLTEFASTV----CAKEA--DGLAD 288
Cdd:PRK12467 751 LKIVPSH-LQALLQASRValprPQRALVCGGEALQVDLLARVRAlgPGARLINHYGPTETTVGVstyeLSDEErdFGNVP 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 289 VGSPLPGREVKI-----------VNDEVWLRAASMAEGYWRNGQLV-------PLVNDEGWC-ATRDRGEMH-NGKLTIV 348
Cdd:PRK12467 830 IGQPLANLGLYIldhylnpvpvgVVGELYIGGAGLARGYHRRPALTaerfvpdPFGADGGRLyRTGDLARYRaDGVIEYL 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVpVADKEFGHRPVAVVEYDQQTVD-----LGEWVKDKLAR----FQ 419
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL-AQPGDAGLQLVAYLVPAAVADGaehqaTRDELKAQLRQvlpdYM 988
|
490 500
....*....|....*....|....*...
gi 446499693 420 QPVRWLTLP--PELKNGgiKISRQALKE 445
Cdd:PRK12467 989 VPAHLLLLDslPLTPNG--KLDRKALPK 1014
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
19-443 |
2.99e-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: 77.59 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNpqlpqplleellpnl 98
Cdd:cd17645 15 VAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID--------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 99 tlqfalvPDgentFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDw 178
Cdd:cd17645 80 -------PD----YPGERIAYMLADSSAKILLTNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 179 llSLPLFHVSGQGIMWR---WLYAGARMTVRD---KQPLDQMLAGC-THA---SLVPTQLWRLLVNRSSVSLKAVLLGGA 248
Cdd:cd17645 148 --SLVYASFSFDASAWEifpHLTAGAALHVVPserRLDLDALNDYFnQEGitiSFLPTGAAEQFMQLDNQSLRVLLTGGD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 249 AIPVelteqAREQGIRCFCGYGLTEFASTVCAKEAD---GLADVGSPLPGREVKIVND-----------EVWLRAASMAE 314
Cdd:cd17645 226 KLKK-----IERKGYKLVNNYGPTENTVVATSFEIDkpyANIPIGKPIDNTRVYILDEalqlqpigvagELCIAGEGLAR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 315 GYWRNGQLV-------PLVNDEGWCATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVA 386
Cdd:cd17645 301 GYLNRPELTaekfivhPFVPGERMYRTGDLAKFLPdGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 387 DKefGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17645 381 DA--DGRKYLVAYVTAPEEipheELREWLKNDLPDYMIPTYFVHLKalPLTANG--KVDRKAL 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
142-445 |
6.96e-15 |
|
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: 76.80 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIpFGDH---DDWLLS-LPLFHVSGQGIMWRWLYAGAR---MTVRDKQPLDQM 214
Cdd:cd17642 192 SSGSTGLPKGVQLTHKNIVARFSHARDPI-FGNQiipDTAILTvIPFHHGFGMFTTLGYLICGFRvvlMYKFEEELFLRS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 215 LAG--CTHASLVPTQLWRL----LVNRSSVS-LKAVLLGGAAIPVELTEQAREQ----GIRCfcGYGLTEFASTVCA--K 281
Cdd:cd17642 271 LQDykVQSALLVPTLFAFFakstLVDKYDLSnLHEIASGGAPLSKEVGEAVAKRfklpGIRQ--GYGLTETTSAILItpE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 282 EADGLADVGSPLPGREVKIVN------------DEVWLRAASMAEGYWRNGQLV-PLVNDEGWCATRDRGEMHN-GKLTI 347
Cdd:cd17642 349 GDDKPGAVGKVVPFFYAKVVDldtgktlgpnerGELCVKGPMIMKGYVNNPEATkALIDKDGWLHSGDIAYYDEdGHFFI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 348 VGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVeYDQQTVDLGE-----WVKDKLA---RFQ 419
Cdd:cd17642 429 VDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV-VLEAGKTMTEkevmdYVASQVStakRLR 507
|
330 340
....*....|....*....|....*.
gi 446499693 420 QPVRWLTLPPelKNGGIKISRQALKE 445
Cdd:cd17642 508 GGVKFVDEVP--KGLTGKIDRRKIRE 531
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
239-445 |
8.59e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.45 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTEQARE-QGIRCFCGYGLTEFASTVCA-----KEADGlaDVGSPLPGREVKIVND--------- 303
Cdd:PRK08751 330 SLKMTLGGGMAVQRSVAERWKQvTGLTLVEAYGLTETSPAACInpltlKEYNG--SIGLPIPSTDACIKDDagtvlaige 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --EVWLRAASMAEGYWRNGQLVPLVND-EGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:PRK08751 408 igELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMdEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 380 VFIVPVADKEFGHR-PVAVVEYDQQTV--DLGEWVKDKLARFQQPvRWLTLPPELKNGGI-KISRQALKE 445
Cdd:PRK08751 488 VAAVGVPDEKSGEIvKVVIVKKDPALTaeDVKAHARANLTGYKQP-RIIEFRKELPKTNVgKILRRELRD 556
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
142-446 |
8.81e-15 |
|
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: 76.00 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQA---HLASAEGVLSLIPfgdhDD--WLLSLPLFhVSGQ--GIMWRWLYaGARMTVRDKQ----- 209
Cdd:cd05969 97 TSGTTGTPKGVLHVHDAmifYYFTGKYVLDLHP----DDiyWCTADPGW-VTGTvyGIWAPWLN-GVTNVVYEGRfdaes 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 210 ---PLDQMlaGCTHASLVPTQLWRLLvnRSSV---------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFAS 276
Cdd:cd05969 171 wygIIERV--KVTVWYTAPTAIRMLM--KEGDelarkydlsSLRFIHSVGEPLNPEAIRWGMEVfGVPIHDTWWQTETGS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 277 TVCAKEADGLADVGS---PLPGREVKIVNDE-----------VWLRAA--SMAEGYWRNGQLVPLVNDEGWCATRDRGEM 340
Cdd:cd05969 247 IMIANYPCMPIKPGSmgkPLPGVKAAVVDENgnelppgtkgiLALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY-------DQQTVDLGEWVK 412
Cdd:cd05969 327 dEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLkegfepsDELKEEIINFVR 406
|
330 340 350
....*....|....*....|....*....|....*.
gi 446499693 413 DKLARFQQP--VRWLTLPPELKNGgiKISRQALKEW 446
Cdd:cd05969 407 QKLGAHVAPreIEFVDNLPKTRSG--KIMRRVLKAK 440
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
17-445 |
1.58e-14 |
|
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: 75.04 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd17653 12 DAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALVPDGENtfpaltslhiqlvEGAHAAAwqptrlcsmtlTSGSTGLPKAAVHTYQA--HLASAEGVLSLIPFGD 174
Cdd:cd17653 92 TSGATLLLTTDSPD-------------DLAYIIF-----------TSGSTGIPKGVMVPHRGvlNYVSQPPARLDVGPGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 175 HDDWLLSlPLFHVSgQGIMWRWLYAGARMTVRD-KQPLDQMLAGCTHASLVPTQLWRLLVNRSSvSLKAVLLGGAAIPVE 253
Cdd:cd17653 148 RVAQVLS-IAFDAC-IGEIFSTLCNGGTLVLADpSDPFAHVARTVDALMSTPSILSTLSPQDFP-NLKTIFLGGEAVPPS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 254 LTEQAREqGIRCFCGYGLTEfaSTVCAKEADGLADV----GSPLPG----------REVKI-VNDEVWLRAASMAEGYWR 318
Cdd:cd17653 225 LLDRWSP-GRRLYNAYGPTE--CTISSTMTELLPGQpvtiGKPIPNstcyildadlQPVPEgVVGEICISGVQVARGYLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 319 NGQL-------VPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVI-AAHPAVLQVFIVPVADke 389
Cdd:cd17653 302 NPALtaskfvpDPFWPGSRMYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAIVVNG-- 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446499693 390 fghRPVAVVEydQQTVDLgEWVKDKLAR----FQQPVRWLTLP--PELKNGgiKISRQALKE 445
Cdd:cd17653 380 ---RLVAFVT--PETVDV-DGLRSELAKhlpsYAVPDRIIALDsfPLTANG--KVDRKALRE 433
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
24-445 |
2.27e-14 |
|
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: 75.22 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 24 NDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfA 103
Cdd:cd05970 44 EERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIK-M 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 104 LVPDGENTFPaltslhiQLVEGAHAAAWQPTRL---------------------------------------CSMTLTSG 144
Cdd:cd05970 123 IVAIAEDNIP-------EEIEKAAPECPSKPKLvwvgdpvpegwidfrkliknaspdferptansypcgediLLVYFSSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 145 STGLPK--AAVHTYQ-AHLASAEGVLSLIPFGDHddwllslplFHVSGQG---IMWRWLY----AGARMTVRDKQPLD-- 212
Cdd:cd05970 196 TTGMPKmvEHDFTYPlGHIVTAKYWQNVREGGLH---------LTVADTGwgkAVWGKIYgqwiAGAAVFVYDYDKFDpk 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 213 QMLA-----GCTHASLVPTqLWRLLVnRSSVS------LKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTV-- 278
Cdd:cd05970 267 ALLEklskyGVTTFCAPPT-IYRFLI-REDLSrydlssLRYCTTAGEALNPEVFNTFKEKtGIKLMEGFGQTETTLTIat 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 279 --CAKEADGlaDVGSPLPGREVKIVND-----------EVWLRAAS-----MAEGYWRNGQLVPLVNDEGWCATRDRGEM 340
Cdd:cd05970 345 fpWMEPKPG--SMGKPAPGYEIDLIDRegrsceageegEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWM 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV----EY---DQQTVDLGEWVK 412
Cdd:cd05970 423 dEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIvlakGYepsEELKKELQDHVK 502
|
490 500 510
....*....|....*....|....*....|....
gi 446499693 413 DKLARFQQPvRWLTLPPEL-KNGGIKISRQALKE 445
Cdd:cd05970 503 KVTAPYKYP-RIVEFVDELpKTISGKIRRVEIRE 535
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
239-391 |
2.29e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 75.09 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTEQARE-QGIRCFCGYGLTEFASTVCA-----KEADGlaDVGSPLPGREVKIVND--------- 303
Cdd:PRK08974 326 SLKLSVGGGMAVQQAVAERWVKlTGQYLLEGYGLTECSPLVSVnpydlDYYSG--SIGLPVPSTEIKLVDDdgnevppge 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK08974 404 pgELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
170
....*....|.
gi 446499693 381 FIVPVADKEFG 391
Cdd:PRK08974 484 AAVGVPSEVSG 494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
25-451 |
2.42e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.94 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQ-----------------------CGARVLP 81
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRsglyytpinwhltaaeiayivddSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 82 VNP--QLPQPLLEELLPNLTLQFALV---PDGENTFPAltslhiqlvegahAAAWQPTRL-------CSMTLTSGSTGLP 149
Cdd:PRK08276 89 VSAalADTAAELAAELPAGVPLLLVVagpVPGFRSYEE-------------ALAAQPDTPiadetagADMLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 150 K----AAVHTYQAHLASAEGVLSLIPFGDHDD--WLLSLPLFHVS-GQGIMWRwLYAGARMTVRDKQPLDQMLAG----- 217
Cdd:PRK08276 156 KgikrPLPGLDPDEAPGMMLALLGFGMYGGPDsvYLSPAPLYHTApLRFGMSA-LALGGTVVVMEKFDAEEALALieryr 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 CTHASLVPTQLWRLLV------NRSSVS-LKAVLLGGAAIPVELTEQ--------------AREQGircfcgyGLTeFAS 276
Cdd:PRK08276 235 VTHSQLVPTMFVRMLKlpeevrARYDVSsLRVAIHAAAPCPVEVKRAmidwwgpiiheyyaSSEGG-------GVT-VIT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 277 TVCAKEADG------------LADVGSPLPGREVKIV------------NDEVWLRAAsmaegywrngqlvplVNDEGWC 332
Cdd:PRK08276 307 SEDWLAHPGsvgkavlgevriLDEDGNELPPGEIGTVyfemdgypfeyhNDPEKTAAA---------------RNPHGWV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 333 ATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE-------YDQQT 404
Cdd:PRK08276 372 TVGDVGYLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQpadgadaGDALA 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446499693 405 VDLGEWVKDKLARFQQPvRWLTLPPEL---KNGgiKISRQALKE--WVQRQQ 451
Cdd:PRK08276 452 AELIAWLRGRLAHYKCP-RSIDFEDELprtPTG--KLYKRRLRDryWEGRQR 500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
12-443 |
3.05e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.58 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQV--RGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQP 89
Cdd:PRK12467 3103 AQVarTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 90 LLEELLPNLTLQFALVPDG-ENTFPALTSLHIQLVEGAH---------AAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAH 159
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLTQAHlLEQLPAPAGDTALTLDRLDlngysennpSTRVMGENLAYVIYTSGSTGKPKGVGVRHGAL 3262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 160 LASAEGVLSLIPFGDHDDWLLSLPLfhvSGQGIMWRW---LYAGARMTVRDKQPLD------QMLA-GCTHASLVPTQLW 229
Cdd:PRK12467 3263 ANHLCWIAEAYELDANDRVLLFMSF---SFDGAQERFlwtLICGGCLVVRDNDLWDpeelwqAIHAhRISIACFPPAYLQ 3339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 230 RLLVN---RSSVSLKAVLLGGAAIPVELTEQAREQGIR--CFCGYGLTEFASTV----CAKEADGLAD---VGSPLPGRE 297
Cdd:PRK12467 3340 QFAEDaggADCASLDIYVFGGEAVPPAAFEQVKRKLKPrgLTNGYGPTEAVVTVtlwkCGGDAVCEAPyapIGRPVAGRS 3419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 298 VKI-----------VNDEVWLRAASMAEGYWRNGQLVP---LVNDEGWCATR--DRGEM----HNGKLTIVGRLDNLFFS 357
Cdd:PRK12467 3420 IYVldgqlnpvpvgVAGELYIGGVGLARGYHQRPSLTAerfVADPFSGSGGRlyRTGDLaryrADGVIEYLGRIDHQVKI 3499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 358 GGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVAVVEYDQQTVDLGEWVKDKLA----RFQQPVRWLTLP--PEL 431
Cdd:PRK12467 3500 RGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAaslpDYMVPAQLLVLAamPLG 3578
|
490
....*....|..
gi 446499693 432 KNGgiKISRQAL 443
Cdd:PRK12467 3579 PNG--KVDRKAL 3588
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
142-421 |
3.30e-14 |
|
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: 73.49 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGAR--MTVR-DKQPLDQMLA-- 216
Cdd:cd17636 8 TAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTnvFVRRvDAEEVLELIEae 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 GCTHASLV-PTQLWRLLVNRSSV----SLKAVL---LGGAAIPVELTEQAREQGircfcGYGLTEFA--STVCAKEADGL 286
Cdd:cd17636 88 RCTHAFLLpPTIDQIVELNADGLydlsSLRSSPaapEWNDMATVDTSPWGRKPG-----GYGQTEVMglATFAALGGGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 287 ADVGSPLPGREVKIVND-----------EVWLRAASMAEGYWRNgqlvPLVNDE----GWCATRDRGEMH-NGKLTIVGR 350
Cdd:cd17636 163 GGAGRPSPLVQVRILDEdgrevpdgevgEIVARGPTVMAGYWNR----PEVNARrtrgGWHHTNDLGRREpDGSLSFVGP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 351 LDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV--EYDQQTV--DLGEWVKDKLARFQQP 421
Cdd:cd17636 239 KTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVvlKPGASVTeaELIEHCRARIASYKKP 313
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-443 |
3.56e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.38 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE 3151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALvpdgenTFPALTSLHIQLV---------EGAHAAAWQ----PTRLCSMTLTSGSTGLPKAAVHTYQAHLASA 163
Cdd:PRK12316 3152 DSGAQLLL------SQSHLRLPLAQGVqvldldrgdENYAEANPAirtmPENLAYVIYTSGSTGKPKGVGIRHSALSNHL 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 164 EGVLSLIPFGDhDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVRDKQP----------LDQMLAGCTHAslVPTQLWRLL 232
Cdd:PRK12316 3226 CWMQQAYGLGV-GDRVLQFTTFSFDVFVEELFWpLMSGARVVLAGPEDwrdpallvelINSEGVDVLHA--YPSMLQAFL 3302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 VN---RSSVSLKAVLLGGAAIPVELTEQAREQGiRCFCGYGLTEFASTV----CAKEADGLADVGSPLPGREVKIVND-- 303
Cdd:PRK12316 3303 EEedaHRCTSLKRIVCGGEALPADLQQQVFAGL-PLYNLYGPTEATITVthwqCVEEGKDAVPIGRPIANRACYILDGsl 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ---------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEE 366
Cdd:PRK12316 3382 epvpvgalgELYLGGEGLARGYHNRPGLTaerfvpdPFVPGERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGE 3461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 367 VERVIAAHPAVLQVFIVPVAdkefGHRPVAVVEYDQQTVDLGEWVKDKLAR----FQQPVRWLTLP--PELKNGgiKISR 440
Cdd:PRK12316 3462 IEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKAslpeYMVPAHLLFLErmPLTPNG--KLDR 3535
|
...
gi 446499693 441 QAL 443
Cdd:PRK12316 3536 KAL 3538
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
106-329 |
1.27e-13 |
|
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: 72.85 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 106 PDGENT--FPALTSLHIQL-VEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD-----D 177
Cdd:cd05921 135 VAGRGAisFAELAATPPTAaVDAAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppvlvD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 178 WLlslPLFHVSGQGIMWRW-LYAGARMTVRDKQPLDQMLAGC---------THASLVPTQlWRLLVN--------RSSV- 238
Cdd:cd05921 214 WL---PWNHTFGGNHNFNLvLYNGGTLYIDDGKPMPGGFEETlrnlreispTVYFNVPAG-WEMLVAalekdealRRRFf 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 -SLKAVLLGGAAIP-------VELTEQAREQGIRCFCGYGLTEFA--STVCAKEADGLADVGSPLPGREVKIV-ND---E 304
Cdd:cd05921 290 kRLKLMFYAGAGLSqdvwdrlQALAVATVGERIPMMAGLGATETAptATFTHWPTERSGLIGLPAPGTELKLVpSGgkyE 369
|
250 260
....*....|....*....|....*
gi 446499693 305 VWLRAASMAEGYWRNGQLVPLVNDE 329
Cdd:cd05921 370 VRVKGPNVTPGYWRQPELTAQAFDE 394
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-421 |
1.28e-13 |
|
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: 72.03 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 139 MTLTSGSTGLPKAAV-HTYQAHLASAEGvlslIPFGDHDD-----------------WLLSLPLFHVSGqgiMWRWLYA- 199
Cdd:cd05924 8 ILYTGGTTGMPKGVMwRQEDIFRMLMGG----ADFGTGEFtpsedahkaaaaaagtvMFPAPPLMHGTG---SWTAFGGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 200 ---GARMTVRDKQPLDQMLA-----GCTHASLVPTQLWRLLV-------NRSSVSLKAVLLGGAAipveLTEQAREQGIR 264
Cdd:cd05924 81 lggQTVVLPDDRFDPEEVWRtiekhKVTSMTIVGDAMARPLIdalrdagPYDLSSLFAISSGGAL----LSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 265 C------FCGYGLTEFASTVCAKEADGLADVGS---PLP--------GREVKIVNDEV-WL-RAASMAEGYWRN----GQ 321
Cdd:cd05924 157 LvpnitlVDAFGSSETGFTGSGHSAGSGPETGPftrANPdtvvldddGRVVPPGSGGVgWIaRRGHIPLGYYGDeaktAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 322 LVPLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY 400
Cdd:cd05924 237 TFPEVDGVRYAVPGDRATvEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQL 316
|
330 340
....*....|....*....|....*
gi 446499693 401 DQ-QTVDLGE---WVKDKLARFQQP 421
Cdd:cd05924 317 REgAGVDLEElreHCRTRIARYKLP 341
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
139-377 |
1.33e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 72.72 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 139 MTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLS-LPLFHVSGqgiMWRWLyagarmTVrdkqpldQMLAG 217
Cdd:PRK07768 157 MQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSwLPLFHDMG---MVGFL------TV-------PMYFG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 CTHASLVPTQ------LWRLLVN--RSSV---------------------------SLKAVLLGGAAIPV----ELTEQA 258
Cdd:PRK07768 221 AELVKVTPMDflrdplLWAELISkyRGTMtaapnfayallarrlrrqakpgafdlsSLRFALNGAEPIDPadveDLLDAG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 259 REQGIR---CFCGYGLTE----------------------------FASTVCAKEADGLADVGSPLPGREVKIVND---- 303
Cdd:PRK07768 301 ARFGLRpeaILPAYGMAEatlavsfspcgaglvvdevdadllaalrRAVPATKGNTRRLATLGPPLPGLEVRVVDEdgqv 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -------EVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHP 375
Cdd:PRK07768 381 lpprgvgVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYlTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVE 460
|
..
gi 446499693 376 AV 377
Cdd:PRK07768 461 GV 462
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
239-421 |
2.03e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 72.15 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTEQ------AREQGIrcfcGYGLTEfASTV-CAKEADGLAD-----VGSPLPGREVKIVND--- 303
Cdd:PRK08315 316 SLRTGIMAGSPCPIEVMKRvidkmhMSEVTI----AYGMTE-TSPVsTQTRTDDPLEkrvttVGRALPHLEVKIVDPetg 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 ---------EVWLRAASMAEGYWRNgqlvP-----LVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVE 368
Cdd:PRK08315 391 etvprgeqgELCTRGYSVMKGYWND----PektaeAIDADGWMHTGDLAVMdEEGYVNIVGRIKDMIIRGGENIYPREIE 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 369 RVIAAHPAVLQVFIVPVADKEFGHRPVAVV------EYDQQtvDLGEWVKDKLARFQQP 421
Cdd:PRK08315 467 EFLYTHPKIQDVQVVGVPDEKYGEEVCAWIilrpgaTLTEE--DVRDFCRGKIAHYKIP 523
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
17-445 |
2.32e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 72.68 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK12316 4566 DAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMME 4645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFAL----------VPDGentfpaLTSLHIQLVE-----GAH--AAAWQPTRLCSMTLTSGSTGLPKAAVHTYQ-- 157
Cdd:PRK12316 4646 DSGAALLLtqshllqrlpIPDG------LASLALDRDEdwegfPAHdpAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGsl 4719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 158 -AHLASAEGVLSLIPfgdhDDWLLSLPLFHVSGQGIMWRW-LYAGARMTVRDKQPLD------QML-AGCTHASLVPTQL 228
Cdd:PRK12316 4720 vNHLHATGERYELTP----DDRVLQFMSFSFDGSHEGLYHpLINGASVVIRDDSLWDperlyaEIHeHRVTVLVFPPVYL 4795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 229 WRLL----VNRSSVSLKAVLLGGAAIPVELTEQA--REQGIRCFCGYGLTEFASTV-CAKEADGLAD------VGSPLPG 295
Cdd:PRK12316 4796 QQLAehaeRDGEPPSLRVYCFGGEAVAQASYDLAwrALKPVYLFNGYGPTETTVTVlLWKARDGDACgaaympIGTPLGN 4875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 296 REVKIVND-----------EVWLRAASMAEGYWRNGQL-----VPLVNDEGWCATRDRGEM----HNGKLTIVGRLDNLF 355
Cdd:PRK12316 4876 RSGYVLDGqlnplpvgvagELYLGGEGVARGYLERPALtaerfVPDPFGAPGGRLYRTGDLaryrADGVIDYLGRVDHQV 4955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 356 FSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVA-VVEYDQQTVD-----------LGEWVKDKLARFQQPVR 423
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVREAVVIAQ-EGAVGKQLVGyVVPQDPALADadeaqaelrdeLKAALRERLPEYMVPAH 5034
|
490 500
....*....|....*....|....
gi 446499693 424 WLTLP--PELKNGgiKISRQALKE 445
Cdd:PRK12316 5035 LVFLArmPLTPNG--KLDRKALPQ 5056
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
142-406 |
5.16e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 71.49 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSG-QGIMWRWLYAGARMtVRDKQPLDqmlaGCTH 220
Cdd:PRK08633 790 SSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGlTVTLWLPLLEGIKV-VYHPDPTD----ALGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 221 ASLV-----------PTQLwRLLVNRSSV------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK08633 865 AKLVakhratillgtPTFL-RLYLRNKKLhplmfaSLRLVVAGAEKLKPEVADAFEEKfGIRILEGYGATETSPVASVNL 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 283 ADGLAD------------VGSPLPGREVKIVNDE------------VWLRAASMAEGYWRNGQL----VPLVNDEGWCAT 334
Cdd:PRK08633 944 PDVLAAdfkrqtgskegsVGMPLPGVAVRIVDPEtfeelppgedglILIGGPQVMKGYLGDPEKtaevIKDIDGIGWYVT 1023
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446499693 335 RDRGEM-HNGKLTIVGRLDNlfFS--GGEGIQPEEVE-RVIAAHPAVLQVFIVP-VADKEFGHRPVAVVEYDQQTVD 406
Cdd:PRK08633 1024 GDKGHLdEDGFLTITDRYSR--FAkiGGEMVPLGAVEeELAKALGGEEVVFAVTaVPDEKKGEKLVVLHTCGAEDVE 1098
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
138-445 |
9.60e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 69.73 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 138 SMTLTSGSTGLPK----AAVHTYQAhlASAEGVLSLIpFGDHDDW--LLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPL 211
Cdd:PRK12406 156 SMIYTSGTTGHPKgvrrAAPTPEQA--AAAEQMRALI-YGLKPGIraLLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQMLA-----GCTHASLVPTQLWRLLVNRSSV-------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTV 278
Cdd:PRK12406 233 EELLQlierhRITHMHMVPTMFIRLLKLPEEVrakydvsSLRHVIHAAAPCPADVKRAMIEWwGPVIYEYYGSTESGAVT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 279 CAKEADGLA---DVGSPLPGREVKIVND-----------EVWLRAASMAE-GYWRNGQLVPLVNDEGWCATRDRGEMH-N 342
Cdd:PRK12406 313 FATSEDALShpgTVGKAAPGAELRFVDEdgrplpqgeigEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDaD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 343 GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEYDQQ-TVDLGE---WVKDKLARF 418
Cdd:PRK12406 393 GYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGaTLDEADiraQLKARLAGY 472
|
330 340 350
....*....|....*....|....*....|
gi 446499693 419 QQPVRWL---TLPPElkNGGiKISRQALKE 445
Cdd:PRK12406 473 KVPKHIEimaELPRE--DSG-KIFKRRLRD 499
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
30-414 |
1.21e-12 |
|
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: 69.76 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 30 WRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFALVPDGE 109
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 110 ----------------------------------NTFP-------ALTSLHIQLVEGAHAAAwQPTRLCSMTLTSGSTGL 148
Cdd:cd17641 94 qvdklleiadripsvryviycdprgmrkyddprlISFEdvvalgrALDRRDPGLYEREVAAG-KGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 149 PKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL------FHVSGQGI------------------------------ 192
Cdd:cd17641 173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLpwigeqMYSVGQALvcgfivnfpeepetmmedlreigptfvllp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 193 --MWRWLYAGARMTVRDKQPLDQML----------AGCTHASLVPTQLW-------------RLLVNRSSVS-LKAVLLG 246
Cdd:cd17641 253 prVWEGIAADVRARMMDATPFKRFMfelgmklglrALDRGKRGRPVSLWlrlaswladallfRPLRDRLGFSrLRSAATG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 247 GAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAkEADGLAD---VGSPLPGREVKIVND-EVWLRAASMAEGYWRNGQ- 321
Cdd:cd17641 333 GAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTV-HRDGDVDpdtVGVPFPGTEVRIDEVgEILVRSPGVFVGYYKNPEa 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 322 LVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLF-FSGGEGIQPEEVERVIAAHPAVLQVFIvpvadkeFGH-RP--VA 396
Cdd:cd17641 412 TAEDFDEDGWLHTGDAGYFkENGHLVVIDRAKDVGtTSDGTRFSPQFIENKLKFSPYIAEAVV-------LGAgRPylTA 484
|
490
....*....|....*...
gi 446499693 397 VVEYDQQTVdlGEWVKDK 414
Cdd:cd17641 485 FICIDYAIV--GKWAEQR 500
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
19-399 |
1.68e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 69.29 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 19 IALRLNDEQLNWRELCARVDELASGFAAQGVVEGS---GVMLRawNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELL 95
Cdd:PRK13388 18 IAVRYGDRTWTWREVLAEAAARAAALIALADPDRPlhvGVLLG--NTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 96 PNLTLQFaLVPDGEN-------TFPALTSL------HIQLVEGAHAA----AWQPTRLCSMTLTSGSTGLPKAaVHTYQA 158
Cdd:PRK13388 96 RRADCQL-LVTDAEHrplldglDLPGVRVLdvdtpaYAELVAAAGALtphrEVDAMDPFMLIFTSGTTGAPKA-VRCSHG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 159 HLASAEGVL----SLIPfgdHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVRDK----------------------Q 209
Cdd:PRK13388 174 RLAFAGRALterfGLTR---DDVCYVSMPLFH--SNAVMAGWapaVASGAAVALPAKfsasgflddvrrygatyfnyvgK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 210 PLDQMLAGCTHASLVPTQLwrllvnrssvslkAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADV 289
Cdd:PRK13388 249 PLAYILATPERPDDADNPL-------------RVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 290 GSPLPGreVKIVNDE--------------------------VWLRAASMAEGYWrngqlvplvNDEGWCATRDRGEMH-N 342
Cdd:PRK13388 316 GRGAPG--VAIYNPEtltecavarfdahgallnadeaigelVNTAGAGFFEGYY---------NNPEATAERMRHGMYwS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 343 GKLTIVGRLDNLFFSG---------GEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVE 399
Cdd:PRK13388 385 GDLAYRDADGWIYFAGrtadwmrvdGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALV 450
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
15-449 |
1.83e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 69.00 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 15 RGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNP---------- 84
Cdd:PRK06164 23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTryrshevahi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 85 --------------------QLPQPLLEELLPNLTLQFALVPDGENTFPA--------LTSLHIQL-VEGAHAAAWQPTR 135
Cdd:PRK06164 103 lgrgrarwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADATPApapgarvqLFALPDPApPAAAGERAADPDA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 136 LCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD----KQPL 211
Cdd:PRK06164 183 GALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPvfdaARTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 212 DQML-AGCTHASLVPTQLWRLL----VNRSSVSLK----AVLLGGAAipvELTEQAREQGIRCFCGYGLTEFASTVCAKE 282
Cdd:PRK06164 263 RALRrHRVTHTFGNDEMLRRILdtagERADFPSARlfgfASFAPALG---ELAALARARGVPLTGLYGSSEVQALVALQP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 283 ADGLADV-----GSPL-PGREVKIVN------------DEVWLRAASMAEGYWRNGQLVP-LVNDEGWCATRDRGEM-HN 342
Cdd:PRK06164 340 ATDPVSVrieggGRPAsPEARVRARDpqdgallpdgesGEIEIRAPSLMRGYLDNPDATArALTDDGYFRTGDLGYTrGD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 343 GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPvADKEFGHRPVA-VVEYDQQTVDLGEWV---KDKLARF 418
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG-ATRDGKTVPVAfVIPTDGASPDEAGLMaacREALAGF 498
|
490 500 510
....*....|....*....|....*....|....
gi 446499693 419 QQPVRWLTL---PPELKNGGIKISRQALKEWVQR 449
Cdd:PRK06164 499 KVPARVQVVeafPVTESANGAKIQKHRLREMAQA 532
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-445 |
2.27e-12 |
|
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: 68.36 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 28 LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQlpqplleellpnltlqfaLVPD 107
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTL------------------LTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 108 GENTfpaltslHIQLVEGAHAAAWQPTRLCSMTL---TSGSTGLPKAAVHTYQA----HLASAEGVlSLIPFGDHddWLL 180
Cdd:cd05974 63 DLRD-------RVDRGGAVYAAVDENTHADDPMLlyfTSGTTSKPKLVEHTHRSypvgHLSTMYWI-GLKPGDVH--WNI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 181 SLPLFHVSGQGIMWRWLYAGARMTVRDKQPLD-----QMLAGCTHASL-VPTQLWRLLVN----RSSVSLKAVLLGGAAI 250
Cdd:cd05974 133 SSPGWAKHAWSCFFAPWNAGATVFLFNYARFDakrvlAALVRYGVTTLcAPPTVWRMLIQqdlaSFDVKLREVVGAGEPL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 251 PVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGL--ADVGSPLPGREVKIVN--------DEVWL-----RAASMAE 314
Cdd:cd05974 213 NPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQPVkaGSMGRPLPGYRVALLDpdgapateGEVALdlgdtRPVGLMK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 315 GYWRNGQLVPLVNDEGWCATRDRG-EMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHR 393
Cdd:cd05974 293 GYAGDPDKTAHAMRGGYYRTGDIAmRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 394 PVAVV-------EYDQQTVDLGEWVKDKLARFQQpVRWLTLPPELKNGGIKISRQALKE 445
Cdd:cd05974 373 PKAFIvlragyePSPETALEIFRFSRERLAPYKR-IRRLEFAELPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
17-445 |
2.95e-12 |
|
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: 68.51 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd17655 12 DHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFaLVPDGENTFPALTSLHIQLVE---GAH------AAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVL 167
Cdd:cd17655 92 DSGADI-LLTQSHLQPPIAFIGLIDLLDedtIYHeesenlEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWAN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 168 SLIPFGDHDDWLLSLPL-FHVSGQGIMWRWLYAGARMTVRDKQPLDQML-------AGCTHASLVPTQLWRLLVNRSS-- 237
Cdd:cd17655 171 KVIYQGEHLRVALFASIsFDASVTEIFASLLSGNTLYIVRKETVLDGQAltqyirqNRITIIDLTPAHLKLLDAADDSeg 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 238 VSLKAVLLGGAAIPVELTEQAREQ---GIRCFCGYGLTEfaSTVCA------KEADGLADV--GSPLPGREVKIVND--- 303
Cdd:cd17655 251 LSLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTE--TTVDAsiyqyePETDQQVSVpiGKPLGNTRIYILDQygr 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd17655 329 pqpvgvagELYIGGEGVARGYLNRPELTaekfvddPFVPGERMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17655 409 EARLLQHPDIKEAVVIARKDEQGQNYLCAyiVSEKELPVAQLREFLARELPDYMIPSYFIKLDeiPLTPNG--KVDRKAL 486
|
..
gi 446499693 444 KE 445
Cdd:cd17655 487 PE 488
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
25-431 |
3.09e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.18 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTL-LAWLA----------------------LLQCGARVLP 81
Cdd:PRK13391 22 GEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLeVCWAAersglyytcvnshltpaeaayiVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 82 VNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTSLhiqlvegAHAAAWQP-TRLCS------MTLTSGSTGLPKAAV- 153
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGY-------AEAVAGLPaTPIADeslgtdMLYSSGTTGRPKGIKr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 154 ---HTYQAHLASAEGVL-SLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQPLDQMLA-----GCTHASLV 224
Cdd:PRK13391 175 plpEQPPDTPLPLTAFLqRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLAlieeyGVTHTQLV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 225 PTQLWRLLV------NRSSVS-LKAVLLGGAAIPVelteQAREQGIRcFCG------YGLTEFA-STVCAKEaDGLA--- 287
Cdd:PRK13391 255 PTMFSRMLKlpeevrDKYDLSsLEVAIHAAAPCPP----QVKEQMID-WWGpiiheyYAATEGLgFTACDSE-EWLAhpg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 288 --------------DVGSPLP-----------GREVKIVNDEVWLRAASMAEGYWRNGQLVPLVNDEGWcatrdrgemhn 342
Cdd:PRK13391 329 tvgramfgdlhildDDGAELPpgepgtiwfegGRPFEYLNDPAKTAEARHPDGTWSTVGDIGYVDEDGY----------- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 343 gkLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVeydqQTVD-----------LGEWV 411
Cdd:PRK13391 398 --LYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVV----QPVDgvdpgpalaaeLIAFC 471
|
490 500
....*....|....*....|
gi 446499693 412 KDKLARFQQPvRWLTLPPEL 431
Cdd:PRK13391 472 RQRLSRQKCP-RSIDFEDEL 490
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
239-391 |
3.74e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 68.31 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIpVELTEQAREQ--GIRCFCGYGLTEFASTVCAK---EADGLADVGSPLPGREVKIVND---------- 303
Cdd:PRK12492 334 ALKLTNSGGTAL-VKATAERWEQltGCTIVEGYGLTETSPVASTNpygELARLGTVGIPVPGTALKVIDDdgnelplger 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -EVWLRAASMAEGYWRNGQLVPLVND-EGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK12492 413 gELCIKGPQVMKGYWQQPEATAEALDaEGWFKTGDIAVIDpDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
|
170
....*....|.
gi 446499693 381 FIVPVADKEFG 391
Cdd:PRK12492 493 AAIGVPDERSG 503
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
142-449 |
6.73e-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: 67.18 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWL-LSLPLFHVSGQGIMWRWLYAGarmTV---RDKQPLDQmLAG 217
Cdd:cd05918 114 TSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqFASYTFDVSILEIFTTLAAGG---CLcipSEEDRLND-LAG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 C------THASLVPTqLWRLLVNRSSVSLKAVLLGGAAIPVELTEQArEQGIRCFCGYGLTEfaSTVCA--KEADGLAD- 288
Cdd:cd05918 190 FinrlrvTWAFLTPS-VARLLDPEDVPSLRTLVLGGEALTQSDVDTW-ADRVRLINAYGPAE--CTIAAtvSPVVPSTDp 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 289 --VGSPLPGReVKIVND-------------EVWLRAASMAEGYWRNGQLV--PLVNDEGWCATRDRGE------------ 339
Cdd:cd05918 266 rnIGRPLGAT-CWVVDPdnhdrlvpigavgELLIEGPILARGYLNDPEKTaaAFIEDPAWLKQEGSGRgrrlyrtgdlvr 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 340 -MHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH-PAVLQVFIVPVADKEFGHRP--VAVV----------------- 398
Cdd:cd05918 345 yNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDGSSSPqlVAFVvldgsssgsgdgdslfl 424
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446499693 399 ----EYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQALKEWVQR 449
Cdd:cd05918 425 epsdEFRALVAELRSKLRQRLPSYMVPSVFLPLShlPLTASG--KIDRRALRELAES 479
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
17-443 |
8.16e-12 |
|
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: 67.11 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALVPDGENTFPALTSLHIQLVEG--AHAAAWQPT------RLCSMTLTSGSTGLPKAAV--HTYQAHLASAEGV 166
Cdd:cd17656 83 DSGVRVVLTQRHLKSKLSFNKSTILLEDPsiSQEDTSNIDyinnsdDLLYIIYTSGTTGKPKGVQleHKNMVNLLHFERE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 167 LSLIPFGDhDDWLLSLPLFHVSGQGIMWRWLYAGARMTVRD--KQPLDQMLAGC----THASLVPTQLWRLL------VN 234
Cdd:cd17656 163 KTNINFSD-KVLQFATCSFDVCYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVkrhnIEVVFLPVAFLKFIfserefIN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 235 RSSVSLKAVLLGGAAIPV--ELTEQAREQGIRCFCGYGLTEfASTVCA------KEADGLADVGSPLPGREVKIVND--- 303
Cdd:cd17656 242 RFPTCVKHIITAGEQLVItnEFKEMLHEHNVHLHNHYGPSE-THVVTTytinpeAEIPELPPIGKPISNTWIYILDQeqq 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 --------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:cd17656 321 lqpqgivgELYISGASVARGYLNRQELTaekffpdPFDPNERMYRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:cd17656 401 EAQLLNHPGVSEAVVLDKADDKGEKYLCAyfVMEQELNISQLREYLAKQLPEYMIPSFFVPLDqlPLTPNG--KVDRKAL 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
8-387 |
1.35e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 66.24 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 8 WRHWRQVRGEAIALRLND-----EQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPV 82
Cdd:PRK08008 13 WDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 83 NPQLPQPLLEELLPNLtlQFALVPDGENTFPALTSL---------HIQL-------VEGAH----AAAWQPTRLCSMT-- 140
Cdd:PRK08008 93 NARLLREESAWILQNS--QASLLVTSAQFYPMYRQIqqedatplrHICLtrvalpaDDGVSsftqLKAQQPATLCYAPpl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 141 ---------LTSGSTGLPKAAVHT-----YQAHLASAEGVLSlipfgDHDDWLLSLPLFHVSGQ--GIMwRWLYAGARMT 204
Cdd:PRK08008 171 stddtaeilFTSGTTSRPKGVVIThynlrFAGYYSAWQCALR-----DDDVYLTVMPAFHIDCQctAAM-AAFSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 205 VRDK--------QPLDQMlAGCTHAslVPTQLWRLLVNRSSVSLKAVLLGGAAIPVELTEQAREQ-----GIRCFCGYGL 271
Cdd:PRK08008 245 LLEKysarafwgQVCKYR-ATITEC--IPMMIRTLMVQPPSANDRQHCLREVMFYLNLSDQEKDAfeerfGVRLLTSYGM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 272 TEfasTVCAKEADGLAD------VGSPLPGREVKIVND-----------EVWLRAAS----MAEGYWRNGQLVPLVNDEG 330
Cdd:PRK08008 322 TE---TIVGIIGDRPGDkrrwpsIGRPGFCYEAEIRDDhnrplpageigEICIKGVPgktiFKEYYLDPKATAKVLEADG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446499693 331 WCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAD 387
Cdd:PRK08008 399 WLHTGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-398 |
1.45e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.16 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLAS-AEGVLSLIP---FGDHDDWLLSLPLFHV-SGQGIMWRWLYAGARMTVRDKQPLDQMLA 216
Cdd:PLN02246 187 SSGTTGLPKGVMLTHKGLVTSvAQQVDGENPnlyFHSDDVILCVLPMFHIySLNSVLLCGLRVGAAILIMPKFEIGALLE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 217 -----GCTHASLVPTQLwrLLVNRSSV-------SLKAVLLGGAAIPVELTE--QAREQGIRCFCGYGLTEfASTVCAKe 282
Cdd:PLN02246 267 liqrhKVTIAPFVPPIV--LAIAKSPVvekydlsSIRMVLSGAAPLGKELEDafRAKLPNAVLGQGYGMTE-AGPVLAM- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 283 adGLADVGSPLPGR-----------EVKIVN------------DEVWLRAASMAEGYWRNGQLVPL-VNDEGWCATRDRG 338
Cdd:PLN02246 343 --CLAFAKEPFPVKsgscgtvvrnaELKIVDpetgaslprnqpGEICIRGPQIMKGYLNDPEATANtIDKDGWLHTGDIG 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446499693 339 EM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:PLN02246 421 YIdDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
132-418 |
2.15e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 65.86 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAVHTyQAHLASAeGVLSLIPFG--DHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVR 206
Cdd:PRK07867 150 DPDDLFMLIFTSGTSGDPKAVRCT-HRKVASA-GVMLAQRFGlgPDDVCYVSMPLFH--SNAVMAGWavaLAAGASIALR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 207 DKQPLDQMLA-----GCTHASLVPTQLWRLLV-----NRSSVSLKAVLlGGAAIPVELTEQAREQGIRCFCGYGLTE--- 273
Cdd:PRK07867 226 RKFSASGFLPdvrryGATYANYVGKPLSYVLAtperpDDADNPLRIVY-GNEGAPGDIARFARRFGCVVVDGFGSTEggv 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 274 -FAST------VCAKEADGLA----DVGSPLPGREV---------KIVNDEVWLRAASMAEGYWRNGQlvplvndegwcA 333
Cdd:PRK07867 305 aITRTpdtppgALGPLPPGVAivdpDTGTECPPAEDadgrllnadEAIGELVNTAGPGGFEGYYNDPE-----------A 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 334 TRDR---GEMHNGKLT---------IVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVeyd 401
Cdd:PRK07867 374 DAERmrgGVYWSGDLAyrdadgyayFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAAL--- 450
|
330
....*....|....*..
gi 446499693 402 qQTVDLGEWVKDKLARF 418
Cdd:PRK07867 451 -VLAPGAKFDPDAFAEF 466
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
11-208 |
2.15e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 65.67 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 11 WRQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGS--GVMLRawNTPQTLLAWLALLQCG------------ 76
Cdd:PRK08279 46 AAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDvvALLME--NRPEYLAAWLGLAKLGavvallntqqrg 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 77 -----------ARVLPVNPQLPQPLLEELLPNLTLQFALVPDGENTFPALTslhiqLVEGAHAAAWQPTRL----CSMTL 141
Cdd:PRK08279 124 avlahslnlvdAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEG-----YEDLAAAAAGAPTTNpasrSGVTA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446499693 142 --------TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHvsGQGIMWRW---LYAGARMTVRDK 208
Cdd:PRK08279 199 kdtafyiyTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYH--NTGGTVAWssvLAAGATLALRRK 274
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
16-421 |
2.17e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 65.68 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 16 GEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQcgARVLPVNPqlpqplleell 95
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFK--ARAVPVNV----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 96 pnltlQF-----------------ALVPDGE------NTFPALTSLH--IQLVEGAHA-------------AAWQPTRLC 137
Cdd:PRK07798 84 -----NYryvedelryllddsdavALVYEREfaprvaEVLPRLPKLRtlVVVEDGSGNdllpgavdyedalAAGSPERDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 138 S--------MTLTSGSTGLPK----------------------AAVHTYQAHLASAEGVLSLIpfgdhddWLLSLPLFHV 187
Cdd:PRK07798 159 GerspddlyLLYTGGTTGMPKgvmwrqedifrvllggrdfatgEPIEDEEELAKRAAAGPGMR-------RFPAPPLMHG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 188 SGQGIMWRWLYAGARMTVRDKQPLDqmlagcthaslvPTQLWRLL----VNRSSV----------------------SLK 241
Cdd:PRK07798 232 AGQWAAFAALFSGQTVVLLPDVRFD------------ADEVWRTIerekVNVITIvgdamarplldaleargpydlsSLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 242 AVLLGGAAipveLTEQAREQGIRCFC------GYGLTE--FASTVCAkeADGLADVGSPL--PGREVKIVNDEV------ 305
Cdd:PRK07798 300 AIASGGAL----FSPSVKEALLELLPnvvltdSIGSSEtgFGGSGTV--AKGAVHTGGPRftIGPRTVVLDEDGnpvepg 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 306 -----WL-RAASMAEGYW----RNGQLVPLVNDEGWCATRDRGEMHN-GKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:PRK07798 374 sgeigWIaRRGHIPLGYYkdpeKTAETFPTIDGVRYAIPGDRARVEAdGTITLLGRGSVCINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446499693 375 PAVLQVFIVPVADKEFGHRPVAVVEYDQQTV----DLGEWVKDKLARFQQP 421
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEVVAVVQLREGARpdlaELRAHCRSSLAGYKVP 504
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-208 |
5.96e-11 |
|
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: 64.30 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGArvlpvnpqlpqplleellpnltlqfal 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 105 vpdgentFPALTSLHIQLVEGAHAAAWQPTRLCSMTL-----TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWL 179
Cdd:cd05940 54 -------VAALINYNLRGESLAHCLNVSSAKHLVVDAalyiyTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLY 126
|
170 180 190
....*....|....*....|....*....|
gi 446499693 180 LSLPLFHVSGQGIMW-RWLYAGARMTVRDK 208
Cdd:cd05940 127 TCLPLYHSTALIVGWsACLASGATLVIRKK 156
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
138-419 |
7.50e-11 |
|
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: 63.99 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 138 SMTLTSGSTGLPKAAVHTYQ-AHL-ASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWRWLYAGA-----RMTVRDKQP 210
Cdd:cd05915 157 GMAYTTGTTGLPKGVVYSHRaLVLhSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAkqvlpGPRLDPASL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 211 LDQMLA-GCTHASLVPTQLWRLLVNRSSVSLK-----AVLLGGAAIPVELTEQAREQGIRCFCGYGLTEF--ASTVC--- 279
Cdd:cd05915 237 VELFDGeGVTFTAGVPTVWLALADYLESTGHRlktlrRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETspVVVQNfvk 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 280 -------------AKEADGL------ADVGSP----LP--GREVKIVNdevwLRAASMAEGYWRNGQLV-PLVNDEGWCA 333
Cdd:cd05915 317 shleslseeekltLKAKTGLpiplvrLRVADEegrpVPkdGKALGEVQ----LKGPWITGGYYGNEEATrSALTPDGFFR 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 334 TRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV---EYDQQTVDLGE 409
Cdd:cd05915 393 TGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvprGEKPTPEELNE 472
|
330
....*....|
gi 446499693 410 WVKDKLARFQ 419
Cdd:cd05915 473 HLLKAGFAKW 482
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
123-322 |
9.05e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 63.74 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 123 VEGAHAAAwQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHD-----DWLlslPLFHVSGQ----GIM 193
Cdd:PRK08180 199 VDAAHAAV-GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppvlvDWL---PWNHTFGGnhnlGIV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 194 wrwLYAGARMTVRDKQPLDQMLAGcTHASL----------VPTqLWRLLVN---------RSSVS-LKAVLLGGAAIPV- 252
Cdd:PRK08180 275 ---LYNGGTLYIDDGKPTPGGFDE-TLRNLreisptvyfnVPK-GWEMLVPalerdaalrRRFFSrLKLLFYAGAALSQd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 253 ------ELTEQAREQGIRCFCGYGLTEFA--STVCAKEADGLADVGSPLPGREVKIV-ND---EVWLRAASMAEGYWRNG 320
Cdd:PRK08180 350 vwdrldRVAEATCGERIRMMTGLGMTETApsATFTTGPLSRAGNIGLPAPGCEVKLVpVGgklEVRVKGPNVTPGYWRAP 429
|
..
gi 446499693 321 QL 322
Cdd:PRK08180 430 EL 431
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
110-413 |
2.30e-10 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 62.55 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 110 NTFPALTSLHIQLvegahaAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGD-----HDDWLLSLPL 184
Cdd:PLN02861 202 EEFSLMGSLDCEL------PPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDrvateEDSYFSYLPL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 185 FHVSGQGIMWRWLYAGA---------RMTVRDKQPL------------DQMLAGC----THASLVPTQLW---------- 229
Cdd:PLN02861 276 AHVYDQVIETYCISKGAsigfwqgdiRYLMEDVQALkptifcgvprvyDRIYTGImqkiSSGGMLRKKLFdfaynyklgn 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 230 ---------------RLLVNRSSVSLKA---VLLGGAA-IPVELTEQAREQGIRCFC-GYGLTEFAS---TVCAKEADGL 286
Cdd:PLN02861 356 lrkglkqeeasprldRLVFDKIKEGLGGrvrLLLSGAApLPRHVEEFLRVTSCSVLSqGYGLTESCGgcfTSIANVFSMV 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 287 ADVGSPLPGREVKIVN--------------DEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRL 351
Cdd:PLN02861 436 GTVGVPMTTIEARLESvpemgydalsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQpNGAMKIIDRK 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 352 DNLF-FSGGEGIQPEEVERVIAAHPAVLQVFivpVADKEFGHRPVAVVEYDQQTVDlgEWVKD 413
Cdd:PLN02861 516 KNIFkLSQGEYVAVENLENTYSRCPLIASIW---VYGNSFESFLVAVVVPDRQALE--DWAAN 573
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
132-406 |
3.14e-10 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 62.35 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLI-----PFGDHDDWLLSLPLFHVSGQGI------------MW 194
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanaALTVKDVYLSYLPLAHIFDRVIeecfiqhgaaigFW 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 195 RW--------------------------LYAGARMTVRD-----KQPLD--------QMLAGCTHASLVPTqLWRLLVNR 235
Cdd:PLN02614 301 RGdvklliedlgelkptifcavprvldrVYSGLQKKLSDggflkKFVFDsafsykfgNMKKGQSHVEASPL-CDKLVFNK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 236 SSVSLKA---VLLGGAAiPVELTEQAREQGIRC---FCGYGLTEFASTVCAK---EADGLADVGSPLPGREVKI------ 300
Cdd:PLN02614 380 VKQGLGGnvrIILSGAA-PLASHVESFLRVVACchvLQGYGLTESCAGTFVSlpdELDMLGTVGPPVPNVDIRLesvpem 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 --------VNDEVWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLF-FSGGEGIQPEEVERV 370
Cdd:PLN02614 459 eydalastPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQpNGSMKIIDRKKNIFkLSQGEYVAVENIENI 538
|
330 340 350
....*....|....*....|....*....|....*.
gi 446499693 371 IAAHPAVLQVFivpVADKEFGHRPVAVVEYDQQTVD 406
Cdd:PLN02614 539 YGEVQAVDSVW---VYGNSFESFLVAIANPNQQILE 571
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
239-444 |
3.45e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 61.96 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 239 SLKAVLLGGAAIPVELTEQAREQgIRCFC--GYGLTEFASTVCAKEADGLA---DVGSPLPGREVKIVND---------- 303
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEM-TGCPIteGYGLSETSPVATCNPVDATEfsgTIGLPLPSTEVSIRDDdgndlplgep 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -EVWLRAASMAEGYW-RNGQLVPLVNDEGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQV 380
Cdd:PRK07059 407 gEICIRGPQVMAGYWnRPDETAKVMTADGFFRTGDVGVMDeRGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEV 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 381 FIVPVADKEFGHRPVA-VVEYDQQTV--DLGEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQALK 444
Cdd:PRK07059 487 AAVGVPDEHSGEAVKLfVVKKDPALTeeDVKAFCKERLTNYKRPkfVEFRTELPKTNVG--KILRRELR 553
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
142-329 |
3.68e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 61.99 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQ---AHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGIMWR-WLYAGARMTVRDKQPLDQMLAG 217
Cdd:PRK12582 228 TSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNgLLWGGGTLYIDDGKPLPGMFEE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 218 cTHASL----------VPTQLWRLL-------VNRSSV--SLKAVLLGGAAIPVELTE--QA---REQGIRC--FCGYGL 271
Cdd:PRK12582 308 -TIRNLreisptvygnVPAGYAMLAeamekddALRRSFfkNLRLMAYGGATLSDDLYErmQAlavRTTGHRIpfYTGYGA 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446499693 272 TEFASTVC----AKEADGLadVGSPLPGREVKIVND----EVWLRAASMAEGYWRNGQLVPLVNDE 329
Cdd:PRK12582 387 TETAPTTTgthwDTERVGL--IGLPLPGVELKLAPVgdkyEVRVKGPNVTPGYHKDPELTAAAFDE 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
17-450 |
3.95e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLP 96
Cdd:PRK05691 1146 ERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 97 NLTLQFALVPDGE-NTFPALTSLHIQLVEGAHAAAWQPT---------RLCSMTLTSGSTGLPKAAVHTYQAHLASAEGV 166
Cdd:PRK05691 1226 DSGVELLLTQSHLlERLPQAEGVSAIALDSLHLDSWPSQapglhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWM 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 167 LSLIPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLDQMLA--GCTHASLVPTqLWRLLVNRSS 237
Cdd:PRK05691 1306 QATYALDDSDVLMQKAPIsFDVSVWECFWP-LITGCRLVLagpgehRDPQRIAELVQqyGVTTLHFVPP-LLQLFIDEPL 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 238 V----SLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFASTV----CAKEADGLADVGSPLPGREVKIVND---- 303
Cdd:PRK05691 1384 AaactSLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAINVthwqCQAEDGERSPIGRPLGNVLCRVLDAelnl 1463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 -------EVWLRAASMAEGYWRNGQLV-------PLVND-EGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEV 367
Cdd:PRK05691 1464 lppgvagELCIGGAGLARGYLGRPALTaerfvpdPLGEDgARLYRTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEEI 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 368 ERVIAAHPAVLQVfIVPVADKEFGHRPVAVVEYDQQTVDLGEWVKDKLAR----FQQPVRWLTLP--PELKNGgiKISRQ 441
Cdd:PRK05691 1544 QARLLAQPGVAQA-AVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAelpeYMVPAQLIRLDqmPLGPSG--KLDRR 1620
|
490
....*....|.
gi 446499693 442 ALKE--WVQRQ 450
Cdd:PRK05691 1621 ALPEpvWQQRE 1631
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-443 |
6.82e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.72 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQ----------- 85
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEyprerlaymie 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 86 -------LPQPLLEELLPNLTLQFALVPDGENTFPALTSlhiqlvEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQA 158
Cdd:PRK12467 1669 dsgiellLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYS------DSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGA 1742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 159 HLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGIMWRwLYAGARMTV------RDKQPLDQMLA--GCTHASLVPTQLW 229
Cdd:PRK12467 1743 LVNRLCATQEAYQLSAADVVLQFTSFaFDVSVWELFWP-LINGARLVIappgahRDPEQLIQLIErqQVTTLHFVPSMLQ 1821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 230 RLLVNRSSV----SLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFASTV----CAK---EADGLADVGSPLPGR 296
Cdd:PRK12467 1822 QLLQMDEQVehplSLRRVVCGGEALEVEALRPWLERlpDTGLFNLYGPTETAVDVthwtCRRkdlEGRDSVPIGQPIANL 1901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 297 EVKIVND-----------EVWLRAASMAEGYWRNgqlvPLVNDEGWCA----------------TRDRGEmhnGKLTIVG 349
Cdd:PRK12467 1902 STYILDAslnpvpigvagELYLGGVGLARGYLNR----PALTAERFVAdpfgtvgsrlyrtgdlARYRAD---GVIEYLG 1974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 350 RLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVaDKEFGHRPVA-VVEYDQQTVD-----------LGEWVKDKLAR 417
Cdd:PRK12467 1975 RIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAyVVPTDPGLVDddeaqvalraiLKNHLKASLPE 2053
|
490 500
....*....|....*....|....*...
gi 446499693 418 FQQPVRWLTLP--PELKNGgiKISRQAL 443
Cdd:PRK12467 2054 YMVPAHLVFLArmPLTPNG--KLDRKAL 2079
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
142-446 |
8.03e-10 |
|
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: 60.94 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLasaegvlslIPFGDHDDWLLSLplfhvSGQGIMWR-----------------WLyAGA--- 201
Cdd:cd05928 182 TSGTTGSPKMAEHSHSSLG---------LGLKVNGRYWLDL-----TASDIMWNtsdtgwiksawsslfepWI-QGAcvf 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 202 --RMTVRDKQPLDQMLAG--CTHASLVPTqLWRLLV--NRSSV---SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGL 271
Cdd:cd05928 247 vhHLPRFDPLVILKTLSSypITTFCGAPT-VYRMLVqqDLSSYkfpSLQHCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 272 TEfASTVCA-----KEADGlaDVGSPLPGREVKIVND-----------EVWLRAA-----SMAEGYWRNGQLVPLVNDEG 330
Cdd:cd05928 326 TE-TGLICAnfkgmKIKPG--SMGKASPPYDVQIIDDngnvlppgtegDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 331 WCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV---------EY 400
Cdd:cd05928 403 FYLTGDRGIMdEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVvlapqflshDP 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446499693 401 DQQTVDLGEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQAL--KEW 446
Cdd:cd05928 483 EQLTKELQQHVKSVTAPYKYPrkVEFVQELPKTVTG--KIQRNELrdKEW 530
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
36-379 |
1.14e-09 |
|
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: 60.18 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 36 RVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQFaLVPDGENTFPAL 115
Cdd:cd17654 25 KISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSY-LLQNKELDNAPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 116 TSLHiqlvEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL-FHVSGQGIMW 194
Cdd:cd17654 104 SFTP----EHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLtFDPSVVEIFL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 195 RWLYAGARMTVRDK--------QPLDQMLAGCTHASLVPTQLWRLLV--NRSSV-----SLKAVLLGGAAIPVELTEQAR 259
Cdd:cd17654 180 SLSSGATLLIVPTSvkvlpsklADILFKRHRITVLQATPTLFRRFGSqsIKSTVlsatsSLRVLALGGEPFPSLVILSSW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 260 EQ---GIRCFCGYGLTE---FASTVCAKEADGLADVGSPLPGREVKIVNDEVW-----LRAASMAEGYWRNGQL-VPLVN 327
Cdd:cd17654 260 RGkgnRTRIFNIYGITEvscWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSegtgqVFLGGLNRVCILDDEVtVPKGT 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446499693 328 degWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:cd17654 340 ---MRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVES 388
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
142-398 |
1.52e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.78 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLS-LPLFHVSGQGIMWRWLYAGARM-----TVRDKQP----- 210
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSwLPLYHDMGLAFLLTAALAGAPLwlaptTAFSASPfrwls 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 211 -LDQMLAGCTHAslvPTQLWRLlVNRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFC---------------GYGLTEF 274
Cdd:PRK05851 240 wLSDSRATLTAA---PNFAYNL-IGKYARRVSDVDLGALRVALNGGEPVDCDGFERFAtamapfgfdagaaapSYGLAES 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 275 ASTVCAKE-ADGL----------------ADVGSPLPGREVKI--------VND----EVWLRAASMAEGYWrnGQlVPL 325
Cdd:PRK05851 316 TCAVTVPVpGIGLrvdevttddgsgarrhAVLGNPIPGMEVRIspgdgaagVAGreigEIEIRGASMMSGYL--GQ-API 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 326 VNDEgWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:PRK05851 393 DPDD-WFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVI 464
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-451 |
1.62e-09 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 60.00 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 12 RQVRGEAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGarVLPVNP------- 84
Cdd:PRK10946 33 RHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNAlfshqrs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 85 --QLPQPLLEELLPNLTLQFALVPDGE--NTF----PAL-----------TSLHIQLVEGAHAAAWQPTR---LCSMTLT 142
Cdd:PRK10946 111 elNAYASQIEPALLIADRQHALFSDDDflNTLvaehSSLrvvlllnddgeHSLDDAINHPAEDFTATPSPadeVAFFQLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 143 SGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH---VSGQGIMWRWLYAGARMTVRDKQPLdqmlaGC- 218
Cdd:PRK10946 191 GGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCALPAAHnypMSSPGALGVFLAGGTVVLAPDPSAT-----LCf 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 219 --------THASLVP--TQLWRLLVNRSS-----VSLKAVLLGGAA--------IPVELTEQAREQgircfcgYGLTEfa 275
Cdd:PRK10946 266 pliekhqvNVTALVPpaVSLWLQAIAEGGsraqlASLKLLQVGGARlsetlarrIPAELGCQLQQV-------FGMAE-- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 276 STVCAKEADGLADV-----GSPL-PGREVKIVNDE---VWLRAASM------------------------AEGYWRNGQL 322
Cdd:PRK10946 337 GLVNYTRLDDSDERifttqGRPMsPDDEVWVADADgnpLPQGEVGRlmtrgpytfrgyykspqhnasafdANGFYCSGDL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 323 VPLVNDegwcatrdrgemhnGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA--VVEY 400
Cdd:PRK10946 417 VSIDPD--------------GYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAflVVKE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446499693 401 DQQTVDLGEWVKDK-LARFQQPVRWLTLP--PELKNGgiKISRQALKEWVQRQQ 451
Cdd:PRK10946 483 PLKAVQLRRFLREQgIAEFKLPDRVECVDslPLTAVG--KVDKKQLRQWLASRA 534
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
281-413 |
1.65e-09 |
|
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: 59.81 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 281 KEADGLADVGSPLPGREVKIVNDE-----------VWLRAASMAEGYWRNGQLVPLV-NDEGWCATRDRGEMHNGKLTIV 348
Cdd:cd05908 308 SECLTFVEVGKPIDETDIRICDEDnkilpdgyighIQIRGKNVTPGYYNNPEATAKVfTDDGWLKTGDLGFIRNGRLVIT 387
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446499693 349 GRLDNLFFSGGEGIQPEEVERVIAAHPAVL--QVFIVPVADKEFGHRPV-AVVEYDQQTVDLGEWVKD 413
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNEEIfCFIEHRKSEDDFYPLGKK 455
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
224-444 |
1.72e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 59.28 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 224 VPTQLW---RLLvnRSSVSLKAVLLGGAAIPVELTEQAREQGIRCFCGYGLTEFASTVCAKEADGLADVGSPLPGREVKI 300
Cdd:PRK08308 197 VPLMLHilgRLL--PGTFQFHAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKSHLDLGNPLPHVSVSA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 VNDEVwlraasmaegywRNGQLVPLVNDEGwCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQ 379
Cdd:PRK08308 275 GSDEN------------APEEIVVKMGDKE-IFTKDLGYKsERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446499693 380 VFIVPVADKEFGHRPVAVV--EYDQQTVDLGEWVKDKLARFQQPVRWLTLP--PELKNGgiKISRQALK 444
Cdd:PRK08308 342 AVVYRGKDPVAGERVKAKVisHEEIDPVQLREWCIQHLAPYQVPHEIESVTeiPKNANG--KVSRKLLE 408
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
139-444 |
2.50e-09 |
|
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: 59.07 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 139 MTLTSGSTGLPKAAVH------TYQAHLASAEGVLSLIPFGDHDD--WLLSLpLFHVSGQGIMW--RWLYAGA------- 201
Cdd:cd05973 93 MMFTSGTTGLPKGVPVplralaAFGAYLRDAVDLRPEDSFWNAADpgWAYGL-YYAITGPLALGhpTILLEGGfsvestw 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 202 RMTVRdkqpldqmlAGCTHASLVPTqLWRLLV-------NRSSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTE 273
Cdd:cd05973 172 RVIER---------LGVTNLAGSPT-AYRLLMaagaevpARPKGRLRRVSSAGEPLTPEVIRWFDAAlGVPIHDHYGQTE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 274 FASTVCAKEADG----LADVGSPLPGREVKIVNDE---------------------VWLRaasmaeGYWRNGQLVPlvnD 328
Cdd:cd05973 242 LGMVLANHHALEhpvhAGSAGRAMPGWRVAVLDDDgdelgpgepgrlaidiansplMWFR------GYQLPDTPAI---D 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 329 EGWCATRDRGEMH-NGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVAD-------KEF-----GHRPV 395
Cdd:cd05973 313 GGYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDpertevvKAFvvlrgGHEGT 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446499693 396 AVVEYDQQTvdlgeWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQALK 444
Cdd:cd05973 393 PALADELQL-----HVKKRLSAHAYPrtIHFVDELPKTPSG--KIQRFLLR 436
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-421 |
2.62e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 18 AIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPN 97
Cdd:PRK13390 15 AVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 98 LTLQFALVPDGENTFPALTSLHIQL-------------VEGAHAAAWQP--TRLCS--MTLTSGSTGLPKAAVHTYQAHL 160
Cdd:PRK13390 95 SGARVLVASAALDGLAAKVGADLPLrlsfggeidgfgsFEAALAGAGPRltEQPCGavMLYSSGTTGFPKGIQPDLPGRD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 161 ASAEG------VLSLIPFGDHDDWLLSLPLFHVSGqgimWRW---LYAGARMTVRDKQPLDQMLAG------CTHASLVP 225
Cdd:PRK13390 175 VDAPGdpivaiARAFYDISESDIYYSSAPIYHAAP----LRWcsmVHALGGTVVLAKRFDAQATLGhveryrITVTQMVP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 226 TQLWRLLVNRSSV-------SLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEFASTVCAKEADGLADVGSPlpGRE 297
Cdd:PRK13390 251 TMFVRLLKLDADVrtrydvsSLRAVIHAAAPCPVDVKHAMIDWlGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSV--GRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 298 V----KIVNDEVW-LRAASMAEGYWRNGQLvPL--VNDEG------------WCATRDRGEM-HNGKLTIVGRLDNLFFS 357
Cdd:PRK13390 329 VlgdlHICDDDGNeLPAGRIGTVYFERDRL-PFryLNDPEktaaaqhpahpfWTTVGDLGSVdEDGYLYLADRKSFMIIS 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446499693 358 GGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVVEY-------DQQTVDLGEWVKDKLARFQQP 421
Cdd:PRK13390 408 GGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLvegirgsDELARELIDYTRSRIAHYKAP 478
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
17-385 |
4.07e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.90 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 17 EAIALRLNDEQLNWRELCARVDELASGFAAQGVVEGSGVmlrAWNTPQTL---LAWLALLQCGARVLPVN--------PQ 85
Cdd:PRK10252 473 DAPALADARYQFSYREMREQVVALANLLRERGVKPGDSV---AVALPRSVfltLALHAIVEAGAAWLPLDtgypddrlKM 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 86 LPQPLLEELLPNLTLQFALVPDGENTFPALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEG 165
Cdd:PRK10252 550 MLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 166 VLSLIPFGDHDDWLLSLPL-FHVSGQGIMWRWLyAGARMTV------RDKQPLDQMLA--GCTHASLVPTQLWRLL---- 232
Cdd:PRK10252 630 MQNHYPLTADDVVLQKTPCsFDVSVWEFFWPFI-AGAKLVMaepeahRDPLAMQQFFAeyGVTTTHFVPSMLAAFVaslt 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 233 ---VNRSSVSLKAVLLGGAAIPVELT-EQAREQGIRCFCGYGLTEFASTVCA--KEADGLADV-GSPLP-GREV-----K 299
Cdd:PRK10252 709 pegARQSCASLRQVFCSGEALPADLCrEWQQLTGAPLHNLYGPTEAAVDVSWypAFGEELAAVrGSSVPiGYPVwntglR 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 300 IVND-----------EVWLRAASMAEGYWRNGQLV-------PLVNDEGWCATRDRGE-MHNGKLTIVGRLDNLFFSGGE 360
Cdd:PRK10252 789 ILDArmrpvppgvagDLYLTGIQLAQGYLGRPDLTasrfiadPFAPGERMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQ 868
|
410 420
....*....|....*....|....*
gi 446499693 361 GIQPEEVERVIAAHPAVLQVFIVPV 385
Cdd:PRK10252 869 RIELGEIDRAMQALPDVEQAVTHAC 893
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
133-398 |
1.02e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.49 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 133 PTRLCSMTltsGSTGLPKAAVHTYQAHLASAEGVLSLIPFG-DHDD-WLLSLPLFHVSGQGIMWRWLYAGARMTVRDKQP 210
Cdd:PRK05620 183 AAAICYST---GTTGAPKGVVYSHRSLYLQSLSLRTTDSLAvTHGEsFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGPDL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 211 LDQMLAGCTHASL------VPTqLW-RLLVNR-----SSVSLKAVLLGGAAIPVELTEQAREQ-GIRCFCGYGLTEfAST 277
Cdd:PRK05620 260 SAPTLAKIIATAMprvahgVPT-LWiQLMVHYlknppERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTE-TSP 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 278 V--CAKEADGLA---------DVGSPLPGREVKIVND------------EVWLRAASMAEGYWRN-------------GQ 321
Cdd:PRK05620 338 VgtVARPPSGVSgearwayrvSQGRFPASLEYRIVNDgqvmestdrnegEIQVRGNWVTASYYHSpteegggaastfrGE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 322 LVPLVNDE----GWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVA 396
Cdd:PRK05620 418 DVEDANDRftadGWLRTGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
..
gi 446499693 397 VV 398
Cdd:PRK05620 498 VT 499
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
132-383 |
1.73e-08 |
|
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: 56.60 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAV--H---TYQAHLASAEgvLSLIPFGDHDDWLLS-LPLFHVSGQGI-MWRWLYAGARMT 204
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMlsHdniTWTAKAASQH--MDLRPATVGQESVVSyLPLSHIAAQILdIWLPIKVGGQVY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 205 VRDKQPLDQMLAGcTHASLVPT------QLW------------------RLLVNRS-SVSLKA----------------- 242
Cdd:cd05933 226 FAQPDALKGTLVK-TLREVRPTafmgvpRVWekiqekmkavgaksgtlkRKIASWAkGVGLETnlklmggespsplfyrl 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 243 --------------------VLLGGAAIPVELTEQAREQGIRCFCGYGLTEFAS--TVCAKEADGLADVGSPLPGREVKI 300
Cdd:cd05933 305 akklvfkkvrkalgldrcqkFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGphTISNPQAYRLLSCGKALPGCKTKI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 301 VND------EVWLRAASMAEGYWRNGQLV-PLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLFF-SGGEGIQPEEVE-RV 370
Cdd:cd05933 385 HNPdadgigEICFWGRHVFMGYLNMEDKTeEAIDEDGWLHSGDLGKLdEDGFLYITGRIKELIItAGGENVPPVPIEdAV 464
|
330
....*....|...
gi 446499693 371 IAAHPAVLQVFIV 383
Cdd:cd05933 465 KKELPIISNAMLI 477
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
9-444 |
3.44e-08 |
|
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: 55.57 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 9 RHWRQVRGEAIALRLNDEQ-----LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVN 83
Cdd:cd05968 68 DKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 84 PQLPQPLLEELLPNLTLQFALVPDG---------------ENTFPALTSLHIQLV-----------------------EG 125
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALITADGftrrgrevnlkeeadKACAQCPTVEKVVVVrhlgndftpakgrdlsydeeketAG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 126 AHAAAWQPTRLCSMTLTSGSTGLPKAAVHTYQAH-LASAEGVLSLIPFGDHDDwllslpLFHVSGQG-IMWRWLY----- 198
Cdd:cd05968 228 DGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDL------LTWFTDLGwMMGPWLIfggli 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 199 AGARMTVRDKQP-------LDQMLA--GCTHASLVPTqLWRLL-------VNRSSVSlKAVLLGGAAIPVEL-------- 254
Cdd:cd05968 302 LGATMVLYDGAPdhpkadrLWRMVEdhEITHLGLSPT-LIRALkprgdapVNAHDLS-SLRVLGSTGEPWNPepwnwlfe 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 255 ---------------TEQAreQGIrcFCGYGLTE-----FASTVCAKEADGLADVGSPLPGREVKIVNDEVWLraaSMAE 314
Cdd:cd05968 380 tvgkgrnpiinysggTEIS--GGI--LGNVLIKPikpssFNGPVPGMKADVLDESGKPARPEVGELVLLAPWP---GMTR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 315 GYWRNG--------QLVPLVNDEGWCATRDRGemhnGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVA 386
Cdd:cd05968 453 GFWRDEdryletywSRFDNVWVHGDFAYYDEE----GYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVP 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 387 DKEFGHRPVA-VVEYDQQTV------DLGEWVKDKLARFQQPVRWLTLPPELKNGGIKISRQALK 444
Cdd:cd05968 529 HPVKGEAIVCfVVLKPGVTPtealaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
132-370 |
3.64e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 132 QPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGQGI-MWRWLYAGARMTVRdKQP 210
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLY-PSP 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 211 LdqmlagctHASLVPtqlwRLLVNRSSVSL--KAVLLG-------------------GAAipvELTEQAREQ-----GIR 264
Cdd:PRK08043 442 L--------HYRIVP----ELVYDRNCTVLfgTSTFLGnyarfanpydfarlryvvaGAE---KLQESTKQLwqdkfGLR 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 265 CFCGYGLTEFASTVC--AKEADGLADVGSPLPGREVKIVN-------DEVWLRAASMAEGYWR---NGQL-VPLVNDE-- 329
Cdd:PRK08043 507 ILEGYGVTECAPVVSinVPMAAKPGTVGRILPGMDARLLSvpgieqgGRLQLKGPNIMNGYLRvekPGVLeVPTAENArg 586
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446499693 330 ----GWCATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERV 370
Cdd:PRK08043 587 emerGWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL 632
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
290-399 |
4.70e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 55.40 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 290 GSPLPGREVKIVNDE-----------VWLRAASMAEGYWRNGQLVPLVNDEGWCATRDRGEMHNGKLTIVGRLDNLFFSG 358
Cdd:PRK09192 388 GKALPGHEIEIRNEAgmplpervvghICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLDGYLYITGRAKDLIIIN 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446499693 359 GEGIQPEEVERVIAAHPAVLQ----VFIVpvaDKEFGHRPVAVVE 399
Cdd:PRK09192 468 GRNIWPQDIEWIAEQEPELRSgdaaAFSI---AQENGEKIVLLVQ 509
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
114-379 |
7.63e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 114 ALTSLHIQLVEGAHAAAWQPTRLCSMTLTSGSTGLPKAaVHTYQAHLASAEGVLSL---IPFGDhDDWLLS-LPLFHVSG 189
Cdd:PRK05691 146 CVDTLDPALAEAWQEPALQPDDIAFLQYTSGSTALPKG-VQVSHGNLVANEQLIRHgfgIDLNP-DDVIVSwLPLYHDMG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 190 Q-GIMWRWLYAGARMTVRDKQ-----PLDQMLAGCTHASLV---PTQLWRLLVNR-SSVSLKAVLLGGAAIPVELTEQAR 259
Cdd:PRK05691 224 LiGGLLQPIFSGVPCVLMSPAyflerPLRWLEAISEYGGTIsggPDFAYRLCSERvSESALERLDLSRWRVAYSGSEPIR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 260 EQGIRCF------CG---------YGLTE-----------------------FASTVcAKEADG--LADVGSPLPGREVK 299
Cdd:PRK05691 304 QDSLERFaekfaaCGfdpdsffasYGLAEatlfvsggrrgqgipaleldaeaLARNR-AEPGTGsvLMSCGRSQPGHAVL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 300 IVN------------DEVWLRAASMAEGYWRNGQLVP--LVNDEG--WCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQ 363
Cdd:PRK05691 383 IVDpqslevlgdnrvGEIWASGPSIAHGYWRNPEASAktFVEHDGrtWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLY 462
|
330
....*....|....*.
gi 446499693 364 PEEVERVIAAHPAVLQ 379
Cdd:PRK05691 463 PQDIEKTVEREVEVVR 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
142-373 |
3.07e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGqgimwrwLYAGARMTvrdkqpldqMLAGctha 221
Cdd:PRK06814 801 TSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFG-------LTGGLVLP---------LLSG---- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 222 slVPTQLWRLLVNRSSV--------------------------------SLKAVLLGgaAIPV-ELTEQ--AREQGIRCF 266
Cdd:PRK06814 861 --VKVFLYPSPLHYRIIpeliydtnatilfgtdtflngyaryahpydfrSLRYVFAG--AEKVkEETRQtwMEKFGIRIL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 267 CGYGLTEfASTVCAKE---ADGLADVGSPLPGREVKIvnDEV---------WLRAASMAEGYWR---NGQLVPLVndEGW 331
Cdd:PRK06814 937 EGYGVTE-TAPVIALNtpmHNKAGTVGRLLPGIEYRL--EPVpgideggrlFVRGPNVMLGYLRaenPGVLEPPA--DGW 1011
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446499693 332 CATRDRGEM-HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAA 373
Cdd:PRK06814 1012 YDTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAE 1054
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
366-421 |
5.04e-07 |
|
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: 47.15 E-value: 5.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 366 EVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV----EYDQQTVDLGEWVKDKLARFQQP 421
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVvlkpGVELLEEELVAHVREELGPYAVP 60
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
129-405 |
1.03e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 51.05 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 129 AAWQPTRLCSMTLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFHVSGqgimwrwLYAGARMTVRDK 208
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFG-------PALGMTSVIPDM 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 209 QPL-------DQMLA-----GCTHASLVPTqLWRLL----VNRSSV--SLKAVLLGGAAIPVELTEQARE---QGIRCFC 267
Cdd:PRK09274 242 DPTrpatvdpAKLFAaieryGVTNLFGSPA-LLERLgrygEANGIKlpSLRRVISAGAPVPIAVIERFRAmlpPDAEILT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 268 GYGLTE------------FASTVCAKEADGLADVGSPLPGREVKI--VNDEV---WLRAASMAEGywRNGQLV---PLV- 326
Cdd:PRK09274 321 PYGATEalpissiesreiLFATRAATDNGAGICVGRPVDGVEVRIiaISDAPipeWDDALRLATG--EIGEIVvagPMVt 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 327 -----NDEgwcATR-----DRGEMHNGKLTIVGRLDN---LFFSG---------GEGIQPEEVERVIAAHPAVLQVFIVP 384
Cdd:PRK09274 399 rsyynRPE---ATRlakipDGQGDVWHRMGDLGYLDAqgrLWFCGrkahrvetaGGTLYTIPCERIFNTHPGVKRSALVG 475
|
330 340
....*....|....*....|.
gi 446499693 385 VADKEfGHRPVAVVEYDQQTV 405
Cdd:PRK09274 476 VGVPG-AQRPVLCVELEPGVA 495
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
142-192 |
1.18e-05 |
|
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: 47.67 E-value: 1.18e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAeGVLSLIPFGDHDDWLLSLPLFHVSGQGI 192
Cdd:cd05938 152 TSGTTGLPKAARISHLRVLQCS-GFLSLCGVTADDVIYITLPLYHSSGFLL 201
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
25-193 |
3.73e-05 |
|
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: 45.88 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 25 DEQLNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGARVLPVNPQLPQPLLEELLPNLTLQfAL 104
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAK-AL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 105 VPDGENTFPALTSLHIQLVEGAHAAawqpTRLCSMtLTSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPL 184
Cdd:cd05939 80 IFNLLDPLLTQSSTEPPSQDDVNFR----DKLFYI-YTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPL 154
|
....*....
gi 446499693 185 FHVSGqGIM 193
Cdd:cd05939 155 YHSAG-GIM 162
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
142-444 |
4.89e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.88 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIP-FGDHDDWLLSLPLFHV---SGQGIMwrwLYAGAR--------------- 202
Cdd:PLN02387 258 TSGSTGLPKGVMMTHGNIVATVAGVMTVVPkLGKNDVYLAYLPLAHIlelAAESVM---AAVGAAigygspltltdtsnk 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 203 ----------------MT--------VRD---------------------KQPLDQMLAGCTHASLVPTQLWRLLVNRS- 236
Cdd:PLN02387 335 ikkgtkgdasalkptlMTavpaildrVRDgvrkkvdakgglakklfdiayKRRLAAIEGSWFGAWGLEKLLWDALVFKKi 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 237 ----SVSLKAVLLGGAaiPVELTEQaREQGIrCFC-----GYGLTEfastVCA----KEAD--GLADVGSPLPGREVKIV 301
Cdd:PLN02387 415 ravlGGRIRFMLSGGA--PLSGDTQ-RFINI-CLGapigqGYGLTE----TCAgatfSEWDdtSVGRVGPPLPCCYVKLV 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 302 N---------------DEVWLRAASMAEGYWRNGQL---VPLVNDEG--WCATRDRGEMH-NGKLTIVGRL-DNLFFSGG 359
Cdd:PLN02387 487 SweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKtdeVYKVDERGmrWFYTGDIGQFHpDGCLEIIDRKkDIVKLQHG 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 360 EGIQPEEVERVIAAHPAVLQV-------------FIVP-------------VADKEFG---HRPVAVVEYDQQTVDLGEw 410
Cdd:PLN02387 567 EYVSLGKVEAALSVSPYVDNImvhadpfhsycvaLVVPsqqalekwakkagIDYSNFAelcEKEEAVKEVQQSLSKAAK- 645
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446499693 411 vKDKLARFQQPVRWLTLP----PE--LKNGGIKISRQALK 444
Cdd:PLN02387 646 -AARLEKFEIPAKIKLLPepwtPEsgLVTAALKLKREQIR 684
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
142-374 |
4.99e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.58 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 142 TSGSTGLPKAAVHTYQAHLASAEGVLSLIPFGDHDDWLLSLPLFH------------VSGQGIMWRW--LYAGARMTVRD 207
Cdd:PRK06334 191 TSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHaygfnsctlfplLSGVPVVFAYnpLYPKKIVEMID 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 208 KqpldqmlagcTHASLV---PTQLWRLLV-----NRSSVSLKAVLLGGAAIPVELTEQAREQ--GIRCFCGYGLTEFAST 277
Cdd:PRK06334 271 E----------AKVTFLgstPVFFDYILKtakkqESCLPSLRFVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTECSPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 278 VCAKEADGLAD---VGSPLPGREVKIVNDE------------VWLRAASMAEGYWRN--GQLVPLVNDEGWCATRDRGEM 340
Cdd:PRK06334 341 ITINTVNSPKHescVGMPIRGMDVLIVSEEtkvpvssgetglVLTRGTSLFSGYLGEdfGQGFVELGGETWYVTGDLGYV 420
|
250 260 270
....*....|....*....|....*....|....*
gi 446499693 341 -HNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAH 374
Cdd:PRK06334 421 dRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
290-398 |
1.10e-04 |
|
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: 44.61 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 290 GSPLPGREVKIVNDE-------------------------VWLRAASMAEGYWRNgqlvplvnDEGWCATRDRGEM-HNG 343
Cdd:cd05967 414 GKPVPGYQVQVLDEDgepvgpnelgniviklplppgclltLWKNDERFKKLYLSK--------FPGYYDTGDAGYKdEDG 485
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 344 KLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV 398
Cdd:cd05967 486 YLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLV 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
304-416 |
2.02e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 43.78 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 304 EVWLRAASMAEGYWRN---------GQLV---PLVNDEGWCATRDRGEMHNGKLTIVGRLDNLFFSGGEGIQPEEVE--- 368
Cdd:PRK05850 399 EIWVHGDNVAAGYWQKpeetertfgATLVdpsPGTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDGRNHYPDDIEati 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446499693 369 ------RVIAahpavlqvFIVPVADKEfghRPVAVVEYDQQTvDLGEWVKDKLA 416
Cdd:PRK05850 479 qeitggRVAA--------ISVPDDGTE---KLVAIIELKKRG-DSDEEAMDRLR 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
290-377 |
3.32e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 42.96 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 290 GSPLPGREVKIVND-----------EVWLRAA--SMAEGYWRNGQLVPLVNDEGWCATRDRGEM-HNGKLTIVGRLDNLF 355
Cdd:PRK04319 379 GKPLPGIEAAIVDDqgnelppnrmgNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMdEDGYFWFQGRVDDVI 458
|
90 100
....*....|....*....|..
gi 446499693 356 FSGGEGIQPEEVERVIAAHPAV 377
Cdd:PRK04319 459 KTSGERVGPFEVESKLMEHPAV 480
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
12-71 |
4.84e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 42.47 E-value: 4.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446499693 12 RQVRGEAIALRLNDE-----QLNWRELCARVDELASGFAAQGVVEG---SGVMLrawNTPQTLLAWLA 71
Cdd:PRK03584 94 RHRRDDRPAIIFRGEdgprrELSWAELRRQVAALAAALRALGVGPGdrvAAYLP---NIPETVVAMLA 158
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
9-77 |
1.45e-03 |
|
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: 41.15 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446499693 9 RHWRQVRGEAIAL-----RLNDEQ-LNWRELCARVDELASGFAAQGVVEGSGVMLRAWNTPQTLLAWLALLQCGA 77
Cdd:cd05967 58 RHVEAGRGDQIALiydspVTGTERtYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA 132
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
286-399 |
4.19e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 39.64 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 286 LADVGSPLPGREVKIVND------------EVWLRAASMAEGYWR-------------NGQLVPLVNDEGWCATRDRGEM 340
Cdd:cd05905 360 LQDSGKVLPGAQVAIVNPetkglckdgeigEIWVNSPANASGYFLldgetndtfkvfpSTRLSTGITNNSYARTGLLGFL 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446499693 341 HNGKLT-----------IVGRLDNLFFSGGEGIQPEEVER-VIAAHPAVLQ--VFivpvadkEFGHRPVAVVE 399
Cdd:cd05905 440 RPTKCTdlnveehdllfVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRcaVF-------SITGLVVVVAE 505
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
333-444 |
8.30e-03 |
|
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: 38.70 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446499693 333 ATRDrgemHNGKLTIVGRLDNLFFSGGEGIQPEEVERVIAAHPAVLQVFIVPVADKEFGHRPVAVV------EYDQQTV- 405
Cdd:cd05966 477 ARRD----EDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVtlkdgeEPSDELRk 552
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446499693 406 DLGEWVKDKLARFQQP--VRWLTLPPELKNGgiKISRQALK 444
Cdd:cd05966 553 ELRKHVRKEIGPIATPdkIQFVPGLPKTRSG--KIMRRILR 591
|
|
| |
