|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1-718 |
0e+00 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 1580.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 1 MLFSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLD 80
Cdd:PRK08043 1 MLFSFFRNLFRVLYRVRVTGDTQALKGERVLITPNHVSFLDGILLALFLPVRPVFAVYTSISQQWYMRWLKPYIDFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 81 PTQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQI 160
Cdd:PRK08043 81 PTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 161 TLHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTK 240
Cdd:PRK08043 161 TLHILPPTQLPMPDAPRARDRRKLAGEMLHQIMMEARMAVRPRETLYEALLSAQYRYGAGKPCIEDVNFTPDSYRKLLKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 241 TLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
Cdd:PRK08043 241 TLFVGRILEKYSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 321 LPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK08043 321 LPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 401 ADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYR 480
Cdd:PRK08043 401 ADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRNCTVLFGTSTFLGNYARFANPYDFAR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKG 560
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQLKG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 561 PNIMNGYLRVEKPGVLEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
Cdd:PRK08043 561 PNIMNGYLRVEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDK 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 641 VHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHD 718
Cdd:PRK08043 641 QHATAIKSDASKGEALVLFTTDSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDEPEQHD 718
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
4-714 |
0e+00 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 953.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 4 SFFRNLCRVLYRVRVTGdTQALK--GERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDP 81
Cdd:PRK06814 429 DIFSILFRAFYRVEVKG-LENLQkaGKKAVIAANHVSFLDGPLLAAYLPEEPTFAIDTDIAKAWWVKPFLKLAKALPVDP 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 82 TQPMAIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRLFPQIT 161
Cdd:PRK06814 508 TNPMATRTLIKEVQKGEKLVIFPEGRITVTGSLMKIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQVRRKWFPKVT 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 162 LHILPPTQVAMPDAPRARDRRKIAGEMLHQIMMEARMAVRPR-ETLYESLLSAMYRFGAGKKCVEDVNFTPDSYRKLLTK 240
Cdd:PRK06814 588 VTILPPVKLAVDPELKGRERRSAAGAALYDIMSDMMFETSDYdRTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTG 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 241 TLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWH 320
Cdd:PRK06814 668 AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRAFIEKARLGP 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 321 LPEQL-TQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK06814 748 LIEALeFGIRIIYLEDVRAQIGLADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAA 827
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 400 IADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFY 479
Cdd:PRK06814 828 RIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPLHYRIIPELIYDTNATILFGTDTFLNGYARYAHPYDFR 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLK 559
Cdd:PRK06814 908 SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGIDEGGRLFVR 987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 560 GPNIMNGYLRVEKPGVLEVPtaenvrgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPD 639
Cdd:PRK06814 988 GPNVMLGYLRAENPGVLEPP---------ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPD 1058
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130740 640 KVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEA 714
Cdd:PRK06814 1059 ALHAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEA 1133
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
225-711 |
0e+00 |
|
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: 728.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 225 EDVNFTPDSYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIK 304
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 305 TIFTSRQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMP------RLAQVKQQPEEEALILFTSGSEG 378
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPpkwllrIFGVAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 379 HPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTV 458
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 459 LFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP-MAAKPGTVGRIL 537
Cdd:cd05909 241 LLGTPTFLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPqSPNKEGTVGRPL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 538 PGMDARLLSVPG-----IEEGGRLQLKGPNIMNGYLRVEKPGVLevptaenvrgEMERGWYDTGDIVRFDEQGFVQIQGR 612
Cdd:cd05909 321 PGMEVKIVSVETheevpIGEGGLLLVRGPNVMLGYLNEPELTSF----------AFGDGWYDTGDIGKIDGEGFLTITGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 613 AKRFAKIAGEMVSLEMVEQLALGVSP-DKVHATAIKSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYL 691
Cdd:cd05909 391 LSRFAKIAGEMVSLEAIEDILSEILPeDNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQV 470
|
490 500
....*....|....*....|
gi 16130740 692 KQMPLLGSGKPDFVTLKSWV 711
Cdd:cd05909 471 EEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
11-709 |
7.67e-165 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 504.84 E-value: 7.67e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 11 RVLYRVRVTGDTQ-ALKGeRVLITPNHVSFIDGILLGLFLPvRPV-FAVYTSISQQWYMRWLKSFIDFVPLDPTQPMAIK 88
Cdd:PRK08633 424 HTRYRLRVEGRENiPAKG-GALLLGNHVSWIDWALLQAASP-RPIrFVMERSIYEKWYLKWFFKLFGVIPISSGGSKESL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 89 HLVR-LVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSR----LKGLVKRRLFPQITLH 163
Cdd:PRK08633 502 EFIRkALDDGEVVCIFPEGAITRNGQLNEFKRGFELIVKGTDVPIIPFYIRGLWGSIFSRasgkFLWRWPTRIPYPVTVA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 164 ILPPtqvaMPDAPRARDRRKIAGEmLHQIMMEARMAVRPreTLYESLLSAMYRFGaGKKCVEDVNFTPDSYRKLLTKTLF 243
Cdd:PRK08633 582 FGKP----MPAHSTAHEVKQAVFE-LSFDSWKSRKEALP--PLAEAWIDTAKRNW-SRLAVADSTGGELSYGKALTGALA 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 244 VGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPE 323
Cdd:PRK08633 654 LARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 324 QLTQ-VRWVYLEDLKADVTTADKVWIF-AHLLMP-----RLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQ 396
Cdd:PRK08633 734 ELPEnVKVIYLEDLKAKISKVDKLTALlAARLLParllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQ 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 397 IKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARF--AN 474
Cdd:PRK08633 814 ISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNkkLH 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 475 PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP----------MAAKPGTVGRILPGMDAR- 543
Cdd:PRK08633 894 PLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaadfkrqTGSKEGSVGMPLPGVAVRi 973
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 544 -----LLSVPGIEEgGRLQLKGPNIMNGYL-RVEKpgvlevpTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFA 617
Cdd:PRK08633 974 vdpetFEELPPGED-GLILIGGPQVMKGYLgDPEK-------TAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFA 1045
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 618 KIAGEMVSLEMVE---QLALGVSPDKVHATAIkSDASKGEALVLFTTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQM 694
Cdd:PRK08633 1046 KIGGEMVPLGAVEeelAKALGGEEVVFAVTAV-PDEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEAL 1124
|
730
....*....|....*
gi 16130740 695 PLLGSGKPDFVTLKS 709
Cdd:PRK08633 1125 PLLGSGKLDLKGLKE 1139
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
233-716 |
3.48e-95 |
|
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: 302.50 E-value: 3.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTsrq 311
Cdd:COG0318 26 TYAELDARARRLAAALRALGVGpGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 312 fldkgklwhlpeqltqvrwvyledlkadvttadkvwifahllmprlaqvkqqpeeeALILFTSGSEGHPKGVVHSHKSIL 391
Cdd:COG0318 103 --------------------------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 392 ANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSpLHYRIVPELVYDRSCTVLFGTSTF---LGH 468
Cdd:COG0318 127 ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMlarLLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 469 YARFAnPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINV--PMAAKPGTVGRILPGMDARLLS 546
Cdd:COG0318 206 HPEFA-RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 547 VPGIE----EGGRLQLKGPNIMNGYLRvekpgvLEVPTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGE 622
Cdd:COG0318 285 EDGRElppgEVGEIVVRGPNVMKGYWN------DPEATAEAFRD----GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 623 MVSLEMVEQLALGVspDKVHATAI--KSDASKGEALVLFTT---DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLL 697
Cdd:COG0318 355 NVYPAEVEEVLAAH--PGVAEAAVvgVPDEKWGERVVAFVVlrpGAELDAEELRAFLRER-LARYKVPRRVEFVDELPRT 431
|
490
....*....|....*....
gi 16130740 698 GSGKPDFVTLKSWVDEAEQ 716
Cdd:COG0318 432 ASGKIDRRALRERYAAGAL 450
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
368-703 |
8.94e-83 |
|
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: 266.07 E-value: 8.94e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSPLhYRIV 447
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFD-PEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 PELVYDRSCTVLFGTSTFLGHYARFAN--PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP 525
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPEsaGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 --MAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRVEkpgvlevptaENVRGEMERGWYDTGDIV 599
Cdd:cd04433 161 ddDARKPGSVGRPVPGVEVRIVDPDGGElppgEIGELVVRGPSVMKGYWNNP----------EATAAVDEDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 600 RFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsPDKVHATAIKS-DASKGEALVLFTTDNE---LTRDKLQQYAR 675
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGH-PGVAEAAVVGVpDPEWGERVVAVVVLRPgadLDAEELRAHVR 309
|
330 340
....*....|....*....|....*...
gi 16130740 676 EHGVPeLAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd04433 310 ERLAP-YKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
233-614 |
1.70e-65 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 222.57 E-value: 1.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNaGISAAVIFGAIARRRM-PAMMNYTAGVKGLTSAITAAEIKTIFTSR 310
Cdd:pfam00501 23 TYRELDERANRLAAGLRALGVGkGDRVAILLPN-SPEWVVAFLACLKAGAvYVPLNPRLPAEELAYILEDSGAKVLITDD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 311 QFLDKG--KLWHLPEQLTQVRWVYLED-LKADVTTADKVWIFAHLLMPrlaqVKQQPEEEALILFTSGSEGHPKGVVHSH 387
Cdd:pfam00501 102 ALKLEEllEALGKLEVVKLVLVLDRDPvLKEEPLPEEAKPADVPPPPP----PPPDPDDLAYIIYTSGTTGKPKGVMLTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 388 KSILANVEQIKTIAD----FTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS--PLHYRIVPELVYDRSCTVLFG 461
Cdd:pfam00501 178 RNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGfpALDPAALLELIERYKVTVLYG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 462 TSTFLgHY---ARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPM---AAKPGTVGR 535
Cdd:pfam00501 258 VPTLL-NMlleAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLGSVGR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 536 ILPGMDARLLSVPGIE-----EGGRLQLKGPNIMNGYL-RVEKpgvlevpTAENVRgemERGWYDTGDIVRFDEQGFVQI 609
Cdd:pfam00501 337 PLPGTEVKIVDDETGEpvppgEPGELCVRGPGVMKGYLnDPEL-------TAEAFD---EDGWYRTGDLGRRDEDGYLEI 406
|
....*
gi 16130740 610 QGRAK 614
Cdd:pfam00501 407 VGRKK 411
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
233-701 |
3.02e-65 |
|
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: 223.59 E-value: 3.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNAGISAAVIFGAIARRRMPAMMN--YTAgvKGLTSAITAAEIKTIFTS 309
Cdd:cd05936 26 TYRELDALAEAFAAGLQNLGVQpGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNplYTP--RELEHILNDSGAKALIVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 310 RQFLDKGKLWHLPEQLTQVRwvyledlkadvttadkvwifahllmprlaqvkqqPEEEALILFTSGSEGHPKGVVHSHKS 389
Cdd:cd05936 104 VSFTDLLAAGAPLGERVALT----------------------------------PEDVAVLQYTSGTTGVPKGAMLTHRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 390 ILANVEQIKTIA--DFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRsCTVLFGTST--- 464
Cdd:cd05936 150 LVANALQIKAWLedLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRKHR-VTIFPGVPTmyi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 465 -FLGHYARfaNPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGMDA 542
Cdd:cd05936 229 aLLNAPEF--KKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNpLDGPRKPGSIGIPLPGTEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 543 RLLSVPGIE----EGGRLQLKGPNIMNGYLRveKPGVlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAK 618
Cdd:cd05936 307 KIVDDDGEElppgEVGELWVRGPQVMKGYWN--RPEE----TAEAFVD----GWLRTGDIGYMDEDGYFFIVDRKKDMII 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 619 IAGEMVSLEMVEQlALGVSPDKVHATAIK-SDASKGEALVLFTT---DNELTRDKLQQYAREHgvpeLA---VPRDIRYL 691
Cdd:cd05936 377 VGGFNVYPREVEE-VLYEHPAVAEAAVVGvPDPYSGEAVKAFVVlkeGASLTEEEIIAFCREQ----LAgykVPRQVEFR 451
|
490
....*....|
gi 16130740 692 KQMPLLGSGK 701
Cdd:cd05936 452 DELPKSAVGK 461
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
197-709 |
1.78e-59 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 209.67 E-value: 1.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 197 RMAVRPRETLYESLLSAMYRFGAGKKCVeDVNFTPDSYRKLLTKTLFVGRILEKYSveGERIGLMLPNAGISAAVIFGAI 276
Cdd:PRK06334 12 RGKLRSGKTVLESFLKLCSEMTTATVCW-DEQLGKLSYNQVRKAVIALATKVSKYP--DQHIGIMMPASAGAYIAYFATL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 277 ARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDK-----GKLWHLPEQLtqvrwVYLEDLKADVTTADKVWIFAH 351
Cdd:PRK06334 89 LSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqthGEDAEYPFSL-----IYMEEVRKELSFWEKCRIGIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 352 LLMP-----RLAQV-KQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGL-TVG 424
Cdd:PRK06334 164 MSIPfewlmRWFGVsDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnSCT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 425 LFtPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYD--FYRLRYVVAGAEKLQESTKQLWQDK 502
Cdd:PRK06334 244 LF-PLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQEscLPSLRFVVIGGDAFKDSLYQEALKT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 503 F-GLRILEGYGVTECAPVVSINVPMAAKPGT-VGRILPGMDARLLS----VP-GIEEGGRLQLKGPNIMNGYLRvEKPGv 575
Cdd:PRK06334 323 FpHIQLRQGYGTTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSeetkVPvSSGETGLVLTRGTSLFSGYLG-EDFG- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 576 levptaenvRGEMERG---WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL-GVS-PDKVHATAIKSDA 650
Cdd:PRK06334 401 ---------QGFVELGgetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMeGFGqNAADHAGPLVVCG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 651 SKGEA--LVLFT---TDNELTRDKLQQYAREHGVpelavprDIRYLKQM---PLLGSGKPDFVTLKS 709
Cdd:PRK06334 472 LPGEKvrLCLFTtfpTSISEVNDILKNSKTSSIL-------KISYHHQVesiPMLGTGKPDYCSLNA 531
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
205-701 |
5.51e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 205.14 E-value: 5.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 205 TLYESLLSAMYRFGAGKKCV-EDVNFTpdsYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNagiSAAVIFGAIArrrmp 282
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVfGDQRLT---YAELNARVRRAAAALAALGIGkGDRVAIWAPN---SPHWVIAALG----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 283 AMMnytAG--VKGLTSAITAAEI---------KTIFTSRQFLdkGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAH 351
Cdd:PRK07656 75 ALK---AGavVVPLNTRYTADEAayilargdaKALFVLGLFL--GVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 352 LL---MPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTP 428
Cdd:PRK07656 150 FLaagDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 429 LLTGAEVFLYP--SPLHyriVPELVYDRSCTVLFGTST----FLGHYARfaNPYDFYRLRYVVAGAEKLQESTKQLWQDK 502
Cdd:PRK07656 230 LMRGATILPLPvfDPDE---VFRLIETERITVLPGPPTmynsLLQHPDR--SAEDLSSLRLAVTGAASMPVALLERFESE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 503 FGLR-ILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRvekpg 574
Cdd:PRK07656 305 LGVDiVLTGYGLSEASGVTTFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEvpvgEVGELLVRGPNVMKGYYD----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 575 vLEVPTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKG 653
Cdd:PRK07656 380 -DPEATAAAIDAD---GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEV-LYEHPAVAEAAVIGvPDERLG 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16130740 654 E---ALVLFTTDNELTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK07656 455 EvgkAYVVLKPGAELTEEELIAYCREH----LAkykVPRSIEFLDELPKNATGK 504
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
301-709 |
5.69e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 202.34 E-value: 5.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 301 AEIKTIFTSRQFLdkGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLmprlaqvKQQPEEE----------ALI 370
Cdd:PRK06187 102 AEDRVVLVDSEFV--PLLAAILPQLPTVRTVIVEGDGPAAPLAPEVGEYEELL-------AAASDTFdfpdidendaAAM 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 371 LFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGlFTPLLTGAEVfLYPSPLHYRIVPEL 450
Cdd:PRK06187 173 LYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLP-YLALMAGAKQ-VIPRRFDPENLLDL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 451 VYDRSCTVLFGTST---FLGHYARfANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP-- 525
Cdd:PRK06187 251 IETERVTFFFAVPTiwqMLLKAPR-AYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPed 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 ----MAAKPGTVGRILPGMDARLL-----SVP-GIEEGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVRGemerGWYDT 595
Cdd:PRK06187 330 qlpgQWTKRRSAGRPLPGVEARIVdddgdELPpDGGEVGEIIVRGPWLMQGYWNRPE------ATAETIDG----GWLHT 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 596 GDIVRFDEQGFVQIQGRAKRFAKIAGEMV-SLEmVEQlALGVSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKL 670
Cdd:PRK06187 400 GDVGYIDEDGYLYITDRIKDVIISGGENIyPRE-LED-ALYGHPAVAEVAVIgVPDEKWGErpvAVVVLKPGATLDAKEL 477
|
410 420 430
....*....|....*....|....*....|....*....
gi 16130740 671 QQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKS 709
Cdd:PRK06187 478 RAFLRGR-LAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
224-701 |
6.04e-51 |
|
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: 184.72 E-value: 6.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 224 VEDVNFTPDSYRKLLTKTLFVGRILEKYSV-EGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAE 302
Cdd:cd05911 3 IDADTGKELTYAQLRTLSRRLAAGLRKLGLkKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 303 IKTIFTSRQFLDKgkLWHLPEQLTQVRWVY-LEDLKADVTTADKVW-IFAHLLMPRLAQVKQQPEEE-ALILFTSGSEGH 379
Cdd:cd05911 83 PKVIFTDPDGLEK--VKEAAKELGPKDKIIvLDDKPDGVLSIEDLLsPTLGEEDEDLPPPLKDGKDDtAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 380 PKGVVHSHKSILANVEQIKTI--ADFTTNDRFMSALPLFHSFGLTVGLFTPLLtGAEVFLYPSPlHYRIVPELVYDRSCT 457
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKF-DSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 458 VLFGTSTflgHYARFAN-----PYDFYRLRYVVAGAEKLQESTKQLWQDKFGL-RILEGYGVTECAPVVSINVPMAAKPG 531
Cdd:cd05911 239 FLYLVPP---IAAALAKsplldKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 532 TVGRILPGMDARLLSVP-----GIEEGGRLQLKGPNIMNGYLRVEKpgvlevptaENVRGEMERGWYDTGDIVRFDEQGF 606
Cdd:cd05911 316 SVGRLLPNVEAKIVDDDgkdslGPNEPGEICVRGPQVMKGYYNNPE---------ATKETFDEDGWLHTGDIGYFDEDGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 607 VQIQGRAKRFAKIAGEMVSLEMVEQLALgvSPDKVHATAI--KSDASKGE---ALVLFTTDNELTRDKLQQYAREH---- 677
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLL--EHPGVADAAVigIPDEVSGElprAYVVRKPGEKLTEKEVKDYVAKKvasy 464
|
490 500
....*....|....*....|....*....
gi 16130740 678 -----GVpelavprdiRYLKQMPLLGSGK 701
Cdd:cd05911 465 kqlrgGV---------VFVDEIPKSASGK 484
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
233-718 |
4.30e-48 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 178.77 E-value: 4.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKtlfVGRI---LEKYSVE-GERIGLMLPNagISAAVIF-------GAIArrrMPAMMNYTAgvKGLTSAITAA 301
Cdd:COG0365 41 TYAELRRE---VNRFanaLRALGVKkGDRVAIYLPN--IPEAVIAmlacariGAVH---SPVFPGFGA--EALADRIEDA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 302 EIKTIFTSRQFLDKGKLWHLPEQLTQVR--------WVYLEDLKADVTTADKVWiFAHLLM---PRLAQVKQQPEEEALI 370
Cdd:COG0365 111 EAKVLITADGGLRGGKVIDLKEKVDEALeelpslehVIVVGRTGADVPMEGDLD-WDELLAaasAEFEPEPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 371 LFTSGSEGHPKGVVHSHKSILANVE-QIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PSPLHYRI 446
Cdd:COG0365 190 LYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYegrPDFPDPGR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 VPELVYDRSCTVLFGTST----FLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CAPVVS 521
Cdd:COG0365 270 LWELIEKYGVTVFFTAPTairaLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFIS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 522 INVPMAAKPGTVGRILPGMDARLL-----SVPGiEEGGRLQLKG--PNIMNGYLR-VEKpgvlevpTAENVRGEMErGWY 593
Cdd:COG0365 350 NLPGLPVKPGSMGKPVPGYDVAVVdedgnPVPP-GEEGELVIKGpwPGMFRGYWNdPER-------YRETYFGRFP-GWY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 594 DTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS-LEMVEQLalgVSPDKVHATAI--KSDASKGEALVLF------TTDNE 664
Cdd:COG0365 421 RTGDGARRDEDGYFWILGRSDDVINVSGHRIGtAEIESAL---VSHPAVAEAAVvgVPDEIRGQVVKAFvvlkpgVEPSD 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16130740 665 LTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHD 718
Cdd:COG0365 498 ELAKELQAHVREE-LGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGD 550
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
368-614 |
5.10e-48 |
|
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: 175.56 E-value: 5.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsPLHYRIV 447
Cdd:cd05941 92 ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLP-KFDPKEV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 PELVYDRSCTVLFGTSTFlghYARFANPYDFY-------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVT 514
Cdd:cd05941 171 AISRLMPSITVFMGVPTI---YTRLLQYYEAHftdpqfaraaaaeRLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECapVVSINVPMAA--KPGTVGRILPGMDARLLSVPGIEEG-----GRLQLKGPNIMNGYLRveKPGVlevpTAENVRGE 587
Cdd:cd05941 248 EI--GMALSNPLDGerRPGTVGMPLPGVQARIVDEETGEPLprgevGEIQVRGPSVFKEYWN--KPEA----TKEEFTDD 319
|
250 260
....*....|....*....|....*..
gi 16130740 588 merGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:cd05941 320 ---GWFKTGDLGVVDEDGYYWILGRSS 343
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
365-701 |
5.89e-48 |
|
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: 175.11 E-value: 5.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd17631 98 DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 riVPELVYDRS----CTVLFGTST---FLGHYARFANpYDFYRLRYVVAGAEKLQESTKQLWQDkFGLRILEGYGVTECA 517
Cdd:cd17631 175 --DPETVLDLIerhrVTSFFLVPTmiqALLQHPRFAT-TDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVVSINVP--MAAKPGTVGRILPGMDARLL-----SVPgIEEGGRLQLKGPNIMNGYLRvekpgvLEVPTAENVRGemer 590
Cdd:cd17631 251 PGVTFLSPedHRRKLGSAGRPVFFVEVRIVdpdgrEVP-PGEVGEIVVRGPHVMAGYWN------RPEATAAAFRD---- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 591 GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsPDKVHATAI-KSDASKGE---ALVLFTTDNELT 666
Cdd:cd17631 320 GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEH-PAVAEVAVIgVPDEKWGEavvAVVVPRPGAELD 398
|
330 340 350
....*....|....*....|....*....|....*...
gi 16130740 667 RDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:cd17631 399 EDELIAHCRER----LArykIPKSVEFVDALPRNATGK 432
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
364-638 |
3.64e-47 |
|
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: 173.55 E-value: 3.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSP-- 441
Cdd:cd05907 86 PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAet 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 -------LHYRI---VP---ELVYDRSCTVLfgTSTFLGHYARFANpydFYRLRYVVAGAEKLQESTKQLWQdKFGLRIL 508
Cdd:cd05907 166 llddlseVRPTVflaVPrvwEKVYAAIKVKA--VPGLKRKLFDLAV---GGRLRFAASGGAPLPAELLHFFR-ALGIPVY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEEGGRLQLKGPNIMNGYLRvekpgvLEVPTAENVrgeM 588
Cdd:cd05907 240 EGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR------IADDGEILVRGPNVMLGYYK------NPEATAEAL---D 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16130740 589 ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQlALGVSP 638
Cdd:cd05907 305 ADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIEN-ALKASP 354
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
349-701 |
4.76e-47 |
|
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: 174.48 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 349 FAHLL---MPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQ-IKTIADFTTNDRFMSALPLFHSFGLTVG 424
Cdd:cd05959 144 LAELVaaeAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELyARNVLGIREDDVCFSAAKLFFAYGLGNS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 425 LFTPLLTGAEVFLYPSplhyRIVPELVYDR----SCTVLFGTSTFlghYARF-ANP----YDFYRLRYVVAGAEKLQEST 495
Cdd:cd05959 224 LTFPLSVGATTVLMPE----RPTPAAVFKRirryRPTVFFGVPTL---YAAMlAAPnlpsRDLSSLRLCVSAGEALPAEV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 496 KQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYL-RV 570
Cdd:cd05959 297 GERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDvadgEPGELYVRGPSSATMYWnNR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 571 EKpgvlevpTAENVRGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDA 650
Cdd:cd05959 377 DK-------TRDTFQGE----WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVES-ALVQHPAVLEAAVVGVED 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 651 SKG----EALVLF---TTDNELTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05959 445 EDGltkpKAFVVLrpgYEDSEALEEELKEFVKD-RLAPYKYPRWIVFVDELPKTATGK 501
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
253-708 |
4.90e-47 |
|
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: 173.40 E-value: 4.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 253 VEGERIGLMLPN----AGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFtsrqfLDKGKLWHLPEQLTQV 328
Cdd:cd05922 16 VRGERVVLILPNrftyIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVL-----ADAGAADRLRDALPAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 329 R----WVYLEDLKADVTTADkvwifAHLLmprlaqvkqQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFT 404
Cdd:cd05922 91 PdpgtVLDADGIRAARASAP-----AHEV---------SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 405 TNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFA-NPYDFYRLRY 483
Cdd:cd05922 157 ADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGfDPAKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 484 VVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAPVVSINVP--MAAKPGTVGRILPGMDARLLSVPGIEEG----GRL 556
Cdd:cd05922 236 LTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPerILEKPGSIGLAIPGGEFEILDDDGTPTPpgepGEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 557 QLKGPNIMNGYLRVEKpgvlevPTAENVRGEMeRGWydTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGV 636
Cdd:cd05922 316 VHRGPNVMKGYWNDPP------YRRKEGRGGG-VLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA-AARS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130740 637 SPDKVHATAIKSDASKGEALVLFTT-DNELTRDKLQQYAREHGvPELAVPRDIRYLKQMPLLGSGKPDFVTLK 708
Cdd:cd05922 386 IGLIIEAAAVGLPDPLGEKLALFVTaPDKIDPKDVLRSLAERL-PPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
254-710 |
1.95e-45 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 172.06 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 254 EGERIGLMLPNAGISAAVIFGAIArrrmpammnytAGV----------KGLTSAITAAEIKTIFTSRQFLDKG---KLWH 320
Cdd:PRK07529 82 PGDVVAFLLPNLPETHFALWGGEA-----------AGIanpinpllepEQIAELLRAAGAKVLVTLGPFPGTDiwqKVAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 321 LPEQLTQVRWVYLEDLkADVTTADKVWIfAHLLMPR--------LAQVKQQPEEEALI-----------LF-TSGSEGHP 380
Cdd:PRK07529 151 VLAALPELRTVVEVDL-ARYLPGPKRLA-VPLIRRKaharildfDAELARQPGDRLFSgrpigpddvaaYFhTGGTTGMP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 381 KGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLyPSPLHYRivPELVYDR------ 454
Cdd:PRK07529 229 KLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVL-ATPQGYR--GPGVIANfwkive 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 455 --SCTVLFGTSTFLGHYA-RFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAA-KP 530
Cdd:PRK07529 306 ryRINFLSGVPTVYAALLqVPVDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGErRI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 531 GTVGRILPGMDARLLSVPG---------IEEGGRLQLKGPNIMNGYLRVEKpgvlevptaeNVRGEMERGWYDTGDIVRF 601
Cdd:PRK07529 386 GSVGLRLPYQRVRVVILDDagrylrdcaVDEVGVLCIAGPNVFSGYLEAAH----------NKGLWLEDGWLNTGDLGRI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 602 DEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKLQQYAREH 677
Cdd:PRK07529 456 DADGYFWLTGRAKDLIIRGGHNIDPAAIEE-ALLRHPAVALAAAVgRPDAHAGElpvAYVQLKPGASATEAELLAFARDH 534
|
490 500 510
....*....|....*....|....*....|....
gi 16130740 678 gVPE-LAVPRDIRYLKQMPLLGSGKPDFVTLKSW 710
Cdd:PRK07529 535 -IAErAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
301-680 |
3.12e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 168.36 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 301 AEIKTIFTSRQF-LDKgkLWHLPEQLTQVRWVYLEDLKA-----------DVTTADKVWIFAHLLMPRLAQVKqqPEEEA 368
Cdd:COG1022 111 SGAKVLFVEDQEqLDK--LLEVRDELPSLRHIVVLDPRGlrddprllsldELLALGREVADPAELEARRAAVK--PDDLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTpLLTGAEVFLYPSP------L 442
Cdd:COG1022 187 TIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPdtlaedL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 -----HYRI-VP---ELVYDR--------------------------SCTVLFGTSTFLGHYARFAnpydFY-------- 479
Cdd:COG1022 266 revkpTFMLaVPrvwEKVYAGiqakaeeagglkrklfrwalavgrryARARLAGKSPSLLLRLKHA----LAdklvfskl 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 ------RLRYVVAGAEKLQESTkqlwqDKF----GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpg 549
Cdd:COG1022 342 realggRLRFAVSGGAALGPEL-----ARFfralGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVK------ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 550 IEEGGRLQLKGPNIMNGYLRveKPGVlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEM 628
Cdd:COG1022 411 IAEDGEILVRGPNVMKGYYK--NPEA----TAEAFDAD---GWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQP 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130740 629 VEQlalgvspdkvhatAIKSDASKGEALV----------LFTTDneltRDKLQQYAREHGVP 680
Cdd:COG1022 482 IEN-------------ALKASPLIEQAVVvgdgrpflaaLIVPD----FEALGEWAEENGLP 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
373-703 |
1.05e-43 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 161.49 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 373 TSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSPLHYR---IVPE 449
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHV-VLAGPAGYRnpgLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 450 ---LVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP- 525
Cdd:cd05944 89 fwkLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 MAAKPGTVGRILPGMDARLLSVPGI---------EEGGRLQLKGPNIMNGYLRVEKpgvlevptaeNVRGEMERGWYDTG 596
Cdd:cd05944 169 GPKRPGSVGLRLPYARVRIKVLDGVgrllrdcapDEVGEICVAGPGVFGGYLYTEG----------NKNAFVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKLQQ 672
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEE-ALLRHPAVAFAGAVgQPDAHAGElpvAYVQLKPGAVVEEEELLA 317
|
330 340 350
....*....|....*....|....*....|..
gi 16130740 673 YAREHgVPE-LAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd05944 318 WARDH-VPErAAVPKHIEVLEELPVTAVGKVF 348
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
229-701 |
9.11e-42 |
|
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: 158.01 E-value: 9.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 229 FTPD---SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNAGISAAVIFGAIARRRMPAMMNytagvkgltsaitaaeik 304
Cdd:cd05919 5 YAADrsvTYGQLHDGANRLGSALRNLGVSsGDRVLLLMLDSPELVQLFLGCLARGAIAVVIN------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 305 TIFTSRQFLDKGklwhlpeQLTQVRWVYLEDlkadvttadkvwifahllmprlaqvkqqpEEEALILFTSGSEGHPKGVV 384
Cdd:cd05919 67 PLLHPDDYAYIA-------RDCEARLVVTSA-----------------------------DDIAYLLYSSGTTGPPKGVM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 385 HSHKSILANVEQI-KTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyrIVPELVYDRSC----TVL 459
Cdd:cd05919 111 HAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGW----PTAERVLATLArfrpTVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 460 FGTSTFLGHYARFAN--PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRIL 537
Cdd:cd05919 187 YGVPTFYANLLDSCAgsPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 538 PGMDARLLSVPG--IEEG--GRLQLKGPNIMNGYLRvekpgvlevpTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRA 613
Cdd:cd05919 267 PGYEIRLVDEEGhtIPPGeeGDLLVRGPSAAVGYWN----------NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 614 KRFAKIAGEMVSLEMVEQLA---LGVSPDKVHATAIKSDASKGEALVL----FTTDNELTRDkLQQYAREHgVPELAVPR 686
Cdd:cd05919 337 DDMLKVGGQWVSPVEVESLIiqhPAVAEAAVVAVPESTGLSRLTAFVVlkspAAPQESLARD-IHRHLLER-LSAHKVPR 414
|
490
....*....|....*
gi 16130740 687 DIRYLKQMPLLGSGK 701
Cdd:cd05919 415 RIAFVDELPRTATGK 429
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
364-698 |
3.92e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 158.62 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQ----IKTIADftTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
Cdd:PRK05605 218 PDDVALILYTSGTTGKPKGAQLTHRNLFANAAQgkawVPGLGD--GPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPlhyriVPELVYD----RSCTVLFGTSTFlghYARFA-----NPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEG 510
Cdd:PRK05605 296 AP-----DIDLILDamkkHPPTWLPGVPPL---YEKIAeaaeeRGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 511 YGVTECAPVVSINvPMAA--KPGTVGRILPGMDARLL-------SVPGIEEgGRLQLKGPNIMNGYLRVEKpgvlevPTA 581
Cdd:PRK05605 368 YGLTETSPIIVGN-PMSDdrRPGYVGVPFPDTEVRIVdpedpdeTMPDGEE-GELLVRGPQVFKGYWNRPE------ETA 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI---KSDASKG-EALV 657
Cdd:PRK05605 440 KSFLD----GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEE-VLREHPGVEDAAVVglpREDGSEEvVAAV 514
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16130740 658 LFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMP--LLG 698
Cdd:PRK05605 515 VLEPGAALDPEGLRAYCREH-LTRYKVPRRFYHVDELPrdQLG 556
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
356-701 |
1.58e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 153.67 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 356 RLAQVKQQ--PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR---FMSALPLFHSFGLTVG--LFTP 428
Cdd:PRK08974 195 RMQYVKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHPGkelVVTALPLYHIFALTVNclLFIE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 429 LltGAEVFLYPSPlhyRIVPELVYDRS---CTVLFGTSTFLGhyARFANP----YDFYRLRYVVAGAEKLQESTKQLWQD 501
Cdd:PRK08974 275 L--GGQNLLITNP---RDIPGFVKELKkypFTAITGVNTLFN--ALLNNEefqeLDFSSLKLSVGGGMAVQQAVAERWVK 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 KFGLRILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGMDARLL----SVPGIEEGGRLQLKGPNIMNGYL-RVEKpgv 575
Cdd:PRK08974 348 LTGQYLLEGYGLTECSPLVSVNpYDLDYYSGSIGLPVPSTEIKLVdddgNEVPPGEPGELWVKGPQVMLGYWqRPEA--- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 576 levpTAEnvrgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ-LALGVSPDKVHATAIKSDASkGE 654
Cdd:PRK08974 425 ----TDE----VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDvVMLHPKVLEVAAVGVPSEVS-GE 495
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16130740 655 ALVLFTT--DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK08974 496 AVKIFVVkkDPSLTEEELITHCRRH-LTGYKVPKLVEFRDELPKSNVGK 543
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
363-703 |
1.70e-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: 148.44 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSF--SFDVSVWeIFGALLAGATLVVLPEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 LHYRI--VPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAP 518
Cdd:cd05930 169 VRKDPeaLADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 519 VVSINV--PMAAKPGTV--GRILPGMDARLLS-----VPgIEEGGRLQLKGPNIMNGYLRveKPG-----VLEVPTAENV 584
Cdd:cd05930 249 DATYYRvpPDDEEDGRVpiGRPIPNTRVYVLDenlrpVP-PGVPGELYIGGAGLARGYLN--RPEltaerFVPNPFGPGE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 585 RGemergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPdkVHATAI--KSDASKGEALVLFTT- 661
Cdd:cd05930 326 RM------YRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPG--VREAAVvaREDGDGEKRLVAYVVp 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16130740 662 --DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd05930 398 deGGELDEEELRAHLAER-LPDYMVPSAFVVLDALPLTPNGKVD 440
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
364-614 |
8.50e-38 |
|
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: 147.20 E-value: 8.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY---PS 440
Cdd:cd05914 88 EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLdkiPS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 PL-----HYRI-------VPELVYDRSCTVLFGTSTFLGHYARFANPY---DFY-------------RLRYVVAGAEKL- 491
Cdd:cd05914 168 AKiialaFAQVtptlgvpVPLVIEKIFKMDIIPKLTLKKFKFKLAKKInnrKIRklafkkvheafggNIKEFVIGGAKIn 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 492 QESTKQLWqdKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNIMNGYLRVE 571
Cdd:cd05914 248 PDVEEFLR--TIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPNVMKGYYKNP 325
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16130740 572 KpgvlevPTAENVrgeMERGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:cd05914 326 E------ATAEAF---DKDGWFHTGDLGKIDAEGYLYIRGRKK 359
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
365-701 |
3.97e-37 |
|
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: 144.40 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGP--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RIVPELVYDR----SCTVLFGTSTFlghYARFANP----YDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEC 516
Cdd:cd05972 158 RFDAERILELleryGVTSFCGPPTA---YRMLIKQdlssYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINVPMAAKPGTVGRILPGMDARLLS------VPGiEEGG-RLQLKGPNIMNGYLRVEKpgvlevPTAENVRGeme 589
Cdd:cd05972 235 GLTVGNFPDMPVKPGSMGRPTPGYDVAIIDddgrelPPG-EEGDiAIKLPPPGLFLGYVGDPE------KTEASIRG--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 590 rGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKS-DASKGE---ALVLFTTDNEL 665
Cdd:cd05972 305 -DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES-ALLEHPAVAEAAVVGSpDPVRGEvvkAFVVLTSGYEP 382
|
330 340 350
....*....|....*....|....*....|....*....
gi 16130740 666 TR---DKLQQYAREHGVPElAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05972 383 SEelaEELQGHVKKVLAPY-KYPREIEFVEELPKTISGK 420
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
355-710 |
5.84e-37 |
|
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: 144.18 E-value: 5.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQvKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRF-MSALPLFHSfGLTVGLFTPLLTGA 433
Cdd:cd05969 80 EELYE-RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYwCTADPGWVT-GTVYGIWAPWLNGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 434 EVFLYPSPLHYRIVPELVYDRSCTVLFGTST----FLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILE 509
Cdd:cd05969 158 TNVVYEGRFDAESWYGIIERVKVTVWYTAPTairmLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 GYGVTECAPVVSINVP-MAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKG--PNIMNGYLRVEkpgvlevptaE 582
Cdd:cd05969 238 TWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVDENGNElppgTKGILALKPgwPSMFRGIWNDE----------E 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 583 NVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGEALVLFTT 661
Cdd:cd05969 308 RYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES-ALMEHPAVAEAGVIgKPDPLRGEIIKAFIS 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16130740 662 DNE--LTRDKLQQYAREHGVPELA---VPRDIRYLKQMPLLGSGKPDFVTLKSW 710
Cdd:cd05969 387 LKEgfEPSDELKEEIINFVRQKLGahvAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
364-701 |
9.17e-37 |
|
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: 141.26 E-value: 9.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPSP-L 442
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATM-VFPSPsF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 HYRIVPELVYDRSCTVLFGTSTF----LGHyARFANpYDFYRLRY-VVAGAEKLQESTKQLWQDKFGLRILEGYGVTECA 517
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPTMfiaeLEH-PDFDK-FDLSSLRTgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVV---SINVPMAAKPGTVGRILPGMDARLL-----SVPGIEEGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVRGEme 589
Cdd:cd05917 158 PVStqtRTDDSIEKRVNTVGRIMPHTEAKIVdpeggIVPPVGVPGELCIRGYSVMKGYWNDPE------KTAEAIDGD-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 590 rGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPD--KVHATAIKsDASKGE---ALVLFTTDNE 664
Cdd:cd05917 230 -GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEF-LHTHPKvsDVQVVGVP-DERYGEevcAWIRLKEGAE 306
|
330 340 350
....*....|....*....|....*....|....*..
gi 16130740 665 LTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05917 307 LTEEDIKAYCKG-KIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
233-703 |
1.54e-36 |
|
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: 143.99 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPNaGISAAVIFGAIARRRmpammnytAGVKGLTSAITAAEIKTIF---- 307
Cdd:cd05926 16 TYADLAELVDDLARQLAALGIKkGDRVAIALPN-GLEFVVAFLAAARAG--------AVVAPLNPAYKKAEFEFYLadlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 308 TSRQFLDKGklWHLPEQ-LTQVRWVYLEDLKADVTTADKVWIfAHLLMPRLA-------QVKQQPEEEALILFTSGSEGH 379
Cdd:cd05926 87 SKLVLTPKG--ELGPASrAASKLGLAILELALDVGVLIRAPS-AESLSNLLAdkknaksEGVPLPDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 380 PKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--------------SPLHYR 445
Cdd:cd05926 164 PKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPrfsastfwpdvrdyNATWYT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 446 IVPelvydrscTVLfgtSTFLGHYARfaNPYDFY-RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSIN- 523
Cdd:cd05926 244 AVP--------TIH---QILLNRPEP--NPESPPpKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 524 -VPMAAKPGTVG-------RILPgmDARLLSVPGIEegGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGEmerGWYDT 595
Cdd:cd05926 311 lPPGPRKPGSVGkpvgvevRILD--EDGEILPPGVV--GEICLRGPNVTRGYLNNPEA------NAEAAFKD---GWFRT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 596 GDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIK-SDASKGEALVLFTTDNE---LTRDKLQ 671
Cdd:cd05926 378 GDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLS-HPAVLEAVAFGvPDEKYGEEVAAAVVLREgasVTEEELR 456
|
490 500 510
....*....|....*....|....*....|....*
gi 16130740 672 QYAREHgvpeLA---VPRDIRYLKQMPLLGSGKPD 703
Cdd:cd05926 457 AFCRKH----LAafkVPKKVYFVDELPKTATGKIQ 487
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
362-701 |
2.15e-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: 142.52 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSP 441
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ-DI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 LHYRIVPELVYDRSCTVLFGTSTFLGHYARFAN--PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECA-P 518
Cdd:cd05903 169 WDPDKALALMREHGVTFMMGATPFLTDLLNAVEeaGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 519 VVSINVPMAAKP-GTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRvekpgvlevpTAENVRGEMERGWY 593
Cdd:cd05903 249 VTSITPAPEDRRlYTDGRPLPGVEIKVVDDTGATlapgVEGELLSRGPSVFLGYLD----------RPDLTADAAPEGWF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 594 DTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSpdKVHATAI--KSDASKGE---ALVLFTTDNELTRD 668
Cdd:cd05903 319 RTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP--GVIEAAVvaLPDERLGEracAVVVTKSGALLTFD 396
|
330 340 350
....*....|....*....|....*....|...
gi 16130740 669 KLQQYAREHGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05903 397 ELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
260-614 |
3.44e-36 |
|
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: 143.14 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 260 LMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKgklwhLPEQLTQVrwVYLEDLKAD 339
Cdd:cd05904 62 LLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEK-----LASLALPV--VLLDSAEFD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 340 VTTADKVWIFAHLLMPRLAQVKQqpEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD--FTTNDRFMSALPLFH 417
Cdd:cd05904 135 SLSFSDLLFEADEAEPPVVVIKQ--DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMFH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 418 SFGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrsctvlFGTSTFLGHYARF--------------------ANPYD 477
Cdd:cd05904 213 IYGLSSFALGLLRLGATVVVMPR-------------------FDLEELLAAIERYkvthlpvvppivlalvkspiVDKYD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 478 FYRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGMDARLLSV------ 547
Cdd:cd05904 274 LSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPetgesl 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 548 -PGieEGGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:cd05904 354 pPN--QTGELWIRGPSIMKGYLNNPEA------TAATIDKE---GWLHTGDLCYIDEDGYLFIVDRLK 410
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
370-701 |
1.19e-35 |
|
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: 137.63 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVflYP-SPLHYRIVP 448
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATV--VPvAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 449 ELVYDRSCTVLFGTST----FLGHYARfaNPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLR-ILEGYGVTECapvvsiN 523
Cdd:cd17638 83 EAIERERITVLPGPPTlfqsLLDHPGR--KKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEA------G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 524 VPMAAKPG--------TVGRILPGMDARllsvpgIEEGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVRgemERGWYDT 595
Cdd:cd17638 155 VATMCRPGddaetvatTCGRACPGFEVR------IADDGEVLVRGYNVMQGYLDDPE------ATAEAID---ADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 596 GDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASK----GEALVLFTTDNELTRDKLQ 671
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEG-ALAEHPGVAQVAVIGVPDERmgevGKAFVVARPGVTLTEEDVI 298
|
330 340 350
....*....|....*....|....*....|
gi 16130740 672 QYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd17638 299 AWCRER-LANYKVPRFVRFLDELPRNASGK 327
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
355-614 |
2.22e-35 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 140.78 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:PRK07514 146 DDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGAS 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 435 VFLYPsplhyRIVPELVYDR--SCTVLFGTSTFlghYARF-ANPyDFYR-----LRYVVAGAEKLQESTKQLWQDKFGLR 506
Cdd:PRK07514 226 MIFLP-----KFDPDAVLALmpRATVMMGVPTF---YTRLlQEP-RLTReaaahMRLFISGSAPLLAETHREFQERTGHA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECAPVVSiNvPMAAK--PGTVGRILPGMDARllsVPGIEEG--------GRLQLKGPNIMNGYLRV-EKpgv 575
Cdd:PRK07514 297 ILERYGMTETNMNTS-N-PYDGErrAGTVGFPLPGVSLR---VTDPETGaelppgeiGMIEVKGPNVFKGYWRMpEK--- 368
|
250 260 270
....*....|....*....|....*....|....*....
gi 16130740 576 levpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:PRK07514 369 ----TAEEFRAD---GFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PlsC |
COG0204 |
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ... |
1-204 |
6.00e-34 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis
Pssm-ID: 439974 [Multi-domain] Cd Length: 215 Bit Score: 129.36 E-value: 6.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 1 MLFSFFRNLCRVL-----YRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFID 75
Cdd:COG0204 11 FRYRLVRLWARLLlrllgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 76 FVPLDPTQPM----AIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGaelTHFSRLKGL 151
Cdd:COG0204 91 AIPVDRSKRRaalrALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDG---TERALPKGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130740 152 VKRRlfPQITLHILPPTQvamPDAPRARDRRKIAgEMLHQIMMEARMAVRPRE 204
Cdd:COG0204 168 LPRP--GKVTVRIGPPID---PSDLEGEDRRELA-ERLRAAIEALLAELRAEA 214
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
365-701 |
7.01e-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: 134.91 E-value: 7.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY 444
Cdd:cd05935 84 DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM-ARWDR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RIVPELVYDRSCTVLFGTSTF---LGHYARFANpYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVS 521
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMlvdLLATPEFKT-RDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 522 INVPMAAKPGTVGRILPGMDARLLSVP-GIE----EGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVRGEMERGWYDTG 596
Cdd:cd05935 242 TNPPLRPKLQCLGIP*FGVDARVIDIEtGRElppnEVGEIVVRGPQIFKGYWNRPE------ETEESFIEIKGRRFFRTG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAI-KSDASKGE---ALVLFTTD--NELTRDKL 670
Cdd:cd05935 316 DLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK-LYKHPAI*EVCVIsVPDERVGEevkAFIVLRPEyrGKVTEEDI 394
|
330 340 350
....*....|....*....|....*....|.
gi 16130740 671 QQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05935 395 IEWAREQ-MAAYKYPREVEFVDELPRSASGK 424
|
|
| LPLAT_AGPAT-like |
cd07989 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ... |
9-188 |
1.26e-33 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.
Pssm-ID: 153251 [Multi-domain] Cd Length: 184 Bit Score: 127.39 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 9 LCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPM--- 85
Cdd:cd07989 5 LRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRsar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 86 -AIKHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSRLKGLVKRRlfpqITLHI 164
Cdd:cd07989 85 eALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLPKGKKLPRPGR----VTVRI 160
|
170 180
....*....|....*....|....
gi 16130740 165 LPPTQVAmPDAPRARDRRKIAGEM 188
Cdd:cd07989 161 GEPIPPE-GLELAEEDRKELREKV 183
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
357-701 |
1.83e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 135.66 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 357 LAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTND---RFMSALPLFHSFGLTVGLFTPLLTGA 433
Cdd:PRK05677 199 VTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 434 EVFLYPSPlhyRIVPELVYDRSCTVLFGtstFLGHYARFA--------NPYDFYRLRYVVAGAEKLQESTKQLWQDKFGL 505
Cdd:PRK05677 279 HNILISNP---RDLPAMVKELGKWKFSG---FVGLNTLFValcnneafRKLDFSALKLTLSGGMALQLATAERWKEVTGC 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 506 RILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLrvEKPGVlevpTA 581
Cdd:PRK05677 353 AICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNElplgEVGELCVKGPQVMKGYW--QRPEA----TD 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGEALVLFT 660
Cdd:PRK05677 427 EILDSD---GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV-LAALPGVLQCAAIGvPDEKSGEAIKVFV 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16130740 661 ---TDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK05677 503 vvkPGETLTKEQVMEHMRAN-LTGYKVPKAVEFRDELPTTNVGK 545
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
338-614 |
2.16e-33 |
|
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: 134.02 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 338 ADVTTADKVWIFAHLLmPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFH 417
Cdd:cd17640 62 SDSSVEELLYILNHSE-SVALVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 418 SFGLTVGLFTPLLTGAEVFLYPSPL---------HYRI-VPEL-------VYDRSCTVLFgTSTFLGHYARFANpydfyR 480
Cdd:cd17640 141 SYERSAEYFIFACGCSQAYTSIRTLkddlkrvkpHYIVsVPRLweslysgIQKQVSKSSP-IKQFLFLFFLSGG-----I 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 481 LRYVVAGAEKLQESTkqlwqDKF----GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----- 551
Cdd:cd17640 215 FKFGISGGGALPPHV-----DTFfeaiGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVvlppg 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130740 552 EGGRLQLKGPNIMNGYLRvEKPGVLEVPTAEnvrgemerGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:cd17640 290 EKGIVWVRGPQVMKGYYK-NPEATSKVLDSD--------GWFNTGDLGWLTCGGELVLTGRAK 343
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
364-703 |
2.20e-33 |
|
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: 133.91 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFlypspl 442
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPF--SFDLSVmDLYPALASGATLV------ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 hyrIVPELVYD-----------RSCTVLFGTSTFLGHYARFA--NPYDFYRLRYVVAGAEKLQESTKQLWQDKF-GLRIL 508
Cdd:cd05945 168 ---PVPRDATAdpkqlfrflaeHGITVWVSTPSFAAMCLLSPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIY 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 509 EGYGVTEC-APVVSINVP----MAAKPGTVGRILPGMDARLLSVPG--IEEG--GRLQLKGPNIMNGYLRVEKpgvlevP 579
Cdd:cd05945 245 NTYGPTEAtVAVTYIEVTpevlDGYDRLPIGYAKPGAKLVILDEDGrpVPPGekGELVISGPSVSKGYLNNPE------K 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 580 TAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLF 659
Cdd:cd05945 319 TAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAF 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16130740 660 TTDNELTRDKLQQYAREH---GVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd05945 399 VVPKPGAEAGLTKAIKAElaeRLPPYMIPRRFVYLDELPLNANGKID 445
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
364-709 |
3.28e-33 |
|
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: 132.82 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFL--Y 438
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVA----QVLSIAFDACigeIFSTLCNGGTLVLadP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 439 PSPLHYRIvpelvydRSCTVLFGTSTFLGHYarfaNPYDFYRLRYVVAGAEKLQESTKQLWqdKFGLRILEGYGVTECAP 518
Cdd:cd17653 180 SDPFAHVA-------RTVDALMSTPSILSTL----SPQDFPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 519 VVSINVPMAAKPGTVGRILPGMDARLLS-----VPgIEEGGRLQLKGPNIMNGYLRVEK---PGVLEVPTAENVRgeMer 590
Cdd:cd17653 247 SSTMTELLPGQPVTIGKPIPNSTCYILDadlqpVP-EGVVGEICISGVQVARGYLGNPAltaSKFVPDPFWPGSR--M-- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 591 gwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDaskgEALVLFTTDNELTRDKL 670
Cdd:cd17653 322 --YRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVN----GRLVAFVTPETVDVDGL 395
|
330 340 350
....*....|....*....|....*....|....*....
gi 16130740 671 QQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKS 709
Cdd:cd17653 396 RSELAKH-LPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
358-701 |
1.08e-32 |
|
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: 130.93 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 358 AQVKQqpEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFL 437
Cdd:cd05912 72 SDVKL--DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 438 YPsplHY--RIVPELVYDRSCTVLFGTSTFLGHY-ARFANPYDfYRLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGVT 514
Cdd:cd05912 149 VD---KFdaEQVLHLINSGKVTIISVVPTMLQRLlEILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 E-CAPVVSINVPMA-AKPGTVGRILPGMDARLLSVPGIEEG-GRLQLKGPNIMNGYLRVEKPGvlevptaenvRGEMERG 591
Cdd:cd05912 224 EtCSQIVTLSPEDAlNKIGSAGKPLFPVELKIEDDGQPPYEvGEILLKGPNVTKGYLNRPDAT----------EESFENG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 592 WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLF-TTDNELTRDKL 670
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFvVSERPISEEEL 373
|
330 340 350
....*....|....*....|....*....|....
gi 16130740 671 QQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:cd05912 374 IAYCSEK----LAkykVPKKIYFVDELPRTASGK 403
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
357-634 |
3.37e-32 |
|
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: 129.69 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 357 LAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEV 435
Cdd:TIGR01733 112 PPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASL--SFDASVeEIFGALLAGATL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLYPSPLHYRIVPE---LVYDRSCTVLFGTSTFLGHYARfANPYDFYRLRYVVAGAEKLQESTKQLWQDKFG-LRILEGY 511
Cdd:TIGR01733 190 VVPPEDEERDDAALlaaLIAEHPVTVLNLTPSLLALLAA-ALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 512 GVTECAPVVSINVPMAAKPG-----TVGRILPGMDARLLS-----VPgIEEGGRLQLKGPNIMNGYLrvEKPGVlevpTA 581
Cdd:TIGR01733 269 GPTETTVWSTATLVDPDDAPrespvPIGRPLANTRLYVLDddlrpVP-VGVVGELYIGGPGVARGYL--NRPEL----TA 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 582 EN-----VRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL 634
Cdd:TIGR01733 342 ERfvpdpFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
301-701 |
5.68e-32 |
|
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: 130.83 E-value: 5.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 301 AEIKTIFTSRQFLDKgkLWHLPEQLTQVR--WVYLEDLKADVTTADKVWIFAHLLMPR--LAQVKQQPEEE-ALILFTSG 375
Cdd:cd12119 96 AEDRVVFVDRDFLPL--LEAIAPRLPTVEhvVVMTDDAAMPEPAGVGVLAYEELLAAEspEYDWPDFDENTaAAICYTSG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 376 SEGHPKGVVHSHKSILANVEQIKTiAD---FTTNDRFMSALPLFH--SFGLTvglFTPLLTGAEvFLYPSP-LHYRIVPE 449
Cdd:cd12119 174 TTGNPKGVVYSHRSLVLHAMAALL-TDglgLSESDVVLPVVPMFHvnAWGLP---YAAAMVGAK-LVLPGPyLDPASLAE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 450 LVYDRSCTVLFGTSTF----LGHYArfANPYDFYRLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGVTECAPVVSINVP 525
Cdd:cd12119 249 LIEREGVTFAAGVPTVwqglLDHLE--ANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPLGTVARP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 MAAKPG-----------TVGRILPGMDARLLSVPGI------EEGGRLQLKGPNIMNGYLRVEkpgvlevptaENVRGEM 588
Cdd:cd12119 326 PSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRelpwdgKAVGELQVRGPWVTKSYYKND----------EESEALT 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 589 ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASK-GE---ALVLFTTDNE 664
Cdd:cd12119 396 EDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMA-HPAVAEAAVIGVPHPKwGErplAVVVLKEGAT 474
|
410 420 430
....*....|....*....|....*....|....*..
gi 16130740 665 LTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd12119 475 VTAEELLEFLAD-KVAKWWLPDDVVFVDEIPKTSTGK 510
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
368-702 |
7.12e-32 |
|
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: 128.95 E-value: 7.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyriv 447
Cdd:cd05934 84 ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPR------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 pelvydrsctvlFGTSTFLGHYARF-------------------ANPYDF-YRLRyVVAGAEKLqESTKQLWQDKFGLRI 507
Cdd:cd05934 157 ------------FSASRFWSDVRRYgatvtnylgamlsyllaqpPSPDDRaHRLR-AAYGAPNP-PELHEEFEERFGVRL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 508 LEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL-----SVPgIEEGGRLQLK---GPNIMNGYLRVEKPgvlevp 579
Cdd:cd05934 223 LEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgqELP-AGEPGELVIRglrGWGFFKGYYNMPEA------ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 580 TAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD--KVHATAIKSDASKGE--A 655
Cdd:cd05934 296 TAEAMRN----GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER-AILRHPAvrEAAVVAVPDEVGEDEvkA 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16130740 656 LVLFTTDNELTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGKP 702
Cdd:cd05934 371 VVVLRPGETLDPEELFAFCEG-QLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
368-711 |
7.50e-32 |
|
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: 126.68 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFL---------- 437
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLlernqalaed 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 438 --YPSPLHYRIVP-ELVYdrsctVLfgtstflghyARFANPYDFYRLRYVVAG-----AEKLQESTKQlwqdkfGLRILE 509
Cdd:cd17630 82 laPPGVTHVSLVPtQLQR-----LL----------DSGQGPAALKSLRAVLLGgapipPELLERAADR------GIPLYT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 GYGVTECAPVVSINVPMAAKPGTVGRILPGmdARLlsvpGIEEGGRLQLKGPNIMNGYLRvekpGVLEVPTAENvrgeme 589
Cdd:cd17630 141 TYGMTETASQVATKRPDGFGRGGVGVLLPG--REL----RIVEDGEIWVGGASLAMGYLR----GQLVPEFNED------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 590 rGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSP--DKVHATAIKsDASKGEALVLF-TTDNELT 666
Cdd:cd17630 205 -GWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEA-ALAAHPavRDAFVVGVP-DEELGQRPVAViVGRGPAD 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16130740 667 RDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWV 711
Cdd:cd17630 282 PAELRAWLKDK-LARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
255-701 |
1.20e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 130.28 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 255 GERIGLMLPN-----------AGISAAVIFGAIARRRmpAMMNYTAGVKGLTSAITAAEIKT---------IFTSRQFLD 314
Cdd:PRK12583 70 GDRVGIWAPNcaewlltqfatARIGAILVNINPAYRA--SELEYALGQSGVRWVICADAFKTsdyhamlqeLLPGLAEGQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 315 KGKLwhLPEQLTQVRWVYLEDLKA--DVTTADKVWIFAH-LLMPRLAQVKQQ--PEEEALILFTSGSEGHPKGVVHSHKS 389
Cdd:PRK12583 148 PGAL--ACERLPELRGVVSLAPAPppGFLAWHELQARGEtVSREALAERQASldRDDPINIQYTSGTTGFPKGATLSHHN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 390 ILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVfLYPS----PLhyrIVPELVYDRSCTVLFGTST- 464
Cdd:PRK12583 226 ILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACL-VYPNeafdPL---ATLQAVEEERCTALYGVPTm 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 465 FLGH--YARFANpYDFYRLRY-VVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVV---SINVPMAAKPGTVGRILP 538
Cdd:PRK12583 302 FIAEldHPQRGN-FDLSSLRTgIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSlqtTAADDLERRVETVGRTQP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 539 GMDARLLSVPG----IEEGGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAK 614
Cdd:PRK12583 381 HLEVKVVDPDGatvpRGEIGELCTRGYSVMKGYWNNPEA------TAESIDED---GWMHTGDLATMDEQGYVRIVGRSK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 615 RFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIKSDASK-GE---ALVLFTTDNELTRDKLQQYAREhGVPELAVPRDIRY 690
Cdd:PRK12583 452 DMIIRGGENIYPREIEEF-LFTHPAVADVQVFGVPDEKyGEeivAWVRLHPGHAASEEELREFCKA-RIAHFKVPRYFRF 529
|
490
....*....|.
gi 16130740 691 LKQMPLLGSGK 701
Cdd:PRK12583 530 VDEFPMTVTGK 540
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
356-701 |
5.68e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 128.40 E-value: 5.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 356 RLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD---------FTTNDRFMSA-LPLFHSFGLTVGL 425
Cdd:PRK12492 198 SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIApLPLYHIYAFTANC 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 426 FTPLLTGAEVFLYPSPlhyRIVPELVYDRS---CTVLFGTSTFLghYARFANP----YDFYRLRYVVAGAEKLQESTKQL 498
Cdd:PRK12492 278 MCMMVSGNHNVLITNP---RDIPGFIKELGkwrFSALLGLNTLF--VALMDHPgfkdLDFSALKLTNSGGTALVKATAER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 499 WQDKFGLRILEGYGVTECAPVVSINvPMA--AKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLrvEK 572
Cdd:PRK12492 353 WEQLTGCTIVEGYGLTETSPVASTN-PYGelARLGTVGIPVPGTALKVIDDDGNElplgERGELCIKGPQVMKGYW--QQ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 573 PGVlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIK-SDAS 651
Cdd:PRK12492 430 PEA----TAEALDAE---GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMA-HPKVANCAAIGvPDER 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 652 KGEALVLFTTDNE--LTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK12492 502 SGEAVKLFVVARDpgLSVEELKAYCKEN-FTGYKVPKHIVLRDSLPMTPVGK 552
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
369-701 |
6.11e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 127.28 E-value: 6.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSILAN-VEQIKTIaDFTTNDRFMSALPLFHSFGltVGLFT-PLLTGAEVFLYPSPLHYRI 446
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMFWNaLNNTFAI-DLTMHDRSIVLLPLFHIGG--IGLFAfPTLFAGGVIIVPRKFEPTK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 VPELVYDRSCTVLFGTSTF---LGHYARFANPyDFYRLRYVVAGAEKLQESTKQLWQDKfGLRILEGYGVTECAPVVSI- 522
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIhqaLINCSKFETT-NLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMl 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 523 -NVPMAAKPGTVGRILPGMDARLLSVPG--IEEG--GRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGemerGWYDTGD 597
Cdd:PRK06839 308 sEEDARRKVGSIGKPVLFCDYELIDENKnkVEVGevGELLIRGPNVMKEYWNRPDA------TEETIQD----GWLCTGD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 598 IVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKLqqy 673
Cdd:PRK06839 378 LARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQ-VINKLSDVYEVAVVgRQHVKWGEipiAFIVKKSSSVLIEKDV--- 453
|
330 340 350
....*....|....*....|....*....|.
gi 16130740 674 aREHGVPELA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK06839 454 -IEHCRLFLAkykIPKEIVFLKELPKNATGK 483
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
364-681 |
6.74e-31 |
|
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: 127.33 E-value: 6.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKT-IADF-TTNDRFMSALPLFHSF-----------GLTVGLFTP-- 428
Cdd:cd17639 87 PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDrVPELlGPDDRYLAYLPLAHIFelaaenvclyrGGTIGYGSPrt 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 429 -------------------LLTG-AEVF----------LYPSPLHYRIVPELVYD-RSCTVLFGTSTFLGHYARFANPYD 477
Cdd:cd17639 167 ltdkskrgckgdltefkptLMVGvPAIWdtirkgvlakLNPMGGLKRTLFWTAYQsKLKALKEGPGTPLLDELVFKKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 478 FY--RLRYVVAGAEKLQESTkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgIEEG-- 553
Cdd:cd17639 247 ALggRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVD---WEEGgy 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 554 --------GRLQLKGPNIMNGYL-RVEKpgvlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
Cdd:cd17639 323 stdkppprGEILIRGPNVFKGYYkNPEK-------TKEAFDGD---GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEY 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 624 VSLEMVEQLALGVS-PDKVHATAiKSDASKGEALVLfttDNEltrDKLQQYAREHGVPE 681
Cdd:cd17639 393 IALEKLESIYRSNPlVNNICVYA-DPDKSYPVAIVV---PNE---KHLTKLAEKHGVIN 444
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
364-701 |
7.29e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 127.77 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplh 443
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 yR----IVPELVYDRSCTVLFGTSTFLGHYarFANP----YDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE 515
Cdd:PRK08314 265 -RwdreAAARLIERYRVTHWTNIPTMVVDF--LASPglaeRDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 516 CAPVVSINVPMAAKPGTVGRILPGMDARLLS-VPGIE----EGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVrgeMER 590
Cdd:PRK08314 342 TMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEElppgEVGEIVVHGPQVFKGYWNRPE------ATAEAF---IEI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 591 G---WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIKS-DASKGE---ALVLFTTDN 663
Cdd:PRK08314 413 DgkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENL-LYKHPAIQEACVIATpDPRRGEtvkAVVVLRPEA 491
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16130740 664 E--LTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK08314 492 RgkTTEEEIIAWAREH----MAaykYPRIVEFVDSLPKSGSGK 530
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
229-701 |
1.04e-30 |
|
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: 125.67 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 229 FTPD---SYRKLLTKTLFVGRIL--EKYSVEGERIGLMLPNAGISAAVIFGAIarrrmpammnyTAGvkgltsAItAAEI 303
Cdd:cd05958 5 RSPErewTYRDLLALANRIANVLvgELGIVPGNRVLLRGSNSPELVACWFGIQ-----------KAG------AI-AVAT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 304 KTIFTSR---QFLDKGKLWHLpeqltqvrwvyledLKAD-VTTADKVWIFAhllmprlaqvkqqpeeealilFTSGSEGH 379
Cdd:cd05958 67 MPLLRPKelaYILDKARITVA--------------LCAHaLTASDDICILA---------------------FTSGTTGA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 380 PKGVVHSHKSILANVEQI-KTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplhyRIVPELVYD----R 454
Cdd:cd05958 112 PKATMHFHRDPLASADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLE-----EATPDLLLSaiarY 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 455 SCTVLFGTST----FLGHyARFANPyDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKP 530
Cdd:cd05958 187 KPTVLFTAPTayraMLAH-PDAAGP-DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 531 GTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNgylrvekpGVLEVPTAENVRGemerGWYDTGDIVRFDEQGF 606
Cdd:cd05958 265 GATGKPVPGYEAKVVDDEGNPvpdgTIGRLAVRGPTGCR--------YLADKRQRTYVQG----GWNITGDTYSRDPDGY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 607 VQIQGRAKRFAKIAGEMVSLEMVEQLALG---VSPDKVHATAIKSDASKGEALVLF---TTDNELTRDKLQQYAREHGVP 680
Cdd:cd05958 333 FRHQGRSDDMIVSGGYNIAPPEVEDVLLQhpaVAECAVVGHPDESRGVVVKAFVVLrpgVIPGPVLARELQDHAKAHIAP 412
|
490 500
....*....|....*....|.
gi 16130740 681 eLAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05958 413 -YKYPRAIEFVTELPRTATGK 432
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
364-638 |
2.10e-30 |
|
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: 126.18 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANV----EQIKTIADFTTNDRFMSALPLFHSF-----------GLTVGLF-- 426
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFervvealflyhGAKIGFYsg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 427 -TPLLTGAEVFLYPS--PLhyriVPEL---VYDR-------SCTVL-----FGTSTFLGHYAR---FANPY-DFY----- 479
Cdd:cd05927 193 dIRLLLDDIKALKPTvfPG----VPRVlnrIYDKifnkvqaKGPLKrklfnFALNYKLAELRSgvvRASPFwDKLvfnki 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 ------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVP----- 548
Cdd:cd05927 269 kqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPemnyd 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 549 --GIEEGGRLQLKGPNIMNGYLRVEKpgvlevPTAENVRgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVS 625
Cdd:cd05927 349 akDPNPRGEVCIRGPNVFSGYYKDPE------KTAEALD---EDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVA 419
|
330
....*....|...
gi 16130740 626 LEMVEQLALGVSP 638
Cdd:cd05927 420 PEKIENIYARSPF 432
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
305-701 |
2.78e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 126.02 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 305 TIFTSRQFLDKgkLWHLPEQLTQVRWVYLEDLKADVTTADKVwifAHLLM---PRLAQVKQQPEEEALILFTSGSEGHPK 381
Cdd:PRK06087 129 TLFKQTRPVDL--ILPLQNQLPQLQQIVGVDKLAPATSSLSL---SQIIAdyePLTTAITTHGDELAAVLFTSGTEGLPK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 382 GVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPsplHYRIVP--ELVYDRSCTVL 459
Cdd:PRK06087 204 GVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD---IFTPDAclALLEQQRCTCM 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 460 FGTSTF----LGHYArfANPYDFYRLR-YVVAGAEKLQESTKQLWQdkFGLRILEGYGVTECAP--VVSINVPMAAKPGT 532
Cdd:PRK06087 281 LGATPFiydlLNLLE--KQPADLSALRfFLCGGTTIPKKVARECQQ--RGIKLLSVYGSTESSPhaVVNLDDPLSRFMHT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 533 VGRILPGMDARLL-----SVPGIEEGGRLQlKGPNIMNGYLrvekpgvlEVPTAENvRGEMERGWYDTGDIVRFDEQGFV 607
Cdd:PRK06087 357 DGYAAAGVEIKVVdearkTLPPGCEGEEAS-RGPNVFMGYL--------DEPELTA-RALDEEGWYYSGDLCRMDEAGYI 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 608 QIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEAL----VLFTTDNELTRDKLQQYAREHGVPELA 683
Cdd:PRK06087 427 KITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERScayvVLKAPHHSLTLEEVVAFFSRKRVAKYK 506
|
410
....*....|....*...
gi 16130740 684 VPRDIRYLKQMPLLGSGK 701
Cdd:PRK06087 507 YPEHIVVIDKLPRTASGK 524
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
364-719 |
8.90e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.76 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEE-ALILFTSGSEGHPKGVVHSHKSILAN-VEQIKTIADFTTNDRF-MSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:PRK06710 204 PENDlALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVvLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 pLHYRIVPELVYDRSCTVLFGTSTFlgHYARFANP----YDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEC 516
Cdd:PRK06710 284 -FDMKMVFEAIKKHKVTLFPGAPTI--YIALLNSPllkeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTES 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINVPMAAK-PGTVGRILPGMDARLLSV-------PGieEGGRLQLKGPNIMNGYLrvEKPgvlevptaENVRGEM 588
Cdd:PRK06710 361 SPVTHSNFLWEKRvPGSIGVPWPDTEAMIMSLetgealpPG--EIGEIVVKGPQIMKGYW--NKP--------EETAAVL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 589 ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALgvSPDKVHATAIKS--DASKGE---ALVLFTTDN 663
Cdd:PRK06710 429 QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY--EHEKVQEVVTIGvpDPYRGEtvkAFVVLKEGT 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 664 ELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKpdfVTLKSWVDEAEQHDE 719
Cdd:PRK06710 507 ECSEEELNQFARKY-LAAYKVPKVYEFRDELPKTTVGK---ILRRVLIEEEKRKNE 558
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
364-613 |
1.92e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 122.41 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGaevflypSPLH 443
Cdd:PRK07787 127 PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIG-------NRFV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 Y--RIVPElVYDRSC----TVLFGTSTFlghYARFANPYD----FYRLRYVVAGA--------EKLQESTkqlwqdkfGL 505
Cdd:PRK07787 200 HtgRPTPE-AYAQALseggTLYFGVPTV---WSRIAADPEaaraLRGARLLVSGSaalpvpvfDRLAALT--------GH 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 506 RILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGI------EEGGRLQLKGPNIMNGYLrvEKPGVlevp 579
Cdd:PRK07787 268 RPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGpvphdgETVGELQVRGPTLFDGYL--NRPDA---- 341
|
250 260 270
....*....|....*....|....*....|....
gi 16130740 580 TAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRA 613
Cdd:PRK07787 342 TAAAFTAD---GWFRTGDVAVVDPDGMHRIVGRE 372
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
356-701 |
4.09e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 122.68 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 356 RLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTT-----NDRFMSALPLFHSFGLTVGLFTPLL 430
Cdd:PRK08751 199 SMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGkleegCEVVITALPLYHIFALTANGLVFMK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 431 TGAEVFLYPSPLHYR-IVPELVYDRScTVLFGTSTF---LGHYARFANpYDFYRLRYVVAGAEKLQESTKQLWQDKFGLR 506
Cdd:PRK08751 279 IGGCNHLISNPRDMPgFVKELKKTRF-TAFTGVNTLfngLLNTPGFDQ-IDFSSLKMTLGGGMAVQRSVAERWKQVTGLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECAPVVSINvPMAAKP--GTVGRILPGMDARLLSVPG----IEEGGRLQLKGPNIMNGYLRveKPGvlevPT 580
Cdd:PRK08751 357 LVEAYGLTETSPAACIN-PLTLKEynGSIGLPIPSTDACIKDDAGtvlaIGEIGELCIKGPQVMKGYWK--RPE----ET 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 581 AENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGEAL--V 657
Cdd:PRK08751 430 AKVMDAD---GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDV-IAMMPGVLEVAAVGvPDEKSGEIVkvV 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16130740 658 LFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK08751 506 IVKKDPALTAEDVKAHARAN-LTGYKQPRIIEFRKELPKTNVGK 548
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
233-701 |
6.49e-29 |
|
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: 121.96 E-value: 6.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGL--TSAITA-AEIKTIFTS 309
Cdd:cd05931 26 TYAELDRRARAIAARLQAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHAerLAAILAdAGPRVVLTT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 310 RQFLDKGKLWHLPEQLTQVRWVYLEDLKADVTTADkvWIFAHLlmprlaqvkqQPEEEALILFTSGSEGHPKGVVHSHKS 389
Cdd:cd05931 106 AAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAAD--WPPPSP----------DPDDIAYLQYTSGSTGTPKGVVVTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 390 ILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAE-VFLypSPLHY----RIVPELVYDRSCTVLFGTST 464
Cdd:cd05931 174 LLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPsVLM--SPAAFlrrpLRWLRLISRYRATISAAPNF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 465 FLGHYARFANP-----YDFYRLRYVVAGAEKLQESTKQLWQDKF---GLR---ILEGYGVTEC----------APVVSIN 523
Cdd:cd05931 252 AYDLCVRRVRDedlegLDLSSWRVALNGAEPVRPATLRRFAEAFapfGFRpeaFRPSYGLAEAtlfvsggppgTGPVVLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 524 VPMAAKPGTV----------------GRILPGMDAR------LLSVPGIEEgGRLQLKGPNIMNGYLRveKPGVLEVpTA 581
Cdd:cd05931 332 VDRDALAGRAvavaaddpaarelvscGRPLPDQEVRivdpetGRELPDGEV-GEIWVRGPSVASGYWG--RPEATAE-TF 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENVRGEMERGWYDTGDIvrfdeqGFVQ-----IQGRAKRFAKIAGEMVS---LE-MVEQLALGVSPDKVHATAIksDASK 652
Cdd:cd05931 408 GALAATDEGGWLRTGDL------GFLHdgelyITGRLKDLIIVRGRNHYpqdIEaTAEEAHPALRPGCVAAFSV--PDDG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 653 GEALV----LFTTDNELTRDKL-----QQYAREHGVPelavPRDIRYLKQ--MPLLGSGK 701
Cdd:cd05931 480 EERLVvvaeVERGADPADLAAIaaairAAVAREHGVA----PADVVLVRPgsIPRTSSGK 535
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
233-703 |
6.74e-29 |
|
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: 121.48 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSV-EGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQ 311
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLkQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 312 FLDKgkLWHLPEQLTQVRWVYLEDLKADVTTADKVWIFAHLLMPRLAQVKQ-------QPEEEALILFTSGSEGHPKGVV 384
Cdd:cd17642 126 GLQK--VLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDfkppsfdRDEQVALIMNSSGSTGLPKGVQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 385 HSHKSILANVEQ------IKTIADFTTndrFMSALPLFHSFG-------LTVGLFTPLLTGAEVFLYPSPLH-YRI---- 446
Cdd:cd17642 204 LTHKNIVARFSHardpifGNQIIPDTA---ILTVIPFHHGFGmfttlgyLICGFRVVLMYKFEEELFLRSLQdYKVqsal 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 -VPELVydrsctVLFGTSTFLghyarfaNPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLR-ILEGYGVTECAPVVSINV 524
Cdd:cd17642 281 lVPTLF------AFFAKSTLV-------DKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 525 PMAAKPGTVGRILPGMDARLLSVP-----GIEEGGRLQLKGPNIMNGYLRVEKpgvlEVPTAENvrgemERGWYDTGDIV 599
Cdd:cd17642 348 EGDDKPGAVGKVVPFFYAKVVDLDtgktlGPNERGELCVKGPMIMKGYVNNPE----ATKALID-----KDGWLHSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 600 RFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGE---ALVLFTTDNELTRDKLQQYARE 676
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGElpaAVVVLEAGKTMTEKEVMDYVAS 498
|
490 500
....*....|....*....|....*..
gi 16130740 677 HGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17642 499 QVSTAKRLRGGVKFVDEVPKGLTGKID 525
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
363-703 |
3.99e-28 |
|
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: 118.18 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMsalpLFHS--FGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWT----LFHSyaFDFSVwEIWGALLHGGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 -----SPLHYRivpELVYDRSCTVLFGT-STFLGHY-ARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGL---RILE 509
Cdd:cd17643 167 yevarSPEDFA---RLLRDEGVTVLNQTpSAFYQLVeAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 GYGVTECAPVVSI------NVPMAAKpGTVGRILPG-----MDARLLSVPGIEEgGRLQLKGPNIMNGYLRveKPG---- 574
Cdd:cd17643 244 MYGITETTVHVTFrpldaaDLPAAAA-SPIGRPLPGlrvyvLDADGRPVPPGVV-GELYVSGAGVARGYLG--RPEltae 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 575 --VLEVPTAENVRGemergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASK 652
Cdd:cd17643 320 rfVANPFGGPGSRM------YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEA-ALATHPSVRDAAVIVREDEP 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16130740 653 GE-ALVLFTTDNELTRD---KLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17643 393 GDtRLVAYVVADDGAAAdiaELRALLKEL-LPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
350-701 |
5.63e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 119.00 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 350 AHLLMPR----------LAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSF 419
Cdd:PRK13295 172 ALLITPAweqepdapaiLARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 420 GLTVGLFTPLLTGAEVFLYPSPLHYRIVpELVYDRSCTVLFGTSTFLGHYARFAN--PYDFYRLR-YVVAGAEKLQESTK 496
Cdd:PRK13295 252 GFMYGLMMPVMLGATAVLQDIWDPARAA-ELIRTEGVTFTMASTPFLTDLTRAVKesGRPVSSLRtFLCAGAPIPGALVE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 497 QLWQdKFGLRILEGYGVTECApVVSINVPMAAKP---GTVGRILPGM-----DARLLSVPGIEEGgRLQLKGPNIMNGYL 568
Cdd:PRK13295 331 RARA-ALGAKIVSAWGMTENG-AVTLTKLDDPDErasTTDGCPLPGVevrvvDADGAPLPAGQIG-RLQVRGCSNFGGYL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 569 RvekpgvlevptaenvRGEMER----GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDkVHAT 644
Cdd:PRK13295 408 K---------------RPQLNGtdadGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEAL-LYRHPA-IAQV 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 645 AIKS--DASKGE---ALVLFTTDNELTRDKLQQYAREHGV-----PELAVPRDirylkQMPLLGSGK 701
Cdd:PRK13295 471 AIVAypDERLGEracAFVVPRPGQSLDFEEMVEFLKAQKVakqyiPERLVVRD-----ALPRTPSGK 532
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
356-701 |
1.64e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 117.81 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 356 RLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD--FTTNDR-----FMSALPLFHSFGLTVGLFTP 428
Cdd:PRK07059 195 TFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRpdqlnFVCALPLYHIFALTVCGLLG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 429 LLTGAEVFLYPSPlhyRIVPELV-----YDRSC----TVLFGTstfLGHYARFANpYDFYRLRYVVAGAEKLQESTKQLW 499
Cdd:PRK07059 275 MRTGGRNILIPNP---RDIPGFIkelkkYQVHIfpavNTLYNA---LLNNPDFDK-LDFSKLIVANGGGMAVQRPVAERW 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 500 QDKFGLRILEGYGVTECAPVVSINVPMAAK-PGTVGRILPGMDARLL-----SVPgIEEGGRLQLKGPNIMNGYLrvEKP 573
Cdd:PRK07059 348 LEMTGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRdddgnDLP-LGEPGEICIRGPQVMAGYW--NRP 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 574 gvlevptAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAlGVSPDKVHATAIK-SDASK 652
Cdd:PRK07059 425 -------DETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV-ASHPGVLEVAAVGvPDEHS 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 16130740 653 GEALVLFTT--DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK07059 497 GEAVKLFVVkkDPALTEEDVKAFCKER-LTNYKRPKFVEFRTELPKTNVGK 546
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
368-701 |
1.65e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 117.34 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILAnvEQIKTIA--DFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyr 445
Cdd:PRK08316 174 AQILYTSGTESLPKGAMLTHRALIA--EYVSCIVagDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP---- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 446 iVPELVYDR----SCTVLFGTST----FLGHyARFAnPYDFYRLRYVVAGA-----EKLQESTKQLwqdkFGLRILEGYG 512
Cdd:PRK08316 248 -DPELILRTieaeRITSFFAPPTvwisLLRH-PDFD-TRDLSSLRKGYYGAsimpvEVLKELRERL----PGLRFYNCYG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 513 VTECAPVVSINVP--MAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRveKPgvleVPTAENVRG 586
Cdd:PRK08316 321 QTEIAPLATVLGPeeHLRRPGSAGRPVLNVETRVVDDDGNDvapgEVGEIVHRSPQLMLGYWD--DP----EKTAEAFRG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 587 emerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlAL----GVS-------PDKVHATAIKsdaskgeA 655
Cdd:PRK08316 395 ----GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE-ALythpAVAevaviglPDPKWIEAVT-------A 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16130740 656 LVLFTTDNELTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK08316 463 VVVPKAGATVTEDELIAHCRAR----LAgfkVPKRVIFVDELPRNPSGK 507
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
315-659 |
2.02e-27 |
|
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: 117.38 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 315 KGKLWHLPEQLTQVRWVYLEDLKADVTTADKVWifaHLLMPRLAQVK-------------QQPEEEALILFTSGSEGHPK 381
Cdd:cd05906 107 LRKLRHIWQLLGSPVVLTDAELVAEFAGLETLS---GLPGIRVLSIEelldtaadhdlpqSRPDDLALLMLTSGSTGFPK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 382 GVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLT-VGLFtPLLTGAEVFLYPSPLHYRIVP---ELVYDRSCT 457
Cdd:cd05906 184 AVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLR-AVYLGCQQVHVPTEEILADPLrwlDLIDRYRVT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 458 VLFGTSTFLGHYARFAN-----PYDFYRLRYVVAGAEKLQESTKQLWQ---DKFGLR---ILEGYGVTECAPVVSINVPM 526
Cdd:cd05906 263 ITWAPNFAFALLNDLLEeiedgTWDLSSLRYLVNAGEAVVAKTIRRLLrllEPYGLPpdaIRPAFGMTETCSGVIYSRSF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 527 AAKPGT-------VGRILPGMDARLLSV--PGIEEG--GRLQLKGPNIMNGYLRVEKpgvlevPTAENVRgemERGWYDT 595
Cdd:cd05906 343 PTYDHSqalefvsLGRPIPGVSMRIVDDegQLLPEGevGRLQVRGPVVTKGYYNNPE------ANAEAFT---EDGWFRT 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 596 GDIVrFDEQGFVQIQGRAKRFAKIAG---EMVSLE-MVEQLAlGVSPDKVHATAIKSDASKGEALVLF 659
Cdd:cd05906 414 GDLG-FLDNGNLTITGRTKDTIIVNGvnyYSHEIEaAVEEVP-GVEPSFTAAFAVRDPGAETEELAIF 479
|
|
| Acyltransferase |
pfam01553 |
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ... |
15-137 |
3.64e-27 |
|
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.
Pssm-ID: 366704 [Multi-domain] Cd Length: 131 Bit Score: 106.98 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 15 RVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLP---VRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQPM----AI 87
Cdd:pfam01553 1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKdaagTL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 16130740 88 KHLVRLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRI 137
Cdd:pfam01553 81 EYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
363-711 |
6.69e-27 |
|
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: 114.95 E-value: 6.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFM--SAlplfHSFGLTVG-LFTPLLTGAEVFLyP 439
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLqfAS----YTFDVSILeIFTTLAAGGCLCI-P 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SpLHYRI--VPELVYDRSCTVLFGTSTFlghyARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKfgLRILEGYGVTECA 517
Cdd:cd05918 179 S-EEDRLndLAGFINRLRVTWAFLTPSV----ARLLDPEDVPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVVSINVPMA-AKPGTVGRILPG----MDA----RLLSVPGIEEggrLQLKGPNIMNGYL-RVEKPGVLEVPTAENVRGE 587
Cdd:cd05918 252 IAATVSPVVPsTDPRNIGRPLGAtcwvVDPdnhdRLVPIGAVGE---LLIEGPILARGYLnDPEKTAAAFIEDPAWLKQE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 588 MERG---WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE-QLALGVSPDK-VHATAIK-SDASKGEALV---- 657
Cdd:cd05918 329 GSGRgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEhHLRQSLPGAKeVVVEVVKpKDGSSSPQLVafvv 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 658 -------------LFTTDNELTRD---KLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWV 711
Cdd:cd05918 409 ldgsssgsgdgdsLFLEPSDEFRAlvaELRSKLRQR-LPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
368-637 |
7.50e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 115.48 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTT-NDRFMSALPLFHSFGLTVGLFTPLLTGAE-VFLYP-----S 440
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVeTDVMVSWLPLFHDMGMVGFLTVPMYFGAElVKVTPmdflrD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 PLhyrIVPELVYDRSCTVL----FGTSTFLGHYARFANP--YDFYRLRYVVAGAEKLQESTKQLWQD---KFGLR---IL 508
Cdd:PRK07768 235 PL---LWAELISKYRGTMTaapnFAYALLARRLRRQAKPgaFDLSSLRFALNGAEPIDPADVEDLLDagaRFGLRpeaIL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 509 EGYGVTECAPVVSIN----------------------VPmAAKPGT-----VGRILPGMDARLL----SVPGIEEGGRLQ 557
Cdd:PRK07768 312 PAYGMAEATLAVSFSpcgaglvvdevdadllaalrraVP-ATKGNTrrlatLGPPLPGLEVRVVdedgQVLPPRGVGVIE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 558 LKGPNIMNGYLRVEKPgvleVPTAEnvrgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVS 637
Cdd:PRK07768 391 LRGESVTPGYLTMDGF----IPAQD------ADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVE 460
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
364-703 |
1.11e-25 |
|
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: 111.14 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIaDFTTNDRFMSALPLfhSF-GLTVGLFTPLLTGAEVFLYPS-- 440
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV-TLGPDDRVLQTSPL--AFdASTFEIWGALLNGARLVLAPKgt 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 PLHYRIVPELVYDRSCTVLFGTSTFLGHYARfANPYDFYRLRYVVAGAEKLQ-ESTKQLWQDKFGLRILEGYGVTECAPV 519
Cdd:cd12117 212 LLDPDALGALIAEEGVTVLWLTAALFNQLAD-EDPECFAGLRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTTF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 520 VSINV--PMAAKPGTV--GRILPGMDARLLSV------PGIEegGRLQLKGPNIMNGYLRveKPGVlevpTAE----NVR 585
Cdd:cd12117 291 TTSHVvtELDEVAGSIpiGRPIANTRVYVLDEdgrpvpPGVP--GELYVGGDGLALGYLN--RPAL----TAErfvaDPF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 586 GEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD--KVHATAIKSDASKGEALVLFTTDN 663
Cdd:cd12117 363 GPGER-LYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGvrEAVVVVREDAGGDKRLVAYVVAEG 440
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16130740 664 ELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd12117 441 ALDAAELRAFLRER-LPAYMVPAAFVVLDELPLTANGKVD 479
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
360-701 |
1.76e-25 |
|
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: 110.21 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 360 VKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSF--GLTVGLFTPLLTGAEVFL 437
Cdd:cd05971 83 VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADWAWigGLLDVLLPSLYFGVPVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 438 Y-PSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFY--RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVT 514
Cdd:cd05971 163 HrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECAPVVSIN-VPMAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPN--IMNGYLRVEkpgvlevptaENVRGE 587
Cdd:cd05971 243 ECNLVIGNCsALFPIKPGSMGKPIPGHRVAIVDDNGTPlppgEVGEIAVELPDpvAFLGYWNNP----------SATEKK 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 588 MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGEA----LVL---F 659
Cdd:cd05971 313 MAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE-CLLKHPAVLMAAVVgIPDPIRGEIvkafVVLnpgE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16130740 660 TTDNELTRDkLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05971 392 TPSDALARE-IQELVKTR-LAAHEYPREIEFVNELPRTATGK 431
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
323-710 |
2.05e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 111.14 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 323 EQLTQVRWVYLEDlkADVTTADKVWIFAHLLM---PRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK04319 162 DDLPSLKHVLLVG--EDVEEGPGTLDFNALMEqasDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKY 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 400 IADFTTNDRFM-SALPLFHSfGLTVGLFTPLLTGA------EVFlypSPLH-YRIVPELvydrSCTVLFGTST----FLG 467
Cdd:PRK04319 240 VLDLHEDDVYWcTADPGWVT-GTSYGIFAPWLNGAtnvidgGRF---SPERwYRILEDY----KVTVWYTAPTairmLMG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 468 HYARFANPYDFYRLRYVVAGAEKLQ-ESTKqlW-QDKFGLRILEGYGVTECAPVVSINVP-MAAKPGTVGRILPGMDARL 544
Cdd:PRK04319 312 AGDDLVKKYDLSSLRHILSVGEPLNpEVVR--WgMKVFGLPIHDNWWMTETGGIMIANYPaMDIKPGSMGKPLPGIEAAI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 545 LSVPGIE----EGGRLQLKG--PNIMNGYLRVEkpgvlevptaENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK 618
Cdd:PRK04319 390 VDDQGNElppnRMGNLAIKKgwPSMMRGIWNNP----------EKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 619 IAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGE---ALVL----FTTDNELTRDkLQQYAREhGVPELAVPRDIRY 690
Cdd:PRK04319 460 TSGERVGPFEVES-KLMEHPAVAEAGVIgKPDPVRGEiikAFVAlrpgYEPSEELKEE-IRGFVKK-GLGAHAAPREIEF 536
|
410 420
....*....|....*....|
gi 16130740 691 LKQMPLLGSGKPDFVTLKSW 710
Cdd:PRK04319 537 KDKLPKTRSGKIMRRVLKAW 556
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
2.65e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 113.13 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 359 QVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFL 437
Cdd:PRK12316 4688 AVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF--SFDGSHeGLYHPLINGASVVI 4765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 438 YPSPLH--YRIVPELVYDRSCTVLFGTSTF---LGHYARFANPydfYRLRYVVAGAEKLQ-ESTKQLWQDKFGLRILEGY 511
Cdd:PRK12316 4766 RDDSLWdpERLYAEIHEHRVTVLVFPPVYLqqlAEHAERDGEP---PSLRVYCFGGEAVAqASYDLAWRALKPVYLFNGY 4842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 512 GVTECAPVVSI-----NVPMAAKPGTVGRILPGMDARLLSVPG----IEEGGRLQLKGPNIMNGYLrvEKPGVlevpTAE 582
Cdd:PRK12316 4843 GPTETTVTVLLwkardGDACGAAYMPIGTPLGNRSGYVLDGQLnplpVGVAGELYLGGEGVARGYL--ERPAL----TAE 4916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 583 ----NVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASKGEALV- 657
Cdd:PRK12316 4917 rfvpDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEA-RLREHPAVREAVVIAQEGAVGKQLVg 4995
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 658 -LFTTDNELT---------RDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK12316 4996 yVVPQDPALAdadeaqaelRDELKAALRER-LPEYMVPAHLVFLARMPLTPNGKLD 5050
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
362-703 |
7.41e-25 |
|
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: 108.22 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLY 438
Cdd:cd17649 91 HHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQ----FASFNFDGAheqLLPPLICGACVVLR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 439 PSPL------HYRIVPELvydrSCTVLFGTSTFLGHYARFA---NPYDFYRLRYVVAGAEKLQESTKQLWQdKFGLRILE 509
Cdd:cd17649 167 PDELwasadeLAEMVREL----GVTVLDLPPAYLQQLAEEAdrtGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 GYGVTECapVVSinvPMAAKPGT----------VGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYLrvEKPG 574
Cdd:cd17649 242 AYGPTEA--TVT---PLVWKCEAgaaragasmpIGRPLGGrsayiLDADLNPVP-VGVTGELYIGGEGLARGYL--GRPE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 575 VlevpTAENV-----RGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSD 649
Cdd:cd17649 314 L----TAERFvpdpfGAPGSR-LYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEA-ALLEHPGVREAAVVALD 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 650 ASKGEALVLF-----TTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17649 388 GAGGKQLVAYvvlraAAAQPELRAQLRTALRAS-LPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
361-703 |
2.12e-24 |
|
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: 106.79 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 361 KQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTND-RFMSALPLFHSFglTVGLFTPLLTGAeVFLYp 439
Cdd:cd17654 114 IRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDiLFLTSPLTFDPS--VVEIFLSLSSGA-TLLI- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPLHYRIVPELVYD-----RSCTVLFGTSTFLghyARFANPYDFYR-------LRYVVAGAEKLQEST-KQLWQDKF-GL 505
Cdd:cd17654 190 VPTSVKVLPSKLADilfkrHRITVLQATPTLF---RRFGSQSIKSTvlsatssLRVLALGGEPFPSLViLSSWRGKGnRT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 506 RILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPGMDARLLSVPGIEEGGRLQLKGPNimNGYLRvekPGVLEVPTAEnv 584
Cdd:cd17654 267 RIFNIYGITEVSCWALAYkVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLN--RVCIL---DDEVTVPKGT-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 585 rgemergWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIksdaSKGEALVLFTTDnE 664
Cdd:cd17654 340 -------MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTL----SDQQRLIAFIVG-E 406
|
330 340 350
....*....|....*....|....*....|....*....
gi 16130740 665 LTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17654 407 SSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVD 445
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
338-703 |
7.85e-24 |
|
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: 105.82 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 338 ADVTTADKvWIFAHLlMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfh 417
Cdd:cd17646 113 GDVALLGD-EALAAP-PATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 418 SFGLTVG-LFTPLLTGAEVFLYPSPLH----YriVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQ 492
Cdd:cd17646 189 SFDVSVWeLFWPLVAGARLVVARPGGHrdpaY--LAALIREHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFCSGEALP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 493 ESTKQLWQDKFGLRILEGYGVTECA-PVVSINVPMAAKPGTV--GRILPG-----MDARLLSVP-GIeeGGRLQLKGPNI 563
Cdd:cd17646 267 PELAARFLALPGAELHNLYGPTEAAiDVTHWPVRGPAETPSVpiGRPVPNtrlyvLDDALRPVPvGV--PGELYLGGVQL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 564 MNGYLRveKPGVlevpTAE----NVRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD 639
Cdd:cd17646 345 ARGYLG--RPAL----TAErfvpDPFGPGSR-MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPA 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 640 KVHATAIKSDASKGEA-----LVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17646 417 VTHAVVVARAAPAGAArlvgyVVPAAGAAGPDTAALRAHLAER-LPEYMVPAAFVVLDALPLTANGKLD 484
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
366-707 |
8.87e-24 |
|
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: 105.49 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 366 EEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTV-GLFTPLLTGAEVFLYPSP--- 441
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPspd 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 -----------LHYRIVPELVydrsctvlfgtSTFLGHYARfaNPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEG 510
Cdd:cd05920 220 aafplieregvTVTALVPALV-----------SLWLDAAAS--RRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 511 YGVTE---CapVVSINVPMAAKPGTVGR-ILPG-----MDARLLSVPGIEEGgRLQLKGPNIMNGYLRVEkpgvlevptA 581
Cdd:cd05920 287 FGMAEgllN--YTRLDDPDEVIIHTQGRpMSPDdeirvVDEEGNPVPPGEEG-ELLTRGPYTIRGYYRAP---------E 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVspDKVHATA--IKSDASKGEALVLF 659
Cdd:cd05920 355 HNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRH--PAVHDAAvvAMPDELLGERSCAF 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16130740 660 T--TDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTL 707
Cdd:cd05920 433 VvlRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
372-703 |
1.15e-23 |
|
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: 102.48 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 372 FTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAevFLYPSPLHYRIVPELV 451
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGT--FIGQRKFNPKSWIRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 452 YDRSCTVLFGTSTFLGHYARFANPYDfyRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTEcAPVVSINVPM-AAK 529
Cdd:cd17633 85 NQYNATVIYLVPTMLQALARTLEPES--KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQeSRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 530 PGTVGRILPGMDARLLSVPGiEEGGRLQLKGPNIMNGYLRVekpgvlevptaenvRGEMERGWYDTGDIVRFDEQGFVQI 609
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADG-GEIGKIFVKSEMVFSGYVRG--------------GFSNPDGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 610 QGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGEALVLFTTDNELTRDKLQQYAREHgVPELAVPRDI 688
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESV-LKAIPGIEEAIVVGiPDARFGEIAVALYSGDKLTYKQLKRFLKQK-LSRYEIPKKI 304
|
330
....*....|....*
gi 16130740 689 RYLKQMPLLGSGKPD 703
Cdd:cd17633 305 IFVDSLPYTSSGKIA 319
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
360-716 |
1.82e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.17 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 360 VKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP 439
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATLHLLP 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPLHYRivPELVYDRSC----TVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDK-FGLRILEGYGVT 514
Cdd:PRK12467 730 PDCARD--AEAFAALMAdqgvTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALgPGARLINHYGPT 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECAPVVSI------NVPMAAKPgtVGRILPG-----MDARLLSVPGiEEGGRLQLKGPNIMNGYLRveKPGVLE---VPT 580
Cdd:PRK12467 808 ETTVGVSTyelsdeERDFGNVP--IGQPLANlglyiLDHYLNPVPV-GVVGELYIGGAGLARGYHR--RPALTAerfVPD 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 581 AENVRGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIKSDASKGEALVLF- 659
Cdd:PRK12467 883 PFGADGGR---LYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR-LLAQPGVREAVVLAQPGDAGLQLVAYl 958
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130740 660 -------TTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQ 716
Cdd:PRK12467 959 vpaavadGAEHQATRDELKAQLRQV-LPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQ 1021
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
370-701 |
2.22e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 104.89 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGA------EVFlypSPLH 443
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAtmvypgEGF---DPLA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 yriVPELVYDRSCTVLFGTST-F---LGHyARFANpYDFYRLRY-VVAGAEKLQESTKQLwQDKFGLR-ILEGYGVTECA 517
Cdd:PRK08315 281 ---TLAAVEEERCTALYGVPTmFiaeLDH-PDFAR-FDLSSLRTgIMAGSPCPIEVMKRV-IDKMHMSeVTIAYGMTETS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVV---SINVPMAAKPGTVGRILPGMDARLLS------VPgIEEGGRLQLKGPNIMNGYLR-VEKpgvlevpTAENVRGE 587
Cdd:PRK08315 355 PVStqtRTDDPLEKRVTTVGRALPHLEVKIVDpetgetVP-RGEQGELCTRGYSVMKGYWNdPEK-------TAEAIDAD 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 588 merGWYDTGDIVRFDEQGFVQIQGRAK----RfakiAGEMVSLEMVEQLaLGVSPD--KVHATAIkSDASKGEALVLFTT 661
Cdd:PRK08315 427 ---GWMHTGDLAVMDEEGYVNIVGRIKdmiiR----GGENIYPREIEEF-LYTHPKiqDVQVVGV-PDEKYGEEVCAWII 497
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 16130740 662 ---DNELTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK08315 498 lrpGATLTEEDVRDFCRGK----IAhykIPRYIRFVDEFPMTVTGK 539
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
368-657 |
2.24e-23 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 105.50 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIA-DFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRI 446
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKAlRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 VPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAPVVSINVP 525
Cdd:PRK06060 228 AAILSARFGPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFgGIPILDGIGSTEVGQTFVSNRV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 MAAKPGTVGRILPGMDARLLSVPGIEEG----GRLQLKGPNIMNGYLRVEKPgVLEvptaenvrgemERGWYDTGDIVRF 601
Cdd:PRK06060 308 DEWRLGTLGRVLPPYEIRVVAPDGTTAGpgveGDLWVRGPAIAKGYWNRPDS-PVA-----------NEGWLDTRDRVCI 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 602 DEQGFVQIQGRAKRfAKIAGemvslemveqlALGVSPDKVHATAIKSDASKGEALV 657
Cdd:PRK06060 376 DSDGWVTYRCRADD-TEVIG-----------GVNVDPREVERLIIEDEAVAEAAVV 419
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
370-703 |
3.39e-23 |
|
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: 101.19 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypSPLHYRIVPE 449
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVM--EKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 450 LVYDRSCTVLFGTSTFLGHY--ARFANPYDFYRLRYvVAGAEKLQesTKQLWQDKFGLRILEGYGVTECAPVVSINvPMA 527
Cdd:cd17637 83 LIEEEKVTLMGSFPPILSNLldAAEKSGVDLSSLRH-VLGLDAPE--TIQRFEETTGATFWSLYGQTETSGLVTLS-PYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 528 AKPGTVGRILPGMDARLLS-----VPgIEEGGRLQLKGPNIMNGYLRvekpgvLEVPTAENVRGemerGWYDTGDIVRFD 602
Cdd:cd17637 159 ERPGSAGRPGPLVRVRIVDdndrpVP-AGETGEIVVRGPLVFQGYWN------LPELTAYTFRN----GWHHTGDLGRFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 603 EQGFVQIQGR--AKRFAKIAGEMVSLEMVEQLAL-----------GVsPDKVHATAIKSDASKGEALVLftTDNELTR-- 667
Cdd:cd17637 228 EDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILehpaiaevcviGV-PDPKWGEGIKAVCVLKPGATL--TADELIEfv 304
|
330 340 350
....*....|....*....|....*....|....*..
gi 16130740 668 -DKLQQYARehgvpelavPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17637 305 gSRIARYKK---------PRYVVFVEALPKTADGSID 332
|
|
| PlsC |
smart00563 |
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ... |
30-140 |
3.40e-23 |
|
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.
Pssm-ID: 214724 [Multi-domain] Cd Length: 118 Bit Score: 95.11 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 30 VLITPNHVSFIDGILLGLFLP---VRPVFAVYTSISQQWYMRWLKSFIDFVPLDPTQP----MAIKHLVRLVEQGRPVVI 102
Cdd:smart00563 1 ALVVANHQSFLDPLVLSALLPrklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGrkarAALREAVELLKEGEWLLI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130740 103 FPEGRITTTGSLMKIYDGAGFVAAKSGATVIPVRIEGA 140
Cdd:smart00563 81 FPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
364-620 |
4.57e-23 |
|
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: 103.32 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS--- 440
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESldt 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 ---------PLHYRIVPEL-------VYDR----------SCTVLfgtSTFLGHyaRFANPYDFYRLRYVVAGAEKLQES 494
Cdd:cd05932 216 fvedvqrarPTLFFSVPRLwtkfqqgVQDKipqqklnlllKIPVV---NSLVKR--KVLKGLGLDQCRLAGCGSAPVPPA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 495 TkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEEGGRLQLKGPNIMNGYLRVekpg 574
Cdd:cd05932 291 L-LEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR------ISEDGEILVRSPALMMGYYKD---- 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16130740 575 vlEVPTAENVRgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA 620
Cdd:cd05932 360 --PEATAEAFT---ADGFLRTGDKGELDADGNLTITGRVKDIFKTS 400
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
233-701 |
7.82e-23 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 103.43 E-value: 7.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKT-LFVGRILEKYSVEGERIGLMLPNagISAAVIfGAIARRRMPAMMNYTAG---VKGLTSAITAAEIKTIFT 308
Cdd:cd17634 86 SYRELHREVcRFAGTLLDLGVKKGDRVAIYMPM--IPEAAV-AMLACARIGAVHSVIFGgfaPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 309 SRQFLDKGKLWHLPE--------QLTQVRWVYLED-LKADVTTADKVWIFAHLLM----PRLAQVKQQPEEEALILFTSG 375
Cdd:cd17634 163 ADGGVRAGRSVPLKKnvddalnpNVTSVEHVIVLKrTGSDIDWQEGRDLWWRDLIakasPEHQPEAMNAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 376 SEGHPKGVVHSHKS-ILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY------PSPLHYRivp 448
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYegvpnwPTPARMW--- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 449 ELVYDRSCTVLFGTSTFLgHYARFANP-----YDFYRLRYVVAGAEKLQESTKQLWQDKFGLR---ILEGYGVTE----C 516
Cdd:cd17634 320 QVVDKHGVNILYTAPTAI-RALMAAGDdaiegTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTEtggfM 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINVPMaaKPGTVGRILPGMDARLL-----SVPGIEEGG-RLQLKGPNIMNGYLRvekpgvlEVPTAENVRGEMER 590
Cdd:cd17634 399 ITPLPGAIEL--KAGSATRPVFGVQPAVVdneghPQPGGTEGNlVITDPWPGQTRTLFG-------DHERFEQTYFSTFK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 591 GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqlALGVSPDKVHATAIKS--DASKGEALVLFT------TD 662
Cdd:cd17634 470 GMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE--SVLVAHPKVAEAAVVGipHAIKGQAPYAYVvlnhgvEP 547
|
490 500 510
....*....|....*....|....*....|....*....
gi 16130740 663 NELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd17634 548 SPELYAELRNWVRKE-IGPLATPDVVHWVDSLPKTRSGK 585
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
355-701 |
1.92e-22 |
|
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: 101.80 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:cd05970 175 RPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAA 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 435 VFLYPsplHYRIVPELVYDRSCTvlFGTSTFLG--HYARF-----ANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRI 507
Cdd:cd05970 255 VFVYD---YDKFDPKALLEKLSK--YGVTTFCAppTIYRFliredLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 508 LEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLL-----SVPGIEEGG---RLQLKGP-NIMNGYLRvekpgvlev 578
Cdd:cd05970 330 MEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIdregrSCEAGEEGEiviRTSKGKPvGLFGGYYK--------- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 579 pTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLAL-----------GVsPDKVHATAIK 647
Cdd:cd05970 401 -DAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIqhpavlecavtGV-PDPIRGQVVK 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 648 SdaskgeALVL---FTTDNELTRDkLQQYAREHGVPELAvPRDIRYLKQMPLLGSGK 701
Cdd:cd05970 479 A------TIVLakgYEPSEELKKE-LQDHVKKVTAPYKY-PRIVEFVDELPKTISGK 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
364-703 |
3.93e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.73 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPL 442
Cdd:PRK12316 654 PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVVAAPGD 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 HYRI--VPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKL-QESTKQLWQDKFGLRILEGYGVTECAPV 519
Cdd:PRK12316 732 HRDPakLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALpADAQEQVFAKLPQAGLYNLYGPTEAAID 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 520 VSINVPMAAKPGTV--GRILPG-----MDARLLSVP-GIEegGRLQLKGPNIMNGYLRveKPGVlevpTAE----NVRGE 587
Cdd:PRK12316 812 VTHWTCVEEGGDSVpiGRPIANlacyiLDANLEPVPvGVL--GELYLAGRGLARGYHG--RPGL----TAErfvpSPFVA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 588 MERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASKGEALVLFTTDNELTR 667
Cdd:PRK12316 884 GER-MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGKQLVGYVVLESEGGDWR 961
|
330 340 350
....*....|....*....|....*....|....*.
gi 16130740 668 DKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK12316 962 EALKAHLAAS-LPEYMVPAQWLALERLPLTPNGKLD 996
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
365-701 |
4.09e-22 |
|
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: 98.10 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTTNDRFMSALPLFHSFGLTVGLfTPLLTGAEVFLYPSPLH 443
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWIL-TCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 YRIVPELV--YDRSCTVLFGTS-TFLGHYARFANPYdFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVV 520
Cdd:cd17635 80 YKSLFKILttNAVTTTCLVPTLlSKLVSELKSANAT-VPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 521 SINVPMAAKP-GTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGemerGWYDT 595
Cdd:cd17635 159 CLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAgpsaSFGTIWIKSPANMLGYWNNPER------TAEVLID----GWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 596 GDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLFTTDNEL---TRDKLQQ 672
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEldeNAIRALK 308
|
330 340
....*....|....*....|....*....
gi 16130740 673 YAREHGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGK 337
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
364-710 |
4.24e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 100.27 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP---- 439
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNgfep 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 ------------SPLHYRIVPELVydrsctvlfgtstflghyARF-ANP-YDFYRLRYVVA----GAEKLQESTKQlWQD 501
Cdd:PRK09088 214 krtlgrlgdpalGITHYFCVPQMA------------------QAFrAQPgFDAAALRHLTAlftgGAPHAAEDILG-WLD 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 KfGLRILEGYGVTECAPVVSINVP---MAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRveKPg 574
Cdd:PRK09088 275 D-GIPMVDGFGMSEAGTVFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQGNDcpagVPGELLLRGPNLSPGYWR--RP- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 575 vlevptAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIK-SDASKG 653
Cdd:PRK09088 351 ------QATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEA-VLADHPGIRECAVVGmADAQWG 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 654 EALVLFTTDNELTRDKLQQyAREHGVPELA---VPRDIRYLKQMPLLGSGKPDFVTLKSW 710
Cdd:PRK09088 424 EVGYLAIVPADGAPLDLER-IRSHLSTRLAkykVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
331-680 |
4.35e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 101.59 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 331 VYLEDLKADVTTAD-KVWIFAHLLMPRLAQVKQQP-------EEEALILFTSGSEGHPKGVVHSHKSILANVEQI----- 397
Cdd:PTZ00216 222 IYLDSLPASVDTEGcRLVAWTDVVAKGHSAGSHHPlnipennDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALedrln 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 398 KTIADFTTNDRFMSALPLFHSFGLTVglftplltgAEVFLYpsplhyrivpelvydRSCTVLFGTS-TFLGHYAR----- 471
Cdd:PTZ00216 302 DLIGPPEEDETYCSYLPLAHIMEFGV---------TNIFLA---------------RGALIGFGSPrTLTDTFARphgdl 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 472 -------------------------------------------------------------FANPYDFY--RLRYVVAGA 488
Cdd:PTZ00216 358 tefrpvfligvprifdtikkaveaklppvgslkrrvfdhayqsrlralkegkdtpywnekvFSAPRAVLggRVRAMLSGG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 489 EKLQESTKQLWQDKFGlRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGI------EEGGRLQLKGPN 562
Cdd:PTZ00216 438 GPLSAATQEFVNVVFG-MVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEYkhtdtpEPRGEILLRGPF 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 563 IMNGYLRVEKPgvlevpTAENVrgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALG------ 635
Cdd:PTZ00216 517 LFKGYYKQEEL------TREVL---DEDGWFHTGDVGSIAANGTLRIIGRVKALAKNClGEYIALEALEALYGQnelvvp 587
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16130740 636 ------VSPDKVHATaiksdaskgeALVLftTDNEltrdKLQQYAREHGVP 680
Cdd:PTZ00216 588 ngvcvlVHPARSYIC----------ALVL--TDEA----KAMAFAKEHGIE 622
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
368-701 |
9.75e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 99.73 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSIlanveqIKTIADFT-------TNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP- 439
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDM------VYTAAAAYavavvggEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLAr 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 -SPL-------HYRIVpelvydrSCTVLFGTSTFLGHYARFANpYDFYRLRYV--VAGAEKLQESTKQLWQDKFGLRILE 509
Cdd:PRK06178 286 wDAVafmaaveRYRVT-------RTVMLVDNAVELMDHPRFAE-YDLSSLRQVrvVSFVKKLNPDYRQRWRALTGSVLAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 G-YGVTECAPVVSINVPMA-------AKPGTVGRILPGMDARLLS------VPGIEEGgRLQLKGPNIMNGYLRveKPGV 575
Cdd:PRK06178 358 AaWGMTETHTCDTFTAGFQdddfdllSQPVFVGLPVPGTEFKICDfetgelLPLGAEG-EIVVRTPSLLKGYWN--KPEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 576 levpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPdKVHATAI--KSDASKG 653
Cdd:PRK06178 435 ----TAEALRD----GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEAL-LGQHP-AVLGSAVvgRPDPDKG 504
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16130740 654 EALVLFTT---DNELTRDKLQQYAREH----GVPElavprdIRYLKQMPLLGSGK 701
Cdd:PRK06178 505 QVPVAFVQlkpGADLTAAALQAWCRENmavyKVPE------IRIVDALPMTATGK 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
359-703 |
1.47e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 359 QVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDrfmsALPLFHSFGLTV---GLFTPLLTGAEV 435
Cdd:PRK12467 1712 AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD----VVLQFTSFAFDVsvwELFWPLINGARL 1787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLYPSPLHYRivPELVYDRSC----TVLFGTST----FLGHYARFANPydfYRLRYVVAGAEKLQESTKQLWQDKFGLR- 506
Cdd:PRK12467 1788 VIAPPGAHRD--PEQLIQLIErqqvTTLHFVPSmlqqLLQMDEQVEHP---LSLRRVVCGGEALEVEALRPWLERLPDTg 1862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECA----------------PVVSINVPMAAKPGTVgrilpgMDARLLSVPgIEEGGRLQLKGPNIMNGYLRv 570
Cdd:PRK12467 1863 LFNLYGPTETAvdvthwtcrrkdlegrDSVPIGQPIANLSTYI------LDASLNPVP-IGVAGELYLGGVGLARGYLN- 1934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 571 eKPGVlevpTAE----NVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI 646
Cdd:PRK12467 1935 -RPAL----TAErfvaDPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEA-RLREQGGVREAVVI 2008
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 647 KSDASKGEALV--LFTTDNELTRDKLQQYA-----REH---GVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK12467 2009 AQDGANGKQLVayVVPTDPGLVDDDEAQVAlrailKNHlkaSLPEYMVPAHLVFLARMPLTPNGKLD 2075
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
255-673 |
2.30e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 98.51 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 255 GERIGLMLPN------AGISAAVIfGAIARRRMPAmmnYTAGvkGLTSAITAAEIKTIFTSRQFLDKGKlwhlpeQLTQV 328
Cdd:PLN02246 75 GDVVMLLLPNcpefvlAFLGASRR-GAVTTTANPF---YTPA--EIAKQAKASGAKLIITQSCYVDKLK------GLAED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 329 RWVYLEDLKADVttaDKVWIFAHLLMP---RLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIktiAD--- 402
Cdd:PLN02246 143 DGVTVVTIDDPP---EGCLHFSELTQAdenELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQ---VDgen 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 403 ----FTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhYRIVP--ELVYDRSCTVlfgtstflghyARFANP- 475
Cdd:PLN02246 217 pnlyFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK---FEIGAllELIQRHKVTI-----------APFVPPi 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 476 ------------YDFYRLRYVVAGAEKLQestKQLwQDKFGLR----IL-EGYGVTECAPVVSINV-----PMAAKPGTV 533
Cdd:PLN02246 283 vlaiakspvvekYDLSSIRMVLSGAAPLG---KEL-EDAFRAKlpnaVLgQGYGMTEAGPVLAMCLafakePFPVKSGSC 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 534 GRILPGMDARL------LSVPGiEEGGRLQLKGPNIMNGYLR-VEKpgvlevpTAENVRGEmerGWYDTGDIVRFDEQGF 606
Cdd:PLN02246 359 GTVVRNAELKIvdpetgASLPR-NQPGEICIRGPQIMKGYLNdPEA-------TANTIDKD---GWLHTGDIGYIDDDDE 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130740 607 VQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKLQQY 673
Cdd:PLN02246 428 LFIVDRLKELIKYKGFQVAPAELEALLIS-HPSIADAAVVpMKDEVAGEvpvAFVVRSNGSEITEDEIKQF 497
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
345-659 |
2.37e-21 |
|
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: 97.94 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 345 KVW--IFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLT 422
Cdd:cd05908 84 KVWntLKNPYLITEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 423 VGLFTPLLTGAEVFLYPSPLHYRiVPEL----VYDRSCTVL----FGTSTFLGHY-ARFANPYDFYRLRYVVAGAEKL-- 491
Cdd:cd05908 164 AFHLAPLIAGMNQYLMPTRLFIR-RPILwlkkASEHKATIVsspnFGYKYFLKTLkPEKANDWDLSSIRMILNGAEPIdy 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 492 ---QESTKQLwqDKFGLR---ILEGYGVTECApvVSINVPMAAKPG----------TVGRILPGMD------ARLLSV-- 547
Cdd:cd05908 243 elcHEFLDHM--SKYGLKrnaILPVYGLAEAS--VGASLPKAQSPFktitlgrrhvTHGEPEPEVDkkdsecLTFVEVgk 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 548 --------------PGIEEG--GRLQLKGPNIMNGYLRVEKpgvlevptaENVRGEMERGWYDTGDivrfdeQGFVQ--- 608
Cdd:cd05908 319 pidetdiricdednKILPDGyiGHIQIRGKNVTPGYYNNPE---------ATAKVFTDDGWLKTGD------LGFIRngr 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 609 --IQGRAKRFAKIAGEMVSLEMVEQLAL---GVSPDKVHATAIKSDASKGEALVLF 659
Cdd:cd05908 384 lvITGREKDIIFVNGQNVYPHDIERIAEeleGVELGRVVACGVNNSNTRNEEIFCF 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
320-703 |
2.89e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.85 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 320 HLPEQLTQVRWVYLEDLKADVTTAdkvwifahlLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK12467 3201 HLLEQLPAPAGDTALTLDRLDLNG---------YSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE 3271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 400 IADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH--YRIVPELVYDRSCTVLFGTStFLGHYARFANPY 476
Cdd:PRK12467 3272 AYELDANDRVLLFMSF--SFDGAQeRFLWTLICGGCLVVRDNDLWdpEELWQAIHAHRISIACFPPA-YLQQFAEDAGGA 3348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 477 DFYRLRYVVAGAEKLQESTKQLWQDKFGLRIL-EGYGVTECAPVVSI-NVPMAAKPGT----VGRILPG-----MDARLL 545
Cdd:PRK12467 3349 DCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTEAVVTVTLwKCGGDAVCEApyapIGRPVAGrsiyvLDGQLN 3428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 546 SVPgIEEGGRLQLKGPNIMNGYLRveKPGVlevpTAEN-----VRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIA 620
Cdd:PRK12467 3429 PVP-VGVAGELYIGGVGLARGYHQ--RPSL----TAERfvadpFSGSGGR-LYRTGDLARYRADGVIEYLGRIDHQVKIR 3500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 621 GEMVSLEMVEQLALGVSPDKvHATAIKSDASKGEALVLFTTDNELTRDKLQQYARE--HGVPELAVPRDIRYLKQMPLLG 698
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVR-EAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHlaASLPDYMVPAQLLVLAAMPLGP 3579
|
....*
gi 16130740 699 SGKPD 703
Cdd:PRK12467 3580 NGKVD 3584
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
233-695 |
3.38e-21 |
|
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: 98.33 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPnAGISAAVIFGAIARRRM---PAMMNYtaGVKGLTSAITAAEIKTIFT 308
Cdd:cd05968 93 TYGELLYEVKRLANGLRALGVGkGDRVGIYLP-MIPEIVPAFLAVARIGGivvPIFSGF--GKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 309 SRQFLDKGKLWHLPE-------QLTQVRWVYLE-DLKADVTTADKVWIFAHLLM----PRLAqvKQQPEEEALILFTSGS 376
Cdd:cd05968 170 ADGFTRRGREVNLKEeadkacaQCPTVEKVVVVrHLGNDFTPAKGRDLSYDEEKetagDGAE--RTESEDPLMIIYTSGT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 377 EGHPKGVVHSHKSI-LANVEQIKTIADFTTNDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFLYPS----PLHYRIVp 448
Cdd:cd05968 248 TGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLT----WFTDLGWMMGpwlIFGGLILGATMVLYDGapdhPKADRLW- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 449 ELVYDRSCTVLfGTS-----TFLGHYARFANPYDFYRLRYVVAGAEKLQ-ESTKQLWQDKFGLR--ILEGYGVTECAPVV 520
Cdd:cd05968 323 RMVEDHEITHL-GLSptlirALKPRGDAPVNAHDLSSLRVLGSTGEPWNpEPWNWLFETVGKGRnpIINYSGGTEISGGI 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 521 SINVPMAA-KPGTVGRILPGMDARLLS---VPGIEEGGRLQLKGP--NIMNGYLRVEKPGVlevptaENVRGEMERGWYD 594
Cdd:cd05968 402 LGNVLIKPiKPSSFNGPVPGMKADVLDesgKPARPEVGELVLLAPwpGMTRGFWRDEDRYL------ETYWSRFDNVWVH 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 595 tGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGEALVLFT------TDNELTR 667
Cdd:cd05968 476 -GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV-LNAHPAVLESAAIGvPHPVKGEAIVCFVvlkpgvTPTEALA 553
|
490 500
....*....|....*....|....*....
gi 16130740 668 DKLQQYAREH-GVPelAVPRDIRYLKQMP 695
Cdd:cd05968 554 EELMERVADElGKP--LSPERILFVKDLP 580
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
372-701 |
5.28e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 97.47 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 372 FTSGSEGHPKGVVHSHKSIL--ANVEQIKTIADFTTNDRFMSALPLFH--SFGLTvglFTPLLTGAEVFLyPSP-LHYRI 446
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHvnAWGLP---YSAPLTGAKLVL-PGPdLDGKS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 VPELVYDRSCTVLFGTST----FLGHYArfANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAP---V 519
Cdd:PRK07008 259 LYELIEAERVTFSAGVPTvwlgLLNHMR--EAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPlgtL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 520 VSINVPMAAKPGTV--------GRILPGMDARLLSVPGIE---EG---GRLQLKGPNIMNGYLRVE-KPGVlevptaenv 584
Cdd:PRK07008 337 CKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDGRElpwDGkafGDLQVRGPWVIDRYFRGDaSPLV--------- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 585 rgemeRGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASKGEA----LVLFT 660
Cdd:PRK07008 408 -----DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA-HPAVAEAACIACAHPKWDErpllVVVKR 481
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 16130740 661 TDNELTRDKLQQYArEHGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK07008 482 PGAEVTREELLAFY-EGKVAKWWIPDDVVFVDAIPHTATGK 521
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
333-701 |
5.45e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.14 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 333 LEDLKADVTTADKVWI------------FAHLLMPRLAQ----VKQQPEEEALILFTSGSEGHPKGVVHSHKSI----LA 392
Cdd:PRK06155 132 LEAADPGDLPLPAVWLldapasvsvpagWSTAPLPPLDApapaAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 393 NVEQIKTIADfttnDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRsCTVLFgtstFLGHY--- 469
Cdd:PRK06155 212 SAEDLEIGAD----DVLYTTLPLFHTNALNA-FFQALLAGATYVLEPRFSASGFWPAVRRHG-ATVTY----LLGAMvsi 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 470 --ARFANPYD-FYRLRYVVAGAEKLQesTKQLWQDKFGLRILEGYGVTECapvvsiNVPMA-----AKPGTVGRILPGMD 541
Cdd:PRK06155 282 llSQPARESDrAHRVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTET------NFVIAvthgsQRPGSMGRLAPGFE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 542 ARLLSVPGIE----EGGRLQLKGPN---IMNGYLRV-EKpgvlevpTAENVRGEmergWYDTGDIVRFDEQGFVQIQGRA 613
Cdd:PRK06155 354 ARVVDEHDQElpdgEPGELLLRADEpfaFATGYFGMpEK-------TVEAWRNL----WFHTGDRVVRDADGWFRFVDRI 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 614 KRFAKIAGEMVSLEMVEQlALGVSPD--KVHATAIKSDASKGE--ALVLFTTDNELTRDKLQQYArEHGVPELAVPRDIR 689
Cdd:PRK06155 423 KDAIRRRGENISSFEVEQ-VLLSHPAvaAAAVFPVPSELGEDEvmAAVVLRDGTALEPVALVRHC-EPRLAYFAVPRYVE 500
|
410
....*....|..
gi 16130740 690 YLKQMPLLGSGK 701
Cdd:PRK06155 501 FVAALPKTENGK 512
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
354-714 |
5.72e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 96.96 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 354 MPRLAQVKQQPEEE------ALILFTSGSEGHPKGVVHSHK----SILANVEQIktiaDFTTNDRFMSALPLFHSFGLTV 423
Cdd:PRK03640 124 LMNGPKEEAEIQEEfdldevATIMYTSGTTGKPKGVIQTYGnhwwSAVGSALNL----GLTEDDCWLAAVPIFHISGLSI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 424 gLFTPLLTGAEVFLYPsplHYRI--VPELVYDRSCTVLFGTSTFL---------GHYarfanPYDFyrlRYVVAGAEKLQ 492
Cdd:PRK03640 200 -LMRSVIYGMRVVLVE---KFDAekINKLLQTGGVTIISVVSTMLqrllerlgeGTY-----PSSF---RCMLLGGGPAP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 493 ESTKQLWQDKfGLRILEGYGVTE-CAPVVSINvP--MAAKPGTVGRILPGMDARL---LSVPGIEEGGRLQLKGPNIMNG 566
Cdd:PRK03640 268 KPLLEQCKEK-GIPVYQSYGMTEtASQIVTLS-PedALTKLGSAGKPLFPCELKIekdGVVVPPFEEGEIVVKGPNVTKG 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 567 YLRVEKPgvlevpTAENvrgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAI 646
Cdd:PRK03640 346 YLNREDA------TRET----FQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVG 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130740 647 KSDASKGEALVLF-TTDNELTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGKPDFVTLKSWVDEA 714
Cdd:PRK03640 416 VPDDKWGQVPVAFvVKSGEVTEEELRHFCEEK----LAkykVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
1.86e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 359 QVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPlFHSFGLTVGLFTPLLTGAEVFLY 438
Cdd:PRK12316 3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLA 3268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 439 PSPLHY--RIVPELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQdkFGLRILEGYGVTEC 516
Cdd:PRK12316 3269 GPEDWRdpALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVF--AGLPLYNLYGPTEA 3346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINVPMAAKPGT--VGRILPGMDARLLSVPGIEE----GGRLQLKGPNIMNGYLrvEKPGVLEVPTAENVRGEMER 590
Cdd:PRK12316 3347 TITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVpvgaLGELYLGGEGLARGYH--NRPGLTAERFVPDPFVPGER 3424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 591 gWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASKGEALVLFTTDNELTRDKL 670
Cdd:PRK12316 3425 -LYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEA-RLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREAL 3502
|
330 340 350
....*....|....*....|....*....|...
gi 16130740 671 QQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK12316 3503 KAHLKAS-LPEYMVPAHLLFLERMPLTPNGKLD 3534
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
363-703 |
2.26e-20 |
|
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: 94.81 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMsalpLFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVL----QFASIAFDVAaeeIYVTLLSGATLVLRP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 ----SPLHYRIvpELVYDRSCTVLFGTSTFLGHYARFANPYDF---YRLRYVVAGAEKLQESTKQLWQDKFGLRI--LEG 510
Cdd:cd17644 180 eemrSSLEDFV--QYIQQWQLTVLSLPPAYWHLLVLELLLSTIdlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 511 YGVTEC---APVVSINVPMAAKPG--TVGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYLrvEKPGVlevpT 580
Cdd:cd17644 258 YGPTEAtiaATVCRLTQLTERNITsvPIGRPIANtqvyiLDENLQPVP-VGVPGELHIGGVGLARGYL--NRPEL----T 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 581 AEN------VRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGE 654
Cdd:cd17644 331 AEKfishpfNSSESER-LYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 655 ALVLFT---TDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17644 410 RLVAYIvphYEESPSTVELRQFLKAK-LPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
332-703 |
2.35e-20 |
|
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: 95.21 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 332 YLEDLKADVTTADKVWI---------FAHLLMPRLAQVKQ--QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTI 400
Cdd:COG1021 140 LARELQAEVPSLRHVLVvgdageftsLDALLAAPADLSEPrpDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 401 ADFTTNDRFMSALPLFHSFGLTV-GLFTPLLTGAEVFLYPSPlhyrivpelvydrSCTVLF-------GTSTFLG--HYA 470
Cdd:COG1021 220 CGLDADTVYLAALPAAHNFPLSSpGVLGVLYAGGTVVLAPDP-------------SPDTAFpliererVTVTALVppLAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 471 RFAN-----PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE---CapVVSINVPMAAKPGTVGR-ILPGMD 541
Cdd:COG1021 287 LWLDaaersRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEglvN--YTRLDDPEEVILTTQGRpISPDDE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 542 ARLLSVPGIE----EGGRLQLKGPNIMNGYLRVEkpgvlevptAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAK--- 614
Cdd:COG1021 365 VRIVDEDGNPvppgEVGELLTRGPYTIRGYYRAP---------EHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdqi 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 615 -RfakiAGEMVSLEMVEQLALgvSPDKVHATAIKS--DASKGEALVLF--TTDNELTRDKLQQYAREHGVPELAVPRDIR 689
Cdd:COG1021 436 nR----GGEKIAAEEVENLLL--AHPAVHDAAVVAmpDEYLGERSCAFvvPRGEPLTLAELRRFLRERGLAAFKLPDRLE 509
|
410
....*....|....
gi 16130740 690 YLKQMPLLGSGKPD 703
Cdd:COG1021 510 FVDALPLTAVGKID 523
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
363-703 |
2.93e-20 |
|
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: 94.70 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSP 441
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI--SFDASVTeIFASLLSGNTLYIVRKE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 LHYRIVPELVY--DRSCTVLFGTSTFLGHYArFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGL--RILEGYGVTECA 517
Cdd:cd17655 213 TVLDGQALTQYirQNRITIIDLTPAHLKLLD-AADDSEGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVVSINV--PMAAKPGTV--GRILPGM-----DARLLSVPgIEEGGRLQLKGPNIMNGYLRveKPGVlevpTAEN----- 583
Cdd:cd17655 292 VDASIYQyePETDQQVSVpiGKPLGNTriyilDQYGRPQP-VGVAGELYIGGEGVARGYLN--RPEL----TAEKfvddp 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 -VRGE-MergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEAL-VLFT 660
Cdd:cd17655 365 fVPGErM----YRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLcAYIV 440
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16130740 661 TDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17655 441 SEKELPVAQLREFLARE-LPDYMIPSYFIKLDEIPLTPNGKVD 482
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
350-701 |
3.09e-20 |
|
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: 94.12 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 350 AHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPL 429
Cdd:cd05973 73 ARLVVTDAANRHKLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 430 LTGAEVFLYPSPLhyriVPELVYDrsCTVLFGTSTFLGHYARF---------ANPYDFYRLRYVVAGAEKLQESTKQLWQ 500
Cdd:cd05973 153 ALGHPTILLEGGF----SVESTWR--VIERLGVTNLAGSPTAYrllmaagaeVPARPKGRLRRVSSAGEPLTPEVIRWFD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 501 DKFGLRILEGYGVTECAPVVSiNVPMAAKP---GTVGRILPGMDARLLSVPGIEEG----GRLQLKGPN--IM--NGYLR 569
Cdd:cd05973 227 AALGVPIHDHYGQTELGMVLA-NHHALEHPvhaGSAGRAMPGWRVAVLDDDGDELGpgepGRLAIDIANspLMwfRGYQL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 570 VEKPGVlevptaenvrgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KS 648
Cdd:cd05973 306 PDTPAI-------------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES-ALIEHPAVAEAAVIgVP 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 649 DASKGE---ALVLFTTDNELT---RDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05973 372 DPERTEvvkAFVVLRGGHEGTpalADELQLHVKKR-LSAHAYPRTIHFVDELPKTPSGK 429
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
369-701 |
4.22e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 94.61 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGL-TVGLFTPLltGAEVFlypspLHYRIV 447
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWaHLTLAMAL--GSTVV-----LRRRFD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 PE----LVYDRSCTVLFGTSTFL----GHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECApV 519
Cdd:PRK07788 284 PEatleDIAKHKATALVVVPVMLsrilDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVA-F 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 520 VSINVP--MAAKPGTVGRILPGMDARLLSVPG--IEEG--GRLQLKGPNIMNGYlrvekpgvlevptaENVRG-EMERGW 592
Cdd:PRK07788 363 ATIATPedLAEAPGTVGRPPKGVTVKILDENGneVPRGvvGRIFVGNGFPFEGY--------------TDGRDkQIIDGL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 593 YDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGE---ALVLFTTDNELTRD 668
Cdd:PRK07788 429 LSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDL-LAGHPDVVEAAVIGvDDEEFGQrlrAFVVKAPGAALDED 507
|
330 340 350
....*....|....*....|....*....|....*.
gi 16130740 669 KLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGK 701
Cdd:PRK07788 508 AIKDYVRDN----LArykVPRDVVFLDELPRNPTGK 539
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
366-703 |
6.00e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 94.18 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 366 EEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsPLH-- 443
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLL---PARgr 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 -----------------YRIVP---ELVYDRSCTVLFGTSTflghyarfanpydfYRLRYVVAGAEKLQESTKQLWQDKF 503
Cdd:PRK05852 254 fsahtfwddikavgatwYTAVPtihQILLERAATEPSGRKP--------------AALRFIRSCSAPLTAETAQALQTEF 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 504 GLRILEGYGVTECA-PVVSINVPMA-------AKPGTVGRIlPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLrvE 571
Cdd:PRK05852 320 AAPVVCAFGMTEAThQVTTTQIEGIgqtenpvVSTGLVGRS-TGAQIRIVGSDGLPlpagAVGEVWLRGTTVVRGYL--G 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 572 KPGVlevpTAENvrgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqlalGV--SPDKVHATAI--K 647
Cdd:PRK05852 397 DPTI----TAAN----FTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE----GVlaSHPNVMEAAVfgV 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 648 SDASKGEALVLFTTDNEL---TRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK05852 465 PDQLYGEAVAAVIVPRESappTAEELVQFCRE-RLAAFEIPASFQEASGLPHTAKGSLD 522
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
360-703 |
6.12e-20 |
|
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: 93.56 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 360 VKQQPEEEALILFTSGSEGHPKGVVHSHKSiLANVEQiktiadftTNDRFMSALP-----LFHSFGLTVG---LFTPLLT 431
Cdd:cd17651 131 PALDADDLAYVIYTSGSTGRPKGVVMPHRS-LANLVA--------WQARASSLGPgartlQFAGLGFDVSvqeIFSTLCA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 432 GAEVFLYPSplHYRIVPE----LVYDRSCTVLFGTSTFLGHYARFANPYDFY--RLRYVVAGAEKLQ--ESTKQLWQDKF 503
Cdd:cd17651 202 GATLVLPPE--EVRTDPPalaaWLDEQRISRVFLPTVALRALAEHGRPLGVRlaALRYLLTGGEQLVltEDLREFCAGLP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 504 GLRILEGYGVTECAPVVSINVPMAAK----PGTVGRILPG-----MDARLLSVP-GIEegGRLQLKGPNIMNGYLRveKP 573
Cdd:cd17651 280 GLRLHNHYGPTETHVVTALSLPGDPAawpaPPPIGRPIDNtrvyvLDAALRPVPpGVP--GELYIGGAGLARGYLN--RP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 574 GVlevpTAEN------VRGE-MergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqLALGVSPDKVHATAI 646
Cdd:cd17651 356 EL----TAERfvpdpfVPGArM----YRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVVL 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130740 647 KSDASKGE----ALVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17651 427 AREDRPGEkrlvAYVVGDPEAPVDAAELRAALATH-LPEYMVPSAFVLLDALPLTPNGKLD 486
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
360-701 |
1.89e-19 |
|
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: 92.53 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 360 VKQQPEEEALILFTSGSEGHPKGVVHSHKSI-LANVEQIKTIADFTTNDRF--MSALPLFHSFGLTVglFTPLLTGAEVF 436
Cdd:cd05928 169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMwnTSDTGWIKSAWSSL--FEPWIQGACVF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 437 LYPSPlhyRIVPELVYDR----SCTVLFGTSTFlghYARFA----NPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRIL 508
Cdd:cd05928 247 VHHLP---RFDPLVILKTlssyPITTFCGAPTV---YRMLVqqdlSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 509 EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSV------PGIEEGGRLQLKgPN----IMNGYlrVEKPgvleV 578
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDngnvlpPGTEGDIGIRVK-PIrpfgLFSGY--VDNP----E 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 579 PTAENVRGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKS-DASKGE--- 654
Cdd:cd05928 394 KTAATIRGD----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVES-ALIEHPAVVESAVVSSpDPIRGEvvk 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16130740 655 ALVLFTTD------NELTRDkLQQYAREHGVPeLAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05928 469 AFVVLAPQflshdpEQLTKE-LQQHVKSVTAP-YKYPRKVEFVQELPKTVTGK 519
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
256-716 |
1.96e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 92.15 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 256 ERIGLMLPNaGISAAVIF-GAiarrrmpAMMNYTA-------GVKGLTSAITAAEIKTIFTSRQFLDKgklwhLPEQLTQ 327
Cdd:PRK07638 51 KTIAILLEN-RIEFLQLFaGA-------AMAGWTCvpldikwKQDELKERLAISNADMIVTERYKLND-----LPDEEGR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 328 VrwVYLEDLKADVTTAdkvwifahllMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEqiKTIADF--TT 405
Cdd:PRK07638 118 V--IEIDEWKRMIEKY----------LPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFD--CNVHDFhmKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 406 NDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPsplhyRIVPELVYDRSCT----VLFGTSTFLGHYARfANPYDFYRL 481
Cdd:PRK07638 184 EDSVLIAGTLVHSLFL-YGAISTLYVGQTVHLMR-----KFIPNQVLDKLETenisVMYTVPTMLESLYK-ENRVIENKM 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 482 RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECApVVSINVP--MAAKPGTVGRILPGMDARLLSVPGIE----EGGR 555
Cdd:PRK07638 257 KIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELS-FVTALVDeeSERRPNSVGRPFHNVQVRICNEAGEEvqkgEIGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 556 LQLKGPNIMNGYlrvekpgvleVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALG 635
Cdd:PRK07638 336 VYVKSPQFFMGY----------IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 636 VsPDKVHATAI-KSDASKGEALVLFTTDNElTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEA 714
Cdd:PRK07638 406 H-PAVDEIVVIgVPDSYWGEKPVAIIKGSA-TKQQLKSFCLQR-LSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
..
gi 16130740 715 EQ 716
Cdd:PRK07638 483 EK 484
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
372-708 |
2.25e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 92.12 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 372 FTSGSEGHPKGVVHSHKSilaNVEQ--IKTIAD---FTTNDRFMSALPLFH--SFGLTvglFTPLLTGAEVFLYPSPLHY 444
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRS---NVLHalMANNGDalgTSAADTMLPVVPLFHanSWGIA---FSAPSMGTKLVMPGAKLDG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RIVPELVYDRSCTVLFGTST----FLGHYArfANPYDFYRLRYVVAGAEKLQESTKQLWQDkFGLRILEGYGVTECAPVv 520
Cdd:PRK06018 258 ASVYELLDTEKVTFTAGVPTvwlmLLQYME--KEGLKLPHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMSPL- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 521 sinvpmaakpGTVGRILPGM-----DARL-------LSVPGIE------EG----------GRLQLKGPNIMNGYLRVEK 572
Cdd:PRK06018 334 ----------GTLAALKPPFsklpgDARLdvlqkqgYPPFGVEmkitddAGkelpwdgktfGRLKVRGPAVAAAYYRVDG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 573 PgVLEvptaenvrgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASK 652
Cdd:PRK06018 404 E-ILD-----------DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVG-HPKVAEAAVIGVYHPK 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 653 -GEA---LVLFTTDNELTRDKLQQYArEHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLK 708
Cdd:PRK06018 471 wDERpllIVQLKPGETATREEILKYM-DGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
233-695 |
2.85e-19 |
|
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: 91.80 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTK-TLFVGRILEKYSVEGERIGLMLPNAgISAAVIFGAIAR-RRMPAMMNYTAGVKGLTSAITAAEIKTIFTSr 310
Cdd:cd05923 30 TYSELRARiEAVAARLHARGLRPGQRVAVVLPNS-VEAVIALLALHRlGAVPALINPRLKAAELAELIERGEMTAAVIA- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 311 qfLDKGklwhlPEQLTQVRWVYLEDLKADVTTADkvwifAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSI 390
Cdd:cd05923 108 --VDAQ-----VMDAIFQSGVRVLALSDLVGLGE-----PESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 391 LANVEQIKTIAD--FTTNDRFMSALPLFHSFGLtVGLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTF--- 465
Cdd:cd05923 176 ESRVLFMSTQAGlrHGRHNVVLGLMPLYHVIGF-FAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHlda 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 466 LGHYARFAnPYDFYRLRYVV-AGAEKLQESTKQLWQDKFGlRILEGYGVTEcapVVSINVPMAAKPGTVGRilPGMDARL 544
Cdd:cd05923 255 LAAAAEFA-GLKLSSLRHVTfAGATMPDAVLERVNQHLPG-EKVNIYGTTE---AMNSLYMRDARTGTEMR--PGFFSEV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 545 LSVPgieEGGRLQLKGPNIMNGYLRVEKP------GVLEVP--TAENVRgemeRGWYDTGDIVRFDEQGFVQIQGRAKRF 616
Cdd:cd05923 328 RIVR---IGGSPDEALANGEEGELIVAAAadaaftGYLNQPeaTAKKLQ----DGWYRTGDVGYVDPSGDVRILGRVDDM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 617 AKIAGEMVSLEMVEQLaLGVSPDKVHATAIK-SDASKGEALVLFTTDNE--LTRDKLQQYAREHGVPELAVPRDIRYLKQ 693
Cdd:cd05923 401 IISGGENIHPSEIERV-LSRHPGVTEVVVIGvADERWGQSVTACVVPREgtLSADELDQFCRASELADFKRPRRYFFLDE 479
|
..
gi 16130740 694 MP 695
Cdd:cd05923 480 LP 481
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
363-630 |
2.92e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 92.47 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFH-----------SFGLTVGLFT---- 427
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHiyervnqivmlHYGVAVGFYQgdnl 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 428 PLLTGAEVFlypSPLHYRIVPEL---VYDRsCTVLFGTSTFLG----HYARFA---------NPYDFY------------ 479
Cdd:PLN02736 299 KLMDDLAAL---RPTIFCSVPRLynrIYDG-ITNAVKESGGLKerlfNAAYNAkkqalengkNPSPMWdrlvfnkikakl 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 --RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE------ 551
Cdd:PLN02736 375 ggRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNytsedq 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 552 --EGGRLQLKGPNIMNGYLRVekpgvlEVPTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEM 628
Cdd:PLN02736 455 pyPRGEICVRGPIIFKGYYKD------EVQTREVIDED---GWLHTGDIGLWLPGGRLKIIDRKKNIFKLAqGEYIAPEK 525
|
..
gi 16130740 629 VE 630
Cdd:PLN02736 526 IE 527
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-703 |
8.02e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 91.94 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 359 QVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR---FMSalplFHSFGLTVGLFTPLLTGAEV 435
Cdd:PRK12316 2140 AVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCelqFMS----FSFDGAHEQWFHPLLNGARV 2215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLYPSPLHyriVPELVYD----RSCTVLFGTSTFL----GHYARFANPydfYRLRYVVAGAEKL-QESTKQLWQDKFGLR 506
Cdd:PRK12316 2216 LIRDDELW---DPEQLYDemerHGVTILDFPPVYLqqlaEHAERDGRP---PAVRVYCFGGEAVpAASLRLAWEALRPVY 2289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECAPVVSI-----NVPMAAKPGTVGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYLrvEKPGVL 576
Cdd:PRK12316 2290 LFNGYGPTEAVVTPLLwkcrpQDPCGAAYVPIGRALGNrrayiLDADLNLLA-PGMAGELYLGGEGLARGYL--NRPGLT 2366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 577 E---VPTAENVRGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASKG 653
Cdd:PRK12316 2367 AerfVPDPFSASGER---LYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEA-RLQAHPAVREAVVVAQDGASG 2442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 654 EALVLFTTDNELTRDKLQQYAREHG--VPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK12316 2443 KQLVAYVVPDDAAEDLLAELRAWLAarLPAYMVPAHWVVLERLPLNPNGKLD 2494
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
368-701 |
9.21e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 90.22 E-value: 9.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILAN-VEQIKTIADFTTNDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYPSPlhyRI 446
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYPLG---AF 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 447 VPELVYDrsctVLFG---TSTFLGHY-------ARFANPYDFyRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTE 515
Cdd:PRK07786 253 DPGQLLD----VLEAekvTGIFLVPAqwqavcaEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 516 CAPVVSINVPMAA--KPGTVGRILPGMDARLLS-----VPgIEEGGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGem 588
Cdd:PRK07786 328 MSPVTCMLLGEDAirKLGSVGKVIPTVAARVVDenmndVP-VGEVGEIVYRAPTLMSGYWNNPEA------TAEAFAG-- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 589 erGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGEA----LVLFTTDN 663
Cdd:PRK07786 399 --GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVEN-VLASHPDIVEVAVIgRADEKWGEVpvavAAVRNDDA 475
|
330 340 350
....*....|....*....|....*....|....*...
gi 16130740 664 ELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK07786 476 ALTLEDLAEFLTDR-LARYKHPKALEIVDALPRNPAGK 512
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-612 |
1.19e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.44 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFhsfgltvGLFTPLLTGAEV-----FLYP 439
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGLTSVipdmdPTRP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPLHYRIVPELVYDRSCTVLFGTSTFLGHYARF--ANPYDFYRLRYVV-AGAE---KLQESTKQLWQDkfGLRILEGYGV 513
Cdd:cd05910 158 ARADPQKLVGAIRQYGVSIVFGSPALLERVARYcaQHGITLPSLRRVLsAGAPvpiALAARLRKMLSD--EAEILTPYGA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 514 TECAPVVSI---------NVPMAAKPGT-VGRILPGMDARLLSV---PGIEEGGRLQL----------KGPNIMNGYlrV 570
Cdd:cd05910 236 TEALPVSSIgsrellattTAATSGGAGTcVGRPIPGVRVRIIEIddePIAEWDDTLELprgeigeitvTGPTVTPTY--V 313
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16130740 571 EKPgvlEVPTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGR 612
Cdd:cd05910 314 NRP---VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGR 352
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
332-701 |
1.53e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 89.44 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 332 YLEDLKA--------DVTTAdkvwifAHllMPRLAQVKQQPEEEALIL-FTSGSEGHPKGVVHSHKSILANVEQIKTIAD 402
Cdd:PRK05851 118 HLERLRAvdssvtvhDLATA------AH--TNRSASLTPPDSGGPAVLqGTAGSTGTPRTAILSPGAVLSNLRGLNARVG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 403 FTT-NDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYP------SPLH-----------YRIVPELVYDrsctvlfgtst 464
Cdd:PRK05851 190 LDAaTDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPttafsaSPFRwlswlsdsratLTAAPNFAYN----------- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 465 FLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQD---KFGLR---ILEGYGVTECAPVVSINVP------------- 525
Cdd:PRK05851 258 LIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATamaPFGFDagaAAPSYGLAESTCAVTVPVPgiglrvdevttdd 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 --MAAKPGTVGRILPGMDARLL-----SVPGIEEGGRLQLKGPNIMNGYLRvEKPgvlevptaenvrgeMERG-WYDTGD 597
Cdd:PRK05851 338 gsGARRHAVLGNPIPGMEVRISpgdgaAGVAGREIGEIEIRGASMMSGYLG-QAP--------------IDPDdWFPTGD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 598 IVRFDEQGFVqIQGRAKRFAKIAGEMVSLEMVEQLAL---GVSPDKVHATAIKSDASKgEALVLFT----TDNELTRDKL 670
Cdd:PRK05851 403 LGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAqvrGVREGAVVAVGTGEGSAR-PGLVIAAefrgPDEAGARSEV 480
|
410 420 430
....*....|....*....|....*....|....
gi 16130740 671 -QQYAREHGVpelaVPRDIRYLK--QMPLLGSGK 701
Cdd:PRK05851 481 vQRVASECGV----VPSDVVFVApgSLPRTSSGK 510
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
363-703 |
1.71e-18 |
|
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: 88.68 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANV---EQIKTIADFTTNDRFMSALplfhSFGLTVGLFT-PLLTGAEvfLY 438
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAhawRREYELDSFPVRLLQMASF----SFDVFAGDFArSLLNGGT--LV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 439 PSPLHYRIVPELVYD----RSCTVLFGTSTF---LGHYArFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFG--LRILE 509
Cdd:cd17650 165 ICPDEVKLDPAALYDlilkSRITLMESTPALirpVMAYV-YRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIIN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 510 GYGVTEC-----------APVVSI-NVPmaakpgtVGRILPGM-----DARLLSVPgIEEGGRLQLKGPNIMNGYLrvEK 572
Cdd:cd17650 244 SYGVTEAtidstyyeegrDPLGDSaNVP-------IGRPLPNTamyvlDERLQPQP-VGVAGELYIGGAGVARGYL--NR 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 573 PGVLEVPTAENVRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASK 652
Cdd:cd17650 314 PELTAERFVENPFAPGER-MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIES-QLARHPAIDEAVVAVREDKG 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16130740 653 GEA-LVLF-TTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17650 392 GEArLCAYvVAAATLNTAELRAFLAKE-LPSYMIPSYYVQLDALPLTPNGKVD 443
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
301-613 |
1.89e-18 |
|
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: 90.30 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 301 AEIKTIFTSRQFLDKgklwhLPEQltQVRWVYLEDLKADVTTADkvwifahllmprLAQVKQQPEEEALILFTSGSEGHP 380
Cdd:COG1020 572 AGARLVLTQSALAAR-----LPEL--GVPVLALDALALAAEPAT------------NPPVPVTPDDLAYVIYTSGSTGRP 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 381 KGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLYPSPLHY---RIVpELVYDRSC 456
Cdd:COG1020 633 KGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASL--SFDASVWeIFGALLSGATLVLAPPEARRdpaALA-ELLARHRV 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 457 TVLFGTSTFLGHYARFANPyDFYRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAPVVSINVPMAAKPG---- 531
Cdd:COG1020 710 TVLNLTPSLLRALLDAAPE-ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADggsv 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 532 TVGRILPGM-----DARLLSVP-GIEegGRLQLKGPNIMNGYLRveKPGVlevpTAE-------NVRGemERgWYDTGDI 598
Cdd:COG1020 789 PIGRPIANTrvyvlDAHLQPVPvGVP--GELYIGGAGLARGYLN--RPEL----TAErfvadpfGFPG--AR-LYRTGDL 857
|
330
....*....|....*
gi 16130740 599 VRFDEQGFVQIQGRA 613
Cdd:COG1020 858 ARWLPDGNLEFLGRA 872
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
319-701 |
1.98e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.47 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 319 WHLPEQLTQ---VRW-VYLEDLK-------ADVTTADKVWifAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSH 387
Cdd:PLN02860 117 WYEELQNDRlpsLMWqVFLESPSssvfiflNSFLTTEMLK--QRALGTTELDYAWAPDDAVLICFTSGTTGRPKGVTISH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 388 KSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLfTPLLTGAEVFLYPSpLHYRIVPELVYDRSCTVLFGTSTFLG 467
Cdd:PLN02860 195 SALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPK-FDAKAALQAIKQHNVTSMITVPAMMA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 468 HYARFA----NPYDFYRLRYVVAGA----EKLQESTKQLWQDKfglRILEGYGVTE-CAPV--VSINVPMAAKP------ 530
Cdd:PLN02860 273 DLISLTrksmTWKVFPSVRKILNGGgslsSRLLPDAKKLFPNA---KLFSAYGMTEaCSSLtfMTLHDPTLESPkqtlqt 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 531 -------------GT-VGRILPGMDARLlSVPGIEEGGRLQLKGPNIMNGY--LRVEKPGVLevpTAEnvrgemerGWYD 594
Cdd:PLN02860 350 vnqtksssvhqpqGVcVGKPAPHVELKI-GLDESSRVGRILTRGPHVMLGYwgQNSETASVL---SND--------GWLD 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 595 TGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqLALGVSPDKVHATAIK-SDASKGEALVLFT--------TDNE- 664
Cdd:PLN02860 418 TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE-AVLSQHPGVASVVVVGvPDSRLTEMVVACVrlrdgwiwSDNEk 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 16130740 665 --------LTRDKLQQYAREHGVPELAVPRDI-RYLKQMPLLGSGK 701
Cdd:PLN02860 497 enakknltLSSETLRHHCREKNLSRFKIPKLFvQWRKPFPLTTTGK 542
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
255-634 |
2.25e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.07 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 255 GERIGLMLPNAGISAAVIF-----GAIARRRMPAMMNytagvKGLTSAITAAEIKTIFTSRQflDKGKLWHLPEQLTQVR 329
Cdd:PRK05620 64 DQRVGSMMYNCAEHLEVLFavacmGAVFNPLNKQLMN-----DQIVHIINHAEDEVIVADPR--LAEQLGEILKECPCVR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 330 WV-YLEDLKADVTTAD-----KVWIFAHLLMPRLAQVK--QQPEEE-ALILFTSGSEGHPKGVVHSHKSILANVEQIKTI 400
Cdd:PRK05620 137 AVvFIGPSDADSAAAHmpegiKVYSYEALLDGRSTVYDwpELDETTaAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 401 ADF--TTNDRFMSALPLFH--SFGLTVGLF---TPL-LTGAEVflypSPLHYRIVPELVYDRsctVLFGTST----FLGH 468
Cdd:PRK05620 217 DSLavTHGESFLCCVPIYHvlSWGVPLAAFmsgTPLvFPGPDL----SAPTLAKIIATAMPR---VAHGVPTlwiqLMVH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 469 YARfaNPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTV--------GRILPGM 540
Cdd:PRK05620 290 YLK--NPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEArwayrvsqGRFPASL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 541 DARLLSVPGIEEG-----GRLQLKGPNIMNGYLrvEKPGVLEVPTAENVRGE---------MERGWYDTGDIVRFDEQGF 606
Cdd:PRK05620 368 EYRIVNDGQVMEStdrneGEIQVRGNWVTASYY--HSPTEEGGGAASTFRGEdvedandrfTADGWLRTGDVGSVTRDGF 445
|
410 420
....*....|....*....|....*...
gi 16130740 607 VQIQGRAKRFAKIAGEMVSLEMVEQLAL 634
Cdd:PRK05620 446 LTIHDRARDVIRSGGEWIYSAQLENYIM 473
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
360-621 |
6.61e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 87.59 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 360 VKQQpeEEALILFTSGSEGHPKGVVHSHKSILANVE-----QIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
Cdd:PLN02574 195 IKQD--DVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 435 VFLYP--------------SPLHYRIVPELVydrsctvlfgtsTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQ 500
Cdd:PLN02574 273 IVVMRrfdasdmvkvidrfKVTHFPVVPPIL------------MALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 501 DKFG-LRILEGYGVTECAPVVS--INVPMAAKPGTVGRILPGMDARLLSV-------PGieEGGRLQLKGPNIMNGYLRV 570
Cdd:PLN02574 341 QTLPhVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWstgcllpPG--NCGELWIQGPGVMKGYLNN 418
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 16130740 571 EKPGVLEVptaenvrgeMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
Cdd:PLN02574 419 PKATQSTI---------DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKG 460
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
290-648 |
2.61e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 86.32 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 290 GVKGLTSAITAAEIKTIFTSRQFLDKgkLWHLPEQLTQV-RWVYLEDLKADVTTADKV---WI---FAHL--------LM 354
Cdd:PLN02387 166 GEEALCHSLNETEVTTVICDSKQLKK--LIDISSQLETVkRVIYMDDEGVDSDSSLSGssnWTvssFSEVeklgkenpVD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQvkqqPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTI-ADFTTNDRFMSALPLFHSF-----------GLT 422
Cdd:PLN02387 244 PDLPS----PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLAHILelaaesvmaavGAA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 423 VGLFTPL-LT-----------GAEVFLYPSPLhyRIVP-------------------------ELVYDRSCTVLFGtsTF 465
Cdd:PLN02387 320 IGYGSPLtLTdtsnkikkgtkGDASALKPTLM--TAVPaildrvrdgvrkkvdakgglakklfDIAYKRRLAAIEG--SW 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 466 LGHYARFANPYDFY-----------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CA---------PVVsinv 524
Cdd:PLN02387 396 FGAWGLEKLLWDALvfkkiravlggRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTEtCAgatfsewddTSV---- 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 525 pmaakpGTVGRILPGMDARLLSvpgIEEGGRLQ-----------LKGPNIMNGYLRVEKpgvlevPTAENVRGEmERG-- 591
Cdd:PLN02387 472 ------GRVGPPLPCCYVKLVS---WEEGGYLIsdkpmprgeivIGGPSVTLGYFKNQE------KTDEVYKVD-ERGmr 535
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130740 592 WYDTGDIVRFDEQGFVQIQGRAKRFAKI-AGEMVSLEMVEQlALGVSP--DK--VHATAIKS 648
Cdd:PLN02387 536 WFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEA-ALSVSPyvDNimVHADPFHS 596
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
332-702 |
2.73e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.83 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 332 YLEDLKADVTTADKVWIFAHLLMPRLAQV-----KQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIA-DFTT 405
Cdd:PRK09192 138 LLPWVNEATHGNPLLHVLSHAWFKALPEAdvalpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGlKVRP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 406 NDRFMSALPLFHSFGLtVGLF-TPLLTGAEVFLYPS------PLHYRivpELVYDRSCTVLFGTSTFLGHYARFAN---- 474
Cdd:PRK09192 218 GDRCVSWLPFYHDMGL-VGFLlTPVATQLSVDYLPTrdfarrPLQWL---DLISRNRGTISYSPPFGYELCARRVNskdl 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 475 -PYDFYRLRYVVAGAEKLQESTKQLWQDKFGLR------ILEGYGVTECAPVVS----------------------INVP 525
Cdd:PRK09192 294 aELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSfsplgsgivveevdrdrleyqgKAVA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 MAAKPGTV------GRILPGMDARLLSVPGIEEG----GRLQLKGPNIMNGYLRVEkpgvlevptaENVRGEMERGWYDT 595
Cdd:PRK09192 374 PGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPervvGHICVRGPSLMSGYFRDE----------ESQDVLAADGWLDT 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 596 GDIvRFDEQGFVQIQGRAKRFAKIAGEMV---SLE-MVEQLAlGVSPDKVHATAIKSDAskGEALVLF----TTDNE--- 664
Cdd:PRK09192 444 GDL-GYLLDGYLYITGRAKDLIIINGRNIwpqDIEwIAEQEP-ELRSGDAAAFSIAQEN--GEKIVLLvqcrISDEErrg 519
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 16130740 665 LTRDKLQQYAR-EHGVP---ELAVPRDIrylkqmPLLGSGKP 702
Cdd:PRK09192 520 QLIHALAALVRsEFGVEaavELVPPHSL------PRTSSGKL 555
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
364-703 |
3.13e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 85.42 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLtvgLFTP-LLTGAEVFLYPS-- 440
Cdd:PRK06188 167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA---FFLPtLLRGGTVIVLAKfd 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 P-------LHYRI-----VPELVYdrsctvlfgtsTFLGHYArfANPYDFYRLRYVVAGAE-----KLQESTkqlwqDKF 503
Cdd:PRK06188 244 PaevlraiEEQRItatflVPTMIY-----------ALLDHPD--LRTRDLSSLETVYYGASpmspvRLAEAI-----ERF 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 504 GLRILEGYGVTECAPVVSINVP---MAAKPGTV---GRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRveKP 573
Cdd:PRK06188 306 GPIFAQYYGQTEAPMVITYLRKrdhDPDDPKRLtscGRPTPGLRVALLDEDGREvaqgEVGEICVRGPLVMDGYWN--RP 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 574 GVlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDkVHATAI--KSDAS 651
Cdd:PRK06188 384 EE----TAEAFRD----GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED-VLAEHPA-VAQVAVigVPDEK 453
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 652 KGEAL---VLFTTDNELTRDKLQQYAREH-GVPelAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK06188 454 WGEAVtavVVLRPGAAVDAAELQAHVKERkGSV--HAPKQVDFVDSLPLTALGKPD 507
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
365-704 |
4.08e-17 |
|
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: 83.59 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 365 EEEALILFTSGSEGHPKGVVHSHKSI---LANVEQIKTIADFTTND-----------RFMSALPLFHSFGLTVGlFTPLL 430
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDahkaaaaaagtVMFPAPPLMHGTGSWTA-FGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 431 TGAEVFLYPSPLHYRIVPELVYDRSCTVLfgtsTFLGH-YAR-------FANPYDFYRLRYVVAGAEKLQESTKQLWQD- 501
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSM----TIVGDaMARplidalrDAGPYDLSSLFAISSGGALLSPEVKQGLLEl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 KFGLRILEGYGVTEC-APVVSINVPMAAKPGTvgRILPGMDARLLS------VPGIEEGGRLQLKGpNIMNGYLRVEKPG 574
Cdd:cd05924 158 VPNITLVDAFGSSETgFTGSGHSAGSGPETGP--FTRANPDTVVLDddgrvvPPGSGGVGWIARRG-HIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 575 VLEVPTAENVRgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKG 653
Cdd:cd05924 235 AETFPEVDGVR------YAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEE-ALKSHPAVYDVLVVgRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 654 E---ALVLFTTDNELTRDKLqqyaREHGVPELA---VPRDIRYLKQMPLLGSGKPDF 704
Cdd:cd05924 308 QevvAVVQLREGAGVDLEEL----REHCRTRIArykLPKQVVFVDEIERSPAGKADY 360
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
361-624 |
4.20e-17 |
|
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: 85.49 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 361 KQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR----FMSALPLFHSFGLTVGLFTPLLTGAEV- 435
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVy 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLYPSPLHYRIVPEL-------------VYDR---SCTVLFGTSTFL----GHYARFA-------------NPYDFYRL- 481
Cdd:cd05933 226 FAQPDALKGTLVKTLrevrptafmgvprVWEKiqeKMKAVGAKSGTLkrkiASWAKGVgletnlklmggesPSPLFYRLa 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 482 RYVV-----------------AGAEKLQESTKQLWQDkFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARL 544
Cdd:cd05933 306 KKLVfkkvrkalgldrcqkffTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 545 LSvPGIEEGGRLQLKGPNIMNGYLRvekpgvLEVPTAENVRgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEM 623
Cdd:cd05933 385 HN-PDADGIGEICFWGRHVFMGYLN------MEDKTEEAID---EDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGEN 454
|
.
gi 16130740 624 V 624
Cdd:cd05933 455 V 455
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
255-694 |
6.27e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.93 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 255 GERIGLMLPN-----AGISAAVIFGAIArrrmpAMMNYTAGVKGLTSAITAAEIKTIF----------TSRQFLDKGKLW 319
Cdd:PRK08279 87 GDVVALLMENrpeylAAWLGLAKLGAVV-----ALLNTQQRGAVLAHSLNLVDAKHLIvgeelveafeEARADLARPPRL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 320 HLPEQLTQVRWVYLEDLKADVTTADKvwifahlLMPRLAQvKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKT 399
Cdd:PRK08279 162 WVAGGDTLDDPEGYEDLAAAAAGAPT-------TNPASRS-GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 400 IADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELV-YDrsCTvLFGtstFLGHYARF-----A 473
Cdd:PRK08279 234 LLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRrYR--AT-AFQ---YIGELCRYllnqpP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 474 NPYDF-YRLRYVV-AGaekLQESTKQLWQDKFGL-RILEGYGVTEcAPVVSINVpmAAKPGTVGRIlPGMDARLLSVPGI 550
Cdd:PRK08279 308 KPTDRdHRLRLMIgNG---LRPDIWDEFQQRFGIpRILEFYAASE-GNVGFINV--FNFDGTVGRV-PLWLAHPYAIVKY 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 551 EEGGRLQLKGPnimNGYLRVEKPGvlEV------------------PTAEN---VRGEMERG--WYDTGDIVRFDEQGFV 607
Cdd:PRK08279 381 DVDTGEPVRDA---DGRCIKVKPG--EVglligritdrgpfdgytdPEASEkkiLRDVFKKGdaWFNTGDLMRDDGFGHA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 608 QIQGRA------KrfakiaGEMVSLEMVEQlALGVSPDKVHATAI-----KSDASKGEALVLFTTDNELTRDKLQQYARE 676
Cdd:PRK08279 456 QFVDRLgdtfrwK------GENVATTEVEN-ALSGFPGVEEAVVYgvevpGTDGRAGMAAIVLADGAEFDLAALAAHLYE 528
|
490
....*....|....*...
gi 16130740 677 HgVPELAVPRDIRYLKQM 694
Cdd:PRK08279 529 R-LPAYAVPLFVRLVPEL 545
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
233-701 |
6.54e-17 |
|
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: 84.67 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGL-----------MLPNAGISA--AVIFGAIArrrmpammnytagVKGLTSAI 298
Cdd:cd05967 84 TYAELLDEVSRLAGVLRKLGVVkGDRVIIympmipeaaiaMLACARIGAihSVVFGGFA-------------AKELASRI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 299 TAAEIKTIFTSRQFLDKGKL--------------WHLPE------------QLTQV-RWVYLEDLKADVTTADKVWIFAH 351
Cdd:cd05967 151 DDAKPKLIVTASCGIEPGKVvpykplldkalelsGHKPHhvlvlnrpqvpaDLTKPgRDLDWSELLAKAEPVDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 352 llmprlaqvkqqpeEEALILFTSGSEGHPKGVV-----HShksiLANVEQIKTIADFTTNDRFMSALPLfhsfGLTVG-- 424
Cdd:cd05967 231 --------------DPLYILYTSGTTGKPKGVVrdnggHA----VALNWSMRNIYGIKPGDVWWAASDV----GWVVGhs 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 425 --LFTPLLTGAEVFLY-------PSPLHY-RIVPElvYDRSCtvLFGTSTFL---------GHYARfanPYDFYRLRYVV 485
Cdd:cd05967 289 yiVYGPLLHGATTVLYegkpvgtPDPGAFwRVIEK--YQVNA--LFTAPTAIrairkedpdGKYIK---KYDLSSLRTLF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 486 AGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSIN----VPMAAKPGTVGRILPGMDARLLSvpgiEEGGRLqlkGP 561
Cdd:cd05967 362 LAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANpvglEPLPIKAGSPGKPVPGYQVQVLD----EDGEPV---GP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 562 NIMnGYLRVEKPgvLEVPTAENVRGEMER----------GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ 631
Cdd:cd05967 435 NEL-GNIVIKLP--LPPGCLLTLWKNDERfkklylskfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 632 lALGVSPDKVHATAI-KSDASKGE---ALVLFTTDNELTRDKLQ----QYAREHGVPeLAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05967 512 -SVLSHPAVAECAVVgVRDELKGQvplGLVVLKEGVKITAEELEkelvALVREQIGP-VAAFRLVIFVKRLPKTRSGK 587
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
364-703 |
1.23e-16 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 83.22 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRfmSALPLFHS--FGLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD--EAVLFFSNyvFDFFVEQMTLALLNGQKLVVPPD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 lHYRIVPELVYD----RSCTVLFGTSTFLGHYarfanpyDFYR---LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVT 514
Cdd:cd17648 171 -EMRFDPDRFYAyinrEKVTYLSGTPSVLQQY-------DLARlphLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECApVVSINVPM---AAKPGTVGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYL-RVEKPGVLEVPTAENVR 585
Cdd:cd17648 243 ETT-VTNHKRFFpgdQRFDKSLGRPVRNtkcyvLNDAMKRVP-VGAVGELYLGGDGVARGYLnRPELTAERFLPNPFQTE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 586 GEMERG----WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEA-----L 656
Cdd:cd17648 321 QERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyL 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 16130740 657 VLFTTDNE--LTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17648 401 VGYYLPEPghVPESDLLSFLRAK-LPRYMVPARLVRLEGIPVTINGKLD 448
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
363-703 |
1.39e-16 |
|
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: 82.75 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKtiADFTTNDR--FMSALPLfhSFGLTV-GLFTPLLTGAEVFLYP 439
Cdd:cd12115 103 DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAA--AAFSAEELagVLASTSI--CFDLSVfELFGPLATGGKVVLAD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPLHYRIVPElvydRSCTVLFGT-----STFLGHYARFANpydfyrLRYV-VAGaEKL-QESTKQLWQDKFGLRILEGYG 512
Cdd:cd12115 179 NVLALPDLPA----AAEVTLINTvpsaaAELLRHDALPAS------VRVVnLAG-EPLpRDLVQRLYARLQVERVVNLYG 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 513 VTE------CAPVVsinvPMAAKPGTVGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYLRveKPGVlevpTA 581
Cdd:cd12115 248 PSEdttystVAPVP----PGASGEVSIGRPLANtqayvLDRALQPVP-LGVPGELYIGGAGVARGYLG--RPGL----TA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 E----NVRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGvSPDKVHATAI--KSDASKGEA 655
Cdd:cd12115 317 ErflpDPFGPGAR-LYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEA-ALR-SIPGVREAVVvaIGDAAGERR 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 16130740 656 LVLFTT---DNELTRDKLQQYAReHGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd12115 394 LVAYIVaepGAAGLVEDLRRHLG-TRLPAYMVPSRFVRLDALPLTPNGKID 443
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
355-703 |
2.37e-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: 82.32 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSilanveQIKTIADFTT------NDRFMSALPLfhSFGLTV-GLFT 427
Cdd:cd12114 116 APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRA------ALNTILDINRrfavgpDDRVLALSSL--SFDLSVyDIFG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 428 PLLTGAEVFLyPS------PLH-------YRI-----VPELVyDRSCTVLFGTSTFLGHyarfanpydfyrLRYVVAG-- 487
Cdd:cd12114 188 ALSAGATLVL-PDearrrdPAHwaelierHGVtlwnsVPALL-EMLLDVLEAAQALLPS------------LRLVLLSgd 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 488 --AEKLQESTKQLWQDkfgLRILEGYGVTEcAPVVSI-----NVPMAAKPGTVGRILPG-----MDARLLSVP-GIEegG 554
Cdd:cd12114 254 wiPLDLPARLRALAPD---ARLISLGGATE-ASIWSIyhpidEVPPDWRSIPYGRPLANqryrvLDPRGRDCPdWVP--G 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 555 RLQLKGPNIMNGYLR-VEKpgvlevpTAEN-VRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQl 632
Cdd:cd12114 328 ELWIGGRGVALGYLGdPEL-------TAARfVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEA- 399
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130740 633 ALGVSPDKVHATAIKSDASKGEALVLFTT----DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd12114 400 ALQAHPGVARAVVVVLGDPGGKRLAAFVVpdndGTPIAPDALRAFLAQT-LPAYMIPSRVIALEALPLTANGKVD 473
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
333-607 |
5.59e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 81.85 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 333 LEDLKADVTTADkvwifahlLMPRLAQVkqQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTTND-RFM 410
Cdd:PRK08180 187 FAALLATPPTAA--------VDAAHAAV--GPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLaQTFPFLAEEPpVLV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 411 SALPLFHSFG--LTVGLFtplltgaevfLYPSPLHY----RIVPELVyDR--------SCTVLF----GTSTFLGHY--- 469
Cdd:PRK08180 257 DWLPWNHTFGgnHNLGIV----------LYNGGTLYiddgKPTPGGF-DEtlrnlreiSPTVYFnvpkGWEMLVPALerd 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 470 ----ARFanpydFYRLRYVV-AGA-------EKLQESTKQLWQDKfgLRILEGYGVTECAPVVSINVPMAAKPGTVGRIL 537
Cdd:PRK08180 326 aalrRRF-----FSRLKLLFyAGAalsqdvwDRLDRVAEATCGER--IRMMTGLGMTETAPSATFTTGPLSRAGNIGLPA 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 538 PGMDARLlsVPgieEGGRLQL--KGPNIMNGYLRvekpgvLEVPTAENVRgemERGWYDTGDIVRF-D----EQGFV 607
Cdd:PRK08180 399 PGCEVKL--VP---VGGKLEVrvKGPNVTPGYWR------APELTAEAFD---EEGYYRSGDAVRFvDpadpERGLM 461
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
363-703 |
9.27e-16 |
|
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: 80.29 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRfmSALPLFHSF-GLTVGLFTPLLTGAEVFLYPSP 441
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK--SLVYASFSFdASAWEIFPHLTAGAALHVVPSE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 LHYRIVP--ELVYDRSCTVLFGTSTFLGHYARFANpydfYRLRYVVAGAEKLQESTKQlwqdkfGLRILEGYGVTECAPV 519
Cdd:cd17645 180 RRLDLDAlnDYFNQEGITISFLPTGAAEQFMQLDN----QSLRVLLTGGDKLKKIERK------GYKLVNNYGPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 520 VSI--------NVPMaAKPGTVGRILPGMDARLLSVPGIeeGGRLQLKGPNIMNGYLRVEKPGVLEVPTAENVRGEMerg 591
Cdd:cd17645 250 ATSfeidkpyaNIPI-GKPIDNTRVYILDEALQLQPIGV--AGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGER--- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 592 WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGEALVLF-TTDNELTRDKL 670
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYvTAPEEIPHEEL 403
|
330 340 350
....*....|....*....|....*....|...
gi 16130740 671 QQYAREhGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17645 404 REWLKN-DLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
350-709 |
1.63e-15 |
|
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: 79.71 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 350 AHLLmpRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSIL--ANVEQIKTIAdfTTNDRFMSALPLFHSFGLTVGLFT 427
Cdd:cd05940 68 AHCL--NVSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWrgGAFFAGSGGA--LPSDVLYTCLPLYHSTALIVGWSA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 428 PLLTGAEVFLYPSPLHYRIVPELVYDRsCTVLfgtsTFLGHYARF-----ANPYDF-YRLRYVVAGAekLQESTKQLWQD 501
Cdd:cd05940 144 CLASGATLVIRKKFSASNFWDDIRKYQ-ATIF----QYIGELCRYllnqpPKPTERkHKVRMIFGNG--LRPDIWEEFKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 KFGL-RILEGYGVTECApVVSINVPmaAKPGTVGRILP----GMDARLLSVPgiEEGGRLqLKGPnimNGYLR---VEKP 573
Cdd:cd05940 217 RFGVpRIAEFYAATEGN-SGFINFF--GKPGAIGRNPSllrkVAPLALVKYD--LESGEP-IRDA---EGRCIkvpRGEP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 574 GVL--EV-----------PTAEN---VRGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALG 635
Cdd:cd05940 288 GLLisRInplepfdgytdPAATEkkiLRDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAA-VLG 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 636 VSPDKVHATAI-----KSDASKGEALVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKS 709
Cdd:cd05940 367 AFPGVEEANVYgvqvpGTDGRAGMAAIVLQPNEEFDLSALAAHLEKN-LPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
314-601 |
1.73e-15 |
|
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: 80.17 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 314 DKGKLWHLPEQLTQvRWVYLED-------LKADVTT------------ADKVWIFAHLL-MPRLAQV-----KQQPEEEA 368
Cdd:cd05921 90 DLAKLKHLFELLKP-GLVFAQDaapfaraLAAIFPLgtplvvsrnavaGRGAISFAELAaTPPTAAVdaafaAVGPDTVA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSILANVEQI-KTIADFTTNDRFM-SALPLFHSFGLTVGLFTPLLTGAEVFL---YPSPLH 443
Cdd:cd05921 169 KFLFTSGSTGLPKAVINTQRMLCANQAMLeQTYPFFGEEPPVLvDWLPWNHTFGGNHNFNLVLYNGGTLYIddgKPMPGG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 YRIVPELVYDRSCTVLF----GTSTFLGHY-------ARFanpydFYRLRYVVAGAEKLQEST----KQLWQDKFGLRI- 507
Cdd:cd05921 249 FEETLRNLREISPTVYFnvpaGWEMLVAALekdealrRRF-----FKRLKLMFYAGAGLSQDVwdrlQALAVATVGERIp 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 508 -LEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEggrLQLKGPNIMNGYLRveKPGVlevpTAENVRg 586
Cdd:cd05921 324 mMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSGGKYE---VRVKGPNVTPGYWR--QPEL----TAQAFD- 393
|
330
....*....|....*
gi 16130740 587 emERGWYDTGDIVRF 601
Cdd:cd05921 394 --EEGFYCLGDAAKL 406
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
197-701 |
1.86e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 79.66 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 197 RMAVRPRETLYESLLSAMYRFGAGKKCVEDVNFTpdSYRKLLTKTLFVGRILEKYSV-EGERIGLMLPNAG--ISAAVIF 273
Cdd:PRK13383 28 REASRGGTNPYTLLAVTAARWPGRTAIIDDDGAL--SYRELQRATESLARRLTRDGVaPGRAVGVMCRNGRgfVTAVFAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 274 GAIARRRMPAMMNYTAgvKGLTSAITAAEIKTIFTSRQFLDkgklwhlpeqltQVRWVYLEDLKADVTTADKVWIFAHll 353
Cdd:PRK13383 106 GLLGADVVPISTEFRS--DALAAALRAHHISTVVADNEFAE------------RIAGADDAVAVIDPATAGAEESGGR-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 354 mPRLAQVKQqpeeeaLILFTSGSEGHPKGVVHSHKsILANVEQIKTIADFT---TNDRFMSALPLFHSFG-----LTVGL 425
Cdd:PRK13383 170 -PAVAAPGR------IVLLTSGTTGKPKGVPRAPQ-LRSAVGVWVTILDRTrlrTGSRISVAMPMFHGLGlgmlmLTIAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 426 FTPLLT----GAEVFLYPSPLH----YRIVPelvydrsctVLFGTSTFLGHYARFANPydFYRLRYVVAGAEKLQESTKQ 497
Cdd:PRK13383 242 GGTVLThrhfDAEAALAQASLHradaFTAVP---------VVLARILELPPRVRARNP--LPQLRVVMSSGDRLDPTLGQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 498 LWQDKFGLRILEGYGVTECApVVSINVPMAAK--PGTVGRILPGMDARLLSVPGIEEG----GRLQLKGPNIMNGYLRVE 571
Cdd:PRK13383 311 RFMDTYGDILYNGYGSTEVG-IGALATPADLRdaPETVGKPVAGCPVRILDRNNRPVGprvtGRIFVGGELAGTRYTDGG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 572 KPGVLEvptaenvrgemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIK-SDA 650
Cdd:PRK13383 390 GKAVVD-------------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVEN-ALAAHPAVADNAVIGvPDE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16130740 651 SKGEALVLFTT---DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK13383 456 RFGHRLAAFVVlhpGSGVDAAQLRDYLKDR-VSRFEQPRDINIVSSIPRNPTGK 508
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
254-701 |
2.16e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 79.80 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 254 EGERIGLMLPNagiSAAVIFGAIARRRMPA---MMNYTAGVKGLTSAITAAEIKTIFTSRQF---LDKGkLWHLPEQLTQ 327
Cdd:PRK13382 92 EPRVVGIMCRN---HRGFVEALLAANRIGAdilLLNTSFAGPALAEVVTREGVDTVIYDEEFsatVDRA-LADCPQATRI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 328 VRWVyleDLKADVTTAdkVWIFAHLLmprlAQVKQQPEEEALILFTSGSEGHPKGVVHSHKsilANVEQIKTIADFT--- 404
Cdd:PRK13382 168 VAWT---DEDHDLTVE--VLIAAHAG----QRPEPTGRKGRVILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpwr 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 405 TNDRFMSALPLFHSFGLTVGLFTPLLTGAEVflypspLHYRIVPE----LVYDRSCTVLFGTSTFLGHY----ARFANPY 476
Cdd:PRK13382 236 AEEPTVIVAPMFHAWGFSQLVLAASLACTIV------TRRRFDPEatldLIDRHRATGLAVVPVMFDRImdlpAEVRNRY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 477 DFYRLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEcAPVVSINVP--MAAKPGTVGRILPGMDARLLSVPGIE--- 551
Cdd:PRK13382 310 SGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE-AGMIATATPadLRAAPDTAGRPAEGTEIRILDQDFREvpt 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 552 -EGGRLQLKGPNIMNGYlrveKPGVLEvptaenvrgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
Cdd:PRK13382 389 gEVGTIFVRNDTQFDGY----TSGSTK---------DFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVE 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130740 631 QlALGVSPDKVHATAIKSDASK-GEAL---VLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK13382 456 K-TLATHPDVAEAAVIGVDDEQyGQRLaafVVLKPGASATPETLKQHVRDN-LANYKVPRDIVVLDELPRGATGK 528
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
363-703 |
5.04e-15 |
|
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: 78.06 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLYP 439
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQ----FASPSFDASvweLLMALLAGATLVLAP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SplhYRIVP-----ELVYDRSCTVLFGTSTFLghyaRFANPYDFYRLRYVVAGAEKLQESTKQLWQDkfGLRILEGYGVT 514
Cdd:cd17652 167 A---EELLPgeplaDLLREHRITHVTLPPAAL----AALPPDDLPDLRTLVVAGEACPAELVDRWAP--GRRMINAYGPT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECAPVVSINVPMAAKPG-TVGRILPG-----MDARLLSVPgIEEGGRLQLKGPNIMNGYLRveKPGVlevpTAEN----- 583
Cdd:cd17652 238 ETTVCATMAGPLPGGGVpPIGRPVPGtrvyvLDARLRPVP-PGVPGELYIAGAGLARGYLN--RPGL----TAERfvadp 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 VRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGEALVLFTT- 661
Cdd:cd17652 311 FGAPGSR-MYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA-ALTEHPGVAEAVVVvRDDRPGDKRLVAYVVp 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16130740 662 --DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17652 389 apGAAPTAAELRAHLAER-LPGYMVPAAFVVLDALPLTPNGKLD 431
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
363-605 |
5.80e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.40 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFhsfgltvGLFTPLLTGAEvflypspl 442
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF-------ALFGPALGMTS-------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 hyrIVPEL----------------VYDRSCTVLFGTSTF---LGHYARfANPYDFYRLRYV-VAGA----EKLQESTKQL 498
Cdd:PRK09274 237 ---VIPDMdptrpatvdpaklfaaIERYGVTNLFGSPALlerLGRYGE-ANGIKLPSLRRViSAGApvpiAVIERFRAML 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 499 WQDkfgLRILEGYGVTECAPVVSI--------NVPMAAK-PGT-VGRILPGMDARLLSV-----PGIEEGGRLQ------ 557
Cdd:PRK09274 313 PPD---AEILTPYGATEALPISSIesreilfaTRAATDNgAGIcVGRPVDGVEVRIIAIsdapiPEWDDALRLAtgeige 389
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16130740 558 --LKGPNIMNGYLRvekpgvlevPTAENVRGEMERG----WYDTGDIVRFDEQG 605
Cdd:PRK09274 390 ivVAGPMVTRSYYN---------RPEATRLAKIPDGqgdvWHRMGDLGYLDAQG 434
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
362-703 |
6.09e-15 |
|
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: 78.10 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPS 440
Cdd:cd12116 123 VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTY--AFDISLlELLLPLLAGARVVIAPR 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 PLHY--RIVPELVYDRSCTVLFGTSTFLgHYARFANPYDFYRLRYVVAG-------AEKLQESTKQLWQdkfglrileGY 511
Cdd:cd12116 201 ETQRdpEALARLIEAHSITVMQATPATW-RMLLDAGWQGRAGLTALCGGealppdlAARLLSRVGSLWN---------LY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 512 GVTE------CAPVVSinvpmAAKPGTVGRILPG-----MDARLLSVPgieEG--GRLQLKGPNIMNGYLRveKPGVlev 578
Cdd:cd12116 271 GPTEttiwstAARVTA-----AAGPIPIGRPLANtqvyvLDAALRPVP---PGvpGELYIGGDGVAQGYLG--RPAL--- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 579 pTAENVR-----GEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE-QLALGVSPDKVHATAIKSDASK 652
Cdd:cd12116 338 -TAERFVpdpfaGPGSR-LYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEaALAAHPGVAQAAVVVREDGGDR 415
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 653 G-EALVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd12116 416 RlVAYVVLKAGAAPDAAALRAHLRAT-LPAYMVPSAFVRLDALPLTANGKLD 466
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
364-701 |
8.01e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 77.62 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSI-LANVEQIKTIAdFTTNDRFMSALPLFHsfgltVGLFTplLTGAEVFLYPSPL 442
Cdd:PRK06145 148 PTDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIALG-LTASERLLVVGPLYH-----VGAFD--LPGIAVLWVGGTL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 443 --HYRIVPELVY-----DRSCTVLFG---TSTFLGHYARFAnpYDFYRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGY 511
Cdd:PRK06145 220 riHREFDPEAVLaaierHRLTCAWMApvmLSRVLTVPDRDR--FDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYIDAY 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 512 GVTEcapVVSINVPMAA-----KPGTVGRILPGMDARLLSVPG----IEEGGRLQLKGPNIMNGYLRV-EKpgvlevpTA 581
Cdd:PRK06145 298 GLTE---TCSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGrwlpPNMKGEICMRGPKVTKGYWKDpEK-------TA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKVHATAIKSDASKGE---ALVL 658
Cdd:PRK06145 368 EAFYG----DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGEritAVVV 443
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 16130740 659 FTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK06145 444 LNPGATLTLEALDRHCRQR-LASFKVPRQLKVRDELPRNPSGK 485
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
368-719 |
1.65e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH--- 443
Cdd:PRK05691 1276 AYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPI--SFDVSVwECFWPLITGCRLVLAGPGEHrdp 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 YRIVpELVYDRSCTVLFGTSTFLGHYARFANPYDFYRLRYVVAGAEKLQ-ESTKQLWQDKFGLRILEGYGVTECApvvsI 522
Cdd:PRK05691 1354 QRIA-ELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPaELRNRVLQRLPQVQLHNRYGPTETA----I 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 523 NVP---MAAKPGT---VGRILPGMDARLLSV------PGIeeGGRLQLKGPNIMNGYLRveKPGVlevpTAE----NVRG 586
Cdd:PRK05691 1429 NVThwqCQAEDGErspIGRPLGNVLCRVLDAelnllpPGV--AGELCIGGAGLARGYLG--RPAL----TAErfvpDPLG 1500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 587 EMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASKGEALVLFTT----D 662
Cdd:PRK05691 1501 EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA-QPGVAQAAVLVREGAAGAQLVGYYTgeagQ 1579
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 663 NELTRDKLQQYAREhgVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEAEQHDE 719
Cdd:PRK05691 1580 EAEAERLKAALAAE--LPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVE 1634
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
362-701 |
2.35e-14 |
|
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: 76.18 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEE--ALIL-FTSGSEGHPKGVVHSHKSilANVEQIKTIADFT--TNDRFMSALPLFHSFGLTVGLFTPLLTGAEVF 436
Cdd:cd12118 127 IPPADEwdPIALnYTSGTTGRPKGVVYHHRG--AYLNALANILEWEmkQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVC 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 437 L--YPSPLHYRivpeLVYDRSCTVLFGTSTFLGHYA----RFANPYDfYRLRYVVAGA---EKLQESTKQLwqdkfGLRI 507
Cdd:cd12118 205 LrkVDAKAIYD----LIEKHKVTHFCGAPTVLNMLAnappSDARPLP-HRVHVMTAGApppAAVLAKMEEL-----GFDV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 508 LEGYGVTECAPVVSINV--------P------MAAKPGTVGRILPGMDAR----LLSVPGI-EEGGRLQLKGPNIMNGYL 568
Cdd:cd12118 275 THVYGLTETYGPATVCAwkpewdelPteerarLKARQGVRYVGLEEVDVLdpetMKPVPRDgKTIGEIVFRGNIVMKGYL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 569 RVEKPgvlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPdKVHATAI-- 646
Cdd:cd12118 355 KNPEA------TAEAFRG----GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG-VLYKHP-AVLEAAVva 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 647 KSDASKGEALVLFTT---DNELTRDKLQQYAREHgVPELAVPRDIRYLkQMPLLGSGK 701
Cdd:cd12118 423 RPDEKWGEVPCAFVElkeGAKVTEEEIIAFCREH-LAGFMVPKTVVFG-ELPKTSTGK 478
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
363-703 |
5.09e-14 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 76.24 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSP 441
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPC--SFDVSVwEFFWPFIAGAKLVMAEPE 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 LH------------YRI-----VPELVydrsctvlfgtSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFG 504
Cdd:PRK10252 674 AHrdplamqqffaeYGVttthfVPSML-----------AAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTG 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 505 LRILEGYGVTECAPVVS---------INVPMAAKP------GTVGRILpgmDARLLSVP-GIeeGGRLQLKGPNIMNGYL 568
Cdd:PRK10252 743 APLHNLYGPTEAAVDVSwypafgeelAAVRGSSVPigypvwNTGLRIL---DARMRPVPpGV--AGDLYLTGIQLAQGYL 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 569 rvEKPGVlevpTAE----NVRGEMERgWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHAT 644
Cdd:PRK10252 818 --GRPDL----TASrfiaDPFAPGER-MYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDR-AMQALPDVEQAV 889
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 645 A-----IKSDASKGEA--LVLFTTDNE---LTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK10252 890 ThacviNQAAATGGDArqLVGYLVSQSglpLDTSALQAQLRE-RLPPHMVPVVLLQLDQLPLSANGKLD 957
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
369-701 |
5.15e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 75.45 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSIL----ANVEQIKTIADfttnDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhy 444
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHGRLAfagrALTERFGLTRD----DVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAK---- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 rivpelvydrsctvlFGTSTFLGHYARFANPYDFY---RLRYVVAGAEKLQESTKQL---------------WQDKFGLR 506
Cdd:PRK13388 226 ---------------FSASGFLDDVRRYGATYFNYvgkPLAYILATPERPDDADNPLrvafgneasprdiaeFSRRFGCQ 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECApvVSINVPMAAKPGTVGRILPGM------DARLLSVPGIEEGGRL-----------QLKGPNIMNGYLR 569
Cdd:PRK13388 291 VEDGYGSSEGA--VIVVREPGTPPGSIGRGAPGVaiynpeTLTECAVARFDAHGALlnadeaigelvNTAGAGFFEGYYN 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 570 veKPGVlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALgvSPDKVHATAIKS- 648
Cdd:PRK13388 369 --NPEA----TAERMRH----GMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILL--RHPAINRVAVYAv 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 649 -DASKGE---ALVLFTTDNELTRDKLQQYAreHGVPEL---AVPRDIRYLKQMPLLGSGK 701
Cdd:PRK13388 437 pDERVGDqvmAALVLRDGATFDPDAFAAFL--AAQPDLgtkAWPRYVRIAADLPSTATNK 494
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
233-701 |
5.41e-14 |
|
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: 75.29 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVE-GERIGLMLPN-----------AGISA--AVIFGAIArrrmpammnytagVKGLTSAI 298
Cdd:cd05966 86 TYRELLREVCRFANVLKSLGVKkGDRVAIYMPMipelviamlacARIGAvhSVVFAGFS-------------AESLADRI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 299 TAAEIKTIFTSRQFLDKGKLWHLP-------EQLTQVRWVY-LEDLKADVTTADKVWIFAHLLMprlaqvKQQPEE---E 367
Cdd:cd05966 153 NDAQCKLVITADGGYRGGKVIPLKeivdealEKCPSVEKVLvVKRTGGEVPMTEGRDLWWHDLM------AKQSPEcepE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 AL-------ILFTSGSEGHPKGVVHSHKSILANVEQ-IKTIADFTTNDRFMSALPLF----HSFGLtvglFTPLLTGAEV 435
Cdd:cd05966 227 WMdsedplfILYTSGSTGKPKGVVHTTGGYLLYAATtFKYVFDYHPDDIYWCTADIGwitgHSYIV----YGPLANGATT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLY---PSPLHYRIVPELVYDRSCTVLFGTSTFLGHYARFAN----PYDFYRLR-----------------YVVAGAEKL 491
Cdd:cd05966 303 VMFegtPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDewvkKHDLSSLRvlgsvgepinpeawmwyYEVIGKERC 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 492 Q-ESTkqLWQDKFGlrileGYGVTeCAPVVsinVPMaaKPGTVGRILPGMDARLLSvpgiEEGGrlQLKGPNimNGYLRV 570
Cdd:cd05966 383 PiVDT--WWQTETG-----GIMIT-PLPGA---TPL--KPGSATRPFFGIEPAILD----EEGN--EVEGEV--EGYLVI 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 571 EK--PGVLEvptaeNVRGEMER----------GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALgVSP 638
Cdd:cd05966 442 KRpwPGMAR-----TIYGDHERyedtyfskfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVES-AL-VAH 514
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130740 639 DKVHATAI--KSDASKGEALVLFTT--DNELTRDKLQQYAREHgVPE----LAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05966 515 PAVAEAAVvgRPHDIKGEAIYAFVTlkDGEEPSDELRKELRKH-VRKeigpIATPDKIQFVPGLPKTRSGK 584
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
363-703 |
1.03e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSalplFHSFGL---TVGLFTPLLTGAEVFLYP 439
Cdd:PRK05691 2331 LPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELH----FYSINFdaaSERLLVPLLCGARVVLRA 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 S-PLHYRIVPELVYDRSCTVLFGTSTFLGHYARF-ANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLRIL-EGYGVTEC 516
Cdd:PRK05691 2407 QgQWGAEEICQLIREQQVSILGFTPSYGSQLAQWlAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTET 2486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 A--PVVSInVPMAAKPGT----VGRILPG-----MDARLLSVPgieEG--GRLQLKGPNIMNGYLRveKPGVlevpTAEN 583
Cdd:PRK05691 2487 VvmPLACL-APEQLEEGAasvpIGRVVGArvayiLDADLALVP---QGatGELYVGGAGLAQGYHD--RPGL----TAER 2556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 V--------RGEMergwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHATAIKSDASKGEA 655
Cdd:PRK05691 2557 FvadpfaadGGRL----YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE-HPAVREAVVLALDTPSGKQ 2631
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 656 LVLFTTDNELT---------RDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK05691 2632 LAGYLVSAVAGqddeaqaalREALKAHLKQQ-LPDYMVPAHLILLDSLPLTANGKLD 2687
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
362-701 |
1.30e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEEALIlFTSGSEGHPKGVVHSHKSI--LANVEQIK-TIADFTTNDRFMSALPLFHS----FGLTVGLFtplltGAE 434
Cdd:PRK12406 150 PVPQPQSMI-YTSGTTGHPKGVRRAAPTPeqAAAAEQMRaLIYGLKPGIRALLTGPLYHSapnaYGLRAGRL-----GGV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 435 VFLYPsplhyRIVPE----LVYDRSCTVLFGTST----FLGHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGLR 506
Cdd:PRK12406 224 LVLQP-----RFDPEellqLIERHRITHMHMVPTmfirLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 507 ILEGYGVTECAPVVSINVPMA-AKPGTVGRILPGMDARLLSvpgiEEGGRLQLKGPnimnGYLRVEKPGVLEVpTAEN-- 583
Cdd:PRK12406 299 IYEYYGSTESGAVTFATSEDAlSHPGTVGKAAPGAELRFVD----EDGRPLPQGEI----GEIYSRIAGNPDF-TYHNkp 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 -VRGEMER-GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSpdKVHATAI--KSDASKGEALVLF 659
Cdd:PRK12406 370 eKRAEIDRgGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP--GVHDCAVfgIPDAEFGEALMAV 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16130740 660 TTDN---ELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK12406 448 VEPQpgaTLDEADIRAQLKAR-LAGYKVPKHIEIMAELPREDSGK 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
369-677 |
1.58e-13 |
|
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: 72.33 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLypsplhYRIVP 448
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV------RRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 449 E----LVYDRSCTVLFGTSTFLGHYARF--ANPYDFYRLRYVVAGAEKLQEST--KQLWQDKFGlrileGYGVTECAPVV 520
Cdd:cd17636 78 EevleLIEAERCTHAFLLPPTIDQIVELnaDGLYDLSSLRSSPAAPEWNDMATvdTSPWGRKPG-----GYGQTEVMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 521 SINVPMAAKPGTVGRILPGMDARLLSVPGIE----EGGRLQLKGPNIMNGYLRveKPGVlevpTAENVRGemerGWYDTG 596
Cdd:cd17636 153 TFAALGGGAIGGAGRPSPLVQVRILDEDGREvpdgEVGEIVARGPTVMAGYWN--RPEV----NARRTRG----GWHHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 597 DIVRFDEQGFVQIQGRAKRFAKIAGEMV----------SLEMVEQLA-LGVsPDKVHATAIKsdaskgeALVLFTTDNEL 665
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIypaeverclrQHPAVADAAvIGV-PDPRWAQSVK-------AIVVLKPGASV 294
|
330
....*....|..
gi 16130740 666 TRDKLQQYAREH 677
Cdd:cd17636 295 TEAELIEHCRAR 306
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
363-632 |
4.21e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 72.54 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 363 QPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD-----FTTNDRFMSALPLFHSF-----------GLTVG-- 424
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHILdrmieeyffrkGASVGyy 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 425 -------------LFTPLLTGA-EVF--LYP---------SPLHYRIVPELvYDRSCTVLFgtstfLGHYARFANPY-DF 478
Cdd:PLN02430 298 hgdlnalrddlmeLKPTLLAGVpRVFerIHEgiqkalqelNPRRRLIFNAL-YKYKLAWMN-----RGYSHKKASPMaDF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 479 Y-----------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVP--MAAKpGTVGRILPGMDARLL 545
Cdd:PLN02430 372 LafrkvkaklggRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPdeMCML-GTVGAPAVYNELRLE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 546 SVP-------GIEEGGRLQLKGPNIMNGYLRvekpgvlevpTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAK 618
Cdd:PLN02430 451 EVPemgydplGEPPRGEICVRGKCLFSGYYK----------NPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIK 520
|
330
....*....|....*
gi 16130740 619 IA-GEMVSLEMVEQL 632
Cdd:PLN02430 521 LSqGEYVALEYLENV 535
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
369-675 |
1.18e-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: 70.67 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSIlaNVEQIKTI-------ADFTTNdrFMSALPLFHSFGltvGLFTPLLTGAEVFLYPSP 441
Cdd:cd05974 89 LLYFTSGTTSKPKLVEHTHRSY--PVGHLSTMywiglkpGDVHWN--ISSPGWAKHAWS---CFFAPWNAGATVFLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 -LHYRIVPELVYDRSCTVLFGTSTFL-----GHYARFANPydfyrLRYVVAGAEKLQ----ESTKQLWqdkfGLRILEGY 511
Cdd:cd05974 162 rFDAKRVLAALVRYGVTTLCAPPTVWrmliqQDLASFDVK-----LREVVGAGEPLNpeviEQVRRAW----GLTIRDGY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 512 GVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE-EGGRLQL-----KGPNIMNGYLRVEkpgvlevptaENVR 585
Cdd:cd05974 233 GQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPaTEGEVALdlgdtRPVGLMKGYAGDP----------DKTA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 586 GEMERGWYDTGDIVRFDEQGFVQIQGRAK--------RFAKIAGEMVSLE--MVEQLALGVSPDKVHATAIK-------- 647
Cdd:cd05974 303 HAMRGGYYRTGDIAMRDEDGYLTYVGRADdvfkssdyRISPFELESVLIEhpAVAEAAVVPSPDPVRLSVPKafivlrag 382
|
330 340
....*....|....*....|....*...
gi 16130740 648 SDASKGEALVLFttdnELTRDKLQQYAR 675
Cdd:cd05974 383 YEPSPETALEIF----RFSRERLAPYKR 406
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
372-701 |
1.25e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 70.82 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 372 FTSGSEGHPKGVVHSHKSilANVEQIKTIA--DFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFL--YPSPLHYRIV 447
Cdd:PLN03102 193 YTSGTTADPKGVVISHRG--AYLSTLSAIIgwEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMrhVTAPEIYKNI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 pEL--VYDRSCT------VLFGTSTFLGHYArfaNPydfyrLRYVVAGAEKLQESTKQLwqDKFGLRILEGYGVTEC-AP 518
Cdd:PLN03102 271 -EMhnVTHMCCVptvfniLLKGNSLDLSPRS---GP-----VHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTEAtGP 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 519 VV-------------SINVPMAAKPGTVGRILPGMDAR----LLSVPgiEEG---GRLQLKGPNIMNGYLRVEKPgvlev 578
Cdd:PLN03102 340 VLfcewqdewnrlpeNQQMELKARQGVSILGLADVDVKnketQESVP--RDGktmGEIVIKGSSIMKGYLKNPKA----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 579 pTAEnvrgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPdKVHATAIKS--DASKGEAL 656
Cdd:PLN03102 413 -TSE----AFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENV-LYKYP-KVLETAVVAmpHPTWGETP 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 657 VLFT------TDNELTRDKLQ-------QYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PLN03102 486 CAFVvlekgeTTKEDRVDKLVtrerdliEYCREN-LPHFMCPRKVVFLQELPKNGNGK 542
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
321-613 |
1.52e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 70.29 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 321 LPEQLTQVrwvYLEDLKAD---VTTADKVWIFAHLLMPRLA----QVKQQPEEEALILFTSGSEGHPKGVVHSHKSILAN 393
Cdd:PRK09029 87 LPQPLLEE---LLPSLTLDfalVLEGENTFSALTSLHLQLVegahAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLAS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 394 VEQIKTIADFTTNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFLYPS-PL--------HYRIVPE-----LVYDRSCTVL 459
Cdd:PRK09029 164 AEGVLSLMPFTAQDSWLLSLPLFHVSGQGI-VWRWLYAGATLVVRDKqPLeqalagctHASLVPTqlwrlLDNRSEPLSL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 460 fgTSTFLGhyarfanpydfyrlryvvaGAEKLQESTKQLWQdkFGLRILEGYGVTECAPVVsinvpmAAKP----GTVGR 535
Cdd:PRK09029 243 --KAVLLG-------------------GAAIPVELTEQAEQ--QGIRCWCGYGLTEMASTV------CAKRadglAGVGS 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130740 536 ILPGMDARLlsvpgieEGGRLQLKGPNIMNGYLRVEKPgvleVPTAEnvrgemERGWYDTGDIVRFDeQGFVQIQGRA 613
Cdd:PRK09029 294 PLPGREVKL-------VDGEIWLRGASLALGYWRQGQL----VPLVN------DEGWFATRDRGEWQ-NGELTILGRL 353
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
364-714 |
1.98e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 70.40 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHK----SILANVEqiktIADFTTNDRFMSALPLFHSFGLT----VGLFtplLTGAEV 435
Cdd:PRK10946 181 ADEVAFFQLSGGSTGTPKLIPRTHNdyyySVRRSVE----ICGFTPQTRYLCALPAAHNYPMSspgaLGVF---LAGGTV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLY--PSPL-------HYRI-----VPELVydrsctvlfgtSTFLGHYARFANPYDFYRLRYVVAGAEKLQESTK----- 496
Cdd:PRK10946 254 VLApdPSATlcfplieKHQVnvtalVPPAV-----------SLWLQAIAEGGSRAQLASLKLLQVGGARLSETLArripa 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 497 ----QLwQDKFGLRilEG---YGVTECAPVVSINvpmaakpgTVGR-ILPGMDARLLSVPGIE----EGGRLQLKGPNIM 564
Cdd:PRK10946 323 elgcQL-QQVFGMA--EGlvnYTRLDDSDERIFT--------TQGRpMSPDDEVWVADADGNPlpqgEVGRLMTRGPYTF 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 565 NGYLRveKPgvlevptAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGvSPDKVHAt 644
Cdd:PRK10946 392 RGYYK--SP-------QHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLR-HPAVIHA- 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130740 645 AIKS--DASKGEALVLF-TTDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGKPDFVTLKSWVDEA 714
Cdd:PRK10946 461 ALVSmeDELMGEKSCAFlVVKEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
364-601 |
2.89e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 70.07 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR---FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:PRK12582 219 PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNGLLWGGGTLYIDDG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 plhyRIVPEL-------VYDRSCTVLFGTSTflgHYARFANPYD---------FYRLRYVVAGAEKLQESTKQLWQD--- 501
Cdd:PRK12582 299 ----KPLPGMfeetirnLREISPTVYGNVPA---GYAMLAEAMEkddalrrsfFKNLRLMAYGGATLSDDLYERMQAlav 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 -KFGLRIL--EGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIEEggrLQLKGPNIMNGYL-RVEKpgvle 577
Cdd:PRK12582 372 rTTGHRIPfyTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAPVGDKYE---VRVKGPNVTPGYHkDPEL----- 443
|
250 260
....*....|....*....|....
gi 16130740 578 vpTAENVRgemERGWYDTGDIVRF 601
Cdd:PRK12582 444 --TAAAFD---EEGFYRLGDAARF 462
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
370-630 |
3.22e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 69.87 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGVVHSHKSILANV---EQIKTIAD--FTTNDRFMSALPLFHSFGLTVGLFTpLLTGAEVFLYPSPLHY 444
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVlstDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIRY 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RI-------------VPElVYDRSCTVLFGTSTFLGHYAR--FANPYDFY------------------------------ 479
Cdd:PLN02861 304 LMedvqalkptifcgVPR-VYDRIYTGIMQKISSGGMLRKklFDFAYNYKlgnlrkglkqeeasprldrlvfdkikeglg 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 -RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGMDARLLSVPgiEEG---- 553
Cdd:PLN02861 383 gRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLESVP--EMGydal 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 554 -----GRLQLKGPNIMNGYLRveKPGVLEVPTAEnvrgemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLE 627
Cdd:PLN02861 461 sdvprGEICLRGNTLFSGYHK--RQDLTEEVLID--------GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVE 530
|
...
gi 16130740 628 MVE 630
Cdd:PLN02861 531 NLE 533
|
|
| LPLAT_ACT14924-like |
cd07986 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
11-156 |
4.05e-12 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.
Pssm-ID: 153248 [Multi-domain] Cd Length: 210 Bit Score: 66.12 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 11 RVLYRVRVTGDTQALKGERVLITPNH-VSFIDGILLG-LFLPVRPVFAVYTSiSQQWYMRWLKSFidFVPLDPTQPMA-- 86
Cdd:cd07986 5 NVQLEVDVSGLENIPKDGPVVIVANHpFGILDGLILAdLLGSVRPDVRILAN-QLLSKIPELRDL--FIPVDPLEGRAal 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 87 ------IKHLVRLVEQGRPVVIFPEGRITT-TGSLMKIYD-----GAGFVAAKSGATVIPVRIEGAELTHFSRLkGLVKR 154
Cdd:cd07986 82 aknresLREALRHLKNGGALIIFPAGRVSTaSPPFGRVSDrpwnpFVARLARKAKAPVVPVYFSGRNSRLFYLA-GLIHP 160
|
..
gi 16130740 155 RL 156
Cdd:cd07986 161 TL 162
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
259-695 |
4.42e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 68.94 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 259 GLMLPNAGISAAVIFGAIARRRMPAmmnytagvkgLTSAITAAEIKTIFTSRQFLDKgklwhLPEQLTQVRWVyledlka 338
Cdd:PRK07867 68 SLLLGAAALSGIVPVGLNPTRRGAA----------LARDIAHADCQLVLTESAHAEL-----LDGLDPGVRVI------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 339 DVTTADKVWIFAHLLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHS 418
Cdd:PRK07867 126 NVDSPAWADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 419 FGLTVGLFTPLLTGAEVFLYPSplhyrivpelvydrsctvlFGTSTFLGHYARFANPYDFY---RLRYVVAGAEKLQEST 495
Cdd:PRK07867 206 NAVMAGWAVALAAGASIALRRK-------------------FSASGFLPDVRRYGATYANYvgkPLSYVLATPERPDDAD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 496 KQL---------------WQDKFGLRILEGYGVTECApvVSINVPMAAKPGTVGRILPGM-----DARLLSVPG-IEEGG 554
Cdd:PRK07867 267 NPLrivygnegapgdiarFARRFGCVVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGVaivdpDTGTECPPAeDADGR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 555 RLQ----------LKGPNIMNGYLRVEKpgvlevPTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMV 624
Cdd:PRK07867 345 LLNadeaigelvnTAGPGGFEGYYNDPE------ADAERMRG----GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 625 SLEMVEQLALGVsPDkVHATAIKS--DASKGE----ALVLfTTDNELTRDKLQQYAREHgvPEL---AVPRDIRYLKQMP 695
Cdd:PRK07867 415 GTAPIERILLRY-PD-ATEVAVYAvpDPVVGDqvmaALVL-APGAKFDPDAFAEFLAAQ--PDLgpkQWPSYVRVCAELP 489
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
362-632 |
6.73e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 68.89 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTI-----ADFTTNDRFMSALPLFHSF-----------GLTVGL 425
Cdd:PLN02614 220 KKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlksanAALTVKDVYLSYLPLAHIFdrvieecfiqhGAAIGF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 426 F---TPLLTGAEVFLYPSPlhYRIVPElVYDRSCTVLFGTSTFLGHYARF----ANPYDFYRL----------------- 481
Cdd:PLN02614 300 WrgdVKLLIEDLGELKPTI--FCAVPR-VLDRVYSGLQKKLSDGGFLKKFvfdsAFSYKFGNMkkgqshveasplcdklv 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 482 ------------RYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTE-CAPVVSINVPMAAKPGTVGRILPGMDARLLSVP 548
Cdd:PLN02614 377 fnkvkqglggnvRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDMLGTVGPPVPNVDIRLESVP 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 549 GIE-------EGGRLQLKGPNIMNGYLRVEkpgvlevptaENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA- 620
Cdd:PLN02614 457 EMEydalastPRGEICIRGKTLFSGYYKRE----------DLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSq 526
|
330
....*....|..
gi 16130740 621 GEMVSLEMVEQL 632
Cdd:PLN02614 527 GEYVAVENIENI 538
|
|
| LPLAT |
cd06551 |
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ... |
3-167 |
8.14e-12 |
|
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).
Pssm-ID: 153244 [Multi-domain] Cd Length: 187 Bit Score: 64.74 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 3 FSFFRNLCRVLYRVRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQ-----WYMRWLKSF-IDF 76
Cdd:cd06551 1 FRYLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGLRRDVYGLMDEElleryPFFTRLGAFsVDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 77 V-PLDPTQPM-AIKHLvrLVEQGRPVVIFPEGRITTTGS-LMKIYDGAGFVAAKSGATVIPVriegaeltHFSRLKGLVK 153
Cdd:cd06551 81 DsPRSAAKSLkYVARL--LSKPGSVVWIFPEGTRTRRDKrPLQFKPGVAHLAEKAGVPIVPV--------ALRYTFELFE 150
|
170
....*....|....
gi 16130740 154 RrlFPQITLHILPP 167
Cdd:cd06551 151 Q--FPEIFVRIGPP 162
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
372-613 |
1.68e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 67.37 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 372 FTSGSEGHPKGVVHSHKS---ILANveqikTIADF----TTNDRFMSALPLFHSFGltVGLFTPLLTGAEVFLYPSPlhy 444
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQmafVITN-----HLADLmpgtTEQDASLVVAPLSHGAG--IHQLCQVARGAATVLLPSE--- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RIVPE----LVYDRSCTVLFGTSTFLG----HYArfANPYDFYRLRYVV-AGAEKLQESTKQLWQdKFGLRILEGYGVTE 515
Cdd:PRK07470 240 RFDPAevwaLVERHRVTNLFTVPTILKmlveHPA--VDRYDHSSLRYVIyAGAPMYRADQKRALA-KLGKVLVQYFGLGE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 516 CAPVVSINVPM--------AAKPGTVGRILPGM-----DARLLSVPGIEEGgRLQLKGPNIMNGYLRVEKPgvlevpTAE 582
Cdd:PRK07470 317 VTGNITVLPPAlhdaedgpDARIGTCGFERTGMevqiqDDEGRELPPGETG-EICVIGPAVFAGYYNNPEA------NAK 389
|
250 260 270
....*....|....*....|....*....|.
gi 16130740 583 NVRGemerGWYDTGDIVRFDEQGFVQIQGRA 613
Cdd:PRK07470 390 AFRD----GWFRTGDLGHLDARGFLYITGRA 416
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
364-708 |
1.77e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 67.07 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLH 443
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 444 YRIVPELVYDRSCTVLfgtstFLGHYARF-----ANPYD-FYRLRyvVAGAEKLQESTKQLWQDKFGLRIL-EGYGVTEc 516
Cdd:cd05937 166 SQFWKDVRDSGATIIQ-----YVGELCRYllstpPSPYDrDHKVR--VAWGNGLRPDIWERFRERFNVPEIgEFYAATE- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINvpMAAKPGTVGRI-LPGMDARLL---------------------------SVPGIEEG---GRLQLKGPNIMN 565
Cdd:cd05937 238 GVFALTN--HNVGDFGAGAIgHHGLIRRWKfenqvvlvkmdpetddpirdpktgfcvRAPVGEPGemlGRVPFKNREAFQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 566 GYLRVEKpgvleVPTAENVRGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDkVHA 643
Cdd:cd05937 316 GYLHNED-----ATESKLVRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADV-LGAHPD-IAE 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130740 644 TAI------KSDASKGEALVLFTTDNELTRDKLQQYAREH---GVPELAVPRDIRYLKQMPLLGSGKPDFVTLK 708
Cdd:cd05937 389 ANVygvkvpGHDGRAGCAAITLEESSAVPTEFTKSLLASLarkNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
368-703 |
2.43e-11 |
|
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: 66.73 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSalplFHSFGLTVG---LFTPLLTGAEVFLYPSPLHy 444
Cdd:cd17656 131 LYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQ----FATCSFDVCyqeIFSTLLSGGTLYIIREETK- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 445 RIVPEL---VYDRSCTVLFGTSTFLGHYA---RFANPYdFYRLRYVVAGAEKLQEStkQLWQDKF---GLRILEGYGVTE 515
Cdd:cd17656 206 RDVEQLfdlVKRHNIEVVFLPVAFLKFIFserEFINRF-PTCVKHIITAGEQLVIT--NEFKEMLhehNVHLHNHYGPSE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 516 CAPVVSINV---------PMAAKPGTVGRILPGMDARLLSVPGIEegGRLQLKGPNIMNGYLRVEK---PGVLEVPTAEN 583
Cdd:cd17656 283 THVVTTYTInpeaeipelPPIGKPISNTWIYILDQEQQLQPQGIV--GELYISGASVARGYLNRQEltaEKFFPDPFDPN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 VRgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqLALGVSPDKVHATAIKSDASKGEALV--LFTT 661
Cdd:cd17656 361 ER------MYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIE-AQLLNHPGVSEAVVLDKADDKGEKYLcaYFVM 433
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16130740 662 DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:cd17656 434 EQELNISQLREYLAKQ-LPEYMIPSFFVPLDQLPLTPNGKVD 474
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
369-709 |
4.14e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.06 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 369 LILFTSGSEGHPKGVVHSHKSI---------LANVEQIKT---IADFTTND---RFMSALPLFHSFGLTvGLFTPLLTGA 433
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQEDIfrvllggrdFATGEPIEDeeeLAKRAAAGpgmRRFPAPPLMHGAGQW-AAFAALFSGQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 434 EVFLYPSP-LHYRIVPELVYDRSCTVLFgtstFLGH-YAR-------FANPYDFYRLRYVVAGAEKLQESTKQLWQDKF- 503
Cdd:PRK07798 246 TVVLLPDVrFDADEVWRTIEREKVNVIT----IVGDaMARplldaleARGPYDLSSLFAIASGGALFSPSVKEALLELLp 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 504 GLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS------VPGIEEGGRLQLKGPnIMNGYLRVEKPGVLE 577
Cdd:PRK07798 322 NVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGPRTVVLDedgnpvEPGSGEIGWIARRGH-IPLGYYKDPEKTAET 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 578 VPTAENVRgemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASK-GE-- 654
Cdd:PRK07798 401 FPTIDGVR------YAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEE-ALKAHPDVADALVVGVPDERwGQev 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 655 -ALVLFTTDNELTRDKLQQYAREHgvpeLA---VPRDIRYLKQMPLLGSGKPDFVTLKS 709
Cdd:PRK07798 474 vAVVQLREGARPDLAELRAHCRSS----LAgykVPRAIWFVDEVQRSPAGKADYRWAKE 528
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
349-708 |
8.21e-11 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 65.09 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 349 FAHLLMPRLAQVKQQP----EEEALILFTSGSEGHPKGVVHSHKSIL-ANVEQIKTIAdFTTNDRFMSALPLFHS-FGLT 422
Cdd:PRK08008 153 FTQLKAQQPATLCYAPplstDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQCA-LRDDDVYLTVMPAFHIdCQCT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 423 VGLftPLLT-GAEVFL---YPSPLHYRIVPElvYDRSCT--VLFGTSTFLghyARFANPYDF-YRLRYVVAGAEkLQEST 495
Cdd:PRK08008 232 AAM--AAFSaGATFVLlekYSARAFWGQVCK--YRATITecIPMMIRTLM---VQPPSANDRqHCLREVMFYLN-LSDQE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 496 KQLWQDKFGLRILEGYGVTECapVVSInvpMAAKPG------TVGRilPGM--DARLLSVPGIE----EGGRLQLKG--- 560
Cdd:PRK08008 304 KDAFEERFGVRLLTSYGMTET--IVGI---IGDRPGdkrrwpSIGR--PGFcyEAEIRDDHNRPlpagEIGEICIKGvpg 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 561 PNIMNGYLRVEKPgvlevpTAENVRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL-------- 632
Cdd:PRK08008 377 KTIFKEYYLDPKA------TAKVLEAD---GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIiathpkiq 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 633 ---ALGVsPDKVHATAIKsdaskgeALVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGKPDFVTLK 708
Cdd:PRK08008 448 divVVGI-KDSIRDEAIK-------AFVVLNEGETLSEEEFFAFCEQN-MAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-614 |
2.69e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVEGERIGLMLPNAGISAAVIFG-----AIARRRMPAMMNYTAGVKGLTSAITAAEIKTIF 307
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGclyagVIAVPAYPPESARRHHQERLLSIIADAEPRLLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 308 TSRQFLDKgklwhlpeqLTQvrwvyLEDLKADvttADKVWIFAHLLMPRLAQVKQ----QPEEEALILFTSGSEGHPKGV 383
Cdd:PRK05691 122 TVADLRDS---------LLQ-----MEELAAA---NAPELLCVDTLDPALAEAWQepalQPDDIAFLQYTSGSTALPKGV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 384 VHSHKSILANVEQIKT--IADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYpSPLHY--RIV------------ 447
Cdd:PRK05691 185 QVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM-SPAYFleRPLrwleaiseyggt 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 ----PELVYdRSCTVLFGTSTFLGhyarfanpYDFYRLRYVVAGAEKLQESTKQLWQDKF---GLR---ILEGYGVTECA 517
Cdd:PRK05691 264 isggPDFAY-RLCSERVSESALER--------LDLSRWRVAYSGSEPIRQDSLERFAEKFaacGFDpdsFFASYGLAEAT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVVSINVP-------------MA---AKPGT------VGRILPG-----MDARLLSVPGIEEGGRLQLKGPNIMNGYLRV 570
Cdd:PRK05691 335 LFVSGGRRgqgipaleldaeaLArnrAEPGTgsvlmsCGRSQPGhavliVDPQSLEVLGDNRVGEIWASGPSIAHGYWRN 414
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 16130740 571 EKpgvlevPTAENVRGEMERGWYDTGDIvRFDEQGFVQIQGRAK 614
Cdd:PRK05691 415 PE------ASAKTFVEHDGRTWLRTGDL-GFLRDGELFVTGRLK 451
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
254-635 |
4.70e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 62.69 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 254 EGERIGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLP-------EQLT 326
Cdd:PLN02330 79 KGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPvivlgeeKIEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 327 QVRWVYLedLKADVTTADKVwifAHllmprlaQVKQQPEEEALIlFTSGSEGHPKGVVHSHKSILANV---------EQI 397
Cdd:PLN02330 159 AVNWKEL--LEAADRAGDTS---DN-------EEILQTDLCALP-FSSGTTGISKGVMLTHRNLVANLcsslfsvgpEMI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 398 KTIADfttndrfMSALPLFHSFGLTVGLFTPLLTGAEVflypsplhyrivpeLVYDRsctvlFGTSTFLG----HYARFA 473
Cdd:PLN02330 226 GQVVT-------LGLIPFFHIYGITGICCATLRNKGKV--------------VVMSR-----FELRTFLNalitQEVSFA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 474 ------------NP----YDF--YRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTE--CAPVVSINVPMA---AK 529
Cdd:PLN02330 280 pivppiilnlvkNPiveeFDLskLKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEhsCITLTHGDPEKGhgiAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 530 PGTVGRILPGMDARL------LSVPGiEEGGRLQLKGPNIMNGYLRVEKpgvlevptaENVRGEMERGWYDTGDIVRFDE 603
Cdd:PLN02330 360 KNSVGFILPNLEVKFidpdtgRSLPK-NTPGELCVRSQCVMQGYYNNKE---------ETDRTIDEDGWLHTGDIGYIDD 429
|
410 420 430
....*....|....*....|....*....|..
gi 16130740 604 QGFVQIQGRAKRFAKIAGEMVSLEMVEQLALG 635
Cdd:PLN02330 430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLT 461
|
|
| AGP_acyltrn |
TIGR00530 |
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ... |
16-135 |
4.96e-10 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129621 [Multi-domain] Cd Length: 130 Bit Score: 57.74 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 16 VRVTGDTQALKGERVLITPNHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLD--PTQPM--AIKHLV 91
Cdd:TIGR00530 4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDreNIRAIatALKAAI 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16130740 92 RLVEQGRPVVIFPEGRITTTGSLMKIYDGAGFVAAKSGATVIPV 135
Cdd:TIGR00530 84 EVLKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPV 127
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
362-432 |
1.24e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 61.50 E-value: 1.24e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 362 QQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIktIADF--------TTNDRFMSALPLFHSFGLTVGLFTPLLTG 432
Cdd:PRK05850 157 RDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQL--MSDYfgdtggvpPPDTTVVSWLPFYHDMGLVLGVCAPILGG 233
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
355-701 |
4.45e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.64 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQVKQQPE---EEAL-ILFTSGSEGHPKGVVHSHKSILA--NVEQIKTIA--DFTTNDRFMSALPLFHSFGLTvGLF 426
Cdd:PRK05857 155 LDAASLAGNADqgsEDPLaMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNwvTWVVGETTYSPLPATHIGGLW-WIL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 427 TPLL------TGAEvflypsplHYRIVPELVYDRSCTVLFGTSTFLGHYA---RFANPyDFYRLRYVVAGAEKLQESTKQ 497
Cdd:PRK05857 234 TCLMhgglcvTGGE--------NTTSLLEILTTNAVATTCLVPTLLSKLVselKSANA-TVPSLRLVGYGGSRAIAADVR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 498 LWQDKfGLRILEGYGVTE------CAPVVSINVPmAAKPGTVGRILPGMDARLL-------SVPGIEEG---GRLQLKGP 561
Cdd:PRK05857 305 FIEAT-GVRTAQVYGLSEtgctalCLPTDDGSIV-KIEAGAVGRPYPGVDVYLAatdgigpTAPGAGPSasfGTLWIKSP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 562 NIMNGYLRvekpgvlevpTAENVRGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKV 641
Cdd:PRK05857 383 ANMLGYWN----------NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVRE 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130740 642 HATAIKSDASKGE----ALVLFTTDNELTRDKLQQ-----YAREHgvPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK05857 453 AACYEIPDEEFGAlvglAVVASAELDESAARALKHtiaarFRRES--EPMARPSTIVIVTDIPRTQSGK 519
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
329-630 |
4.80e-09 |
|
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: 59.36 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 329 RWVYLEDLKADVTTADKVwiFAHLLMPRLAQVKqqPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR 408
Cdd:cd17641 126 RLISFEDVVALGRALDRR--DPGLYEREVAAGK--GEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 409 FMSALPL--FHSFGLTVGlfTPLLTGAEV--------------------FLYP------------------SPLH---YR 445
Cdd:cd17641 202 YVSVLPLpwIGEQMYSVG--QALVCGFIVnfpeepetmmedlreigptfVLLPprvwegiaadvrarmmdaTPFKrfmFE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 446 IVPELVYDRSCTVLFGTSTFLGHYARFA-----------NPYDFYRLRYVVAGAEKLQESTKQLWQdKFGLRILEGYGVT 514
Cdd:cd17641 280 LGMKLGLRALDRGKRGRPVSLWLRLASWladallfrplrDRLGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 515 ECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEEGGRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGEmerGWYD 594
Cdd:cd17641 359 ELAGAYTVHRDGDVDPDTVGVPFPGTEVR------IDEVGEILVRSPGVFVGYYKNPEA------TAEDFDED---GWLH 423
|
330 340 350
....*....|....*....|....*....|....*..
gi 16130740 595 TGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVE 630
Cdd:cd17641 424 TGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIE 460
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
364-701 |
4.96e-09 |
|
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: 59.31 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEA---LILFTSGSEGHPKGVVHSHKSILANVEQIKTIAD---FTTNDRFMSALPLFHSFGLTVgLFTPLLTGAEVFL 437
Cdd:cd05929 121 IEDEAagwKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALgfgPGADSVYLSPAPLYHAAPFRW-SMTALFMGGTLVL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 438 YPsplhyRIVPE----LV--YDRSCTVLFGTstflgHYARFA-------NPYDFYRLRYVVAGAEKLQESTKQLWQDKFG 504
Cdd:cd05929 200 ME-----KFDPEeflrLIerYRVTFAQFVPT-----MFVRLLklpeavrNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 505 LRILEGYGVTECAPVVSIN-VPMAAKPGTVGRILPG----MDARLLSVPGIEEGGRLQLKGPnimnGYLRVEKPgvleVP 579
Cdd:cd05929 270 PIIWEYYGGTEGQGLTIINgEEWLTHPGSVGRAVLGkvhiLDEDGNEVPPGEIGEVYFANGP----GFEYTNDP----EK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 580 TAENVRgemERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQL-----------ALGVsPD-----KVHA 643
Cdd:cd05929 342 TAAARN---EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENAliahpkvldaaVVGV-PDeelgqRVHA 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130740 644 ---TAIKSDASK--GEALVLFTTDNeLTRDKlqqyarehgvpelaVPRDIRYLKQMPLLGSGK 701
Cdd:cd05929 418 vvqPAPGADAGTalAEELIAFLRDR-LSRYK--------------CPRSIEFVAELPRDDTGK 465
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
258-701 |
1.02e-08 |
|
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: 58.21 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 258 IGLMLPNAGISAAVIFGAIARRRMPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKlwhlpEQLTqvrwvYLEDLK 337
Cdd:cd05915 52 VATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVE-----AIRG-----ELKTVQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 338 ADVTTADKVWIFAHLLM---PRLAQVKQQPEEEALIL-FTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDR--FMS 411
Cdd:cd05915 122 HFVVMDEKAPEGYLAYEealGEEADPVRVPERAACGMaYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKdvVLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 412 ALPLFHSFGLTVgLFTPLLTGAEVFLYPSPLHYRIVPELVYDRSCTVLFGTSTFLGhyaRFANPYDFYRLRY-----VVA 486
Cdd:cd05915 202 VVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWL---ALADYLESTGHRLktlrrLVV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 487 GAEKLQESTKQLwqDKFG-LRILEGYGVTECAPVVSI--------------NVPMAAKPGT--VGRILPGMDARLLSVPG 549
Cdd:cd05915 278 GGSAAPRSLIAR--FERMgVEVRQGYGLTETSPVVVQnfvkshleslseeeKLTLKAKTGLpiPLVRLRVADEEGRPVPK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 550 IEEGGR-LQLKGPNIMNGYLRVEkpgvlEVPTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEM 628
Cdd:cd05915 356 DGKALGeVQLKGPWITGGYYGNE-----EATRSALTPD----GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVD 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130740 629 VEQLaLGVSPDKVHATAI-KSDASKGEALVLFT--TDNELTRDKLQQYAREHGVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:cd05915 427 LENA-LMGHPKVKEAAVVaIPHPKWQERPLAVVvpRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGK 501
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
321-703 |
2.41e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 57.21 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 321 LPEQLTQVRWVYLEDLKaDVTTADKVWIFAHllmprlaQVKQqpEEEALILFTSGSEGHPKGVVHSHKSILANVEQIktI 400
Cdd:PRK04813 109 LPLEILGIPVITLDELK-DIFATGNPYDFDH-------AVKG--DDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWM--L 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 401 ADFTT--NDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLHYRivPELVYDRSCTVLFG--TSTflghyARFA-- 473
Cdd:PRK04813 177 EDFALpeGPQFLNQAPY--SFDLSVmDLYPTLASGGTLVALPKDMTAN--FKQLFETLPQLPINvwVST-----PSFAdm 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 474 ---NPyDFY-----RLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTE-CAPVVSINV-----------PMA-AKPG 531
Cdd:PRK04813 248 cllDP-SFNeehlpNLTHFLFCGEELPHKTAKKLLERFpSATIYNTYGPTEaTVAVTSIEItdemldqykrlPIGyAKPD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 532 TVGRIlpgMDARLLSVPGIEEgGRLQLKGPNIMNGYLR-VEKpgvlevpTAENVRGEMERGWYDTGDIVRFDEqGFVQIQ 610
Cdd:PRK04813 327 SPLLI---IDEEGTKLPDGEQ-GEIVISGPSVSKGYLNnPEK-------TAEAFFTFDGQPAYHTGDAGYLED-GLLFYQ 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 611 GRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAI-KSDASKGEALV--------LFTTDNELT---RDKLQQYarehg 678
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQ-NLRQSSYVESAVVVpYNKDHKVQYLIayvvpkeeDFEREFELTkaiKKELKER----- 468
|
410 420
....*....|....*....|....*
gi 16130740 679 VPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKID 493
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
230-713 |
3.40e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 56.68 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 230 TPDSYRKLLTKTLFVGRILEKYSV-EGERIGLMLPNAgISAAVIFGAIAR----------------------RRMPAMMN 286
Cdd:PRK06164 34 RPLSRAELRALVDRLAAWLAAQGVrRGDRVAVWLPNC-IEWVVLFLACARlgatviavntryrshevahilgRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 287 YTAGVKGLTSAITAAEIKtiftsrqfldkgklwhlPEQLTQVRWVYLEDLKADVTTA----DKVWIFAHLLMPRL--AQV 360
Cdd:PRK06164 113 VWPGFKGIDFAAILAAVP-----------------PDALPPLRAIAVVDDAADATPApapgARVQLFALPDPAPPaaAGE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 361 KQQPEEEALILFT-SGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTvGLFTPLLTGAEVFLYP 439
Cdd:PRK06164 176 RAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAPLVCEP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 SPLHYRIVpELVYDRSCTVLFGTSTFLGHYARFA-NPYDFYRLRYV--VAGAEKLQESTKQLWQDKFGLRILegYGVTEC 516
Cdd:PRK06164 255 VFDAARTA-RALRRHRVTHTFGNDEMLRRILDTAgERADFPSARLFgfASFAPALGELAALARARGVPLTGL--YGSSEV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 517 APVVSINvPMA-------------AKPGTVGRILPGMDARLLSvPGieEGGRLQLKGPNIMNGYLrvEKPGVlevpTAEN 583
Cdd:PRK06164 332 QALVALQ-PATdpvsvriegggrpASPEARVRARDPQDGALLP-DG--ESGEIEIRAPSLMRGYL--DNPDA----TARA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 584 VRGEmerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVspDKVHATAIKSDASKGE----ALVLF 659
Cdd:PRK06164 402 LTDD---GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL--PGVAAAQVVGATRDGKtvpvAFVIP 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 660 TTDNELTRDKLQQYAREhGVPELAVPRDIRYLKQMPLLGSG---KPDFVTLKSWVDE 713
Cdd:PRK06164 477 TDGASPDEAGLMAACRE-ALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQA 532
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
362-690 |
5.11e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 56.11 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 362 QQPEEE--ALIL-FTSGSEGHPKGVVHSHK-SILANVEQIkTIADFTTNDRFMSALPLFH----SFGLTVglftPLLTGA 433
Cdd:PRK08162 176 TLPADEwdAIALnYTSGTTGNPKGVVYHHRgAYLNALSNI-LAWGMPKHPVYLWTLPMFHcngwCFPWTV----AARAGT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 434 EVFLYpsplhyRIVPELVYD----RSCTVLFGT----STFLGHYARFANPYDfYRLRYVVAGA---EKLQESTKQLwqdk 502
Cdd:PRK08162 251 NVCLR------KVDPKLIFDlireHGVTHYCGApivlSALINAPAEWRAGID-HPVHAMVAGAappAAVIAKMEEI---- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 503 fGLRILEGYGVTECAPVVSINvpmAAKPGTvgRILPGMD-ARLLSVPGI----EEG-------------------GRLQL 558
Cdd:PRK08162 320 -GFDLTHVYGLTETYGPATVC---AWQPEW--DALPLDErAQLKARQGVryplQEGvtvldpdtmqpvpadgetiGEIMF 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 559 KGPNIMNGYLRVEKPgvlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSP 638
Cdd:PRK08162 394 RGNIVMKGYLKNPKA------TEEAFAG----GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVED-VLYRHP 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 639 DkVHATAI--KSDASKGE---ALVLFTTDNELTRDKLQQYAREHgvpeLA---VPRDIRY 690
Cdd:PRK08162 463 A-VLVAAVvaKPDPKWGEvpcAFVELKDGASATEEEIIAHCREH----LAgfkVPKAVVF 517
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
368-703 |
8.01e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEqiktiadfTTNDR------FMSALPLFHSFGLTVgLFTPLLTGAE-VFLYPS 440
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASAD--------ATHDRlggpgqWLLALPAHHIAGLQV-LVRSVIAGSEpVELDVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 441 -----PLHYRIVPELVYDRSCTVLFGTSTF--LGHYARFANPYDFYRLryVVAGA---EKLQESTKQLwqdkfGLRILEG 510
Cdd:PRK07824 109 agfdpTALPRAVAELGGGRRYTSLVPMQLAkaLDDPAATAALAELDAV--LVGGGpapAPVLDAAAAA-----GINVVRT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 511 YGVTECAPvvsinvpmaakpGTV--GRILPGMDARLlsvpgieEGGRLQLKGPNIMNGYLRVEKPGvlevPTAENvrgem 588
Cdd:PRK07824 182 YGMSETSG------------GCVydGVPLDGVRVRV-------EDGRIALGGPTLAKGYRNPVDPD----PFAEP----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 589 erGWYDTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPdKVHATAI--KSDASKGEALVLFTTDNELT 666
Cdd:PRK07824 234 --GWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEA-ALATHP-AVADCAVfgLPDDRLGQRVVAAVVGDGGP 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16130740 667 RDKLQQYaREHGVPEL---AVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK07824 309 APTLEAL-RAHVARTLdrtAAPRELHVVDELPRRGIGKVD 347
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
291-482 |
3.63e-07 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 53.43 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 291 VKGLTSAItaaeiKTIFTSRQFLDkgklwHLPEQLTQVRWVYLEDLKADVTTADKVWI---FAHLLmprlaqvkqqpeee 367
Cdd:cd05943 197 VKGLPSLL-----AVVVVPYTVAA-----GQPDLSKIAKALTLEDFLATGAAGELEFEplpFDHPL-------------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 aLILFTSGSEGHPKGVVHSHKSILanVEQIKTIA---DFTTNDRFMsalplfhsFGLTVG------LFTPLLTGAEVFLY 438
Cdd:cd05943 253 -YILYSSGTTGLPKCIVHGAGGTL--LQHLKEHIlhcDLRPGDRLF--------YYTTCGwmmwnwLVSGLAVGATIVLY 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 439 P-SPLHYR--IVPELVYDRSCTVlFGTS-TFLGHYAR----FANPYDFYRLR 482
Cdd:cd05943 322 DgSPFYPDtnALWDLADEEGITV-FGTSaKYLDALEKaglkPAETHDLSSLR 372
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
526-701 |
3.90e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 53.61 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 526 MAAKPGTVGRILPGMDARLLSvpgiEEGGrlQLKGPNimNGYLRVEK--PGVLEvptaeNVRGEMER----------GWY 593
Cdd:PRK00174 419 TPLKPGSATRPLPGIQPAVVD----EEGN--PLEGGE--GGNLVIKDpwPGMMR-----TIYGDHERfvktyfstfkGMY 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 594 DTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALgVSPDKVHATAI--KSDASKGEALVLFTT--DNELTRDK 669
Cdd:PRK00174 486 FTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIES-AL-VAHPKVAEAAVvgRPDDIKGQGIYAFVTlkGGEEPSDE 563
|
170 180 190
....*....|....*....|....*....|....*
gi 16130740 670 LQQYAREHGVPE---LAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK00174 564 LRKELRNWVRKEigpIAKPDVIQFAPGLPKTRSGK 598
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
364-522 |
7.54e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.07 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILF-TSGSEGHPKGVVHSHKSILA---NVEQIKTIADFTTNDRFMSALplfhSFGLTVGlFTPLLTGAEVflyp 439
Cdd:COG1541 81 PLEEIVRIHaSSGTTGKPTVVGYTRKDLDRwaeLFARSLRAAGVRPGDRVQNAF----GYGLFTG-GLGLHYGAER---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 440 spLHYRIVP----------ELVYDRSCTVLFGTSTFLGHYARFAN----PYDFYRLRYVVAGAEKLQESTKQLWQDKFGL 505
Cdd:COG1541 152 --LGATVIPagggnterqlRLMQDFGPTVLVGTPSYLLYLAEVAEeegiDPRDLSLKKGIFGGEPWSEEMRKEIEERWGI 229
|
170
....*....|....*..
gi 16130740 506 RILEGYGVTECAPVVSI 522
Cdd:COG1541 230 KAYDIYGLTEVGPGVAY 246
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
333-701 |
8.49e-07 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 52.04 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 333 LEDLKADVTTAD-KVWIFAHLlMPRLAQVKQQP--------EEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADF 403
Cdd:cd05939 64 LESLLHCITVSKaKALIFNLL-DPLLTQSSTEPpsqddvnfRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 404 TTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPLHYRIVPELV-YDrsCTVlfgtSTFLGHYARF--ANPYDFY- 479
Cdd:cd05939 143 RPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSASNFWDDCVkYN--CTI----VQYIGEICRYllAQPPSEEe 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 480 ---RLRYVVAGAEKlqestKQLWQ---DKFGL-RILEGYGVTEC-APVVSINVPMAAkPGTVGRILPGM-DARLLSVPgi 550
Cdd:cd05939 217 qkhNVRLAVGNGLR-----PQIWEqfvRRFGIpQIGEFYGATEGnSSLVNIDNHVGA-CGFNSRILPSVyPIRLIKVD-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 551 EEGGRLqLKGPN------------IMNGYLRVEKP----------GVLEVPTAENV--RGEMergWYDTGDIVRFDEQGF 606
Cdd:cd05939 289 EDTGEL-IRDSDglcipcqpgepgLLVGKIIQNDPlrrfdgyvneGATNKKIARDVfkKGDS---AFLSGDVLVMDELGY 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 607 VQIQGRAKRFAKIAGEMVSLEMVE---QLALGVSPDKVHATAI-KSDASKGEALVLFTTDNeLTRDKLQQYAREHgVPEL 682
Cdd:cd05939 365 LYFKDRTGDTFRWKGENVSTTEVEgilSNVLGLEDVVVYGVEVpGVEGRAGMAAIVDPERK-VDLDRFSAVLAKS-LPPY 442
|
410
....*....|....*....
gi 16130740 683 AVPRDIRYLKQMPLLGSGK 701
Cdd:cd05939 443 ARPQFIRLLPEVDKTGTFK 461
|
|
| PLN02901 |
PLN02901 |
1-acyl-sn-glycerol-3-phosphate acyltransferase |
35-140 |
1.22e-06 |
|
1-acyl-sn-glycerol-3-phosphate acyltransferase
Pssm-ID: 215488 [Multi-domain] Cd Length: 214 Bit Score: 50.11 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 35 NHVSFIDgiLLGLFLPVRPV-FAVYTSISQQWYMRWLKSFIDFVPL---DPTQPM-AIKHLVRLVEQGRPVVIFPEGRIT 109
Cdd:PLN02901 57 NHQSFLD--IYTLFHLGRPFkFISKTSIFLIPIIGWAMYMTGHIPLkrmDRRSQLeCLKRCMELLKKGASVFFFPEGTRS 134
|
90 100 110
....*....|....*....|....*....|.
gi 16130740 110 TTGSLMKIYDGAGFVAAKSGATVIPVRIEGA 140
Cdd:PLN02901 135 KDGKLAAFKKGAFSVAAKTGVPVVPITLVGT 165
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
368-440 |
1.70e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 51.27 E-value: 1.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPA 255
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
364-703 |
1.07e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 364 PEEEALILFTSGSEGHPKGVVHSHKSILANveQIKTIADFTTNDRFMSALPLFHSFGLTVGLF--TPLLtGAEVFLYPSP 441
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNN--QLSKVPYLALSEADVIAQTASQSFDISVWQFlaAPLF-GARVEIVPNA 3944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 442 L--HYRIVPELVYDRSCTVLFGT-STFLGHYARFANPYDfyRLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECA 517
Cdd:PRK05691 3945 IahDPQGLLAHVQAQGITVLESVpSLIQGMLAEDRQALD--GLRWMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 518 PVVSI-NVPMAAKPGTVGRI--------LPGMDARLLSVPgIEEGGRLQLKGPNIMNGYlrVEKPGVLEVPTAENVRGEM 588
Cdd:PRK05691 4023 DDVAFfRVDLASTRGSYLPIgsptdnnrLYLLDEALELVP-LGAVGELCVAGTGVGRGY--VGDPLRTALAFVPHPFGAP 4099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 589 ERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKVHATAIKSDASKGEALV--LFTTDNELT 666
Cdd:PRK05691 4100 GERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEA-RLHEQAEVREAAVAVQEGVNGKHLVgyLVPHQTVLA 4178
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 16130740 667 RDKLQQYAREH---GVPELAVPRDIRYLKQMPLLGSGKPD 703
Cdd:PRK05691 4179 QGALLERIKQRlraELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
|
| LPLAT_LPCAT1-like |
cd07991 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ... |
1-137 |
1.36e-05 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.
Pssm-ID: 153253 [Multi-domain] Cd Length: 211 Bit Score: 46.83 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 1 MLFSFFrnlcrvLYRVRVTGdTQALKGERVLITPNHVSFIDGILLGLFLPvrpvfavYTSISQQW-----YMRWLKSFID 75
Cdd:cd07991 4 LLFAFG------FYVIKVHG-KPDPPEAPRIIVANHTSFIDPLILFSDLF-------PSIVAKKElgklpFIGTILRALG 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 76 FVPLDPTQPMAIKHLVRLVEQ------GRPVVIFPEGriTTTG--SLMKIYDGAgFVAaksGATVIPVRI 137
Cdd:cd07991 70 CIFVDRSEPKDRKKVVEEIKEratdpnWPPILIFPEG--TTTNgkALIMFKKGA-FEP---GVPVQPVAI 133
|
|
| COG3176 |
COG3176 |
Putative hemolysin [General function prediction only]; |
29-145 |
3.37e-05 |
|
Putative hemolysin [General function prediction only];
Pssm-ID: 442409 Cd Length: 270 Bit Score: 46.19 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 29 RVLITPNH-VSFIDGILLG-LFLPVRPVFAVYTS-----ISQQWYMRwlksfiDFVPLDPTQPMAIKHLVRLVEQGRPVV 101
Cdd:COG3176 72 HLLVVANHpLGILDGLALLkLVGTVRPDYRILANdlalrIPGGFYSE------LEFPVDPFNLETLKAARRHLLEGGRSC 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 16130740 102 IFPEGRITTTGSLMkiyD-----GAGFVAAKSGATVIPVRIEGAELTHF 145
Cdd:COG3176 146 VFPAGRVSGARRVI---DllwsgLAAKLARKAGAPVVPVYFDGRNSGLF 191
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
355-701 |
4.07e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 46.57 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 355 PRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSI----LANVEQIKTIADFTTndrfMSALPLFHSFGLTVGLFTPLL 430
Cdd:PRK08308 91 TKLEAVNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIdreiEAYNEALNCEQDETP----IVACPVTHSYGLICGVLAALT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 431 TGAE--VFLYPSPlhyRIVPELVYDRSCTVLFGTSTFLGHYARFAnPYDFYRLRYVVAGA-------EKLQESTKQLWQD 501
Cdd:PRK08308 167 RGSKpvIITNKNP---KFALNILRNTPQHILYAVPLMLHILGRLL-PGTFQFHAVMTSGTplpeawfYKLRERTTYMMQQ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 502 kfglrilegYGVTEcAPVVSINVPMAAkPGTVGRILPGMDarllsvpgIEEGGrlqlkGPNimngylrveKPGVLEVPTA 581
Cdd:PRK08308 243 ---------YGCSE-AGCVSICPDMKS-HLDLGNPLPHVS--------VSAGS-----DEN---------APEEIVVKMG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 582 ENvrgEMErgwydTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVsPDKVHATAIKS-DASKGEAL-VLF 659
Cdd:PRK08308 290 DK---EIF-----TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRL-PGVQEAVVYRGkDPVAGERVkAKV 360
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16130740 660 TTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQH-LAPYQVPHEIESVTEIPKNANGK 401
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
629-701 |
4.70e-05 |
|
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: 42.15 E-value: 4.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 629 VEQlALGVSPDKVHATAI-KSDASKGEALVLFTT---DNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLLGSGK 701
Cdd:pfam13193 2 VES-ALVSHPAVAEAAVVgVPDELKGEAPVAFVVlkpGVELLEEELVAHVREE-LGPYAVPKEVVFVDELPKTRSGK 76
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
368-701 |
3.54e-04 |
|
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: 43.82 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 368 ALILFTSGSEGHPKGVVHSHKSILAnVEQIKTIADFTTNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyriv 447
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPK------- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 448 pelvydrsctvlFGTSTFlghyarfanpYDFYR-------------LRYVVAGAEKLQESTKQL------------W--- 499
Cdd:cd05938 219 ------------FSASQF----------WDDCRkhnvtviqyigelLRYLCNQPQSPNDRDHKVrlaignglradvWref 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 500 QDKFG-LRILEGYGVTEcAPVVSINvpMAAKPGTVGRIlpGMDARLLSV-------PGIEEGGRLQlkgpnimNGY-LRV 570
Cdd:cd05938 277 LRRFGpIRIREFYGSTE-GNIGFFN--YTGKIGAVGRV--SYLYKLLFPfelikfdVEKEEPVRDA-------QGFcIPV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 571 EK--PGVLEVPTAEN-----------------VRGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVS---- 625
Cdd:cd05938 345 AKgePGLLVAKITQQspflgyagdkeqtekklLRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVAttev 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 626 ---LEMVEQLA----LGVS-PDkvHATAIksdaskGEALVLFTTDNELTRDKLQQYAREHgVPELAVPRDIRYLKQMPLL 697
Cdd:cd05938 425 advLGLLDFLQevnvYGVTvPG--HEGRI------GMAAVKLKPGHEFDGKKLYQHVREY-LPAYARPRFLRIQDSLEIT 495
|
....
gi 16130740 698 GSGK 701
Cdd:cd05938 496 GTFK 499
|
|
| LPLAT_LCLAT1-like |
cd07990 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ... |
14-109 |
5.03e-04 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins.
Pssm-ID: 153252 [Multi-domain] Cd Length: 193 Bit Score: 41.84 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 14 YRVRVTGDTQALKGERVLITPNHVSFIDGILL-------GLFLPVR----------PVFavytsisqqWYMRWLKSFIdF 76
Cdd:cd07990 10 VKVVVYGDEPKLPKERALIISNHRSEVDWLVLwmladrfGRLGRLKivlkdslkypPLG---------GWGWQLGEFI-F 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130740 77 VPLDPT--QPMAIKHLVRLVEQGRP--VVIFPEG-RIT 109
Cdd:cd07990 80 LKRKWEkdEKTIKRQLKRLKDSPEPfwLLIFPEGtRFT 117
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
370-463 |
5.27e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 43.25 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGVVHSHKSILanVEQIKTIA---DFTTNDRFMsalplfhsFGLTVG------LFTPLLTGAEVFLYP- 439
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGIL--LEHLKELGlhcDLGPGDRFF--------WYTTCGwmmwnwLVSGLLVGATLVLYDg 337
|
90 100 110
....*....|....*....|....*....|
gi 16130740 440 SPLHyrivP------ELVYDRSCTVlFGTS 463
Cdd:PRK03584 338 SPFY----PdpnvlwDLAAEEGVTV-FGTS 362
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
233-442 |
6.01e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 43.19 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 233 SYRKLLTKTLFVGRILEKYSVEGERIGLMLPN-----AGISAAVIFGAIArrrMPAMMNYTAG-VKGLTSAITAAEIKTI 306
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAGPGDRVAILAPQgidyvAGFFAAIKAGTIA---VPLFAPELPGhAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 307 FTS-------RQFLDKgklwhLPeQLTQVRWVYLEDLKADVttadkvwifAHLLMPrlaqVKQQPEEEALILFTSGSEGH 379
Cdd:PRK12476 147 LTTtaaaeavEGFLRN-----LP-RLRRPRVIAIDAIPDSA---------GESFVP----VELDTDDVSHLQYTSGSTRP 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130740 380 PKGVVHSHKSILANVEQ-IKTIADFTTNDRFMSALPLFHSFGLTVGLFtPLLTGAEVFLYpSPL 442
Cdd:PRK12476 208 PVGVEITHRAVGTNLVQmILSIDLLDRNTHGVSWLPLYHDMGLSMIGF-PAVYGGHSTLM-SPT 269
|
|
| LPLAT_AAK14816-like |
cd07992 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ... |
2-106 |
6.84e-04 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.
Pssm-ID: 153254 [Multi-domain] Cd Length: 203 Bit Score: 41.48 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 2 LFSFFRnlcrvlyRVRVTGDTQALKGERVLITPNHV-SFIDGILLGLFLPVRPVFAVYTSISQQWYMRWLKSFIDFVPLD 80
Cdd:cd07992 9 LRIYFR-------RITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVY 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 16130740 81 PTQPMAIKH------------LVRLVEQGRPVVIFPEG 106
Cdd:cd07992 82 RPKDLARGGigkisnaavfdaVGEALKAGGAIGIFPEG 119
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
370-701 |
1.15e-03 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 42.24 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 370 ILFTSGSEGHPKGV---VHSHKSILANveQIKTIAD-------FTTNDrfmsalplfhsFGLTVG----LFTPLLTGAEV 435
Cdd:PRK10524 238 ILYTSGTTGKPKGVqrdTGGYAVALAT--SMDTIFGgkagetfFCASD-----------IGWVVGhsyiVYAPLLAGMAT 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 436 FLY------PSPlhyRIVPELVYDRSCTVLFGTSTFL----GHYARFANPYDFYRLRYVVAGAEKLQESTKQLWQDKFGL 505
Cdd:PRK10524 305 IMYeglptrPDA---GIWWRIVEKYKVNRMFSAPTAIrvlkKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 506 RILEGYGVTECA-PVVSINVPMAAKP---GTVGRILPGMDARLLSvpgiEEGGrlQLKGPNiMNGYLRVE---KPGVLEV 578
Cdd:PRK10524 382 PVIDNYWQTETGwPILAIARGVEDRPtrlGSPGVPMYGYNVKLLN----EVTG--EPCGPN-EKGVLVIEgplPPGCMQT 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 579 PTAENVR------GEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD--KVHATAIKsDA 650
Cdd:PRK10524 455 VWGDDDRfvktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE-SISSHPAvaEVAVVGVK-DA 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130740 651 SKGEALVLF-------TTDNELTRDKLQQYAREHGVPEL---AVPRDIRYLKQMPLLGSGK 701
Cdd:PRK10524 533 LKGQVAVAFvvpkdsdSLADREARLALEKEIMALVDSQLgavARPARVWFVSALPKTRSGK 593
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
554-701 |
1.19e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 42.14 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 554 GRLQLKGPNIMNGYLRVEKPgvlevpTAENVRGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlA 633
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKA------NEEAFAN----GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVEN-V 471
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130740 634 LGVSPDKVHATAI-KSDASKGEALVLFTT--------DNELTRDKLQQYAREHgVPELAVPRDIRYlKQMPLLGSGK 701
Cdd:PLN02479 472 VYTHPAVLEASVVaRPDERWGESPCAFVTlkpgvdksDEAALAEDIMKFCRER-LPAYWVPKSVVF-GPLPKTATGK 546
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
352-437 |
3.02e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 40.96 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 352 LLMPRLAQVKQQPEEEALILFTSGSEGHPKGVVHSHKSILANVEQIKTIADFTTNDRFMSALPLFHSfGLTVGLFTPLLT 431
Cdd:cd17647 96 LIVIRAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHD-PIQRDMFTPLFL 174
|
....*.
gi 16130740 432 GAEVFL 437
Cdd:cd17647 175 GAQLLV 180
|
|
| LPLAT_LABLAT-like |
cd07984 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; ... |
15-138 |
7.25e-03 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LABLAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lipid A biosynthesis lauroyl/myristoyl (LABLAT, HtrB) acyltransferases and similar proteins.
Pssm-ID: 153246 [Multi-domain] Cd Length: 192 Bit Score: 38.35 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130740 15 RVRVTGD---TQALKGER--VLITPnHVSFIDGILLGLFLPVRPVFAVYTSISQQWYMRWL-----KSFIDFVPLDptqp 84
Cdd:cd07984 3 RVEREGLehlEAALAKGKgvILLTA-HFGNWELAGLALALLGYPVTVVYRPLKNPLLDRLItrgreRFGARLIPRG---- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130740 85 MAIKHLVRLVEQGRPVVIFP------EGRITTT--GSLMKIYDGAGFVAAKSGATVIPVRIE 138
Cdd:cd07984 78 GGLRELIRALKKGEIVGILPdqdpgrKGGVFVPffGRPAATPTGPARLALKTGAPVVPAFAY 139
|
|
| LPLAT_DUF374-like |
cd07983 |
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; ... |
86-137 |
9.22e-03 |
|
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: DUF374; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are the uncharacterized DUF374 phospholipid/glycerol acyltransferases and similar proteins.
Pssm-ID: 153245 [Multi-domain] Cd Length: 189 Bit Score: 37.96 E-value: 9.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16130740 86 AIKHLVRLVEQGRPVVIFPEGritTTGSLMKIYDGAGFVAAKSGATVIPVRI 137
Cdd:cd07983 86 ALREMLRALKDGYNIAITPDG---PRGPRYKVKPGVILLARKSGAPIVPVAI 134
|
|
| |
