|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
31-537 |
0e+00 |
|
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: 946.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESA 110
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VVFVGKLDDWPAMAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACA-PLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFS 189
Cdd:cd05932 81 ALFVGKLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHpPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 190 SFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKFQM 269
Cdd:cd05932 161 SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVPRLWTKFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 270 GVYSKMPAQKLDRLLKLPILGRIVGRKVLAGLGLDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRP 349
Cdd:cd05932 241 GVQDKIPQQKLNLLLKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 350 GRQKTGWIGQNSPGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTS 429
Cdd:cd05932 321 GRDKIGTVGNAGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 430 KGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGLCVLSEVGRREALNGTRGALESSLRAHLEQVNGALDKHERLVGLV 509
Cdd:cd05932 401 KGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEEARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIV 480
|
490 500
....*....|....*....|....*...
gi 489188483 510 LVQETWAVDNGFLTPTLKIKRNMVEGAY 537
Cdd:cd05932 481 VVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-538 |
1.49e-170 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 496.16 E-value: 1.49e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 1 MVTANRLPlEVFFEREKRHPQRRYLVQPIGGGRVEeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA 80
Cdd:COG1022 7 VPPADTLP-DLLRRRAARFPDRVALREKEDGIWQS-LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 81 IWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGKLDDWPAMAPgVPEGIPTV-------AMPLHPEGRFdRQWSDLQA 153
Cdd:COG1022 85 ILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLE-VRDELPSLrhivvldPRGLRDDPRL-LSLDELLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 154 cAPLEGDTPTAAEQ---------LATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMF 224
Cdd:COG1022 163 -LGREVADPAELEArraavkpddLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 225 vEMGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVYSKM-----PAQKL-------------DRL--- 283
Cdd:COG1022 242 -SYYALAAGATVAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAeeaggLKRKLfrwalavgrryarARLagk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 284 -------LKLPILGRIVGRKVLAGLGlDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGW 356
Cdd:COG1022 321 spslllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 357 IGQNSPGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAP 436
Cdd:COG1022 400 VGPPLPGVEVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVGEG---LSAPLGLC--VLSEVGRREALNGT--RGALESS-----LRAHLEQVNGALDKHER 504
Cdd:COG1022 480 QPIENALKASPLIEQAVVVGDGrpfLAALIVPDfeALGEWAEENGLPYTsyAELAQDPevralIQEEVDRANAGLSRAEQ 559
|
570 580 590
....*....|....*....|....*....|....
gi 489188483 505 LVGLVLVQETWAVDNGFLTPTLKIKRNMVEGAYG 538
Cdd:COG1022 560 IKRFRLLPKEFTIENGELTPTLKLKRKVILEKYA 593
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
37-533 |
3.14e-152 |
|
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: 443.96 E-value: 3.14e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGK 116
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 LDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd05907 86 PDD------------------------------------------------LATIIYTSGTTGRPKGVMLSHRNILSNAL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKfqmgVYSKMP 276
Cdd:cd05907 118 ALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVPRVWEK----VYAAIK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 277 AQKLDRLLKLPILGRIVGRkvlaglgldaVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGW 356
Cdd:cd05907 194 VKAVPGLKRKLFDLAVGGR----------LRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 357 IGQNSPGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAP 436
Cdd:cd05907 264 VGKPLPGVEVRIADDGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVGEGLSAPLGLCVLSE--VGRREALNGTRG----------ALESSLRAHLEQVNGALDKHER 504
Cdd:cd05907 344 EPIENALKASPLISQAVVIGDGRPFLVALIVPDPeaLEAWAEEHGIAYtdvaelaanpAVRAEIEAAVEAANARLSRYEQ 423
|
490 500
....*....|....*....|....*....
gi 489188483 505 LVGLVLVQETWAVDNGFLTPTLKIKRNMV 533
Cdd:cd05907 424 IKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
12-429 |
6.50e-100 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 308.47 E-value: 6.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 12 FFEREKRHPQRRYLVqpigGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:pfam00501 1 LERQAARTPDKTALE----VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVVFVGKLDDWPAMAPGVPEgIPTVAMPLHPEGRFDRQWSDLQACAPLEGDTP-----TAAE 166
Cdd:pfam00501 77 NPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGK-LEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpppppPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLATLIYTSGTTGVPKGVMH---NFSSFAFAASR-GVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL 242
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLthrNLVANVLSIKRvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 DT-----FVEDMKRARPTLLFGVPRIWtkfqmgvyskmpaqklDRLLKLPILGRIVgrkvlaglgLDAVRYALCGAAPVP 317
Cdd:pfam00501 236 PAldpaaLLELIERYKVTVLYGVPTLL----------------NMLLEAGAPKRAL---------LSSLRLVLSGGAPLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 318 EALLLWYR-RLGLDVLEVYGMTENSGYSHVCRPGRQKT---GWIGQNSPGVEVRISDE-----------GEVQVRSGATM 382
Cdd:pfam00501 291 PELARRFReLFGGALVNGYGLTETTGVVTTPLPLDEDLrslGSVGRPLPGTEVKIVDDetgepvppgepGELCVRGPGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489188483 383 VGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTS 429
Cdd:pfam00501 371 KGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
10-456 |
1.45e-91 |
|
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: 288.25 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVQpigGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:COG0318 3 DLLRRAAARHPDRPALVF---GGR--RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVFVgklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqlA 169
Cdd:COG0318 78 PLNPRLTAEELAYILEDSGARALVT------------------------------------------------------A 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 TLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVE 247
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDpeRVLE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 248 DMKRARPTLLFGVPRIWTkfqmgvyskmpaqkldRLLKLPilgrivgrkVLAGLGLDAVRYALCGAAPVPEALL-LWYRR 326
Cdd:COG0318 184 LIERERVTVLFGVPTMLA----------------RLLRHP---------EFARYDLSSLRLVVSGGAPLPPELLeRFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 LGLDVLEVYGMTENSGYSHVC--RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAE 394
Cdd:COG0318 239 FGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVDEdgrelppgevGEIVVRGPNVMKGYWNDPEATAE 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 395 VLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:COG0318 319 AF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAEAAVVG 378
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
32-531 |
4.07e-89 |
|
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: 284.88 E-value: 4.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSL--DLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSES 109
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLggKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 110 AVVFVGKlddwpamapgvpeGIPTVAmplhpegrfdrqWSDL--QACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMH- 186
Cdd:cd05927 81 SIVFCDA-------------GVKVYS------------LEEFekLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLt 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 --NFSSFAFAASRGVE-LFGTREDDRMLSYLPLCHVAERMfVEMGSLYGGTTV-FFAESLDTFVEDMKRARPTLLFGVPR 262
Cdd:cd05927 136 hgNIVSNVAGVFKILEiLNKINPTDVYISYLPLAHIFERV-VEALFLYHGAKIgFYSGDIRLLLDDIKALKPTVFPGVPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 263 IWTKFQMGVYSKMPAQ--------------KLDRL-----LKLPILGRIVGRKVLAGLGLDaVRYALCGAAPVPEALLLW 323
Cdd:cd05927 215 VLNRIYDKIFNKVQAKgplkrklfnfalnyKLAELrsgvvRASPFWDKLVFNKIKQALGGN-VRLMLTGSAPLSPEVLEF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 324 YRR-LGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD-------------EGEVQVRSGATMVGYYKEP 389
Cdd:cd05927 294 LRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDvpemnydakdpnpRGEVCIRGPNVFSGYYKDP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 390 EKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGEGL-SAPLGLCVL 468
Cdd:cd05927 374 EKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLkSFLVAIVVP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 469 S-EVGRREAL--NGTRGALE-------------SSLRAHLEQvNGaLDKHERLVGLVLVQETWAVDNGFLTPTLKIKRN 531
Cdd:cd05927 454 DpDVLKEWAAskGGGTGSFEelcknpevkkailEDLVRLGKE-NG-LKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRP 530
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
37-533 |
5.88e-83 |
|
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: 266.15 E-value: 5.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVgk 116
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplEGDTptaaEQLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd17640 84 -----------------------------------------ENDS----DDLATIIYTSGTTGNPKGVMLTHANLLHQIR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFfaESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVY---S 273
Cdd:cd17640 119 SLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQkqvS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 274 KMPAQKlDRLLKLPILGRIVgrkvlaglgldavRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQK 353
Cdd:cd17640 197 KSSPIK-QFLFLFFLSGGIF-------------KFGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 354 TGWIGQNSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRM 422
Cdd:cd17640 263 RGSVGRPLPGTEIKIVDPegnvvlppgekGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 423 KEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSApLGLCVlseVGRREALNGTRGALESSLRAHLEQVNGALD-- 500
Cdd:cd17640 343 KDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKR-LGALI---VPNFEELEKWAKESGVKLANDRSQLLASKKvl 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489188483 501 ------------------KHERLVGLVLVQETWaVDNGFLTPTLKIKRNMV 533
Cdd:cd17640 419 klykneikdeisnrpgfkSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-532 |
4.47e-74 |
|
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: 243.12 E-value: 4.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:cd05914 86 SDEDD------------------------------------------------VALINYTSGTTGNSKGVMLTYRNIVSN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDT-FVEDMKRARPTLLFGVPRIWT---KFQMG 270
Cdd:cd05914 118 VDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSaKIIALAFAQVTPTLGVPVPLViekIFKMD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 271 VYSKMPAQKLDRLLKLPILGR----IVGRKVLAGLGlDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHV 346
Cdd:cd05914 198 IIPKLTLKKFKFKLAKKINNRkirkLAFKKVHEAFG-GNIKEFVIGGAKINPDVEEFLRTIGFPYTIGYGMTETAPIISY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 347 CRPGRQKTGWIGQNSPGVEVRISD------EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTG 420
Cdd:cd05914 277 SPPNRIRLGSAGKVIDGVEVRIDSpdpatgEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 421 RMKEIFKTSKGKYVAPAPIENRL-AVHDRIEQVCVVGEGlsaPLGLCVLSEVGRREALNGTRGALESSLR-AHLEQVNGA 498
Cdd:cd05914 357 RKKEMIVLSSGKNIYPEEIEAKInNMPFVLESLVVVQEK---KLVALAYIDPDFLDVKALKQRNIIDAIKwEVRDKVNQK 433
|
490 500 510
....*....|....*....|....*....|....
gi 489188483 499 LDKHERLVGLVLVQETWAVdngflTPTLKIKRNM 532
Cdd:cd05914 434 VPNYKKISKVKIVKEEFEK-----TPKGKIKRFL 462
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
17-530 |
9.70e-73 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 244.24 E-value: 9.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYL---VQPigGGRVEELSW---GEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVP 90
Cdd:PLN02736 55 ETFRDYKYLgtrIRV--DGTVGEYKWmtyGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 91 LYPNLTAESARQVLEHSESAVVFVgKLDDWPAMAPGVPEgIPTV-----------AMPLHPEG---------RFDRQW-S 149
Cdd:PLN02736 133 LYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE-IPSVrlivvvggadePLPSLPSGtgveivtysKLLAQGrS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 150 DLQA-CAPLEGDtptaaeqLATLIYTSGTTGVPKGVM---HNFSSFAFAASRGVELFGTredDRMLSYLPLCHVAERMFV 225
Cdd:PLN02736 211 SPQPfRPPKPED-------VATICYTSGTTGTPKGVVlthGNLIANVAGSSLSTKFYPS---DVHISYLPLAHIYERVNQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 226 EMGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVYSKMPA-----QKL---------DRLLK----LP 287
Cdd:PLN02736 281 IVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKEsgglkERLfnaaynakkQALENgknpSP 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 288 ILGRIVGRKVLAGLGlDAVRYALCGAAPVPEALLLWYRR-LGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEV 366
Cdd:PLN02736 361 MWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEFLRIcFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEV 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 367 RISD--------------EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGK 432
Cdd:PLN02736 440 KLVDvpemnytsedqpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGE 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 433 YVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGLCVLSEVGRREALNGTRGALESSLR-------------AHLEQV--NG 497
Cdd:PLN02736 520 YIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKYEDLKqlcndprvraavlADMDAVgrEA 599
|
570 580 590
....*....|....*....|....*....|...
gi 489188483 498 ALDKHERLVGLVLVQETWAVDNGFLTPTLKIKR 530
Cdd:PLN02736 600 QLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKR 632
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
30-537 |
7.03e-72 |
|
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: 240.72 E-value: 7.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 30 GGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSES 109
Cdd:cd05933 2 RGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 110 AVVFVgklDDWPAMAP--GVPEGIPTV--------AMPLHPEGRFdrQWSDLQACAPLEGDTP-------TAAEQLATLI 172
Cdd:cd05933 82 NILVV---ENQKQLQKilQIQDKLPHLkaiiqykePLKEKEPNLY--SWDEFMELGRSIPDEQldaiissQKPNQCCTLI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 173 YTSGTTGVPKGVM--H-NFSSFAFAASRGVEL-FGTREDDRMLSYLPLCHVAERMF-VEMGSLYGGTtVFFAEsLD---- 243
Cdd:cd05933 157 YTSGTTGMPKGVMlsHdNITWTAKAASQHMDLrPATVGQESVVSYLPLSHIAAQILdIWLPIKVGGQ-VYFAQ-PDalkg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 244 TFVEDMKRARPTLLFGVPRIWTKFQ---------------------MGV----YSKMPAQKLDRLLKLPILGRIVGRKVL 298
Cdd:cd05933 235 TLVKTLREVRPTAFMGVPRVWEKIQekmkavgaksgtlkrkiaswaKGVgletNLKLMGGESPSPLFYRLAKKLVFKKVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 299 AGLGLDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDE-----GE 373
Cdd:cd05933 315 KALGLDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPdadgiGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLAVH-DRIEQV 452
Cdd:cd05933 395 ICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKElPIISNA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 453 CVVGEG---LSAPLGL-CVL---------------SEVGRR---------EALNGTRGALESSLRAHLEQVNG-ALDKHE 503
Cdd:cd05933 475 MLIGDKrkfLSMLLTLkCEVnpetgepldelteeaIEFCRKlgsqatrvsEIAGGKDPKVYEAIEEGIKRVNKkAISNAQ 554
|
570 580 590
....*....|....*....|....*....|....
gi 489188483 504 RLVGLVLVQETWAVDNGFLTPTLKIKRNMVEGAY 537
Cdd:cd05933 555 KIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKY 588
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
35-457 |
7.49e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 238.55 E-value: 7.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK06187 30 RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GklDDWPAMAPGVPEGIPTV-------AMPLHPEGRFDRQWSDLQACAPLEGDTPTAAEQ-LATLIYTSGTTGVPKGVMH 186
Cdd:PRK06187 110 D--SEFVPLLAAILPQLPTVrtvivegDGPAAPLAPEVGEYEELLAAASDTFDFPDIDENdAAAMLYTSGTTGHPKGVVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 NFSSFaFAASRGVE-LFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTVFFAESLD--TFVEDMKRARPTLLFGVPRI 263
Cdd:PRK06187 188 SHRNL-FLHSLAVCaWLKLSRDDVYLVIVPMFHVHA-WGLPYLALMAGAKQVIPRRFDpeNLLDLIETERVTFFFAVPTI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 264 WtkfQMgvyskmpaqkldrLLKLPilgrIVGRKVLAGLgldavRYALCGAAPVPEALLL-WYRRLGLDVLEVYGMTENSG 342
Cdd:PRK06187 266 W---QM-------------LLKAP----RAYFVDFSSL-----RLVIYGGAALPPALLReFKEKFGIDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 343 YSHVCRPGRQKTGWI------GQNSPGVEVRISDE------------GEVQVRSGATMVGYYKEPEKTAEVLtADGFLRT 404
Cdd:PRK06187 321 VVSVLPPEDQLPGQWtkrrsaGRPLPGVEARIVDDdgdelppdggevGEIIVRGPWLMQGYWNRPEATAETI-DGGWLHT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489188483 405 GDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:PRK06187 400 GDVGYIDEDGYLYITDRIKDVII-SGGENIYPRELEDALYGHPAVAEVAVIGV 451
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
35-537 |
1.26e-71 |
|
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: 239.63 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDWPAMAPGVPEgIPTVAMPLHPEGRFDRQWSD---------------LQACAPLEGDTPTAA---EQLATLIYTSG 176
Cdd:cd17641 90 EDEEQVDKLLEIADR-IPSVRYVIYCDPRGMRKYDDprlisfedvvalgraLDRRDPGLYEREVAAgkgEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 177 TTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDTFVEDMKRARPTL 256
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPETMMEDLREIGPTF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 257 LFGVPRIWTKFQMGVYSKM----------------------PAQKLDRLLKLPI-LGRIVGRKVLAG-----LGLDAVRY 308
Cdd:cd17641 249 VLLPPRVWEGIAADVRARMmdatpfkrfmfelgmklglralDRGKRGRPVSLWLrLASWLADALLFRplrdrLGFSRLRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 309 ALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDEGEVQVRSGATMVGYYKE 388
Cdd:cd17641 329 AATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEVGEILVRSPGVFVGYYKN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 389 PEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGEG---LSAPLGL 465
Cdd:cd17641 409 PEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGrpyLTAFICI 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 466 --CVLSEVGRREALNGT-------RGALESSLRAHLEQVNGALDKHERLVGLVLVQETWAVDNGFLTPTLKIKRNMVEGA 536
Cdd:cd17641 489 dyAIVGKWAEQRGIAFTtytdlasRPEVYELIRKEVEKVNASLPEAQRIRRFLLLYKELDADDGELTRTRKVRRGVIAEK 568
|
.
gi 489188483 537 Y 537
Cdd:cd17641 569 Y 569
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-456 |
3.16e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 226.32 E-value: 3.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK07656 29 QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gkLDDWPAMAPGVPEGIPTVAM-------PLHPEGRFDRQWSDLQACA-PLEGDTPTAAEQLATLIYTSGTTGVPKGVMH 186
Cdd:PRK07656 109 --LGLFLGVDYSATTRLPALEHvviceteEDDPHTEKMKTFTDFLAAGdPAERAPEVDPDDVADILFTSGTTGRPKGAML 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 NFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVF----FaeSLDTFVEDMKRARPTLLFGVPr 262
Cdd:PRK07656 187 THRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILplpvF--DPDEVFRLIETERITVLPGPP- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 263 iwTKFQMgvyskmpaqkldrLLKLPilgrivGRKVLAglgLDAVRYALCGAAPVPEALLLWYR-RLGLD-VLEVYGMTEN 340
Cdd:PRK07656 264 --TMYNS-------------LLQHP------DRSAED---LSSLRLAVTGAASMPVALLERFEsELGVDiVLTGYGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 341 SGYSHVCRPGR-QKT--GWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDK 407
Cdd:PRK07656 320 SGVTTFNRLDDdRKTvaGTIGTAIAGVENKIVNElgeevpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489188483 408 GEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07656 400 GRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
32-530 |
1.00e-66 |
|
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: 224.79 E-value: 1.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAV 111
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 112 VF-VGKLDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHNFSS 190
Cdd:cd17639 81 IFtDGKPDD------------------------------------------------LACIMYTSGSTGNPKGVMLTHGN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 191 FAfAASRGVE--LFGT-REDDRMLSYLPLCHVAERMFvEMGSLYGGTTVFFAeSLDTFVEDMKRA--------RPTLLFG 259
Cdd:cd17639 113 LV-AGIAGLGdrVPELlGPDDRYLAYLPLAHIFELAA-ENVCLYRGGTIGYG-SPRTLTDKSKRGckgdltefKPTLMVG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 260 VPRIWTKFQMGVYSKMPA-----------------QKLDRLLKLPILGRIVGRKVLAGLGlDAVRYALCGAAPVPEALLL 322
Cdd:cd17639 190 VPAIWDTIRKGVLAKLNPmgglkrtlfwtayqsklKALKEGPGTPLLDELVFKKVRAALG-GRLRYMLSGGAPLSADTQE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 323 WYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD-------------EGEVQVRSGATMVGYYKEP 389
Cdd:cd17639 269 FLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDweeggystdkpppRGEILIRGPNVFKGYYKNP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 390 EKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGEGL-SAPLGLCVL 468
Cdd:cd17639 349 EKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDkSYPVAIVVP 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 469 SEVGRR---EALNGTRGALESSL------RAHLEQVNGA-----LDKHERLVGLVLVQETWAVDNGFLTPTLKIKR 530
Cdd:cd17639 429 NEKHLTklaEKHGVINSEWEELCedkklqKAVLKSLAETaraagLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
12-456 |
6.19e-66 |
|
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: 220.56 E-value: 6.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 12 FFEREKRHPQRRYLVQpigGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:cd17631 1 LRRRARRHPDRTALVF---GGR--SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVVFvgklDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATL 171
Cdd:cd17631 76 NFRLTPPEVAYILADSGAKVLF----DD------------------------------------------------LALL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 172 IYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAE-RMFVEMGSLYGGTTV----FFAESLDTFV 246
Cdd:cd17631 104 MYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGlGVFTLPTLLRGGTVVilrkFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EdmkRARPTLLFGVPRIWtkfqmgvyskmpaqklDRLLKLPilgrivgrkVLAGLGLDAVRYALCGAAPVPEALLLWYRR 326
Cdd:cd17631 184 E---RHRVTSFFLVPTMI----------------QALLQHP---------RFATTDLSSLRAVIYGGAPMPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 LGLDVLEVYGMTENSGYSHVCRPG--RQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAE 394
Cdd:cd17631 236 RGVKFVQGYGMTETSPGVTFLSPEdhRRKLGSAGRPVFFVEVRIVDPdgrevppgevGEIVVRGPHVMAGYWNRPEATAA 315
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 395 VLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd17631 316 AF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYEHPAVAEVAVIG 375
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
29-457 |
3.95e-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: 219.36 E-value: 3.95e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 29 IGGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:cd05936 19 IFMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVFVgklddwpamapgvpegiptvamplhpegrfDRQWSDLQACAPLEGDTPT-AAEQLATLIYTSGTTGVPKGVMH- 186
Cdd:cd05936 97 AKALIV------------------------------AVSFTDLLAAGAPLGERVAlTPEDVAVLQYTSGTTGVPKGAMLt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 --NFSSFAFAASRGVElFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKRARPTLLFGVPR 262
Cdd:cd05936 147 hrNLVANALQIKAWLE-DLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRpiGVLKEIRKHRVTIFPGVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 263 IWTKfqmgvyskmpaqkldrllklpilgrIVGRKVLAGLGLDAVRYALCGAAPVPEALLL-WYRRLGLDVLEVYGMTENS 341
Cdd:cd05936 226 MYIA-------------------------LLNAPEFKKRDFSSLRLCISGGAPLPVEVAErFEELTGVPIVEGYGLTETS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSHVCRP-GRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQ 410
Cdd:cd05936 281 PVVAVNPLdGPRKPGSIGIPLPGTEVKIVDDdgeelppgevGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYM 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489188483 411 DAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVG-GFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
36-456 |
8.03e-65 |
|
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: 219.01 E-value: 8.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV- 114
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 -GKLDDWPAMAPGVPEGIPTVAMPLHPEGRFDR----QWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVM---H 186
Cdd:cd05911 90 pDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIedllSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVClshR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 NFSSfAFAASRGVELFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTV-----FFAEsldTFVEDMKRARPTLLFGVP 261
Cdd:cd05911 170 NLIA-NLSQVQTFLYGNDGSNDVILGFLPLYHIYG-LFTTLASLLNGATViimpkFDSE---LFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 262 RIwtkfqmgvyskmpaqkLDRLLKLPILGRIVgrkvlaglgLDAVRYALCGAAPVPEAL--LLWYRRLGLDVLEVYGMTE 339
Cdd:cd05911 245 PI----------------AAALAKSPLLDKYD---------LSSLRVILSGGAPLSKELqeLLAKRFPNATIKQGYGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 340 NSGYSHVCRPGRQKTGWIGQNSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKG 408
Cdd:cd05911 300 TGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDdgkdslgpnepGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIG 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489188483 409 EQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05911 380 YFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
167-456 |
6.82e-62 |
|
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: 207.14 E-value: 6.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVeMGSLYGGTTVFFAESLD--T 244
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLPKFDpeA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 245 FVEDMKRARPTLLFGVPRIWtkfqmgvyskmpaqklDRLLKLPilgrivgrkVLAGLGLDAVRYALCGAAPVPEALL-LW 323
Cdd:cd04433 80 ALELIEREKVTILLGVPTLL----------------ARLLKAP---------ESAGYDLSSLRALVSGGAPLPPELLeRF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 324 YRRLGLDVLEVYGMTENSGYSHVCRP--GRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEK 391
Cdd:cd04433 135 EEAPGIKLVNGYGLTETGGTVATGPPddDARKPGSVGRPVPGVEVRIVDPdggelppgeiGELVVRGPSVMKGYWNNPEA 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 392 TAEVlTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd04433 215 TAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAEAAVVG 277
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
36-531 |
3.62e-56 |
|
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: 196.44 E-value: 3.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV- 114
Cdd:cd05959 29 SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLddWPAMAPGVPEGIPTV--------AMPLHPEGRFDRQWSDLqacAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMH 186
Cdd:cd05959 109 GEL--APVLAAALTKSEHTLvvlivsggAGPEAGALLLAELVAAE---AEQLKPAATHADDPAFWLYSSGSTGRPKGVVH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 NFSSFAFAA---SRGVelFGTREDDRMLSylplchvAERMFVEMG---SLY-----GGTTVFFAE--SLDTFVEDMKRAR 253
Cdd:cd05959 184 LHADIYWTAelyARNV--LGIREDDVCFS-------AAKLFFAYGlgnSLTfplsvGATTVLMPErpTPAAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 254 PTLLFGVPRIwtkfqmgvYSKMPAQkldrllklpilgrivgrKVLAGLGLDAVRYALCGAAPVPEALLL-WYRRLGLDVL 332
Cdd:cd05959 255 PTVFFGVPTL--------YAAMLAA-----------------PNLPSRDLSSLRLCVSAGEALPAEVGErWKARFGLDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 333 EVYGMTEnsgYSHVC---RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTAd 399
Cdd:cd05959 310 DGIGSTE---MLHIFlsnRPGRVRYGTTGKPVPGYEVELRDEdggdvadgepGELYVRGPSSATMYWNNRDKTRDTFQG- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 400 GFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG----EGLSAPLGLCVLsevgRRE 475
Cdd:cd05959 386 EWTRTGDKYVRDDDGFYTYAGRADDMLKVS-GIWVSPFEVESALVQHPAVLEAAVVGvedeDGLTKPKAFVVL----RPG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 476 AlnGTRGALESSLRAHleqVNGALDKHERLVGLVLVQEtwavdngfL--TPTLKIKRN 531
Cdd:cd05959 461 Y--EDSEALEEELKEF---VKDRLAPYKYPRWIVFVDE--------LpkTATGKIQRF 505
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
53-538 |
1.72e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 198.66 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 53 LRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSES-AVVFVGK--------------- 116
Cdd:PTZ00216 138 LAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECkAIVCNGKnvpnllrlmksggmp 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 ------LDDwpamapgVPEGIPTVAMPLHPegrfdrqWSDL-------QACAPLEGdtPTAAEQLATLIYTSGTTGVPKG 183
Cdd:PTZ00216 218 nttiiyLDS-------LPASVDTEGCRLVA-------WTDVvakghsaGSHHPLNI--PENNDDLALIMYTSGTTGDPKG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 184 VMHNFSSFAFAAS----RGVELFG-TREDDRMLSYLPLCHVAE----RMFVEMGSLYG-GT--TVffaesLDTFVE---D 248
Cdd:PTZ00216 282 VMHTHGSLTAGILaledRLNDLIGpPEEDETYCSYLPLAHIMEfgvtNIFLARGALIGfGSprTL-----TDTFARphgD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 249 MKRARPTLLFGVPRIWTKFQMGVYSKMPA------QKLD-----RLLKL------PILGRIV---GRKVLAGlgldAVRY 308
Cdd:PTZ00216 357 LTEFRPVFLIGVPRIFDTIKKAVEAKLPPvgslkrRVFDhayqsRLRALkegkdtPYWNEKVfsaPRAVLGG----RVRA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 309 ALCGAAPVPEALLLWYRR-LGLdVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD------------EGEVQ 375
Cdd:PTZ00216 433 MLSGGGPLSAATQEFVNVvFGM-VIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDteeykhtdtpepRGEIL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 376 VRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVApapIENRLAVHdrieqvcvV 455
Cdd:PTZ00216 512 LRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIA---LEALEALY--------G 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 456 GEGLSAPLGLCVLSEVGR---------REAL-------NGTRGALESSLRAH--LEQVNGALD---------KHERLVGL 508
Cdd:PTZ00216 581 QNELVVPNGVCVLVHPARsyicalvltDEAKamafakeHGIEGEYPAILKDPefQKKATESLQetaraagrkSFEIVRHV 660
|
570 580 590
....*....|....*....|....*....|
gi 489188483 509 VLVQETWAVDNGFLTPTLKIKRNMVEGAYG 538
Cdd:PTZ00216 661 RVLSDEWTPENGVLTAAMKLKRRVIDERYA 690
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
32-494 |
1.32e-53 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 190.71 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAV 111
Cdd:COG0365 35 GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 112 VFV-------GKLDDWPAMAPGVPEGIPTV---------AMPLHPEGrfDRQWSDLQACAPLEGDT-PTAAEQLATLIYT 174
Cdd:COG0365 115 LITadgglrgGKVIDLKEKVDEALEELPSLehvivvgrtGADVPMEG--DLDWDELLAAASAEFEPePTDADDPLFILYT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 175 SGTTGVPKGVMHNFSSFAFAASRGVEL-FGTREDDRM-----------LSYL---PLCHvaermfvemgslyGGTTVFFA 239
Cdd:COG0365 193 SGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFwctadigwatgHSYIvygPLLN-------------GATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 240 ESLDT-----FVEDMKRARPTLLFGVPRIWtkfqmgvyskmpaqkldRLLKLpilgriVGRKVLAGLGLDAVRYALCGAA 314
Cdd:COG0365 260 GRPDFpdpgrLWELIEKYGVTVFFTAPTAI-----------------RALMK------AGDEPLKKYDLSSLRLLGSAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 315 PV-PEALLLWYRRLGLDVLEVYGMTENSGysHV--CRPGR-QKTGWIGQNSPGVEVRISDE----------GEVQVRSG- 379
Cdd:COG0365 317 PLnPEVWEWWYEAVGVPIVDGWGQTETGG--IFisNLPGLpVKPGSMGKPVPGYDVAVVDEdgnpvppgeeGELVIKGPw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 380 -ATMVGYYKEPEKTAEVL--TADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:COG0365 395 pGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489188483 457 ----EGLSAPLGLCVLSEvgrrealnGTRG--ALESSLRAHLEQ 494
Cdd:COG0365 474 vpdeIRGQVVKAFVVLKP--------GVEPsdELAKELQAHVRE 509
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
20-492 |
4.61e-53 |
|
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: 187.90 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 20 PQRRYLVQPiggGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAES 99
Cdd:cd05926 1 PDAPALVVP---GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 100 ARQVLEHSESAVVFVGKLDDWPAMaPGVPEGIPTVAMPLHPEGRFDR--QWSDLQACAPL----EGDTPTAAEQLATLIY 173
Cdd:cd05926 78 FEFYLADLGSKLVLTPKGELGPAS-RAASKLGLAILELALDVGVLIRapSAESLSNLLADkknaKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 174 TSGTTGVPKGVM--H-NFSSFAFAASRGVELfgtREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVED 248
Cdd:cd05926 157 TSGTTGRPKGVPltHrNLAASATNITNTYKL---TPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSasTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 249 MKRARPTLLFGVPRIWTKFqmgvyskmpaqkLDRLLKLPilgrivgRKVLAGLgldavRYALCGAAPVPEALLLWY-RRL 327
Cdd:cd05926 234 VRDYNATWYTAVPTIHQIL------------LNRPEPNP-------ESPPPKL-----RFIRSCSASLPPAVLEALeATF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 328 GLDVLEVYGMTENSG--YSHVCRPGRQKTGWIGQNSpGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEV 395
Cdd:cd05926 290 GAPVLEAYGMTEAAHqmTSNPLPPGPRKPGSVGKPV-GVEVRILDEdgeilppgvvGEICLRGPNVTRGYLNNPEANAEA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 396 LTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGeglsAP---LGLCVLSEVG 472
Cdd:cd05926 369 AFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAVLEAVAFG----VPdekYGEEVAAAVV 443
|
490 500
....*....|....*....|
gi 489188483 473 RREALNGTRGALESSLRAHL 492
Cdd:cd05926 444 LREGASVTEEELRAFCRKHL 463
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
43-457 |
2.09e-52 |
|
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: 184.80 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 43 GDQARRAAAW----LRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVfvgkLD 118
Cdd:cd05941 15 ADLVARAARLanrlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLV----LD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 119 DwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqlATLIYTSGTTGVPKGVMHNFSSFAFAASRG 198
Cdd:cd05941 91 P-------------------------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 199 VELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDTFVEDMKRARP--TLLFGVPRIWTKFqMGVYSKMP 276
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPsiTVFMGVPTIYTRL-LQYYEAHF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 277 AQkldrllklpilgrivgRKVLAGLGLDAVRYALCGAAPVPEALL-LWYRRLGLDVLEVYGMTEnSGYSHVCR-PGRQKT 354
Cdd:cd05941 201 TD----------------PQFARAAAAERLRLMVSGSAALPVPTLeEWEAITGHTLLERYGMTE-IGMALSNPlDGERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 355 GWIGQNSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMK 423
Cdd:cd05941 264 GTVGMPLPGVQARIVDEetgeplprgevGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSS 343
|
410 420 430
....*....|....*....|....*....|....
gi 489188483 424 EIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:cd05941 344 VDIIKSGGYKVSALEIERVLLAHPGVSECAVIGV 377
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
5-456 |
2.37e-50 |
|
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: 180.89 E-value: 2.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 5 NRLPLEVF-FEREKRHPQRRYLVQPIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWM 83
Cdd:cd05904 3 TDLPLDSVsFLFASAHPSRPALIDAATG---RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 84 AGHVSVPLYPNLT-AESARQVlEHSESAVVFVGklddwPAMAPGVPE-GIPTVAMPLHPEGRFDRqwSDLQACAPlEGDT 161
Cdd:cd05904 80 LGAVVTTANPLSTpAEIAKQV-KDSGAKLAFTT-----AELAEKLASlALPVVLLDSAEFDSLSF--SDLLFEAD-EAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 PTA---AEQLATLIYTSGTTGVPKGVM--H-NFSSFAFAASRGVELFGTREDdRMLSYLPLCHVAERMFVEMGSL-YGGT 234
Cdd:cd05904 151 PVVvikQDDVAALLYSSGTTGRSKGVMltHrNLIAMVAQFVAGEGSNSDSED-VFLCVLPMFHIYGLSSFALGLLrLGAT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 235 TVFFAE-SLDTFVEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAVRYALCGA 313
Cdd:cd05904 230 VVVMPRfDLEELLAAIERYKVTHLPVVP-------------------------PIVLALVKSPIVDKYDLSSLRQIMSGA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 314 APVPEALLLWYRRL--GLDVLEVYGMTENSGYSHVCRP---GRQKTGWIGQNSPGVEVRISD-----------EGEVQVR 377
Cdd:cd05904 285 APLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDpetgeslppnqTGELWIR 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 378 SGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAAVIP 442
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
30-456 |
3.60e-50 |
|
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: 180.52 E-value: 3.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 30 GGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSES 109
Cdd:cd12119 19 HEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 110 AVVFVGK--LDDWPAMAPGVPEGIPTVAMPLH---PEGRFDRQWS--DLQACAPLEGDTPTAAE-QLATLIYTSGTTGVP 181
Cdd:cd12119 99 RVVFVDRdfLPLLEAIAPRLPTVEHVVVMTDDaamPEPAGVGVLAyeELLAAESPEYDWPDFDEnTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 182 KGVMhnFS-------SFAFAASRGvelFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKRA 252
Cdd:cd12119 179 KGVV--YShrslvlhAMAALLTDG---LGLSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLPGPYLDpaSLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 253 RPTLLFGVPRIWtkfqMGVYSKMPAQKLDrllklpilgrivgrkvlaglgLDAVRYALCGAAPVPEALLLWYRRLGLDVL 332
Cdd:cd12119 254 GVTFAAGVPTVW----QGLLDHLEANGRD---------------------LSSLRRVVIGGSAVPRSLIEAFEERGVRVI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 333 EVYGMTENSGYSHVCRPG--------------RQKTgwiGQNSPGVEVRISDE------------GEVQVRSGATMVGYY 386
Cdd:cd12119 309 HAWGMTETSPLGTVARPPsehsnlsedeqlalRAKQ---GRPVPGVELRIVDDdgrelpwdgkavGELQVRGPWVTKSYY 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 387 KEPEKTAEvLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd12119 386 KNDEESEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIK-SGGEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
38-456 |
8.74e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 180.58 E-value: 8.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 38 SWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV---PLYpnlTAESARQVLEHSESAVVFV 114
Cdd:PRK05605 59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLY---TAHELEHPFEDHGARVAIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddWPAMAPGV--------PEGIPTV----AMPLH---------PEGRFDRQ-----------WSDLQACAPL-EGDT 161
Cdd:PRK05605 136 -----WDKVAPTVerlrrttpLETIVSVnmiaAMPLLqrlalrlpiPALRKARAaltgpapgtvpWETLVDAAIGgDGSD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 P----TAAEQLATLIYTSGTTGVPKGVM--H-NFSSFAFAASRGVELFGtREDDRMLSYLPLCHV-AERMFVEMGSLYGG 233
Cdd:PRK05605 211 VshprPTPDDVALILYTSGTTGKPKGAQltHrNLFANAAQGKAWVPGLG-DGPERVLAALPMFHAyGLTLCLTLAVSIGG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 234 TTVFF-AESLDTFVEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAVRYALCG 312
Cdd:PRK05605 290 ELVLLpAPDIDLILDAMKKHPPTWLPGVP-------------------------PLYEKIAEAAEERGVDLSGVRNAFSG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 313 AAPVPEALL-LWYRRLGLDVLEVYGMTENSGYShVCRP--GRQKTGWIGQNSPGVEVRISD------------EGEVQVR 377
Cdd:PRK05605 345 AMALPVSTVeLWEKLTGGLLVEGYGLTETSPII-VGNPmsDDRRPGYVGVPFPDTEVRIVDpedpdetmpdgeEGELLVR 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 378 SGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITG-GFNVYPAEVEEVLREHPGVEDAAVVG 500
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
10-543 |
5.61e-49 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 179.83 E-value: 5.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYL-VQPIGGGRVEELSWG---EVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAG 85
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLgRREIVDGKPGKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 86 HVSVPLYPNLTAESARQVLEHSESAVVFV--GKLDDWPAMAPGVPEGIPTVAM--PLHPEGRFDRQ--------WSD-LQ 152
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVeeKKISELFKTCPNSTEYMKTVVSfgGVSREQKEEAEtfglviyaWDEfLK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 153 ACAPLEGDTPTAAEQ-LATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGT-----REDDRMLSYLPLCHVAERMFVE 226
Cdd:PLN02614 209 LGEGKQYDLPIKKKSdICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSanaalTVKDVYLSYLPLAHIFDRVIEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 227 MGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVYSKMP--------------AQKLDRLLK------- 285
Cdd:PLN02614 289 CFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSdggflkkfvfdsafSYKFGNMKKgqshvea 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 286 LPILGRIVGRKVLAGLGLDaVRYALCGAAPVPEALLLWYRRLGL-DVLEVYGMTENSGYSHVCRPGR-QKTGWIGQNSPG 363
Cdd:PLN02614 369 SPLCDKLVFNKVKQGLGGN-VRIILSGAAPLASHVESFLRVVACcHVLQGYGLTESCAGTFVSLPDElDMLGTVGPPVPN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 364 VEVRI-------------SDEGEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSK 430
Cdd:PLN02614 448 VDIRLesvpemeydalasTPRGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQ 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 431 GKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPL------GLCVLSEVGRREALNGTRGALESSLRAHlEQVNGAL---DK 501
Cdd:PLN02614 527 GEYVAVENIENIYGEVQAVDSVWVYGNSFESFLvaianpNQQILERWAAENGVSGDYNALCQNEKAK-EFILGELvkmAK 605
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 489188483 502 HERLVGLVLVQET------WAVDNGFLTPTLKIKRNMVEGAYGSRFHE 543
Cdd:PLN02614 606 EKKMKGFEIIKAIhldpvpFDMERDLLTPTFKKKRPQLLKYYQSVIDE 653
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
36-456 |
7.61e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 177.46 E-value: 7.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWL-RSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK08314 35 AISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GK--------------------------LDDWPAMAPgvPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEGDTPTAAEQL 168
Cdd:PRK08314 115 GSelapkvapavgnlrlrhvivaqysdyLPAEPEIAV--PAWLRAEPPLQALAPGGVVAWKEALAAGLAPPPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFaesldtfved 248
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 249 MKR-ARPTllfgVPRIWTKFQMGVYSKMPAQKLDrLLKLPilgrivgrkVLAGLGLDAVRYALCGAAPVPEAL--LLWyR 325
Cdd:PRK08314 263 MPRwDREA----AARLIERYRVTHWTNIPTMVVD-FLASP---------GLAERDLSSLRYIGGGGAAMPEAVaeRLK-E 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 326 RLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD-----------EGEVQVRSGATMVGYYKEPEKTAE 394
Cdd:PRK08314 328 LTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpetleelppgeVGEIVVHGPQVFKGYWNRPEATAE 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 395 V-LTADG--FLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08314 408 AfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINAS-GFKVWPAEVENLLYKHPAIQEACVIA 471
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
10-531 |
3.29e-48 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 177.70 E-value: 3.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYL-VQPIGGGRVEELSWG---EVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAG 85
Cdd:PLN02430 46 DIFSKSVEKYPDNKMLgWRRIVDGKVGPYMWKtykEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 86 HVSVPLYPNLTAESARQVLEHSESAVVFV------GKLDDWPAMAPGVpEGIPTVAMPLHPE-------GRFDRQWSDL- 151
Cdd:PLN02430 126 LICVPLYDTLGPGAVDYIVDHAEIDFVFVqdkkikELLEPDCKSAKRL-KAIVSFTSVTEEEsdkasqiGVKTYSWIDFl 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 152 --------QACAPLEGDTptaaeqlATLIYTSGTTGVPKGVMHNFSSFAfAASRGVELFGTREDDRM------LSYLPLC 217
Cdd:PLN02430 205 hmgkenpsETNPPKPLDI-------CTIMYTSGTSGDPKGVVLTHEAVA-TFVRGVDLFMEQFEDKMthddvyLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 218 HVAERMFVEMGSLYGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVysKMPAQKLDRLLKL----------- 286
Cdd:PLN02430 277 HILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGI--QKALQELNPRRRLifnalykykla 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 287 ------------PILGRIVGRKVLAGLGlDAVRYALCGAAPVPEALLLWYRRLGLD-VLEVYGMTENSGYSHVCRPGRQ- 352
Cdd:PLN02430 355 wmnrgyshkkasPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLRVTSCAfVVQGYGLTETLGPTTLGFPDEMc 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 353 KTGWIGQNSPGVEVRISD-------------EGEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLT 419
Cdd:PLN02430 434 MLGTVGAPAVYNELRLEEvpemgydplgeppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKII 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 420 GRMKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPL-GLCVLSE--VGRREALNGTRGALE----------- 485
Cdd:PLN02430 513 DRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLvAVVVPNEenTNKWAKDNGFTGSFEelcslpelkeh 592
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 489188483 486 --SSLRAHLEQvnGALDKHERLVGLVLVQETWAVDNGFLTPTLKIKRN 531
Cdd:PLN02430 593 ilSELKSTAEK--NKLRGFEYIKGVILETKPFDVERDLVTATLKKRRN 638
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
34-494 |
5.49e-48 |
|
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: 172.48 E-value: 5.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 34 VEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF 113
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 VgklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeQLATLIYTSGTTGVPKGVMHNFSSFAF 193
Cdd:cd05934 81 V----------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 194 AASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRARPTLLFGVPriwtkfqmgv 271
Cdd:cd05934 109 AGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPrfSASRFWSDVRRYGATVTNYLG---------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 272 ysKMPaqklDRLLKLPILGRivgrkvlaglglDA---VRyaLCGAAPVPEALL-LWYRRLGLDVLEVYGMTENSGYSHVC 347
Cdd:cd05934 179 --AML----SYLLAQPPSPD------------DRahrLR--AAYGAPNPPELHeEFEERFGVRLLEGYGMTETIVGVIGP 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 348 RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSG---ATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEG 414
Cdd:cd05934 239 RDEPRRPGSIGRPAPGYEVRIVDDdgqelpagepGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 415 NLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGeglsaplglcVLSEVGRRE-----ALNGTRGALESSLR 489
Cdd:cd05934 318 FFYFVDRKKDMIRRR-GENISSAEVERAILRHPAVREAAVVA----------VPDEVGEDEvkavvVLRPGETLDPEELF 386
|
....*
gi 489188483 490 AHLEQ 494
Cdd:cd05934 387 AFCEG 391
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
34-494 |
4.77e-47 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 171.56 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 34 VEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF 113
Cdd:TIGR02262 28 ISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 VGK--LDDWPAMAPGVPEGIPTVAMPLHPEGRFDRQwSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSS- 190
Cdd:TIGR02262 108 VSGalLPVIKAALGKSPHLEHRVVVGRPEAGEVQLA-ELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNp 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 191 FAFAASRGVELFGTREDDRMLSYLPLCH---VAERMFVEMGslYGGTTVFFAE--SLDTFVEDMKRARPTLLFGVPRIWT 265
Cdd:TIGR02262 187 YWTAELYARNTLGIREDDVCFSAAKLFFaygLGNALTFPMS--VGATTVLMGErpTPDAVFDRLRRHQPTIFYGVPTLYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 266 KfqMGVYSKMPAQKLDRLlklpilgrivgrkvlaglgldavRYALCGAAPVPEAL-LLWYRRLGLDVLEVYGMTENSGYS 344
Cdd:TIGR02262 265 A--MLADPNLPSEDQVRL-----------------------RLCTSAGEALPAEVgQRWQARFGVDIVDGIGSTEMLHIF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTAdGFLRTGDKGEQDAEG 414
Cdd:TIGR02262 320 LSNLPGDVRYGTSGKPVPGYRLRLVGDggqdvadgepGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSGDKYVRNDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 415 NLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG----EGLSAPLGLCVLSEVGrrealngtrGALESSLRA 490
Cdd:TIGR02262 399 SYTYAGRTDDMLKVS-GIYVSPFEIESALIQHPAVLEAAVVGvadeDGLIKPKAFVVLRPGQ---------TALETELKE 468
|
....
gi 489188483 491 HLEQ 494
Cdd:TIGR02262 469 HVKD 472
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
18-456 |
6.92e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 171.65 E-value: 6.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYLVQpigGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTA 97
Cdd:PRK08316 23 RYPDKTALVF---GDR--SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 98 ESARQVLEHSESAVVFV-----GKLDDWPAMAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEGDTPTAAEQLATLI 172
Cdd:PRK08316 98 EELAYILDHSGARAFLVdpalaPTAEAALALLPVDTLILSLVLGGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQIL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 173 YTSGTTGVPKGVMHNFSSF-AFAASRGVELfGTREDDRMLSYLPLCHVAERMFVEMGSLY-GGTTVFFAE-SLDTFVEDM 249
Cdd:PRK08316 178 YTSGTESLPKGAMLTHRALiAEYVSCIVAG-DMSADDIPLHALPLYHCAQLDVFLGPYLYvGATNVILDApDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 250 KRARPTLLFGVPRIWTKfqmgvyskmpaqkldrLLKLPILGRIvgrkvlaglGLDAVRYALCGAAPVPEALLLWYR-RL- 327
Cdd:PRK08316 257 EAERITSFFAPPTVWIS----------------LLRHPDFDTR---------DLSSLRKGYYGASIMPVEVLKELReRLp 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 328 GLDVLEVYGMTENSGYSHVCRPGRQ--KTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEV 395
Cdd:PRK08316 312 GLRFYNCYGQTEIAPLATVLGPEEHlrRPGSAGRPVLNVETRVVDDdgndvapgevGEIVHRSPQLMLGYWDDPEKTAEA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489188483 396 LtADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08316 392 F-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVIG 450
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
8-530 |
9.19e-46 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 170.79 E-value: 9.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 8 PLEVFFEREKRHPQRRYLVQ-PIGGGRVEELSW---GEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWM 83
Cdd:PLN02861 45 PWQFFSDAVKKYPNNQMLGRrQVTDSKVGPYVWltyKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 84 AGHVSVPLYPNLTAESARQVLEHSESAVVFV--GKLDDWPAMAPGVPEGIPTVA----------MPLHPEGRFDRQWSDL 151
Cdd:PLN02861 125 QGITYVPLYDTLGANAVEFIINHAEVSIAFVqeSKISSILSCLPKCSSNLKTIVsfgdvsseqkEEAEELGVSCFSWEEF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 152 QACAPLEGDTPTAAE-QLATLIYTSGTTGVPKGV-MHNFSSFAFAASRGVELFGT----REDDRMLSYLPLCHVAERMfV 225
Cdd:PLN02861 205 SLMGSLDCELPPKQKtDICTIMYTSGTTGEPKGViLTNRAIIAEVLSTDHLLKVTdrvaTEEDSYFSYLPLAHVYDQV-I 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 226 EMGSLYGGTTV-FFAESLDTFVEDMKRARPTLLFGVPRIWTKFQMGVYSKMPAQ--------------KLDRLLK----- 285
Cdd:PLN02861 284 ETYCISKGASIgFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGgmlrkklfdfaynyKLGNLRKglkqe 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 286 --LPILGRIVGRKVLAGLGlDAVRYALCGAAPVPEALLLWYRRLGLDVL-EVYGMTENSGYSHVCRPGR-QKTGWIGQNS 361
Cdd:PLN02861 364 eaSPRLDRLVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSVLsQGYGLTESCGGCFTSIANVfSMVGTVGVPM 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 362 PGVEVRI-----------SD--EGEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKT 428
Cdd:PLN02861 443 TTIEARLesvpemgydalSDvpRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNIFKL 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 429 SKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGLCVLSEvgrREAL------NGTRGALES---SLRAH---LEQVN 496
Cdd:PLN02861 522 SQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPD---RQALedwaanNNKTGDFKSlckNLKARkyiLDELN 598
|
570 580 590
....*....|....*....|....*....|....*....
gi 489188483 497 GALDKH-----ERLVGLVLVQETWAVDNGFLTPTLKIKR 530
Cdd:PLN02861 599 STGKKLqlrgfEMLKAIHLEPNPFDIERDLITPTFKLKR 637
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
36-456 |
1.14e-43 |
|
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: 160.72 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG 115
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 -KLDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:cd05935 81 sELDD------------------------------------------------LALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDtfvedmkraRPTLlfgvPRIWTKFQMGVYSK 274
Cdd:cd05935 113 ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWD---------RETA----LELIEKYKVTFWTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 275 MPAQKLDRLLKLPILGRIVGR-KVLAGlgldavryalcGAAPVPEALL-LWYRRLGLDVLEVYGMTENSGYSHVCRPGRQ 352
Cdd:cd05935 180 IPTMLVDLLATPEFKTRDLSSlKVLTG-----------GGAPMPPAVAeKLLKLTGLRFVEGYGLTETMSQTHTNPPLRP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 353 KTGWIGQNSPGVEVRISD-----------EGEVQVRSGATMVGYYKEPEKTAEVLTADG---FLRTGDKGEQDAEGNLRL 418
Cdd:cd05935 249 KLQCLGIP*FGVDARVIDietgrelppneVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFF 328
|
410 420 430
....*....|....*....|....*....|....*...
gi 489188483 419 TGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05935 329 VDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVIS 365
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
37-456 |
4.88e-43 |
|
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: 159.08 E-value: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVgk 116
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpamaPGVPEGIPTVAMPlhpegrfdrqwsdlqacaplegdtptaaEQLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd05903 80 --------PERFRQFDPAAMP----------------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLSYLPLCHVAermfvemGSLYGGTTVFFAES----LDTF-----VEDMKRARPTLLFGVPriwtkf 267
Cdd:cd05903 124 QYAERLGLGPGDVFLVASPMAHQT-------GFVYGFTLPLLLGApvvlQDIWdpdkaLALMREHGVTFMMGAT------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 268 qmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAVRYALCGAAPVPEALL--LWyRRLGLDVLEVYGMTENSGYSH 345
Cdd:cd05903 191 -------------------PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLArrAA-ELLGAKVCSAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 346 VCRPGRQKTGWI--GQNSPGVEVRISD----------EGEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAE 413
Cdd:cd05903 251 SITPAPEDRRLYtdGRPLPGVEIKVVDdtgatlapgvEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDED 329
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489188483 414 GNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05903 330 GYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
168-456 |
4.27e-41 |
|
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: 151.11 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 168 LATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDT--F 245
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVdaI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 246 VEDMKRARPTLLFGVPriwTKFQmgvyskmpaqkldRLLKLPILGRivgrkvlagLGLDAVRYALCGAAPVPEALLLWYR 325
Cdd:cd17638 82 LEAIERERITVLPGPP---TLFQ-------------SLLDHPGRKK---------FDLSSLRAAVTGAATVPVELVRRMR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 326 -RLGLD-VLEVYGMTEnSGYSHVCRPGRQKT---GWIGQNSPGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEVLTADG 400
Cdd:cd17638 137 sELGFEtVLTAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADG 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 401 FLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGVAQVAVIG 270
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-456 |
5.20e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 151.28 E-value: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 173 YTSGTTGVPKGVM---HNFSSFAFAASrgvELFGTREDDRMLSYLPLCHVAERMFVEMGSL-YGGTTVFFAESLD--TFV 246
Cdd:cd05917 9 FTSGTTGSPKGATlthHNIVNNGYFIG---ERLGLTEQDRLCIPVPLFHCFGSVLGVLACLtHGATMVFPSPSFDplAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDMKRARPTLLFGVPriwTKFQmgvyskmpaqkldRLLKLPILGRivgrkvlagLGLDAVRYALCGAAPVPEALLlwyRR 326
Cdd:cd05917 86 EAIEKEKCTALHGVP---TMFI-------------AELEHPDFDK---------FDLSSLRTGIMAGAPCPPELM---KR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 ----LGL-DVLEVYGMTENSGYSHVCRPG---RQKTGWIGQNSPGVEVRISDE-----------GEVQVRSGATMVGYYK 387
Cdd:cd05917 138 vievMNMkDVTIAYGMTETSPVSTQTRTDdsiEKRVNTVGRIMPHTEAKIVDPeggivppvgvpGELCIRGYSVMKGYWN 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 388 EPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05917 218 DPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
9-456 |
1.26e-40 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 154.52 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 9 LEVFFEREKRHPQRRYLVQPIGGgrveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVS 88
Cdd:PRK06087 26 ADYWQQTARAMPDKIAVVDNHGA----SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 89 VPLYPNLTAESARQVLEHSESAVVFVG---KLDDWPAMAPGVPEGIPTvampLHPEGRFDR---QWSDL---QACA---P 156
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAPtlfKQTRPVDLILPLQNQLPQ----LQQIVGVDKlapATSSLslsQIIAdyeP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 157 LEGDTPTAAEQLATLIYTSGTTGVPKGVM--HN---FSSFAFAAsrGVELfgtREDDRMLSYLPLCHvAERMF--VEMGS 229
Cdd:PRK06087 178 LTTAITTHGDELAAVLFTSGTEGLPKGVMltHNnilASERAYCA--RLNL---TWQDVFMMPAPLGH-ATGFLhgVTAPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 230 LYGGTTVFfaesLDTF-----VEDMKRARPTLLFGVpriwTKFQMGVYSKMPAQKLDrllklpilgrivgrkvlaglgLD 304
Cdd:PRK06087 252 LIGARSVL----LDIFtpdacLALLEQQRCTCMLGA----TPFIYDLLNLLEKQPAD---------------------LS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 305 AVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVcRPGR---QKTGWIGQNSPGVEVRISDE---------- 371
Cdd:PRK06087 303 ALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVV-NLDDplsRFMHTDGYAAAGVEIKVVDEarktlppgce 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQ 451
Cdd:PRK06087 382 GEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIHD 460
|
....*
gi 489188483 452 VCVVG 456
Cdd:PRK06087 461 ACVVA 465
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
29-456 |
1.31e-39 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 151.74 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 29 IGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVFVGKL---DDWPAMAPGVPEGIPT----VAMPLHPEGRFDR-----QWSDLQ-ACAPLEGDTPtAAEQLATLIYTS 175
Cdd:PRK13295 128 SKVLVVPKTfrgFDHAAMARRLRPELPAlrhvVVVGGDGADSFEAllitpAWEQEPdAPAILARLRP-GPDDVTQLIYTS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 176 GTTGVPKGVMHNFSSfAFAASRG-VELFGTREDDRMLSYLPLCHVAERMF-VEMGSLYGGTTVFfaesLDTFveDMKRAr 253
Cdd:PRK13295 207 GTTGEPKGVMHTANT-LMANIVPyAERLGLGADDVILMASPMAHQTGFMYgLMMPVMLGATAVL----QDIW--DPARA- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 254 ptllfgVPRIWTKfqmGVYSKMPAQkldrllklPILGRIVGRKVLAGLGLDAVRYALCGAAPVPEALLLWYRR-LGLDVL 332
Cdd:PRK13295 279 ------AELIRTE---GVTFTMAST--------PFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAaLGAKIV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 333 EVYGMTENSGYSHVC--RPGRQKTGWIGQNSPGVEVRISD----------EGEVQVRSGATMVGYYKEPEKTAEvlTADG 400
Cdd:PRK13295 342 SAWGMTENGAVTLTKldDPDERASTTDGCPLPGVEVRVVDadgaplpagqIGRLQVRGCSNFGGYLKRPQLNGT--DADG 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 401 FLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK13295 420 WFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQVAIVA 474
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
30-456 |
1.84e-39 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 150.41 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 30 GGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLypNlTAESARQV---LEH 106
Cdd:PRK07514 24 PDGLR--YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL--N-TAYTLAELdyfIGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 107 SESAVVFVGklddwPAMAPGV-----PEGIPTVaMPLHPEGRFDrqWSDLQACAPLEGDT-PTAAEQLATLIYTSGTTGV 180
Cdd:PRK07514 99 AEPALVVCD-----PANFAWLskiaaAAGAPHV-ETLDADGTGS--LLEAAAAAPDDFETvPRGADDLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 181 PKGVM--H-NFSSFAFAAsrgVELFGTREDDRMLSYLPLCHVaERMFVEM-GSLYGGTTVFFAESLD--TFVEDMKRArp 254
Cdd:PRK07514 171 SKGAMlsHgNLLSNALTL---VDYWRFTPDDVLIHALPIFHT-HGLFVATnVALLAGASMIFLPKFDpdAVLALMPRA-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 255 TLLFGVPRIWTkfqmgvyskmpaqkldRLLKLPILGRIVGRKVlaglgldavRYALCGAAPV-PEALLLWYRRLGLDVLE 333
Cdd:PRK07514 245 TVMMGVPTFYT----------------RLLQEPRLTREAAAHM---------RLFISGSAPLlAETHREFQERTGHAILE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 334 VYGMTE-NSGYSHVCRpGRQKTGWIGQNSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTADGF 401
Cdd:PRK07514 300 RYGMTEtNMNTSNPYD-GERRAGTVGFPLPGVSLRVTDPetgaelppgeiGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 402 LRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLavhDRIEQV---CVVG 456
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLI-ISGGYNVYPKEVEGEI---DELPGVvesAVIG 432
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
38-454 |
2.53e-38 |
|
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: 145.49 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 38 SWGEVGDQARRAAAWLRSLD-LPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGk 116
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwPAMAPGVPEGIPTVAMPLhpegrfDRQWSDLQACAPLEG-DTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAA 195
Cdd:TIGR01733 80 ----SALASRLAGLVLPVILLD------PLELAALDDAPAPPPpDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 196 SRGVELFGTREDDRMLSYLPLCH---VAErMFvemGSLYGGTTVFFAesldtfVEDMKRARPTLLFGVPRiwtKFQMGVY 272
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFdasVEE-IF---GALLAGATLVVP------PEDEERDDAALLAALIA---EHPVTVL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 273 SKMPAqkldrllklpILGRIVGRKVLAGLGLDAVryALCGAAPVPEALLLWYRRLG-LDVLEVYGMTENSGYSHVCRPGR 351
Cdd:TIGR01733 217 NLTPS----------LLALLAAALPPALASLRLV--ILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 352 QKTGW-----IGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYKEPEKTAEVLTADGFL--------RTGDKG 408
Cdd:TIGR01733 285 DDAPRespvpIGRPLANTRLYVLDDDLRPVPVGVVgelyiggpgvARGYLNRPELTAERFVPDPFAggdgarlyRTGDLV 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489188483 409 EQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCV 454
Cdd:TIGR01733 365 RYLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3-456 |
5.81e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 147.23 E-value: 5.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 3 TANRLPlevffEREK---RHPQRRYlvqpigggrveelSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDL 79
Cdd:PRK12583 27 TVARFP-----DREAlvvRHQALRY-------------TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 80 AIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG---KLDDWPAM----APGVPEGIPT-VAMPLHPEGR----FDRQ 147
Cdd:PRK12583 89 ATARIGAILVNINPAYRASELEYALGQSGVRWVICAdafKTSDYHAMlqelLPGLAEGQPGaLACERLPELRgvvsLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 148 -------WSDLQACAplEGDTPTA-AEQLATL--------IYTSGTTGVPKGVM---HN-FSSFAFAASRgvelFGTRED 207
Cdd:PRK12583 169 pppgflaWHELQARG--ETVSREAlAERQASLdrddpiniQYTSGTTGFPKGATlshHNiLNNGYFVAES----LGLTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 208 DRMLSYLPLCHVAERMFVEMGSL-YGGTTVFFAESLDTF--VEDMKRARPTLLFGVPriwtkfqmgvysKMPAQKLDRll 284
Cdd:PRK12583 243 DRLCVPVPLYHCFGMVLANLGCMtVGACLVYPNEAFDPLatLQAVEEERCTALYGVP------------TMFIAELDH-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 285 klPILGRivgrkvlagLGLDAVRYALCGAAPVPEALLlwyRRL-----GLDVLEVYGMTENSGYSH---VCRPGRQKTGW 356
Cdd:PRK12583 309 --PQRGN---------FDLSSLRTGIMAGAPCPIEVM---RRVmdemhMAEVQIAYGMTETSPVSLqttAADDLERRVET 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 357 IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIF 426
Cdd:PRK12583 375 VGRTQPHLEVKVVDPdgatvprgeiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI 454
|
490 500 510
....*....|....*....|....*....|
gi 489188483 427 kTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK12583 455 -IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-477 |
1.16e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 145.61 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 29 IGGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSe 108
Cdd:PRK12406 6 ISGDRR--RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDS- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVFVGKLDDWPAMAPGVPEGIPTVAMPLHPEGRFDRQWSDlQACAPLEGD-------------TPTAAEQLATLIYTS 175
Cdd:PRK12406 83 GARVLIAHADLLHGLASALPAGVTVLSVPTPPEIAAAYRISP-ALLTPPAGAidwegwlaqqepyDGPPVPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 176 GTTGVPKGVMHNFSSFAFAASRG---VELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTV----FFAESLDTFVEd 248
Cdd:PRK12406 162 GTTGHPKGVRRAAPTPEQAAAAEqmrALIYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVlqprFDPEELLQLIE- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 249 mkRARPTLLFGVPriwTKFQmgvyskmpaqkldRLLKLPilgrivgRKVLAGLGLDAVRYALCGAAPVP----EALLLWY 324
Cdd:PRK12406 241 --RHRITHMHMVP---TMFI-------------RLLKLP-------EEVRAKYDVSSLRHVIHAAAPCPadvkRAMIEWW 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 325 rrlGLDVLEVYGMTEnSGYSHVCRPGR--QKTGWIGQNSPGVEVRISDE----------GEVQVRS-GATMVGYYKEPEK 391
Cdd:PRK12406 296 ---GPVIYEYYGSTE-SGAVTFATSEDalSHPGTVGKAAPGAELRFVDEdgrplpqgeiGEIYSRIaGNPDFTYHNKPEK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 392 TAEVlTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRL----AVHDrieqvCVV--------GEGL 459
Cdd:PRK12406 372 RAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLhavpGVHD-----CAVfgipdaefGEAL 444
|
490 500
....*....|....*....|.
gi 489188483 460 SA---PLGLCVLSEVGRREAL 477
Cdd:PRK12406 445 MAvvePQPGATLDEADIRAQL 465
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
18-456 |
1.70e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 146.64 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYL-VQPIGGG--RVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVsVPLYPN 94
Cdd:PRK07529 37 RHPDAPALsFLLDADPldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 95 LTAESARQVLEHSE-SAVVFVG---KLDDWP------AMAPGV-------------PEGIPTVAM--PLHPEGRFD---- 145
Cdd:PRK07529 116 LEPEQIAELLRAAGaKVLVTLGpfpGTDIWQkvaevlAALPELrtvvevdlarylpGPKRLAVPLirRKAHARILDfdae 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 146 --RQWSDLqacapLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERM 223
Cdd:PRK07529 196 laRQPGDR-----LFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 224 FVEMGSLYGGTTVFFAESL--------DTFVEDMKRARPTLLFGVPRiwtkfqmgVYSKmpaqkldrLLKLPIlgrivgr 295
Cdd:PRK07529 271 VTGLAPLARGAHVVLATPQgyrgpgviANFWKIVERYRINFLSGVPT--------VYAA--------LLQVPV------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 296 kvlAGLGLDAVRYALCGAAPVPEALLLWY-RRLGLDVLEVYGMTENSGySHVCRP--GRQKTGWIGQNSPGVEVRI---- 368
Cdd:PRK07529 328 ---DGHDISSLRYALCGAAPLPVEVFRRFeAATGVRIVEGYGLTEATC-VSSVNPpdGERRIGSVGLRLPYQRVRVvild 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 369 ----------SDE-GEVQVrSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKE-IFKTskGKYVAP 436
Cdd:PRK07529 404 dagrylrdcaVDEvGVLCI-AGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDlIIRG--GHNIDP 480
|
490 500
....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVG 456
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVG 500
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-457 |
2.54e-37 |
|
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: 142.87 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 41 EVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESavvfvgKLDDw 120
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------KLDD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 121 pamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVE 200
Cdd:cd05912 79 -----------------------------------------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSAL 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 201 LFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTVFFAESLDT--FVEDMKRARPTLlfgvpriwtkfqMGVYSKMpaq 278
Cdd:cd05912 112 NLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDAeqVLHLINSGKVTI------------ISVVPTM--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 279 kLDRLLKlpILGRIVGrkvlaglglDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRP--GRQKTGW 356
Cdd:cd05912 176 -LQRLLE--ILGEGYP---------NNLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPedALNKIGS 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 357 IGQNSPGVEVRISDE-------GEVQVRSGATMVGYYKEPEKTAEVlTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTS 429
Cdd:cd05912 244 AGKPLFPVELKIEDDgqppyevGEILLKGPNVTKGYLNRPDATEES-FENGWFKTGDIGYLDEEGFLYVLDRRSDLI-IS 321
|
410 420
....*....|....*....|....*...
gi 489188483 430 KGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:cd05912 322 GGENIYPAEIEEVLLSHPAIKEAGVVGI 349
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
33-523 |
8.85e-37 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 144.14 E-value: 8.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 33 RVEELSWGEVGDQARR-AAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLY----------------PNL 95
Cdd:cd17632 64 RFETITYAELWERVGAvAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQagasaaqlapilaetePRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 96 TAESARQ-------VLEHS--ESAVVFVGK---------LDDWPAMAPGVPEGIPTVAMplhpEGRFDRQWSDLQACAPl 157
Cdd:cd17632 144 LAVSAEHldlaveaVLEGGtpPRLVVFDHRpevdahraaLESARERLAAVGIPVTTLTL----IAVRGRDLPPAPLFRP- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 158 egdtPTAAEQLATLIYTSGTTGVPKGVMHnfsSFAFAASRGVELFGTREDDR----MLSYLPLCHVAERMFVEMGSLYGG 233
Cdd:cd17632 219 ----EPDDDPLALLIYTSGSTGTPKGAMY---TERLVATFWLKVSSIQDIRPpasiTLNFMPMSHIAGRISLYGTLARGG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 234 TTVFFAES-LDTFVEDMKRARPTLLFGVPRIW----TKFQMGVYSKMP----AQKLDRLLKLPILGRIVGRKVLAglgld 304
Cdd:cd17632 292 TAYFAAASdMSTLFDDLALVRPTELFLVPRVCdmlfQRYQAELDRRSVagadAETLAERVKAELRERVLGGRLLA----- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 305 avryALCGAAPVPEALLLWYRR-LGLDVLEVYGMTENSGYS---HVCRPgrqktgwigqnsPGVEVRISD---------- 370
Cdd:cd17632 367 ----AVCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGAVIldgVIVRP------------PVLDYKLVDvpelgyfrtd 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 371 ----EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLAVH 446
Cdd:cd17632 431 rphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAAS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 447 DRIEQVCVVGEGLSAPLgLCVLseVGRREALNG-----TRGALESSLRAhLEQVNGaLDKHERLVGLVLVQETWAVDNGF 521
Cdd:cd17632 511 PLVRQIFVYGNSERAYL-LAVV--VPTQDALAGedtarLRAALAESLQR-IAREAG-LQSYEIPRDFLIETEPFTIANGL 585
|
..
gi 489188483 522 LT 523
Cdd:cd17632 586 LS 587
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
16-456 |
1.35e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 142.31 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 16 EKR---HPQRRYLVqpiggGRVEELSWGEVGDQARRAAAWLR-SLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:PRK06839 9 EKRaylHPDRIAII-----TEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVVFVGKldDWPAMAPGVpEGIPTVAMPLH---PEGRFDRQWSDLQacaPLEGDTPTaaeql 168
Cdd:PRK06839 84 NIRLTENELIFQLKDSGTTVLFVEK--TFQNMALSM-QKVSYVQRVISitsLKEIEDRKIDNFV---EKNESASF----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 aTLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFV 246
Cdd:PRK06839 153 -IICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEptKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDMKRARPTLLFGVPRIWtkfqmgvyskmpaqklDRLLKLPILgrivgrkvlAGLGLDAVRYALCGAAPVPEALLLWYRR 326
Cdd:PRK06839 232 SMIEKHKVTVVMGVPTIH----------------QALINCSKF---------ETTNLQSVRWFYNGGAPCPEELMREFID 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 LGLDVLEVYGMTENSGYSHVC--RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAE 394
Cdd:PRK06839 287 RGFLFGQGFGMTETSPTVFMLseEDARRKVGSIGKPVLFCDYELIDEnknkvevgevGELLIRGPNVMKEYWNRPDATEE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 395 VLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK06839 367 TIQ-DGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
167-458 |
2.64e-36 |
|
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: 137.85 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVeMGSLYGGTTVFFAESLDTFV 246
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAIL-VRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDMKRARPTLLFGVPRiwtkfqmgvyskMPAQKLDRLLKLPILGRivgrkvlaglgLDAVryaLCGAAPVPEALLLWYRR 326
Cdd:cd17630 80 EDLAPPGVTHVSLVPT------------QLQRLLDSGQGPAALKS-----------LRAV---LLGGAPIPPELLERAAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 LGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDEGEVQVRsGATM-VGYYKEPEKtaEVLTADGFLRTG 405
Cdd:cd17630 134 RGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVG-GASLaMGYLRGQLV--PEFNEDGWFTTK 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489188483 406 DKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVGEG 458
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDAFVVGVP 262
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
17-456 |
6.44e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 140.41 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQpigggRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:PRK06145 13 RRTPDRAALVY-----RDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSESAVVFVgklDDWPAMAPGVpeGIPTVAMPLHPEGRFDRQWSDLQACAPLEgdtPTAAEQLATLIYTSG 176
Cdd:PRK06145 88 ADEVAYILGDAGAKLLLV---DEEFDAIVAL--ETPKIVIDAAAQADSRRLAQGGLEIPPQA---AVAPTDLVRLMYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 177 TTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKRARP 254
Cdd:PRK06145 160 TTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDpeAVLAAIERHRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 255 TLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPILGRivgrkvlagLGLDAVRYALCGAAPVPEALLLWYRRL--GLDVL 332
Cdd:PRK06145 240 TCAWMAPVM----------------LSRVLTVPDRDR---------FDLDSLAWCIGGGEKTPESRIRDFTRVftRARYI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 333 EVYGMTENSGYSHVCRPGRQ--KTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTaDG 400
Cdd:PRK06145 295 DAYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIADGagrwlppnmkGEICMRGPKVTKGYWKDPEKTAEAFY-GD 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 401 FLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK06145 374 WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
36-456 |
2.28e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 139.79 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYP---------------------- 93
Cdd:PRK06178 58 VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPlfrehelsyelndagaevllal 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 94 NLTAESARQVLEHSESAVVFVGKLDDWPAMAPGVPEGIPTVAMPLHPEGrfdrqWSDL----QACAPLEGDTPTAAEQLA 169
Cdd:PRK06178 138 DQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLPLPDSLRAPRLAAAG-----AIDLlpalRACTAPVPLPPPALDALA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 TLIYTSGTTGVPKGVMHNFSSFAF--AASRGVELFGtREDDRMLSYLPLCHVAERMFvemGSLY----GGTTVFFAE-SL 242
Cdd:PRK06178 213 ALNYTGGTTGMPKGCEHTQRDMVYtaAAAYAVAVVG-GEDSVFLSFLPEFWIAGENF---GLLFplfsGATLVLLARwDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 DTFVEDMKRARPTLLFgvpriwtkfqmgvyskMPAQKLDRLLKLPILGRIVGRKvlaglgLDAVRyalcgAAPVPEALLL 322
Cdd:PRK06178 289 VAFMAAVERYRVTRTV----------------MLVDNAVELMDHPRFAEYDLSS------LRQVR-----VVSFVKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 323 WYRR-----LGLDVLEV-YGMTEnsgySHVCRP---GRQKTG--------WIGQNSPGVEVRISD-----------EGEV 374
Cdd:PRK06178 342 DYRQrwralTGSVLAEAaWGMTE----THTCDTftaGFQDDDfdllsqpvFVGLPVPGTEFKICDfetgellplgaEGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 375 QVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCV 454
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAV 495
|
..
gi 489188483 455 VG 456
Cdd:PRK06178 496 VG 497
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
35-457 |
2.58e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 138.56 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK03640 26 KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklDDwpAMAPGVPEGIPTvamplhpegrfdrQWSDLQ--ACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFA 192
Cdd:PRK03640 106 ---DD--DFEAKLIPGISV-------------KFAELMngPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 193 FAASRGVELFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTVFFAESLD-TFV-EDMKRARPTLlfgvpriwtkfqMG 270
Cdd:PRK03640 168 WSAVGSALNLGLTEDDCWLAAVPIFHISG-LSILMRSVIYGMRVVLVEKFDaEKInKLLQTGGVTI------------IS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 271 VYSKMpaqkLDRLL-KLPilgrivgrkvlAGLGLDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSgySHVC-- 347
Cdd:PRK03640 235 VVSTM----LQRLLeRLG-----------EGTYPSSFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETA--SQIVtl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 348 --RPGRQKTGWIGQNSPGVEVRISD---------EGEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNL 416
Cdd:PRK03640 298 spEDALTKLGSAGKPLFPCELKIEKdgvvvppfeEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489188483 417 RLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:PRK03640 377 YVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAEAGVVGV 416
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
35-455 |
4.75e-35 |
|
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: 136.89 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFv 114
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVM---HNFSSF 191
Cdd:cd05930 90 ------------------------------------------------TDPDDLAYVIYTSGSTGKPKGVMvehRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 AFAAsrgVELFGTREDDRMLSYLPLCHVAerMFVEM-GSLYGGTTVFFAE-----SLDTFVEDMKRARPTLLFGVPRIwt 265
Cdd:cd05930 122 LLWM---QEAYPLTPGDRVLQFTSFSFDV--SVWEIfGALLAGATLVVLPeevrkDPEALADLLAEEGITVLHLTPSL-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 266 kfqmgvyskmpaqkLDRLLKLPILGRivgrkvlaglgLDAVRYALCGAAPVPEALLLWYRRLGLD--VLEVYGMTENSGY 343
Cdd:cd05930 195 --------------LRLLLQELELAA-----------LPSLRLVLVGGEALPPDLVRRWRELLPGarLVNLYGPTEATVD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 344 SHVCRPGRQKTGW----IGQNSPGVEVRISDE----------GEVQVrSGATM-VGYYKEPEKTAEVLTADGFL------ 402
Cdd:cd05930 250 ATYYRVPPDDEEDgrvpIGRPIPNTRVYVLDEnlrpvppgvpGELYI-GGAGLaRGYLNRPELTAERFVPNPFGpgermy 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489188483 403 RTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd05930 329 RTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLAHPGVREAAVV 380
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
36-468 |
5.87e-35 |
|
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: 136.44 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFvg 115
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 klddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNF-SSFAFA 194
Cdd:cd05919 88 -----------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHrDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSylplchvAERMFVEMG---SLY-----GGTTVFFAE--SLDTFVEDMKRARPTLLFGVPRIW 264
Cdd:cd05919 121 DAMAREALGLTPGDRVFS-------SAKMFFGYGlgnSLWfplavGASAVLNPGwpTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 TkfqmgvyskmpaqkldRLLKLPILGRivgrkvlagLGLDAVRYALCGAAPVPEAllLWYRRL---GLDVLEVYGMTENs 341
Cdd:cd05919 194 A----------------NLLDSCAGSP---------DALRSLRLCVSAGEALPRG--LGERWMehfGGPILDGIGATEV- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSHVC-RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQ 410
Cdd:cd05919 246 GHIFLSnRPGAWRLGSTGRPVPGYEIRLVDEeghtippgeeGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCR 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 411 DAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG----EGLSAPLGLCVL 468
Cdd:cd05919 325 DADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAAVVAvpesTGLSRLTAFVVL 385
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
31-456 |
4.04e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 135.58 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE-S 109
Cdd:PRK08008 32 GGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQaS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 110 AVV----FVGKLDDWPAMAPGVPEGIpTVAMPLHPE--GRFDRQWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKG 183
Cdd:PRK08008 112 LLVtsaqFYPMYRQIQQEDATPLRHI-CLTRVALPAddGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 184 VMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRARPTLLFGVP 261
Cdd:PRK08008 191 VVITHYNLRFAGYYSAWQCALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEkySARAFWGQVCKYRATITECIP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 262 riwtkfqMGVYSKM--PAQKLDRLLKLpilgrivgRKVLAGLGL-DAVRYALCgaapvpealllwyRRLGLDVLEVYGMT 338
Cdd:PRK08008 271 -------MMIRTLMvqPPSANDRQHCL--------REVMFYLNLsDQEKDAFE-------------ERFGVRLLTSYGMT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 339 ENSGYSHVCRPGrQKTGW--IGQNSPGVEVRISDE----------GEVQVRS--GAT-MVGYYKEPEKTAEVLTADGFLR 403
Cdd:PRK08008 323 ETIVGIIGDRPG-DKRRWpsIGRPGFCYEAEIRDDhnrplpageiGEICIKGvpGKTiFKEYYLDPKATAKVLEADGWLH 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489188483 404 TGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08008 402 TGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVG 453
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-492 |
1.69e-33 |
|
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: 133.19 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamAPGVPEGIPTVAMPLHPEGRFDrqwsdlqACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFA-F 193
Cdd:cd12116 91 ---------DDALPDRLPAGLPVLLLALAAA-------AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 194 AASRGvELFGTREDDRMLS-------------YLPL-----CHVAERmfvemgslyggTTVFFAESLdtfVEDMKRARPT 255
Cdd:cd12116 155 LHSMR-ERLGLGPGDRLLAvttyafdisllelLLPLlagarVVIAPR-----------ETQRDPEAL---ARLIEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 256 LLFGVPRIWtkfQMGVYSkmpaqkldrllklpilgrivGRKVLAGLgldavrYALCGAAPVPEALLLWYRRLGLDVLEVY 335
Cdd:cd12116 220 VMQATPATW---RMLLDA--------------------GWQGRAGL------TALCGGEALPPDLAARLLSRVGSLWNLY 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 336 GMTENSGYSHVCR---PGRQKTgwIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFL 402
Cdd:cd12116 271 GPTETTIWSTAARvtaAAGPIP--IGRPLANTQVYVLDAalrpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPDPFA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 403 -------RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGLcvLSEVGRRE 475
Cdd:cd12116 349 gpgsrlyRTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL--VAYVVLKA 425
|
490
....*....|....*..
gi 489188483 476 ALNGTRGALESSLRAHL 492
Cdd:cd12116 426 GAAPDAAALRAHLRATL 442
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4-456 |
6.15e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.41 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPLEVF-FEREKRHPQRRYLvqpIGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIW 82
Cdd:PLN02246 20 PNHLPLHDYcFERLSEFSDRPCL---IDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 83 MAGHVSVPLYPNLT-AESARQVLEHSESAVV----FVGKLDDWPAmapgvPEGIPTVAMPLHPEG--RFdrqWSDLQACa 155
Cdd:PLN02246 97 RRGAVTTTANPFYTpAEIAKQAKASGAKLIItqscYVDKLKGLAE-----DDGVTVVTIDDPPEGclHF---SELTQAD- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 156 plEGDTPTA---AEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVE----LFGTREDDRMLSYLPLCHVAERMFVEMG 228
Cdd:PLN02246 168 --ENELPEVeisPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPMFHIYSLNSVLLC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 229 SLYGGTTVFFAESLD--TFVEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAV 306
Cdd:PLN02246 246 GLRVGAAILIMPKFEigALLELIQRHKVTIAPFVP-------------------------PIVLAIAKSPVVEKYDLSSI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 307 RYALCGAAPVPEALLLWYR-RLGLDVL-EVYGMTENSGYSHVC-----RPGRQKTGWIGQNSPGVEVRISD--------- 370
Cdd:PLN02246 301 RMVLSGAAPLGKELEDAFRaKLPNAVLgQGYGMTEAGPVLAMClafakEPFPVKSGSCGTVVRNAELKIVDpetgaslpr 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 371 --EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDR 448
Cdd:PLN02246 381 nqPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLISHPS 459
|
....*...
gi 489188483 449 IEQVCVVG 456
Cdd:PLN02246 460 IADAAVVP 467
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
14-426 |
8.87e-33 |
|
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: 131.98 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 14 EREKRHPQR---RYLvqPIGGGRVEELSWGEVGDQARRAAAWLRSLDLPaGSRIAIISKNCAHWIVTDLAIWMAGHVSVP 90
Cdd:cd05931 1 RRAAARPDRpayTFL--DDEGGREETLTYAELDRRARAIAARLQAVGKP-GDRVLLLAPPGLDFVAAFLGCLYAGAIAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 91 LYP---NLTAESARQVLEHSESAVVF--VGKLDDWPAMAPGVPEGiptvamplhpeGRFDRQWSDLQACAPLEGDTPTAA 165
Cdd:cd05931 78 LPPptpGRHAERLAAILADAGPRVVLttAAALAAVRAFAASRPAA-----------GTPRLLVVDLLPDTSAADWPPPSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 166 EQ--LATLIYTSGTTGVPKGVM-------HNFSSfafaasrGVELFGTREDDRMLSYLPLCHvaermfvEMG-------S 229
Cdd:cd05931 147 DPddIAYLQYTSGSTGTPKGVVvthrnllANVRQ-------IRRAYGLDPGDVVVSWLPLYH-------DMGligglltP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 230 LYGGTTVFFAESLDtFVEDmkrarptllfgvPRIW----TKFQmGVYSKMP--AqkldrllkLPILGRIVGRKVLAGLGL 303
Cdd:cd05931 213 LYSGGPSVLMSPAA-FLRR------------PLRWlrliSRYR-ATISAAPnfA--------YDLCVRRVRDEDLEGLDL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 304 DAVRYALCGAAPVPEALLlwyRR-------LGLD---VLEVYGMTENSGY---------------------SHVCRPGRQ 352
Cdd:cd05931 271 SSWRVALNGAEPVRPATL---RRfaeafapFGFRpeaFRPSYGLAEATLFvsggppgtgpvvlrvdrdalaGRAVAVAAD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 353 KTGWI-----GQNSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEV------LTADGFLRTGDKGEQ 410
Cdd:cd05931 348 DPAARelvscGRPLPDQEVRIVDPetgrelpdgevGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFL 427
|
490
....*....|....*.
gi 489188483 411 dAEGNLRLTGRMKEIF 426
Cdd:cd05931 428 -HDGELYITGRLKDLI 442
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
17-523 |
1.01e-32 |
|
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: 132.17 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQPIGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:cd05921 6 RQAPDRTWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESA-----RQVLEHSESAVVFVgklDDWP----AMAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACAPLeGDTPTAAEQ 167
Cdd:cd05921 86 LMSQdlaklKHLFELLKPGLVFA---QDAApfarALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPT-AAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 168 -----LATLIYTSGTTGVPKGVM--HNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVF--- 237
Cdd:cd05921 162 vgpdtVAKFLFTSGSTGLPKAVIntQRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYidd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 238 -------FAESLDTFVEDMkrarPTLLFGVPRIWtkfqmgvysKMPAQKLDRllklpilgrivgRKVLAGLGLDAVRYAL 310
Cdd:cd05921 242 gkpmpggFEETLRNLREIS----PTVYFNVPAGW---------EMLVAALEK------------DEALRRRFFKRLKLMF 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 311 CGAAPVPEAllLWYRRLGLDVLEV---------YGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDEG---EVQVRS 378
Cdd:cd05921 297 YAGAGLSQD--VWDRLQALAVATVgeripmmagLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPSGgkyEVRVKG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 379 GATMVGYYKEPEKTAEVLTADGFLRTGDKGE----QDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRLA------VHDr 448
Cdd:cd05921 375 PNVTPGYWRQPELTAQAFDEEGFYCLGDAAKladpDDPAKGLVFDGRVAEDFKLASGTWVSVGPLRARAVaacaplVHD- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 449 ieqVCVVGEGlSAPLGLCVLSEVGRREALNGT--------------RGALESSLRAHLEQVNGAldkHERLVGLVLVQET 514
Cdd:cd05921 454 ---AVVAGED-RAEVGALVFPDLLACRRLVGLqeasdaevlrhakvRAAFRDRLAALNGEATGS---SSRIARALLLDEP 526
|
....*....
gi 489188483 515 WAVDNGFLT 523
Cdd:cd05921 527 PSIDKGEIT 535
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
37-456 |
1.28e-32 |
|
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: 129.76 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE-SAVVfvg 115
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGaKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 klddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAA 195
Cdd:cd05972 78 -----------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 196 SRGVELFGTREDDRMLSylplchVAERMFVEmGSLYGGTTVFfAESLDTFVEDMKRARPTLLFGvprIWTKFQMGVYSKM 275
Cdd:cd05972 111 PTAAYWLGLRPDDIHWN------IADPGWAK-GAWSSFFGPW-LLGATVFVYEGPRFDAERILE---LLERYGVTSFCGP 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 276 PAQkLDRLLKLPILGRIVGRkvlaglgldaVRYALCGAAPV-PEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKT 354
Cdd:cd05972 180 PTA-YRMLIKQDLSSYKFSH----------LRLVVSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 355 GWIGQNSPGVEVRISD----------EGEVQVRSG--ATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRM 422
Cdd:cd05972 249 GSMGRPTPGYDVAIIDddgrelppgeEGDIAIKLPppGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRDEDGYFWFVGRA 327
|
410 420 430
....*....|....*....|....*....|....
gi 489188483 423 KEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05972 328 DDIIKSS-GYRIGPFEVESALLEHPAVAEAAVVG 360
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
31-457 |
1.61e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 130.11 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVeeLSWGEVGDQARRAAAWLRSLDlpagsRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESA 110
Cdd:PRK07787 22 GGRV--LSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VvfvgklddWPAMAPGVPEGIPTVAMPLHPegrfdRQWSdlqacaPLEGDTPTAAeqlATLIYTSGTTGVPKGVMhnFSS 190
Cdd:PRK07787 95 A--------WLGPAPDDPAGLPHVPVRLHA-----RSWH------RYPEPDPDAP---ALIVYTSGTTGPPKGVV--LSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 191 FAFAASRG--VELFGTREDDRMLSYLPLCHVAERMFVEMGSL-YGGTTVFFAESLDTFVEDMKRARPTLLFGVPRIWTkf 267
Cdd:PRK07787 151 RAIAADLDalAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLrIGNRFVHTGRPTPEAYAQALSEGGTLYFGVPTVWS-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 268 qmgvyskmpaqkldrllklpilgRIVGRKVLAGlGLDAVRYALCGAAPVPEALLLWYRRL-GLDVLEVYGMTENSGYSHV 346
Cdd:PRK07787 229 -----------------------RIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAALtGHRPVERYGMTETLITLST 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 347 CRPGRQKTGWIGQNSPGVEVRISDE------------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEG 414
Cdd:PRK07787 285 RADGERRPGWVGLPLAGVETRLVDEdggpvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDG 364
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 489188483 415 NLRLTGRMKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:PRK07787 365 MHRIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGV 407
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
17-456 |
1.80e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.88 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVqpIGGGRveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:PRK06188 23 KRYPDRPALV--LGDTR---LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSESAVVFVgklDD--WPAMAPGVPEGIPTVA--MPLHPEGRFdrqwSDLQACAPLEGDTPTAAEQL---- 168
Cdd:PRK06188 98 LDDHAYVLEDAGISTLIV---DPapFVERALALLARVPSLKhvLTLGPVPDG----VDLLAAAAKFGPAPLVAAALppdi 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEmgSLYGGTTVFFAESLD--TFV 246
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLP--TLLRGGTVIVLAKFDpaEVL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDMKRARPTLLFGVPRIwtkfqmgVYskmpaqkldRLLKLPILGRivgrkvlAGL-GLDAVRYalcGAAPV-PEALLLWY 324
Cdd:PRK06188 249 RAIEEQRITATFLVPTM-------IY---------ALLDHPDLRT-------RDLsSLETVYY---GASPMsPVRLAEAI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 325 RRLGLDVLEVYGMTENSGYSHVCR-----PGRQKT-GWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKE 388
Cdd:PRK06188 303 ERFGPIFAQYYGQTEAPMVITYLRkrdhdPDDPKRlTSCGRPTPGLRVALLDEdgrevaqgevGEICVRGPLVMDGYWNR 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 389 PEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK06188 383 PEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
35-456 |
2.06e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 130.41 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 -GKLDDWPA-MAPGVPEGIPTVAMPLHPEGRFDRqWSDLQACAPlegDTPTAAEQL-ATLIYTSGTTGVPKGVMHNF--- 188
Cdd:PRK08276 90 sAALADTAAeLAAELPAGVPLLLVVAGPVPGFRS-YEEALAAQP---DTPIADETAgADMLYSSGTTGRPKGIKRPLpgl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 189 ----SSFAFAASRGVELFGTrEDDRMLSYLPLCHVAERMFVEMGSLYGGTTV----FFAEsldTFVEDMKRARPTLLFGV 260
Cdd:PRK08276 166 dpdeAPGMMLALLGFGMYGG-PDSVYLSPAPLYHTAPLRFGMSALALGGTVVvmekFDAE---EALALIERYRVTHSQLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 261 PriwTKFQmgvyskmpaqkldRLLKLPilgrivgRKVLAGLGLDAVRYALCGAAPVP----EALLLWYrrlGLDVLEVYG 336
Cdd:PRK08276 242 P---TMFV-------------RMLKLP-------EEVRARYDVSSLRVAIHAAAPCPvevkRAMIDWW---GPIIHEYYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 337 MTENSGYSHVC------RPGRQKTGWIGqnspgvEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADG 400
Cdd:PRK08276 296 SSEGGGVTVITsedwlaHPGSVGKAVLG------EVRILDEdgnelppgeiGTVYFEMDGYPFEYHNDPEKTAAARNPHG 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 401 FLRTGDKGEQDAEGNLRLTGRmKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08276 370 WVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG 424
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
15-456 |
5.18e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 129.43 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 15 REKRHPQRRYLVQPIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPN 94
Cdd:PRK13391 6 HAQTTPDKPAVIMASTG---EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 95 LTAESARQVLEHSESAVVF--VGKLDdwpaMAPGVPEGIPTVAMPLHPEGRFDRQ-WSDLQACAPLEGDTPTAAEQLAT- 170
Cdd:PRK13391 83 LTPAEAAYIVDDSGARALItsAAKLD----VARALLKQCPGVRHRLVLDGDGELEgFVGYAEAVAGLPATPIADESLGTd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFAFAASRGVE-----LFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTV----FFAEs 241
Cdd:PRK13391 159 MLYSSGTTGRPKGIKRPLPEQPPDTPLPLTaflqrLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIvmehFDAE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 ldTFVEDMKRARPTLLFGVPriwTKFQmgvyskmpaqkldRLLKLPilgrivgRKVLAGLGLDAVRYALCGAAPVP---- 317
Cdd:PRK13391 238 --QYLALIEEYGVTHTQLVP---TMFS-------------RMLKLP-------EEVRDKYDLSSLEVAIHAAAPCPpqvk 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 318 EALLLWYrrlGLDVLEVYGMTENSGYShVCRPGR--QKTGWIGQNSPGVeVRISDE----------GEVQVRsGATMVGY 385
Cdd:PRK13391 293 EQMIDWW---GPIIHEYYAATEGLGFT-ACDSEEwlAHPGTVGRAMFGD-LHILDDdgaelppgepGTIWFE-GGRPFEY 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 386 YKEPEKTAEVLTADGFLRT-GDKGEQDAEGNLRLTGRmKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK13391 367 LNDPAKTAEARHPDGTWSTvGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
12-456 |
5.69e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 129.93 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 12 FFERE-KRHPQRRYLVQPIGGGRveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVP 90
Cdd:PRK08315 21 LLDRTaARYPDREALVYRDQGLR---WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 91 LYPNLTAESARQVLEHSE-SAVVFVG--KLDDWPAM----APGVPEGIPT---------------VAMPLHPeGRFDrqW 148
Cdd:PRK08315 98 INPAYRLSELEYALNQSGcKALIAADgfKDSDYVAMlyelAPELATCEPGqlqsarlpelrrvifLGDEKHP-GMLN--F 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 149 SDLQAcAPLEGDTPTAAEQLATL-----I---YTSGTTGVPKGVM---HNFSSFAFAASRGVELfgtREDDRMLSYLPLC 217
Cdd:PRK08315 175 DELLA-LGRAVDDAELAARQATLdpddpIniqYTSGTTGFPKGATlthRNILNNGYFIGEAMKL---TEEDRLCIPVPLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 218 H----VaermfveMGSL----YGGTTVFFAESLD--TFVEDMKRARPTLLFGVPriwTKFQmgvyskmpAQkldrlLKLP 287
Cdd:PRK08315 251 HcfgmV-------LGNLacvtHGATMVYPGEGFDplATLAAVEEERCTALYGVP---TMFI--------AE-----LDHP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 288 ILGRivgrkvlagLGLDAVRYALCGAAPVPEALLlwyRR----LGL-DVLEVYGMTENSGYSHVCR---PGRQKTGWIGQ 359
Cdd:PRK08315 308 DFAR---------FDLSSLRTGIMAGSPCPIEVM---KRvidkMHMsEVTIAYGMTETSPVSTQTRtddPLEKRVTTVGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 360 NSPGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKE-IFK 427
Cdd:PRK08315 376 ALPHLEVKIVDPetgetvprgeqGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDmIIR 455
|
490 500
....*....|....*....|....*....
gi 489188483 428 tsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08315 456 --GGENIYPREIEEFLYTHPKIQDVQVVG 482
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
18-456 |
5.99e-31 |
|
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: 126.08 E-value: 5.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYLVQPIGGGRveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTA 97
Cdd:cd05923 13 RAPDACAIADPARGLR---LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 98 ESARQVLEHSESAVVFVgklddwpAMAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEgDTPTAAEQLATLIYTSGT 177
Cdd:cd05923 90 AELAELIERGEMTAAVI-------AVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIE-DPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 178 TGVPKGVM----HNFSSFAFAASRGVELFGTREddRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKR 251
Cdd:cd05923 162 TGLPKGAVipqrAAESRVLFMSTQAGLRHGRHN--VVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDpaDALKLIEQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 252 ARPTLLFGVPriwtkfqmgvyskmpaQKLDRLlklpilgriVGRKVLAGLGLDAVRYALCGAAPVPEALL-LWYRRLGLD 330
Cdd:cd05923 240 ERVTSLFATP----------------THLDAL---------AAAAEFAGLKLSSLRHVTFAGATMPDAVLeRVNQHLPGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 331 VLEVYGMTE--NSGYSHVCRPG-RQKTGW--------IGQnSPGVEVRISDEGE--VQVRSGATMVGYYKEPEKTAEVLT 397
Cdd:cd05923 295 KVNIYGTTEamNSLYMRDARTGtEMRPGFfsevrivrIGG-SPDEALANGEEGEliVAAAADAAFTGYLNQPEATAKKLQ 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 398 aDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05923 374 -DGWYRTGDVGYVDPSGDVRILGRVDDMIISG-GENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
32-456 |
1.80e-30 |
|
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: 123.70 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAV 111
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 112 VFVGKLDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSGTTGVPKGVMHnfssf 191
Cdd:cd05971 82 LVTDGSDD------------------------------------------------PALIIYTSGTTGPPKGALH----- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 afaASRGVelfgtreddrmLSYLPLCHVAERMFVEMGSLYGGTT--VFFAESLDTFVedmkrarPTLLFGVPRIWTKFQm 269
Cdd:cd05971 109 ---AHRVL-----------LGHLPGVQFPFNLFPRDGDLYWTPAdwAWIGGLLDVLL-------PSLYFGVPVLAHRMT- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 270 gvysKMPAQKLDRLLK-------------LPILGRIVGRKVLAGLGLDAVryaLCGAAPVPEALLLWYRR-LGLDVLEVY 335
Cdd:cd05971 167 ----KFDPKAALDLMSrygvttaflpptaLKMMRQQGEQLKHAQVKLRAI---ATGGESLGEELLGWAREqFGVEVNEFY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 336 GMTE-NSGYSHVCRPGRQKTGWIGQNSPGVEVRISD----------EGEVQVR--SGATMVGYYKEPEKTaEVLTADGFL 402
Cdd:cd05971 240 GQTEcNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDdngtplppgeVGEIAVElpDPVAFLGYWNNPSAT-EKKMAGDWL 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 489188483 403 RTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVVG 371
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-469 |
5.16e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 122.93 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 48 RAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAG----HVSVPLYPNLTAESARQVLEHSESAVVFV-GKLDDwpA 122
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLAdAGAAD--R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 123 MAPGVPE-GIPTVAMplhpegRFDRQWSDLqacAPLEGdTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVEL 201
Cdd:cd05922 83 LRDALPAsPDPGTVL------DADGIRAAR---ASAPA-HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 202 FGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL--DTFVEDMKRARPTLLFGVPRIWtkfqmgvyskmpaQK 279
Cdd:cd05922 153 LGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVldDAFWEDLREHGATGLAGVPSTY-------------AM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 280 LDRLLKLPIlgrivgrkvlaglGLDAVRYALCGAAPVPEALLLWYRRL--GLDVLEVYGMTENSGYSHVCRPGR--QKTG 355
Cdd:cd05922 220 LTRLGFDPA-------------KLPSLRYLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTYLPPERilEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 356 WIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEI 425
Cdd:cd05922 287 SIGLAIPGGEFEILDDdgtptppgepGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRM 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489188483 426 FKTSkGKYVAPAPIENRLAVHDRIEQVCVVGEG--LSAPLGLCVLS 469
Cdd:cd05922 367 IKLF-GNRISPTEIEAAARSIGLIIEAAAVGLPdpLGEKLALFVTA 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
8-456 |
7.73e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 123.60 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 8 PLEVFFER-EKRHPQRRYLvQPIGggrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGH 86
Cdd:PRK06710 25 PLHKYVEQmASRYPEKKAL-HFLG----KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 87 VSV---PLY------------------------PNLTAESARQVLEHsesavVFVGKLDDW---PA--MAPGVPEGIPTV 134
Cdd:PRK06710 100 IVVqtnPLYtereleyqlhdsgakvilcldlvfPRVTNVQSATKIEH-----VIVTRIADFlpfPKnlLYPFVQKKQSNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 135 AMPLHpEGRFDRQWSDLQACAPLEGDTPTAAEQ-LATLIYTSGTTGVPKGVMHNFSSFAFAASRGVE-LFGTRE-DDRML 211
Cdd:PRK06710 175 VVKVS-ESETIHLWNSVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEgEEVVL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 212 SYLPLCHVAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKRARPTLLFGVPRIWTKfqmgvyskmpaqkldrLLKLPIL 289
Cdd:PRK06710 254 GVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDmkMVFEAIKKHKVTLFPGAPTIYIA----------------LLNSPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 290 GRivgrkvlagLGLDAVRYALCGAAPVPEALLLWYRRL-GLDVLEVYGMTENSGYSHVCRPGRQKT-GWIGQNSPGVEVR 367
Cdd:PRK06710 318 KE---------YDISSIRACISGSAPLPVEVQEKFETVtGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 368 I-----------SDEGEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAP 436
Cdd:PRK06710 389 ImsletgealppGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVAS-GFNVYP 466
|
490 500
....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVG 456
Cdd:PRK06710 467 REVEEVLYEHEKVQEVVTIG 486
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
36-456 |
2.45e-29 |
|
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: 121.25 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG 115
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 KLDDWPAMapgVPEGIPTvamplhpegrFDRQWsdlqacaplegdtPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAA 195
Cdd:cd12118 109 REFEYEDL---LAEGDPD----------FEWIP-------------PADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 196 SRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDTFVED-MKRARPTLLFGVPriwTKFQMGVYSK 274
Cdd:cd12118 163 LANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLRKVDAKAIYDlIEKHKVTHFCGAP---TVLNMLANAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 275 MPAQKldrllklPILGRIVGrkvlaglgldavryaLCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVC--RP--- 349
Cdd:cd12118 240 PSDAR-------PLPHRVHV---------------MTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATVCawKPewd 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 350 -----------GRQKTGWIGQNspGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDK 407
Cdd:cd12118 298 elpteerarlkARQGVRYVGLE--EVDVLDPETmkpvprdgktiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDL 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489188483 408 GEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd12118 375 AVIHPDGYIEIKDRSKDII-ISGGENISSVEVEGVLYKHPAVLEAAVVA 422
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
17-506 |
2.61e-29 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 122.29 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQPIGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKN-CAHWIVTdLAiwmAGHVSVPLYPNL 95
Cdd:PRK08180 50 QEAPDRVFLAERGADGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNsIEHALLA-LA---AMYAGVPYAPVS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 96 TAESA--------RQVLEHSESAVVFVgklDDWPAMAPG----VPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEG-DTP 162
Cdd:PRK08180 126 PAYSLvsqdfgklRHVLELLTPGLVFA---DDGAAFARAlaavVPADVEVVAVRGAVPGRAATPFAALLATPPTAAvDAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 163 TAA---EQLATLIYTSGTTGVPKGVMH---NFSSFAfAASRGVELFGTREDDRMLSYLPLCHVA------ERMFVEMGSL 230
Cdd:PRK08180 203 HAAvgpDTIAKFLFTSGSTGLPKAVINthrMLCANQ-QMLAQTFPFLAEEPPVLVDWLPWNHTFggnhnlGIVLYNGGTL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 231 Y--GGTTVffAESLDTFVEDMKRARPTLLFGVPRIWTKFqmgvyskMPAQKLDRLLKLPILGRIvgrKVL----AGLG-- 302
Cdd:PRK08180 282 YidDGKPT--PGGFDETLRNLREISPTVYFNVPKGWEML-------VPALERDAALRRRFFSRL---KLLfyagAALSqd 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 303 ----LDAVRYALCGAAPVpealllwyrrlgldVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDEG---EVQ 375
Cdd:PRK08180 350 vwdrLDRVAEATCGERIR--------------MMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGgklEVR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 376 VRSGATMVGYYKEPEKTAEVLTADGFLRTGDKG----EQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENRL--AVHDRI 449
Cdd:PRK08180 416 VKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVrfvdPADPERGLMFDGRIAEDFKLSSGTWVSVGPLRARAvsAGAPLV 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489188483 450 EQVCVVGEG-----------------LSAPLGLCVLSEVGRREALngtRGALESSLRAHLEQVNGALDKHERLV 506
Cdd:PRK08180 496 QDVVITGHDrdeigllvfpnldacrrLAGLLADASLAEVLAHPAV---RAAFRERLARLNAQATGSSTRVARAL 566
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
15-454 |
2.71e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 121.79 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 15 REKRHPQRRYLVqpIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPN 94
Cdd:PRK06155 30 QAERYPDRPLLV--FGG---TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 95 LTAESARQVLEHSESAVVFVgklddwpaMAPGVP--EGIPTVAMPLH--------PEGRFDRQWSDL---QACAPLEGDT 161
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVV--------EAALLAalEAADPGDLPLPavwlldapASVSVPAGWSTAplpPLDAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 PTAAEQLATLiYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHV-AERMFVEmgSLYGGTTVFFAE 240
Cdd:PRK06155 177 VQPGDTAAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTnALNAFFQ--ALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 241 --SLDTFVEDMKRARPTLLFgvpriwtkfqmgVYSKMpaqkldrllkLPILgriVGRKVLAGLGLDAVRYALCGAapVPE 318
Cdd:PRK06155 254 rfSASGFWPAVRRHGATVTY------------LLGAM----------VSIL---LSQPARESDRAHRVRVALGPG--VPA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 319 ALLLWYR-RLGLDVLEVYGMTENSGYSHVcRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRS---GATMVG 384
Cdd:PRK06155 307 ALHAAFReRFGVDLLDGYGSTETNFVIAV-THGSQRPGSMGRLAPGFEARVVDEhdqelpdgepGELLLRAdepFAFATG 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 385 YYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCV 454
Cdd:PRK06155 386 YFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAAAAV 453
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
14-434 |
3.04e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 122.08 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 14 EREKRHPQRRYLVQPIGGGRV-EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNC-AHWIVTdLAIWMAGHVSVPL 91
Cdd:PRK12582 57 KWAAEAPDRPWLAQREPGHGQwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSiEHALMT-LAAMQAGVPAAPV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESA-----RQVLEHSESAVVFVgklDDWPAMAPGVPE----GIPTVAMPLHPEGRFDRQWSDLqACAPLEGDTP 162
Cdd:PRK12582 136 SPAYSLMSHdhaklKHLFDLVKPRVVFA---QSGAPFARALAAldllDVTVVHVTGPGEGIASIAFADL-AATPPTAAVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 163 TAAEQL-----ATLIYTSGTTGVPKGVMHNFSSFAfAASRGVELFGTREDDR----MLSYLPLCHVAERMFVEMGSLYGG 233
Cdd:PRK12582 212 AAIAAItpdtvAKYLFTSGSTGMPKAVINTQRMMC-ANIAMQEQLRPREPDPpppvSLDWMPWNHTMGGNANFNGLLWGG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 234 TTVFF------AESLDTFVEDMKRARPTLLFGVPRIWTkfqmgvyskMPAQKLDrllKLPILGRIVGRKvlaglgLDAVR 307
Cdd:PRK12582 291 GTLYIddgkplPGMFEETIRNLREISPTVYGNVPAGYA---------MLAEAME---KDDALRRSFFKN------LRLMA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 308 YalcGAAPVPEALllWYRRLGLDVLEV---------YGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVR---ISDEGEVQ 375
Cdd:PRK12582 353 Y---GGATLSDDL--YERMQALAVRTTghripfytgYGATETAPTTTGTHWDTERVGLIGLPLPGVELKlapVGDKYEVR 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489188483 376 VRSGATMVGYYKEPEKTAEVLTADGFLRTGDKG----EQDAEGNLRLTGRMKEIFKTSKGKYV 434
Cdd:PRK12582 428 VKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAArfvdPDDPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
10-456 |
3.94e-29 |
|
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: 121.02 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVqpiGGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:COG1021 29 DLLRRRAERHPDRIAVV---DGER--RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSE-SAVVFVGKLD--DWPAMAPGVPEGIPTVAMPL-HPEGRFDRQWSDLQAcAPLEGDTP-TA 164
Cdd:COG1021 104 FALPAHRRAEISHFAEQSEaVAYIIPDRHRgfDYRALARELQAEVPSLRHVLvVGDAGEFTSLDALLA-APADLSEPrPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 AEQLATLIYTSGTTGVPKGV--MHNfsSFAFAASRGVELFGTREDDRMLSYLPLCH--------VaermfveMGSLYGGT 234
Cdd:COG1021 183 PDDVAFFQLSGGTTGLPKLIprTHD--DYLYSVRASAEICGLDADTVYLAALPAAHnfplsspgV-------LGVLYAGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 235 TVFFAE--SLDTFVEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPilgrivgrkvLAGLGLDAV---RYA 309
Cdd:COG1021 254 TVVLAPdpSPDTAFPLIERERVTVTALVP-------------------------P----------LALLWLDAAersRYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 310 L-------CGAAPVPEALLlwyRR----LGLDVLEVYGMTEnsGYSHVCRP-----------GRQktgwIgqnSPGVEVR 367
Cdd:COG1021 299 LsslrvlqVGGAKLSPELA---RRvrpaLGCTLQQVFGMAE--GLVNYTRLddpeevilttqGRP----I---SPDDEVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 368 ISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKE-IFKTskGKYVAP 436
Cdd:COG1021 367 IVDEdgnpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDqINRG--GEKIAA 444
|
490 500
....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVG 456
Cdd:COG1021 445 EEVENLLLAHPAVHDAAVVA 464
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-455 |
8.74e-29 |
|
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: 118.89 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVqpiGGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:cd05945 2 AANPDRPAVV---EGGR--TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSESAVVFVgklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplEGDtptaaeQLATLIYTSG 176
Cdd:cd05945 77 AERIREILDAAKPALLIA-------------------------------------------DGD------DNAYIIFTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 177 TTGVPKGVMH---NFSSFAFAAsrgVELFGTREDDRMLSYLPLChvaermF-VEMGSLY-----GGTTVFFAESLDTFVE 247
Cdd:cd05945 108 STGRPKGVQIshdNLVSFTNWM---LSDFPLGPGDVFLNQAPFS------FdLSVMDLYpalasGATLVPVPRDATADPK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 248 DMKRARP----TLLFGVPRIWtkfqmgvyskmpaqklDRLLKLPilgrivgrkVLAGLGLDAVRYAL-CGAA-PVPEALL 321
Cdd:cd05945 179 QLFRFLAehgiTVWVSTPSFA----------------AMCLLSP---------TFTPESLPSLRHFLfCGEVlPHKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 322 LWYRRLGLDVLEVYGMTENSG---YSHVCRP--GRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYY 386
Cdd:cd05945 234 LQQRFPDARIYNTYGPTEATVavtYIEVTPEvlDGYDRLPIGYAKPGAKLVILDEdgrpvppgekGELVISGPSVSKGYL 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 387 KEPEKTAEVL-TADGFL--RTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd05945 314 NNPEKTAAAFfPDEGQRayRTGDLVRLEADGLLFYRGRLDFQVKLN-GYRIELEEIEAALRQVPGVKEAVVV 384
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
29-488 |
9.13e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 120.23 E-value: 9.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 29 IGGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:PRK06164 30 IDEDRP--LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVV----------FVGKLDDW-PAMAPGVPeGIPTV-----AMPLHPEGRfDRQWSDLQACAPLEGDTPTAAEQ--LAT 170
Cdd:PRK06164 108 ARWLvvwpgfkgidFAAILAAVpPDALPPLR-AIAVVddaadATPAPAPGA-RVQLFALPDPAPPAAAGERAADPdaGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTVFFAESLDT--FVED 248
Cdd:PRK06164 186 LFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAPLVCEPVFDAarTARA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 249 MKRARPTLLFGvpriwtkfqmgvyskmPAQKLDRLLKlpilgrivgrkvLAGLGLDAVRYALCGAA---PVPEALLLWYR 325
Cdd:PRK06164 265 LRRHRVTHTFG----------------NDEMLRRILD------------TAGERADFPSARLFGFAsfaPALGELAALAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 326 RLGLDVLEVYGMTE----------NSGYSHVCRPGrqktGWIGqnSPGVEVRISD-----------EGEVQVRSGATMVG 384
Cdd:PRK06164 317 ARGVPLTGLYGSSEvqalvalqpaTDPVSVRIEGG----GRPA--SPEARVRARDpqdgallpdgeSGEIEIRAPSLMRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 385 YYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG---EGLSA 461
Cdd:PRK06164 391 YLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGatrDGKTV 469
|
490 500
....*....|....*....|....*..
gi 489188483 462 PLGLcVLSEVGRREALNGTRGALESSL 488
Cdd:PRK06164 470 PVAF-VIPTDGASPDEAGLMAACREAL 495
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
17-456 |
9.90e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 119.53 E-value: 9.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQPIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:PRK09088 6 RLQPQRLAAVDLALG---RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSESAVVfVGklDDWPAMAPGVPEGIptvamplhpegrfdrqwSDLQACAPLEGDTPTAA---EQLATLIY 173
Cdd:PRK09088 83 ASELDALLQDAEPRLL-LG--DDAVAAGRTDVEDL-----------------AAFIASADALEPADTPSippERVSLILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 174 TSGTTGVPKGVM----------HNFSSFAFAASRGVELFGTreddrmlsylPLCHVAERMFVEMGSLYGGTTVFFAESLD 243
Cdd:PRK09088 143 TSGTSGQPKGVMlsernlqqtaHNFGVLGRVDAHSSFLCDA----------PMFHIIGLITSVRPVLAVGGSILVSNGFE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 244 TFVEDMKRARPTL----LFGVPRIwtkfqMGVYSKMPAQKLDRLLKLPILgrivgrkvlaglgldavryaLCGAAPVPEA 319
Cdd:PRK09088 213 PKRTLGRLGDPALgithYFCVPQM-----AQAFRAQPGFDAAALRHLTAL--------------------FTGGAPHAAE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 320 LLLWYRRLGLDVLEVYGMTENS---GYSHVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYY 386
Cdd:PRK09088 268 DILGWLDDGIPMVDGFGMSEAGtvfGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDqgndcpagvpGELLLRGPNLSPGYW 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 387 KEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK09088 348 RRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
37-456 |
1.19e-28 |
|
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: 118.76 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVgk 116
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpamapgvpegiptvamplHPEgRFDRqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd05969 79 ----------------------TEE-LYER----------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLsylplcHVAERMFVeMGSLYG-------GTTVFFAE---SLDTFVEDMKRARPTLLFGVPriwTK 266
Cdd:cd05969 120 TGKYVLDLHPDDIYW------CTADPGWV-TGTVYGiwapwlnGVTNVVYEgrfDAESWYGIIERVKVTVWYTAP---TA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 267 FQMgvyskmpaqkldrLLKLpilgrivGRKVLAGLGLDAVRYALCGAAPV-PEALLLWYRRLGLDVLEVYGMTENSGY-- 343
Cdd:cd05969 190 IRM-------------LMKE-------GDELARKYDLSSLRFIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETGSImi 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 344 -SHVCRPgrQKTGWIGQNSPGVEVRISDE----------GEVQVRSG--ATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQ 410
Cdd:cd05969 250 aNYPCMP--IKPGSMGKPLPGVKAAVVDEngnelppgtkGILALKPGwpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYR 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 489188483 411 DAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05969 327 DEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEHPAVAEAGVIG 371
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
61-479 |
2.14e-28 |
|
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: 118.59 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 61 GSRIAIISKNCAHWIVTDLAIWMAGHVSVPLypNLTAeSARQV--------LEHSESAVVFVGKLDDWPAMAP------- 125
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVML--NYTA-GLRELraciklagIKTVLTSKQFIEKLKLHHLFDVeydariv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 126 ---------GVPEGIPTVAmplhpEGRFDRQWSDLQacaplEGDTPTAAEQLATLIYTSGTTGVPKGVM---HNFSSFAF 193
Cdd:cd05909 108 yledlrakiSKADKCKAFL-----AGKFPPKWLLRI-----FGVAPVQPDDPAVILFTSGSEGLPKGVVlshKNLLANVE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 194 AASRGVELfgtREDDRMLSYLPLCHVaermFVEMGSLY-----GGTTVFFAESLD--TFVEDMKRARPTLLFGVP---RI 263
Cdd:cd05909 178 QITAIFDP---NPEDVVFGALPFFHS----FGLTGCLWlpllsGIKVVFHPNPLDykKIPELIYDKKATILLGTPtflRG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 264 WTKFqmgvyskmpAQKLDrllklpilgrivgrkvLAGLgldavRYALCGAAPVPEALL-LWYRRLGLDVLEVYGMTENSG 342
Cdd:cd05909 251 YARA---------AHPED----------------FSSL-----RLVVAGAEKLKDTLRqEFQEKFGIRILEGYGTTECSP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 343 YSHVCRPGR-QKTGWIGQNSPGVEVRI-----------SDEGEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQ 410
Cdd:cd05909 301 VISVNTPQSpNKEGTVGRPLPGMEVKIvsvetheevpiGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489188483 411 DAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVV--------GEGLSaplgLCVLSEVGRREALNG 479
Cdd:cd05909 380 DGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPEDNEVAVvsvpdgrkGEKIV----LLTTTTDTDPSSLND 451
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
168-457 |
5.52e-28 |
|
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: 115.27 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 168 LATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL----- 242
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAgyrnp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 ---DTFVEDMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPIlgrivgrkvlaGLGLDAVRYALCGAAPVPEA 319
Cdd:cd05944 84 glfDNFWKLVERYRITSLSTVPTV----------------YAALLQVPV-----------NADISSLRFAMSGAAPLPVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 320 LLLWYR-RLGLDVLEVYGMTENSGYSHVCRPGR-QKTGWIGQNSPGVEVRI---SDEGEVQVRSGATMVG--YYKEP--- 389
Cdd:cd05944 137 LRARFEdATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIkvlDGVGRLLRDCAPDEVGeiCVAGPgvf 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489188483 390 ------EKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:cd05944 217 ggylytEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
10-455 |
8.57e-28 |
|
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: 118.81 E-value: 8.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVqpiGGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:COG1020 480 ELFEAQAARTPDAVAVV---FGDQ--SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVfvgkLDDwPAMAPGVPE-GIPTVAMPlhpegrfDRQWSDLQACAPlegDTPTAAEQL 168
Cdd:COG1020 555 PLDPAYPAERLAYMLEDAGARLV----LTQ-SALAARLPElGVPVLALD-------ALALAAEPATNP---PVPVTPDDL 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVM---HNFSSFAFAASRgveLFGTREDDRMLSYLPLCH---VAErMFveMGSLYGGTTVFFAE-- 240
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMvehRALVNLLAWMQR---RYGLGPGDRVLQFASLSFdasVWE-IF--GALLSGATLVLAPPea 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 241 --SLDTFVEDMKRARPTLLFGVPriwtkfqmGVYSKMPAQKLDRLLKLpilgrivgrkvlaglgldavRYALCGAAPVPE 318
Cdd:COG1020 694 rrDPAALAELLARHRVTVLNLTP--------SLLRALLDAAPEALPSL--------------------RLVLVGGEALPP 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 319 ALL-LWYRRL-GLDVLEVYGMTENSGYS--HVCRPGRQKTGW--IGQNSPGVEVRISDE----------GE-----VQV- 376
Cdd:COG1020 746 ELVrRWRARLpGARLVNLYGPTETTVDStyYEVTPPDADGGSvpIGRPIANTRVYVLDAhlqpvpvgvpGElyiggAGLa 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 377 RsgatmvGYYKEPEKTAEVLTADGFL-------RTGDKGEQDAEGNLRLTGRM----KeIfktsKGKYVAPAPIENRLAV 445
Cdd:COG1020 826 R------GYLNRPELTAERFVADPFGfpgarlyRTGDLARWLPDGNLEFLGRAddqvK-I----RGFRIELGEIEAALLQ 894
|
490
....*....|
gi 489188483 446 HDRIEQVCVV 455
Cdd:COG1020 895 HPGVREAVVV 904
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
30-489 |
9.43e-28 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 117.19 E-value: 9.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 30 GGGRVEELSWGEVGDQARRAAAWLR-SLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 S------------------------AVVFVGKlDDWPAMAPGVPEGIPTVAMPLHPEGR---FDrqWSDLqacaplEGDT 161
Cdd:PRK05620 112 DevivadprlaeqlgeilkecpcvrAVVFIGP-SDADSAAAHMPEGIKVYSYEALLDGRstvYD--WPEL------DETT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 PTAaeqlatLIYTSGTTGVPKGVMHNFSSFAFAAS--RGVELFGTREDDRMLSYLPLCHVAErMFVEMGSLYGGTTVFF- 238
Cdd:PRK05620 183 AAA------ICYSTGTTGAPKGVVYSHRSLYLQSLslRTTDSLAVTHGESFLCCVPIYHVLS-WGVPLAAFMSGTPLVFp 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 239 -----AESLDTFVEDmkrARPTLLFGVPRIWTKFqMGVYSKMPAQKLdrllklpilgrivgrkvlaglgldAVRYALCGA 313
Cdd:PRK05620 256 gpdlsAPTLAKIIAT---AMPRVAHGVPTLWIQL-MVHYLKNPPERM------------------------SLQEIYVGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 314 APVPEALL-LWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTG---WIGQNSPG-----VEVRISD-----------EGE 373
Cdd:PRK05620 308 SAVPPILIkAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGearWAYRVSQGrfpasLEYRIVNdgqvmestdrnEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMVGYYKEP----------------EKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPA 437
Cdd:PRK05620 388 IQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSA 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 438 PIENRLAVHDRIEQVCVVG----EGLSAPLGLCVLSEVGRREALNGTRgaLESSLR 489
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGypddKWGERPLAVTVLAPGIEPTRETAER--LRDQLR 520
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
38-455 |
2.40e-27 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 115.85 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 38 SWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPN-LTAESARQVlEHSESAVVFVGK 116
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTaLESEIKKQA-EAAGAKLIVTND 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 LDDWPAMAPGVP-----EGIPTVAMplhpegrfdrQWSDLQACAPLEGDTPTAAEQLAT----LIYTSGTTGVPKGVM-- 185
Cdd:PLN02330 136 TNYGKVKGLGLPvivlgEEKIEGAV----------NWKELLEAADRAGDTSDNEEILQTdlcaLPFSSGTTGISKGVMlt 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 186 H-----NFSSFAFaaSRGVELFGTREddrMLSYLPLCHVaermfvemgslYGGTTVFFAE-------------SLDTFVE 247
Cdd:PLN02330 206 HrnlvaNLCSSLF--SVGPEMIGQVV---TLGLIPFFHI-----------YGITGICCATlrnkgkvvvmsrfELRTFLN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 248 DMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPIlgriVGRKVLAGLGLDAVRYAlcgAAPV-PEALLLWYRR 326
Cdd:PLN02330 270 ALITQEVSFAPIVPPI----------------ILNLVKNPI----VEEFDLSKLKLQAIMTA---AAPLaPELLTAFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 L-GLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNS-----PGVEVRISD-----------EGEVQVRSGATMVGYYKEP 389
Cdd:PLN02330 327 FpGVQVQEAYGLTEHSCITLTHGDPEKGHGIAKKNSvgfilPNLEVKFIDpdtgrslpkntPGELCVRSQCVMQGYYNNK 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 390 EKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:PLN02330 407 EETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAVV 471
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
19-542 |
5.09e-27 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 114.90 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 19 HPQRRYLVQPIGGGRVEELSwgEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAE 98
Cdd:PLN02860 17 ATLRGNAVVTISGNRRRTGH--EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 99 SARQVLEHSE-SAVVFVGKLDDWPAmaPGVPEGIPTVAMPL---HPEGRFDRQWSDL--------QACAPLEGDTPTAAE 166
Cdd:PLN02860 95 EAKSAMLLVRpVMLVTDETCSSWYE--ELQNDRLPSLMWQVfleSPSSSVFIFLNSFlttemlkqRALGTTELDYAWAPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHV---AERMFVEMgslYGGTTVF---FAE 240
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIgglSSALAMLM---VGACHVLlpkFDA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 241 SLdtFVEDMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKlpilgriVGRKVLAGLGLDAVRYALCGAAPVPEAL 320
Cdd:PLN02860 250 KA--ALQAIKQHNVTSMITVPAM----------------MADLIS-------LTRKSMTWKVFPSVRKILNGGGSLSSRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 321 LLWYRRL--GLDVLEVYGMTENSG-------YSHVCRPGRQKTGW----------------IGQNSPGVEVRI-----SD 370
Cdd:PLN02860 305 LPDAKKLfpNAKLFSAYGMTEACSsltfmtlHDPTLESPKQTLQTvnqtksssvhqpqgvcVGKPAPHVELKIgldesSR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 371 EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIE 450
Cdd:PLN02860 385 VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTG-GENVYPEEVEAVLSQHPGVA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 451 QVCVVG---EGLSAPLGLCVLSEVG------RREALNGTRGALESSLRAHLEQVNGALDKHERLvgLVLVQETWAvdngf 521
Cdd:PLN02860 464 SVVVVGvpdSRLTEMVVACVRLRDGwiwsdnEKENAKKNLTLSSETLRHHCREKNLSRFKIPKL--FVQWRKPFP----- 536
|
570 580
....*....|....*....|.
gi 489188483 522 LTPTLKIKRNMVEGAYGSRFH 542
Cdd:PLN02860 537 LTTTGKIRRDEVRREVLSHLQ 557
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
37-492 |
9.08e-27 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 114.11 E-value: 9.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF--- 113
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVtss 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 --VGKLDDWPAMAPG----VPEGIPTVAMPLHPEGRFDRqWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHN 187
Cdd:TIGR03098 106 erLDLLHPALPGCHDlrtlIIVGDPAHASEGHPGEEPAS-WPKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 188 FSSFAFAASRGVELFGTREDDRMLSYLPLCHVAErmFVEMGS-LYGGTTVFFAESL--DTFVEDMKRARPTLLFGVPRIW 264
Cdd:TIGR03098 185 HRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG--FNQLTTaFYVGATVVLHDYLlpRDVLKALEKHGITGLAAVPPLW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 TK-FQMgvysKMPAQKLDRLLKLPILGRIVGRKVLAglgldAVRYALcgaapvPEAlllwyrrlglDVLEVYGMTE--NS 341
Cdd:TIGR03098 263 AQlAQL----DWPESAAPSLRYLTNSGGAMPRATLS-----RLRSFL------PNA----------RLFLMYGLTEafRS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSHVCRPGRqKTGWIGQNSPGVEVRI----------SDEGEVQVRSGATMVGYYKEPEKTAEVL-TADGF--------- 401
Cdd:TIGR03098 318 TYLPPEEVDR-RPDSIGKAIPNAEVLVlredgsecapGEEGELVHRGALVAMGYWNDPEKTAERFrPLPPFpgelhlpel 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 402 -LRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVgeGLSAP-LGLCVLSEVGRREALNG 479
Cdd:TIGR03098 397 aVWSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVAYATGLVAEAVAF--GVPDPtLGQAIVLVVTPPGGEEL 473
|
490
....*....|...
gi 489188483 480 TRGALESSLRAHL 492
Cdd:TIGR03098 474 DRAALLAECRARL 486
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
50-456 |
1.81e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 113.06 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 50 AAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV---GKLDDWPAMAPG 126
Cdd:PRK05852 57 AGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIdadGPHDRAEPTTRW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 127 VPEGIPTVAMPLHPEGRFDrqwSDLQACAPLEGDTpTAAEQL----ATLIYTSGTTGVPKGV---MHNFSSFAFAASRGV 199
Cdd:PRK05852 137 WPLTVNVGGDSGPSGGTLS---VHLDAATEPTPAT-STPEGLrpddAMIMFTGGTTGLPKMVpwtHANIASSVRAIITGY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 200 ELfGTRedDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE----SLDTFVEDMKRARPTLLFGVPRIwtkFQMgvyskm 275
Cdd:PRK05852 213 RL-SPR--DATVAVMPLYHGHGLIAALLATLASGGAVLLPArgrfSAHTFWDDIKAVGATWYTAVPTI---HQI------ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 276 paqkldrLLKLPilgrivgRKVLAGLGLDAVRYALCGAAPV-PEALLLWYRRLGLDVLEVYGMTENS---------GYSH 345
Cdd:PRK05852 281 -------LLERA-------ATEPSGRKPAALRFIRSCSAPLtAETAQALQTEFAAPVVCAFGMTEAThqvtttqieGIGQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 346 VCRPgRQKTGWIGQnSPGVEVRI--SD--------EGEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGN 415
Cdd:PRK05852 347 TENP-VVSTGLVGR-STGAQIRIvgSDglplpagaVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGD 423
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489188483 416 LRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK05852 424 LSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFG 463
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
37-456 |
1.83e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 113.19 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV---PLYP-------------------- 93
Cdd:PRK07059 49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVnvnPLYTprelehqlkdsgaeaivvle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 94 NLtAESARQVLEHSESAVVFVGKLDDWPAM--------APGVPEGIPTVAMPLHPegRFDrqwSDLQACAPLEGDTPT-A 164
Cdd:PRK07059 129 NF-ATTVQQVLAKTAVKHVVVASMGDLLGFkghivnfvVRRVKKMVPAWSLPGHV--RFN---DALAEGARQTFKPVKlG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 AEQLATLIYTSGTTGVPKGV-------------MHNFSSFAFAASRGVELFGTreddrmLSYLPLCHV-AERMFVEMGSL 230
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGAtllhrnivanvlqMEAWLQPAFEKKPRPDQLNF------VCALPLYHIfALTVCGLLGMR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 231 YGGTTVFFAESLDT--FVEDMKRARPTLLFGVPRIWTkfqmGVYSKMPAQKLDrLLKLpilgrivgrKVLAGLGLdAVRy 308
Cdd:PRK07059 277 TGGRNILIPNPRDIpgFIKELKKYQVHIFPAVNTLYN----ALLNNPDFDKLD-FSKL---------IVANGGGM-AVQ- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 309 alcgaAPVPEAlllWYRRLGLDVLEVYGMTENSGySHVCRP--GRQKTGWIGQNSPGVEVRISDE----------GEVQV 376
Cdd:PRK07059 341 -----RPVAER---WLEMTGCPITEGYGLSETSP-VATCNPvdATEFSGTIGLPLPSTEVSIRDDdgndlplgepGEICI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 377 RSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07059 412 RGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVS-GFNVYPNEIEEVVASHPGVLEVAAVG 490
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
32-425 |
2.05e-26 |
|
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: 113.15 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVtdlAIW---MAGHVSVPL-------YPNLTAESAR 101
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIP---AFWacvLAGFVPAPLtvpptydEPNARLRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 102 QVLEHSESAVVFVGklddwPAMAPGVpEGIPTVAmpLHPEGRFDrQWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVP 181
Cdd:cd05906 112 HIWQLLGSPVVLTD-----AELVAEF-AGLETLS--GLPGIRVL-SIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 182 KGVMHNFSSFaFAASRGVE-LFGTREDDRMLSYLPLCHVAERMFVEMGSLYGG-------TTVFFAESLdTFVEDMKRAR 253
Cdd:cd05906 183 KAVPLTHRNI-LARSAGKIqHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGcqqvhvpTEEILADPL-RWLDLIDRYR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 254 PTLLFGvPriwtKFqmgVYSKMpaqkLDRLLKLPilgrivGRKVLaglgLDAVRYALCGA----APVPEALLLWYRRLGL 329
Cdd:cd05906 261 VTITWA-P----NF---AFALL----NDLLEEIE------DGTWD----LSSLRYLVNAGeavvAKTIRRLLRLLEPYGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 330 --DVLE-VYGMTEN-SG--YSHVCRPGRQKTGW----IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEP 389
Cdd:cd05906 319 ppDAIRpAFGMTETcSGviYSRSFPTYDHSQALefvsLGRPIPGVSMRIVDDegqllpegevGRLQVRGPVVTKGYYNNP 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 489188483 390 EKTAEVLTADGFLRTGDKGEQDaEGNLRLTGRMKEI 425
Cdd:cd05906 399 EANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTKDT 433
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
4-422 |
2.42e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 114.25 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPL-EVFFEREKRHPQRRYLVQPIGGgrveELSwgevGDQARRAAAWLRSL---DLPAGSRIAIISKNCAHWIVTDL 79
Cdd:PRK08633 612 EALPPLaEAWIDTAKRNWSRLAVADSTGG----ELS----YGKALTGALALARLlkrELKDEENVGILLPPSVAGALANL 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 80 AIWMAGHVSVPLypNLTAESA--RQVLEHSESAVV-----FVGKLDDwPAMAPGVPEGIPTVAMplhpE------GRFDR 146
Cdd:PRK08633 684 ALLLAGKVPVNL--NYTASEAalKSAIEQAQIKTVitsrkFLEKLKN-KGFDLELPENVKVIYL----EdlkakiSKVDK 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 147 QWSDLQA--------CAPLEGdtPTAAEQLATLIYTSGTTGVPKGVM---HNFSSFAFAASrgvELFGTREDDRMLSYLP 215
Cdd:PRK08633 757 LTALLAArllparllKRLYGP--TFKPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQIS---DVFNLRNDDVILSSLP 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 216 LCHvaermfvemgSL-YGGTT----------VFFAESLDTF-VEDM-KRARPTLLFGVPriwTKFQMgvYSKMP-AQKLD 281
Cdd:PRK08633 832 FFH----------SFgLTVTLwlpllegikvVYHPDPTDALgIAKLvAKHRATILLGTP---TFLRL--YLRNKkLHPLM 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 282 rllklpilgrivgrkvlaglgLDAVRYALCGAAPVPEALLLWYR-RLGLDVLEVYGMTENSGYSHVCRP-------GRQ- 352
Cdd:PRK08633 897 ---------------------FASLRLVVAGAEKLKPEVADAFEeKFGIRILEGYGATETSPVASVNLPdvlaadfKRQt 955
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 353 --KTGWIGQNSPGVEVRISD-----------EGEVQVRSGATMVGYYKEPEKTAEVLT---ADGFLRTGDKGEQDAEGNL 416
Cdd:PRK08633 956 gsKEGSVGMPLPGVAVRIVDpetfeelppgeDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFL 1035
|
....*.
gi 489188483 417 RLTGRM 422
Cdd:PRK08633 1036 TITDRY 1041
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
37-456 |
4.94e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 111.79 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGk 116
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTE- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwPAMAP---GVPEGIPTVAMPLHPEGR-------FDRQWSDLQACAP---LEGDTPtaaeqlATLIYTSGTTGVPKG 183
Cdd:PRK07786 122 ----AALAPvatAVRDIVPLLSTVVVAGGSsddsvlgYEDLLAEAGPAHApvdIPNDSP------ALIMYTSGTTGRPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 184 VM--H-NFSSFAFAASRGVELFgtREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFF---AESLDTFVEDMKRARPTLL 257
Cdd:PRK07786 192 AVltHaNLTGQAMTCLRTNGAD--INSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYplgAFDPGQLLDVLEAEKVTGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 258 FGVPRIWTkfqmgvySKMPAQKLD-RLLKLPILGrivgrkvlaglgldavryalCGAAPVPEALLlwyRRL-----GLDV 331
Cdd:PRK07786 270 FLVPAQWQ-------AVCAEQQARpRDLALRVLS--------------------WGAAPASDTLL---RQMaatfpEAQI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 332 LEVYGMTENSGYSHVC--RPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLtAD 399
Cdd:PRK07786 320 LAAFGQTEMSPVTCMLlgEDAIRKLGSVGKVIPTVAARVVDEnmndvpvgevGEIVYRAPTLMSGYWNNPEATAEAF-AG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489188483 400 GFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07786 399 GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIG 454
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
10-492 |
7.50e-26 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 110.83 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVqpiGGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:cd17646 2 ALVAEQAARTPDAPAVV---DEGR--TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVfvgkLDDWPAMAPGVPEGIPTVAMplhpegrfDRQWSDLQACAPLEgdtPTAAEQLA 169
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVV----LTTADLAARLPAGGDVALLG--------DEALAAPPATPPLV---PPRPDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 TLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPL---CHVAErMFVEMGSlygGTTVFFAE-----S 241
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsfdVSVWE-LFWPLVA---GARLVVARpgghrD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 LDTFVEDMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPILGRivgrkvlaglgLDAVRYALCGAAPVPEALL 321
Cdd:cd17646 218 PAYLAALIREHGVTTCHFVPSM----------------LRVFLAEPAAGS-----------CASLRRVFCSGEALPPELA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 322 -LWYRRLGLDVLEVYGMTENS-GYSHV-CRPGRQKTGW-IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYK 387
Cdd:cd17646 271 aRFLALPGAELHNLYGPTEAAiDVTHWpVRGPAETPSVpIGRPVPNTRLYVLDDalrpvpvgvpGELYLGGVQLARGYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 388 EPEKTAEVLTADGF------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSA 461
Cdd:cd17646 351 RPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPAVTHAVVVARAAPA 429
|
490 500 510
....*....|....*....|....*....|.
gi 489188483 462 PLGLCVLSEVGRREALNGTRGALESSLRAHL 492
Cdd:cd17646 430 GAARLVGYVVPAAGAAGPDTAALRAHLAERL 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
14-456 |
1.83e-25 |
|
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: 109.72 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 14 EREKRHPQRRYLVQpiGGGRveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYP 93
Cdd:cd05920 23 RSAARHPDRIAVVD--GDRR---LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 94 NLTAESARQVLEHSEsAVVFVGK----LDDWPAMAPGVPEGIPTVAMplhpegrfdrqwsdlqacaplegdtptaaeqla 169
Cdd:cd05920 98 SHRRSELSAFCAHAE-AVAYIVPdrhaGFDHRALARELAESIPEVAL--------------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 tLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHvaerMFV-----EMGSLYGGTTVFFAESldt 244
Cdd:cd05920 144 -FLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAH----NFPlacpgVLGTLLAGGRVVLAPD--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 245 fvedmkrARPTLLFgvPRIwTKFQMGVYSKMPAqkldrLLKLPILGRIVGRKVLAGLGLDAVryalcGAAPVPEALLlwy 324
Cdd:cd05920 216 -------PSPDAAF--PLI-EREGVTVTALVPA-----LVSLWLDAAASRRADLSSLRLLQV-----GGARLSPALA--- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 325 RR----LGLDVLEVYGMTEN-SGYSHVCRPGRQKTGWIGQN-SPGVEVRISDE----------GEVQVRSGATMVGYYKE 388
Cdd:cd05920 273 RRvppvLGCTLQQVFGMAEGlLNYTRLDDPDEVIIHTQGRPmSPDDEIRVVDEegnpvppgeeGELLTRGPYTIRGYYRA 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 389 PEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05920 353 PEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAVHDAAVVA 419
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
166-512 |
2.74e-25 |
|
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: 106.96 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 166 EQLATLIYTSGTTGVPKGVMHNFSSFaFAASRGVELFGTR--EDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--S 241
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTF-FAVPDILQKEGLNwvVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEntT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 LDTFVEDMKRARPTLLFGVPRIWTKFqmgVYSKMPAQKLDRLLKLPILG--RIVGRKVlaglgldavryalcgaapvpeA 319
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKL---VSELKSANATVPSLRLIGYGgsRAIAADV---------------------R 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 320 LLLWYRRLglDVLEVYGMTENSgySHVCRP---GRQKTGWIGQNSPGVEVRISD----------EGEVQVRSGATMVGYY 386
Cdd:cd17635 136 FIEATGLT--NTAQVYGLSETG--TALCLPtddDSIEINAVGRPYPGVDVYLAAtdgiagpsasFGTIWIKSPANMLGYW 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 387 KEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIEnRLAVHDRIEQVCVVGEGLSAPLGLC 466
Cdd:cd17635 212 NNPERTAEVLI-DGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVE-RIAEGVSGVQECACYEISDEEFGEL 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489188483 467 VLSEVGRREALNgtrgalESSLRAHLEQVNGALDKHERLVGLVLVQ 512
Cdd:cd17635 289 VGLAVVASAELD------ENAIRALKHTIRRELEPYARPSTIVIVT 328
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-495 |
4.21e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.64 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 13 FERE-KRHPQRRYLVQpigGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:PRK12467 518 IEAQaRQHPERPALVF---GEQV--LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVVFVgklDDWPAMAPGVPEGIPTVAMPLHpegrfDRQWsdlQACAPLEGDTPTAAEQLATL 171
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLT---QSHLLAQLPVPAGLRSLCLDEP-----ADLL---CGYSGHNPEVALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 172 IYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLchvAERMFVEM--GSLYGGTTVFFAE-----SLDT 244
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF---AFDLGVTElfGALASGATLHLLPpdcarDAEA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 245 FVEDMKRARPTLLFGVPRIWtkfQMGVYSKMPAQKLDRllklpilgrivgrkvlaglgldavRYALCGAAPVPEALLLWY 324
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHL---QALLQASRVALPRPQ------------------------RALVCGGEALQVDLLARV 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 325 RRLGLD--VLEVYGMTENSGYSHV--CRPGRQKTGW--IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKE 388
Cdd:PRK12467 792 RALGPGarLINHYGPTETTVGVSTyeLSDEERDFGNvpIGQPLANLGLYILDHylnpvpvgvvGELYIGGAGLARGYHRR 871
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 389 PEKTAEVLTADGF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSA 461
Cdd:PRK12467 872 PALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVLAQPGDA 950
|
490 500 510
....*....|....*....|....*....|....
gi 489188483 462 PLGLcVLSEVGRREALNGTRGALESSLRAHLEQV 495
Cdd:PRK12467 951 GLQL-VAYLVPAAVADGAEHQATRDELKAQLRQV 983
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
17-456 |
7.46e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 108.20 E-value: 7.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQpigGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:PRK07470 18 RRFPDRIALVW---GDRS--WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 -AESArqVLEHSESAVVFVGKlDDWPAMAPGVPEGIPTVAMPLH-PEGRFDRQWSDLQAcAPLEGDTPTAA---EQLATL 171
Cdd:PRK07470 93 pDEVA--YLAEASGARAMICH-ADFPEHAAAVRAASPDLTHVVAiGGARAGLDYEALVA-RHLGARVANAAvdhDDPCWF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 172 IYTSGTTGVPKGVMHNFSSFAFA-ASRGVELF-GTREDDRMLSYLPLCHVAERMFVeMGSLYGGTTVFF-AESLD----- 243
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGQMAFViTNHLADLMpGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLpSERFDpaevw 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 244 TFVEdmkRARPTLLFGVPRIwtkfqmgvyskmpaqkldrlLKLpilgrIVGRKVLAGLGLDAVRYALCGAAPVpealllw 323
Cdd:PRK07470 248 ALVE---RHRVTNLFTVPTI--------------------LKM-----LVEHPAVDRYDHSSLRYVIYAGAPM------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 324 YR--------RLGLDVLEVYGMTENSG-------YSHVCRPGRQ-KTGWIGQNSPGVEVRISDE----------GEVQVR 377
Cdd:PRK07470 293 YRadqkralaKLGKVLVQYFGLGEVTGnitvlppALHDAEDGPDaRIGTCGFERTGMEVQIQDDegrelppgetGEICVI 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 378 SGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07470 373 GPAVFAGYYNNPEANAKAFR-DGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG 449
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
9-457 |
1.69e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 107.40 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 9 LEVFFEREKRHPQRRYLVQPIGggrVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVS 88
Cdd:PRK05857 17 LDRVFEQARQQPEAIALRRCDG---TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 89 VPLYPNLTAESARQVLEHSESAVVFV---GKLDdwpamAPGVPEGIPTVamplhPEGRFDRQWSDLQACAPLEGDTPTA- 164
Cdd:PRK05857 94 VMADGNLPIAAIERFCQITDPAAALVapgSKMA-----SSAVPEALHSI-----PVIAVDIAAVTRESEHSLDAASLAGn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 ----AEQLATLIYTSGTTGVPKGV-MHNFSSFAFA---ASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTV 236
Cdd:PRK05857 164 adqgSEDPLAMIFTSGTTGEPKAVlLANRTFFAVPdilQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 237 FFAE---SLDTFVEDMKRARPTLlfgVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAVRYALCGA 313
Cdd:PRK05857 244 TGGEnttSLLEILTTNAVATTCL---VP-------------------------TLLSKLVSELKSANATVPSLRLVGYGG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 314 APVPEALLLWYRRLGLDVLEVYGMTEnSGYSHVCRP------GRQKTGWIGQNSPGVEVRISDE---------------- 371
Cdd:PRK05857 296 SRAIAADVRFIEATGVRTAQVYGLSE-TGCTALCLPtddgsiVKIEAGAVGRPYPGVDVYLAATdgigptapgagpsasf 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 GEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIenrlavhDRI-E 450
Cdd:PRK05857 375 GTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEV-------DRIaE 445
|
....*..
gi 489188483 451 QVCVVGE 457
Cdd:PRK05857 446 GVSGVRE 452
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
166-456 |
2.58e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 106.68 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 166 EQLATLIYTSGTTGVPKGVM--H-NFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERM-----FVEMGslygGTTVF 237
Cdd:PRK08974 206 EDLAFLQYTGGTTGVAKGAMltHrNMLANLEQAKAAYGPLLHPGKELVVTALPLYHIFALTvncllFIELG----GQNLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 238 FAESLD--TFVEDMKRARPTLLFGVPriwTKFQMGVYSKmPAQKLDrllklpilgrivgrkvlaglgLDAVRYALCGAAP 315
Cdd:PRK08974 282 ITNPRDipGFVKELKKYPFTAITGVN---TLFNALLNNE-EFQELD---------------------FSSLKLSVGGGMA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 316 VPEALL-LWYRRLGLDVLEVYGMTENSGYSHVCRPGRQK-TGWIGQNSPGVEVRISDE----------GEVQVRSGATMV 383
Cdd:PRK08974 337 VQQAVAeRWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYySGSIGLPVPSTEIKLVDDdgnevppgepGELWVKGPQVML 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489188483 384 GYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08974 417 GYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMLHPKVLEVAAVG 487
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
19-456 |
2.63e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 106.76 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 19 HPQRRYLVQPIGGGRVEElSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAE 98
Cdd:PRK06018 23 HGNREVVTRSVEGPIVRT-TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 99 SARQVLEHSESAVVFVGK--LDDWPAMAPGVP-----------EGIPTVAMP-------LHPEGRFDRQWSDLqacaple 158
Cdd:PRK06018 102 QIAWIINHAEDRVVITDLtfVPILEKIADKLPsveryvvltdaAHMPQTTLKnavayeeWIAEADGDFAWKTF------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 159 gDTPTAAeqlaTLIYTSGTTGVPKGVMHNFSSFAFAA--SRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTV 236
Cdd:PRK06018 175 -DENTAA----GMCYTSGTTGDPKGVLYSHRSNVLHAlmANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 237 FFAESLD--TFVEDMKRARPTLLFGVPRIWtkfQMgVYSKMPAQKLdrllKLPILGRIVgrkvlaglgldavryalCGAA 314
Cdd:PRK06018 250 MPGAKLDgaSVYELLDTEKVTFTAGVPTVW---LM-LLQYMEKEGL----KLPHLKMVV-----------------CGGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 315 PVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCR--------PGRQKTGW-IGQNSP--GVEVRISDE------------ 371
Cdd:PRK06018 305 AMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVlQKQGYPpfGVEMKITDDagkelpwdgktf 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 GEVQVRSGATMVGYYKEpekTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENrLAV-HDRIE 450
Cdd:PRK06018 385 GRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSIDLEN-LAVgHPKVA 459
|
....*.
gi 489188483 451 QVCVVG 456
Cdd:PRK06018 460 EAAVIG 465
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
37-456 |
2.90e-24 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 106.50 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWL-RSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTA-ESARQVLEHSESAVVFV 114
Cdd:PRK08751 51 ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPrELKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GK--------LDDWP---AMAPGVPE--GIPTVAM---------PLHPEGRFDRQWSDLQACAPLEGDT-PT---AAEQL 168
Cdd:PRK08751 131 DNfgttvqqvIADTPvkqVITTGLGDmlGFPKAALvnfvvkyvkKLVPEYRINGAIRFREALALGRKHSmPTlqiEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVM---HNFSSFAFAASRGVELFGTREDDR--MLSYLPLCHVAER-----MFVEMGSLygGTTVFF 238
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMlthRNLVANMQQAHQWLAGTGKLEEGCevVITALPLYHIFALtanglVFMKIGGC--NHLISN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 239 AESLDTFVEDMKRARPTLLFGVPRIWTKfqmgvyskmpaqkldrLLKLPILGRIvgrkvlaglGLDAVRYALCGAAPVPE 318
Cdd:PRK08751 289 PRDMPGFVKELKKTRFTAFTGVNTLFNG----------------LLNTPGFDQI---------DFSSLKMTLGGGMAVQR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 319 ALL-LWYRRLGLDVLEVYGMTENSgyshvcrPG--------RQKTGWIGQNSPGVEVRISDE----------GEVQVRSG 379
Cdd:PRK08751 344 SVAeRWKQVTGLTLVEAYGLTETS-------PAacinpltlKEYNGSIGLPIPSTDACIKDDagtvlaigeiGELCIKGP 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489188483 380 ATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08751 417 QVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVS-GFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-495 |
4.73e-24 |
|
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: 105.50 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 13 FERE-KRHPQRRYLvqpIGGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:cd17651 1 FERQaARTPDAPAL---VAEGRR--LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVVfvgklddwpAMAPGVPEGIPTVAMPLHPEgrfdrQWSDLQACAPLEGDTPTAAEQLATL 171
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLV---------LTHPALAGELAVELVAVTLL-----DQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 172 IYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAerMFVEMGS--LYGGTTVFFAE----SLDTF 245
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDV--SVQEIFStlCAGATLVLPPEevrtDPPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 246 VEDMKRARPTLLFgvpriwtkfqmgvyskMPAQKLDRLLKLPilgrivgrkVLAGLGLDAVRYALCG--AAPVPEALLLW 323
Cdd:cd17651 220 AAWLDEQRISRVF----------------LPTVALRALAEHG---------RPLGVRLAALRYLLTGgeQLVLTEDLREF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 324 YRRL-GLDVLEVYGMTEN----SGYSHVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKE 388
Cdd:cd17651 275 CAGLpGLRLHNHYGPTEThvvtALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAalrpvppgvpGELYIGGAGLARGYLNR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 389 PEKTAEVLTADGFL------RTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAP 462
Cdd:cd17651 355 PELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510
....*....|....*....|....*....|...
gi 489188483 463 LGLCVLSEVGRREAlngtrGALESSLRAHLEQV 495
Cdd:cd17651 434 EKRLVAYVVGDPEA-----PVDAAELRAALATH 461
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
37-456 |
5.22e-24 |
|
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: 105.15 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHsesavvfvgk 116
Cdd:cd05929 18 LLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEI---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpaMAPGVPEGIPTVAMPLHPegrfdrqWSDLQACAPLEGDTPTAAEQLAT-LIYTSGTTGVPKGVMHNFSSFAFAA 195
Cdd:cd05929 88 ------KAAALVCGLFTGGGALDG-------LEDYEAAEGGSPETPIEDEAAGWkMLYSGGTTGRPKGIKRGLPGGPPDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 196 SRGVE---LFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFaESLD--TFVEDMKRARPTLLFGVPriwTKFQmg 270
Cdd:cd05929 155 DTLMAaalGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM-EKFDpeEFLRLIERYRVTFAQFVP---TMFV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 271 vyskmpaqkldRLLKLPilgrivgRKVLAGLGLDAVRYALCGAAPVPEAL-LLWYRRLGLDVLEVYGMTENSGY------ 343
Cdd:cd05929 229 -----------RLLKLP-------EAVRNAYDLSSLKRVIHAAAPCPPWVkEQWIDWGGPIIWEYYGGTEGQGLtiinge 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 344 ---SH---VCRPGRQKTGWIGQNspGVEVRISDEGEVQVRSGATmVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLR 417
Cdd:cd05929 291 ewlTHpgsVGRAVLGKVHILDED--GNEVPPGEIGEVYFANGPG-FEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLY 367
|
410 420 430
....*....|....*....|....*....|....*....
gi 489188483 418 LTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05929 368 LTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG 405
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
36-496 |
8.65e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 105.08 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGhVSVPLYPNLT--------AESARQVLEHS 107
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRG-ASLTMLHQPTprtdlavwAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 108 ESAVVFVGklDDWPAMAPGVPE-GIPTVAMplhpegrfdrqwSDLQACAPLEgDTPTAAEQLATLIYTSGTTGVPKGVM- 185
Cdd:PRK07768 108 GAKAVVVG--EPFLAAAPVLEEkGIRVLTV------------ADLLAADPID-PVETGEDDLALMQLTSGSTGSPKAVQi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 186 -H-NFSSFAFAASRGVELfgTREDDRMLSYLPLCHvaermfvEMGsLYGGTTV--FFAESLdTFVEDMKRARPTLLFgvP 261
Cdd:PRK07768 173 tHgNLYANAEAMFVAAEF--DVETDVMVSWLPLFH-------DMG-MVGFLTVpmYFGAEL-VKVTPMDFLRDPLLW--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 262 RIWTKFQMGV-------YSkmpaqkldrllklpILGRIVGRKVLAG-LGLDAVRYALCGAAPVP----EALLLWYRRLGL 329
Cdd:PRK07768 240 ELISKYRGTMtaapnfaYA--------------LLARRLRRQAKPGaFDLSSLRFALNGAEPIDpadvEDLLDAGARFGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 330 D---VLEVYGMTE----------NSGYSH----------------VCRPGRQKTGWIGQNSPGVEVRISDE--------- 371
Cdd:PRK07768 306 RpeaILPAYGMAEatlavsfspcGAGLVVdevdadllaalrravpATKGNTRRLATLGPPLPGLEVRVVDEdgqvlpprg 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 -GEVQVRsGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIEnRLAVhdRIE 450
Cdd:PRK07768 386 vGVIELR-GESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE-RAAA--RVE 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489188483 451 QV---CVVGEGLSAPlglcvlsevGRREalnGTRGALESSLRAHLEQVN 496
Cdd:PRK07768 461 GVrpgNAVAVRLDAG---------HSRE---GFAVAVESNAFEDPAEVR 497
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
10-455 |
1.18e-23 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 104.21 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVQpigggRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:cd12117 1 ELFEEQAARTPDAVAVVY-----GDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVfvgkLDDwPAMAPGVPEGIPTVAMPLHPEGrfdrqwsdlQACAPLEgdTPTAAEQLA 169
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVL----LTD-RSLAGRAGGLEVAVVIDEALDA---------GPAGNPA--VPVSPDDLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 TLIYTSGTTGVPKGVM---HNFSSFAfaasRGVELFGTREDDRMLSYLPLchvaermfvemgslyggttVFFAESLDTFV 246
Cdd:cd12117 140 YVMYTSGSTGRPKGVAvthRGVVRLV----KNTNYVTLGPDDRVLQTSPL-------------------AFDASTFEIWG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 edmkrarpTLLFGVpriwtkfQMGVYSKmpaqklDRLLKLPILGRIVGRK------VLAGL----------GLDAVRYAL 310
Cdd:cd12117 197 --------ALLNGA-------RLVLAPK------GTLLDPDALGALIAEEgvtvlwLTAALfnqladedpeCFAGLRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 311 CG--AAPVPealllWYRRL-----GLDVLEVYGMTENSGYS--HVCRPGRQKTGW--IGQNSPGVEVRISDEGEVQVRSG 379
Cdd:cd12117 256 TGgeVVSPP-----HVRRVlaacpGLRLVNGYGPTENTTFTtsHVVTELDEVAGSipIGRPIANTRVYVLDEDGRPVPPG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 380 AT----------MVGYYKEPEKTAEVLTADGFL------RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRL 443
Cdd:cd12117 331 VPgelyvggdglALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAAL 409
|
490
....*....|..
gi 489188483 444 AVHDRIEQVCVV 455
Cdd:cd12117 410 RAHPGVREAVVV 421
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
32-456 |
2.61e-23 |
|
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: 103.70 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWG--EVGDQARRAAAWLR-SLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:cd05928 35 GKGDEVKWSfrELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVFVGKlddwpAMAPGVPegipTVA---------MPLHPEGRfdRQWSDLQACAPLEGDT----PTAAEQLATLIYTS 175
Cdd:cd05928 115 AKCIVTSD-----ELAPEVD----SVAsecpslktkLLVSEKSR--DGWLNFKELLNEASTEhhcvETGSQEPMAIYFTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 176 GTTGVPKGVMHNFSSFAFAAS-RGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFfaesldtfVEDMkrarp 254
Cdd:cd05928 184 GTTGSPKMAEHSHSSLGLGLKvNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVF--------VHHL----- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 255 tllfgvPRIWTKFQMGVYSKMPaqkLDRLLKLPILGRIVGRKVLAGLGLDAVRYALCGAAPV-PEALLLWYRRLGLDVLE 333
Cdd:cd05928 251 ------PRFDPLVILKTLSSYP---ITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLnPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 334 VYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD----------EGEVQVRSGAT-----MVGYYKEPEKTAEVLTA 398
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDdngnvlppgtEGDIGIRVKPIrpfglFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 399 DgFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05928 402 D-FYLTGDRGIMDEDGYFWFMGRADDVINSS-GYRIGPFEVESALIEHPAVVESAVVS 457
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
32-537 |
4.12e-23 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 103.66 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAV 111
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 112 VFVG-----KLDDWPAMAPGVP------EGIPTVAMPLHPEGRFD-RQWSDLQAC---APLEGDTPTAAEqLATLIYTSG 176
Cdd:PLN02387 182 VICDskqlkKLIDISSQLETVKrviymdDEGVDSDSSLSGSSNWTvSSFSEVEKLgkeNPVDPDLPSPND-IAVIMYTSG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 177 TTGVPKGVM--H-NFSSFAFAASRGVELFGTRedDRMLSYLPLCHV----AERMFVEMGSLYG-GTTVFFAESLDTFVE- 247
Cdd:PLN02387 261 STGLPKGVMmtHgNIVATVAGVMTVVPKLGKN--DVYLAYLPLAHIlelaAESVMAAVGAAIGyGSPLTLTDTSNKIKKg 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 248 ---DMKRARPTLLFGVPRIWTKFQMGVYSKMP-----AQKL------DRL------------LKLPILGRIVGRKVLAGL 301
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDakgglAKKLfdiaykRRLaaiegswfgawgLEKLLWDALVFKKIRAVL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 302 GlDAVRYALCGAAPV-PEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEV----------RISD 370
Cdd:PLN02387 419 G-GRIRFMLSGGAPLsGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVklvsweeggyLISD 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 371 E----GEVQVRSGATMVGYYKEPEKTAEVLTADG----FLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIENR 442
Cdd:PLN02387 498 KpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 443 LAVHDRIEQVCVVGEGLSAplgLCVLSEVGRREALNG----------------TRGALESSLRAHLEQV--NGALDKHER 504
Cdd:PLN02387 578 LSVSPYVDNIMVHADPFHS---YCVALVVPSQQALEKwakkagidysnfaelcEKEEAVKEVQQSLSKAakAARLEKFEI 654
|
570 580 590
....*....|....*....|....*....|...
gi 489188483 505 LVGLVLVQETWAVDNGFLTPTLKIKRNMVEGAY 537
Cdd:PLN02387 655 PAKIKLLPEPWTPESGLVTAALKLKREQIRKKF 687
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
37-421 |
5.76e-23 |
|
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: 101.62 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFvgk 116
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd17653 100 --------------------------------------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLSYLPL---CHVAErMFVEMGslYGGTTVfFAESLDTFVEDMKR-----ARPTLLfgvpriwtkfq 268
Cdd:cd17653 136 QPPARLDVGPGSRVAQVLSIafdACIGE-IFSTLC--NGGTLV-LADPSDPFAHVARTvdalmSTPSIL----------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 269 mgvySKMPAQKLDRLlklpilgrivgrkvlaglgldavRYALCGAAPVPEALL-LWyrRLGLDVLEVYGMTE---NSGYS 344
Cdd:cd17653 201 ----STLSPQDFPNL-----------------------KTIFLGGEAVPPSLLdRW--SPGRRLYNAYGPTEctiSSTMT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVcRPGRQKTgwIGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYKEPEKTAEVLTADGF------LRTGDKG 408
Cdd:cd17653 252 EL-LPGQPVT--IGKPIPNSTCYILDADLQPVPEGVVgeicisgvqvARGYLGNPALTASKFVPDPFwpgsrmYRTGDYG 328
|
410
....*....|...
gi 489188483 409 EQDAEGNLRLTGR 421
Cdd:cd17653 329 RWTEDGGLEFLGR 341
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
35-456 |
1.50e-22 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 100.25 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAA-AWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSEsavvf 113
Cdd:cd05958 9 REWTYRDLLALANRIAnVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 vgklddwpamapgvpegiPTVAMPLHPEgrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFAF 193
Cdd:cd05958 84 ------------------ITVALCAHAL---------------------TASDDICILAFTSGTTGAPKATMHFHRDPLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 194 AASR-GVELFGTREDDRMLSYLPLCHVAERMFVEMGSLY-GGTTVFFAESL-DTFVEDMKRARPTLLFGVPRiwtkfqmg 270
Cdd:cd05958 125 SADRyAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGvGASGVLLEEATpDLLLSAIARYKPTVLFTAPT-------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 271 VYSKMpaqkldrllklpilgriVGRKVLAGLGLDAVRYALCGAAPVPEALL-LWYRRLGLDVLEVYGMTENSGYSHVCRP 349
Cdd:cd05958 197 AYRAM-----------------LAHPDAAGPDLSSLRKCVSAGEALPAALHrAWKEATGIPIIDGIGSTEMFHIFISARP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 350 GRQKTGWIGQNSPGVEVRISDE----------GEVQVRsGATmvGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLT 419
Cdd:cd05958 260 GDARPGATGKPVPGYEAKVVDDegnpvpdgtiGRLAVR-GPT--GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQ 336
|
410 420 430
....*....|....*....|....*....|....*..
gi 489188483 420 GRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05958 337 GRSDDMIV-SGGYNIAPPEVEDVLLQHPAVAECAVVG 372
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
35-456 |
2.56e-22 |
|
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: 100.68 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GK--LDDwpamAPGVPEGIPTVAMPLHPEGRFDRQW---------SDLQACAPLEGDTPTAA---EQLATLIYTSGTTGV 180
Cdd:cd17642 123 SKkgLQK----VLNVQKKLKIIKTIIILDSKEDYKGyqclytfitQNLPPGFNEYDFKPPSFdrdEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 181 PKGVM--HNFSSFAFAASRGvELFGTR--EDDRMLSYLPLCHvAERMFVEMGSLYGGTTVFFAESLD--TFVEDMKRARP 254
Cdd:cd17642 199 PKGVQltHKNIVARFSHARD-PIFGNQiiPDTAILTVIPFHH-GFGMFTTLGYLICGFRVVLMYKFEeeLFLRSLQDYKV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 255 TLLFGVPRIwtkfqMGVYSKMP-AQKLDrllklpilgrivgrkvlaglgLDAVRYALCGAAP----VPEALllwYRRLGL 329
Cdd:cd17642 277 QSALLVPTL-----FAFFAKSTlVDKYD---------------------LSNLHEIASGGAPlskeVGEAV---AKRFKL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 330 D-VLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISD-----------EGEVQVRSGATMVGYYKEPEKTAEVLT 397
Cdd:cd17642 328 PgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDldtgktlgpneRGELCVKGPMIMKGYVNNPEATKALID 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 398 ADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd17642 408 KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVAG 465
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
35-494 |
3.61e-22 |
|
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: 99.65 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEhsESAVVFV 114
Cdd:cd12114 11 GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA--DAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDWPAMAPGVPEGIPTVAMPLHPEgrfdrqwsdlqacaPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSsfafA 194
Cdd:cd12114 89 LTDGPDAQLDVAVFDVLILDLDALAAP--------------APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHR----A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGV----ELFGTREDDRMLSYLPLCHvaermfvEMgSLY--------GGTTVFFAESLDT----FVEDMKRARPTLLF 258
Cdd:cd12114 151 ALNTIldinRRFAVGPDDRVLALSSLSF-------DL-SVYdifgalsaGATLVLPDEARRRdpahWAELIERHGVTLWN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 259 GVPRIwtkFQMGVysKMPAQKLDRLLKLpilgrivgRKVLagLGLDAVRYALCGAapvpeallLWYRRLGLDVLEVYGMT 338
Cdd:cd12114 223 SVPAL---LEMLL--DVLEAAQALLPSL--------RLVL--LSGDWIPLDLPAR--------LRALAPDARLISLGGAT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 339 ENSGYSHVCRPGRQKTGWI----GQNSPGVEVRISDE----------GEVQVrSGATMV-GYYKEPEKTAE----VLTAD 399
Cdd:cd12114 280 EASIWSIYHPIDEVPPDWRsipyGRPLANQRYRVLDPrgrdcpdwvpGELWI-GGRGVAlGYLGDPELTAArfvtHPDGE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 400 GFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVV--GEGLSAPLGLCVLSEvgrreal 477
Cdd:cd12114 359 RLYRTGDLGRYRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVVvlGDPGGKRLAAFVVPD------- 430
|
490
....*....|....*..
gi 489188483 478 NGTRGALESSLRAHLEQ 494
Cdd:cd12114 431 NDGTPIAPDALRAFLAQ 447
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
4-425 |
4.32e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 100.02 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPLE--VFFER-EKRHPQRRYLVQpigGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA 80
Cdd:PRK08162 13 ANYVPLTplSFLERaAEVYPDRPAVIH---GDRR--RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 81 IWMAGHVSVPLYPNLTAESARQVLEHSESAVV-----FVGKLDDWPAMAPGVPEGIPTVAMPLHPEGRF--DRQWSDLQA 153
Cdd:PRK08162 88 VPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLivdteFAEVAREALALLPGPKPLVIDVDDPEYPGGRFigALDYEAFLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 154 caplEGDTPTAAE------QLATLIYTSGTTGVPKGVM-HNFSSFAFAASRGVElFGTREDDRMLSYLPLCHVAERMFVE 226
Cdd:PRK08162 168 ----SGDPDFAWTlpadewDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILA-WGMPKHPVYLWTLPMFHCNGWCFPW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 227 MGSLYGGTTVFfaesldtfvedMKRARPTLLFGVpriwtkfqmgvyskMPAQKLDRLLKLPIlgrivgrkVLAGL----- 301
Cdd:PRK08162 243 TVAARAGTNVC-----------LRKVDPKLIFDL--------------IREHGVTHYCGAPI--------VLSALinapa 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 302 ----GLDAVRYALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVC--RPG---------RQKTGWIGQNSPGVE- 365
Cdd:PRK08162 290 ewraGIDHPVHAMVAGAAPPAAVIAKMEEIGFDLTHVYGLTETYGPATVCawQPEwdalplderAQLKARQGVRYPLQEg 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489188483 366 VRISDE-------------GEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEI 425
Cdd:PRK08162 370 VTVLDPdtmqpvpadgetiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
35-456 |
4.59e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 99.70 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDWPAMAPGVPegiptVAMPLHPEGRFDrQWSDLQACapLEGDTPTAAEQL--ATLIYTSGTTGVPKGVMHNFSSFA 192
Cdd:PRK13390 103 SAALDGLAAKVGAD-----LPLRLSFGGEID-GFGSFEAA--LAGAGPRLTEQPcgAVMLYSSGTTGFPKGIQPDLPGRD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 193 --------FAASRGveLFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVfFAESLDtfvedmkrARPTLlfgvpRIW 264
Cdd:PRK13390 175 vdapgdpiVAIARA--FYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVV-LAKRFD--------AQATL-----GHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 TKFQMGVYSKMPAQKLdRLLKLpilgrivGRKVLAGLGLDAVRYALCGAAPVP----EALLLWyrrLGLDVLEVYGMTEN 340
Cdd:PRK13390 239 ERYRITVTQMVPTMFV-RLLKL-------DADVRTRYDVSSLRAVIHAAAPCPvdvkHAMIDW---LGPIVYEYYSSTEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 341 SGY---------SHVCRPGRQKTGWI------GQNSPGVEVrisdeGEVQVRSGATMVGYYKEPEKTAEVL-TADGFLRT 404
Cdd:PRK13390 308 HGMtfidspdwlAHPGSVGRSVLGDLhicdddGNELPAGRI-----GTVYFERDRLPFRYLNDPEKTAAAQhPAHPFWTT 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489188483 405 -GDKGEQDAEGNLRLTGRmKEIFKTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK13390 383 vGDLGSVDEDGYLYLADR-KSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
17-456 |
4.88e-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: 99.49 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQPIGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT 96
Cdd:cd05970 28 KEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSESAVVFVGKLDDWPAMAPGVPEGIPTVAM-----PLHPEGrfdrqWSDLQA-CA-------PLEGDTPT 163
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKlvwvgDPVPEG-----WIDFRKlIKnaspdfeRPTANSYP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 164 AAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSylplchVAERMFVEM--GSLYG----GTTVf 237
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLT------VADTGWGKAvwGKIYGqwiaGAAV- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 238 faesldtFVEDMKRARPTLLFgvpriwtkfqmgvySKMPAQKLDRLLKLPILGRIVGRKVLAGLGLDAVRYALCGAAPV- 316
Cdd:cd05970 256 -------FVYDYDKFDPKALL--------------EKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALn 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 317 PEALLLWYRRLGLDVLEVYGMTENSgyshVC---RPGRQ-KTGWIGQNSPGVEVRISD----------EGEVQVRSG--- 379
Cdd:cd05970 315 PEVFNTFKEKTGIKLMEGFGQTETT----LTiatFPWMEpKPGSMGKPAPGYEIDLIDregrsceageEGEIVIRTSkgk 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 380 --ATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05970 391 pvGLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSS-GYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
35-494 |
2.24e-21 |
|
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: 96.77 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFv 114
Cdd:cd17650 11 RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVM---HNFSSF 191
Cdd:cd17650 90 ------------------------------------------------TQPEDLAYVIYTSGTTGKPKGVMvehRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 AFAASRGVELfgTREDDRMLSylplchvaermfveMGSLyggttvffaeSLDTFVEDMKRArptLLFG-----VPRiWTK 266
Cdd:cd17650 122 AHAWRREYEL--DSFPVRLLQ--------------MASF----------SFDVFAGDFARS---LLNGgtlviCPD-EVK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 267 FQMG-VYSKMPAQKLDRLLKLPILGRIVGRKVL-AGLGLDAVRYALCGAAPVPEALLLW-YRRLG--LDVLEVYGMTE-- 339
Cdd:cd17650 172 LDPAaLYDLILKSRITLMESTPALIRPVMAYVYrNGLDLSAMRLLIVGSDGCKAQDFKTlAARFGqgMRIINSYGVTEat 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 340 -NSGYSHVCRPGRQKTGW--IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGF----- 401
Cdd:cd17650 252 iDSTYYEEGRDPLGDSANvpIGRPLPNTAMYVLDErlqpqpvgvaGELYIGGAGVARGYLNRPELTAERFVENPFapger 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 402 -LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRI-EQVCVVGEGLSAPLGLCvlSEVGRREALNg 479
Cdd:cd17650 332 mYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIdEAVVAVREDKGGEARLC--AYVVAAATLN- 407
|
490
....*....|....*
gi 489188483 480 trgalESSLRAHLEQ 494
Cdd:cd17650 408 -----TAELRAFLAK 417
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
35-455 |
3.17e-21 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 96.48 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK09029 27 EVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDWPAMApgvpegipTVAMPLHPEGRFDRQWSdlqacaplegdtptaAEQLATLIYTSGTTGVPKGVMHNFSSFaFA 194
Cdd:PRK09029 107 LEGENTFSAL--------TSLHLQLVEGAHAVAWQ---------------PQRLATMTLTSGSTGLPKAAVHTAQAH-LA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGV-ELFG-TREDDRMLSyLPLCHVaermfvemgS--------LYGGTTVFFAESLDtFVEDmkrarptlLFGVPRIw 264
Cdd:PRK09029 163 SAEGVlSLMPfTAQDSWLLS-LPLFHV---------SgqgivwrwLYAGATLVVRDKQP-LEQA--------LAGCTHA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 tkfqmgvySKMPAQkLDRLLKLPILgRIVGRKVLAGlgldavryalcGAApVPEALLLWYRRLGLDVLEVYGMTENSgyS 344
Cdd:PRK09029 223 --------SLVPTQ-LWRLLDNRSE-PLSLKAVLLG-----------GAA-IPVELTEQAEQQGIRCWCGYGLTEMA--S 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVC------RPGrqktgwIGQNSPGVEVRIsDEGEVQVRsGATM-VGYYKEPEKTAeVLTADGFLRTGDKGEQDaEGNLR 417
Cdd:PRK09029 279 TVCakradgLAG------VGSPLPGREVKL-VDGEIWLR-GASLaLGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELT 348
|
410 420 430
....*....|....*....|....*....|....*...
gi 489188483 418 LTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:PRK09029 349 ILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFVV 385
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-492 |
1.66e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPLEVFFEREKRHPQRRYLVqpIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWM 83
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVV--FDE---EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLK 4623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 84 AGHVSVPLYPNLTAESARQVLEHSESAVVFVGK--LDDWPamapgVPEGIPTVAMPLhpegrfDRQWSDLQACAPLegdT 161
Cdd:PRK12316 4624 AGGAYVPLDPEYPRERLAYMMEDSGAALLLTQShlLQRLP-----IPDGLASLALDR------DEDWEGFPAHDPA---V 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 PTAAEQLATLIYTSGTTGVPKGVMHNFSSF-AFAASRGvELFGTREDDRMLSYLPLchvAERMFVE--MGSLYGGTTVFF 238
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLvNHLHATG-ERYELTPDDRVLQFMSF---SFDGSHEglYHPLINGASVVI 4765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 239 AES----LDTFVEDMKRARPTLLFGVPriwtkfqmgVYSKMPAQKLDRLLKLPILgrivgRKVLAGlgldavryalcGAA 314
Cdd:PRK12316 4766 RDDslwdPERLYAEIHEHRVTVLVFPP---------VYLQQLAEHAERDGEPPSL-----RVYCFG-----------GEA 4820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 315 PVPEALLLWYRRLGLDVL-EVYGMTENSGYSHV--CRPGRQ---KTGWIGQNSPGVEVRISDE----------GEVQVRS 378
Cdd:PRK12316 4821 VAQASYDLAWRALKPVYLfNGYGPTETTVTVLLwkARDGDAcgaAYMPIGTPLGNRSGYVLDGqlnplpvgvaGELYLGG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 379 GATMVGYYKEPEKTAEVLTADGF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRI-E 450
Cdd:PRK12316 4901 EGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVrE 4979
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489188483 451 QVCVVGEG-LSAPLGLCVLSEVGRREALNGTRGALESSLRAHL 492
Cdd:PRK12316 4980 AVVIAQEGaVGKQLVGYVVPQDPALADADEAQAELRDELKAAL 5022
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
37-456 |
1.85e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.83 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSL-DLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV---PLY-------------------- 92
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVntnPLYtaremehqfndsgakalvcl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 93 PNLtAESARQVLEHSESAVVFVGKLDDW---------PAMAPGVPEGIPTVAMPlhPEGRFDRQWSdLQACAPLEGDTPt 163
Cdd:PRK05677 130 ANM-AHLAEKVLPKTGVKHVIVTEVADMlpplkrlliNAVVKHVKKMVPAYHLP--QAVKFNDALA-KGAGQPVTEANP- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 164 AAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDD---RMLSYLPLCHVAERMFVEMGS-LYGGTTVFFA 239
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMmLIGNHNILIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 240 E--SLDTFVEDMKRARPTLLFGVPriwTKFqMGVYSKMPAQKLD-RLLKLPILGrivgrkvlaglgldavryalcGAAPV 316
Cdd:PRK05677 285 NprDLPAMVKELGKWKFSGFVGLN---TLF-VALCNNEAFRKLDfSALKLTLSG---------------------GMALQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 317 PEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYY 386
Cdd:PRK05677 340 LATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDdgnelplgevGELCVKGPQVMKGYW 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 387 KEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK05677 420 QRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLAALPGVLQCAAIG 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
9-462 |
1.90e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 93.92 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 9 LEVFFERE-KRHPQRRYLVQPigggrVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHV 87
Cdd:cd12115 1 LHDLVEAQaARTPDAIALVCG-----DESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 88 SVPLYPNLTAESARQVLEHSESAVVFvgklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQ 167
Cdd:cd12115 76 YVPLDPAYPPERLRFILEDAQARLVL-------------------------------------------------TDPDD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 168 LATLIYTSGTTGVPKGVM---HNFSSFAFAASrgvELFGTREDDRMLSYLPLC---HVAErMFvemGSLYGGTTVFFAES 241
Cdd:cd12115 107 LAYVIYTSGSTGRPKGVAiehRNAAAFLQWAA---AAFSAEELAGVLASTSICfdlSVFE-LF---GPLATGGKVVLADN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 LDTFVEDMKRARPTLLFGVPRiwtkfqmgvyskmPAQKLDRLLKLPILGRIVGrkvLAGlgldavryalcgaAPVPEALL 321
Cdd:cd12115 180 VLALPDLPAAAEVTLINTVPS-------------AAAELLRHDALPASVRVVN---LAG-------------EPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 322 L-WYRRLGLD-VLEVYGMTENSGYS--HVCRPGRQKTGWIGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYK 387
Cdd:cd12115 231 QrLYARLQVErVVNLYGPSEDTTYStvAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPgelyiggagvARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 388 EPEKTAEVLTADGFL------RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSA 461
Cdd:cd12115 311 RPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVREAVVVAIGDAA 389
|
.
gi 489188483 462 P 462
Cdd:cd12115 390 G 390
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
17-494 |
2.36e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 94.58 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 17 KRHPQRRYLVQPIGGG-----RVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPL 91
Cdd:PRK09274 17 QERPDQLAVAVPGGRGadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 92 YPNLTAESARQVLEHSESAVvFVG--------KLDDWpamAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEGdTPT 163
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDA-FIGipkahlarRLFGW---GKPSVRRLVTVGGRLLWGGTTLATLLRDGAAAPFPM-ADL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 164 AAEQLATLIYTSGTTGVPKGVMHNFSSFA--FAASRgvELFGTREDDRMLSYLPLchvaermFVEMGSLYGGTTVffaes 241
Cdd:PRK09274 172 APDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEALR--EDYGIEPGEIDLPTFPL-------FALFGPALGMTSV----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 ldtfVEDMKRARP-----------------TLLFGVPRIWTKfqmgvyskmpaqkldrllklpilgriVGRKVLA-GLGL 303
Cdd:PRK09274 238 ----IPDMDPTRPatvdpaklfaaierygvTNLFGSPALLER--------------------------LGRYGEAnGIKL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 304 DAVRYALCGAAPVPEALLLWYRRL---GLDVLEVYGMTE-----NSGYSHVCRPGRQKT----GW-IGQNSPGVEVR--- 367
Cdd:PRK09274 288 PSLRRVISAGAPVPIAVIERFRAMlppDAEILTPYGATEalpisSIESREILFATRAATdngaGIcVGRPVDGVEVRiia 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 368 ISDE----------------GEVQVrSGAtMV--GYYKEPEKTAEVLTADG----FLRTGDKGEQDAEGNLRLTGRMKEI 425
Cdd:PRK09274 368 ISDApipewddalrlatgeiGEIVV-AGP-MVtrSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHR 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 426 FKTSKGKYVaPAPIENRLAVHDRIEQVCVVGEGLSA---PLgLCVLSEVGRRealnGTRGALESSLRAHLEQ 494
Cdd:PRK09274 446 VETAGGTLY-TIPCERIFNTHPGVKRSALVGVGVPGaqrPV-LCVELEPGVA----CSKSALYQELRALAAA 511
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
49-458 |
3.39e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.14 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 49 AAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLT-AESARQVLEHSeSAVVF-----VGKLDdwpa 122
Cdd:PLN02574 80 AAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSlGEIKKRVVDCS-VGLAFtspenVEKLS---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 123 mapgvPEGIPTVAMPlhPEGRFDRQ-----------WSDLQAC-APLEGDTPTAAeqlatLIYTSGTTGVPKGVMHNFSS 190
Cdd:PLN02574 155 -----PLGVPVIGVP--ENYDFDSKriefpkfyeliKEDFDFVpKPVIKQDDVAA-----IMYSSGTTGASKGVVLTHRN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 191 FAFAasrgVELFGTRE---------DDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESLDT--FVEDMKRARPTLLFG 259
Cdd:PLN02574 223 LIAM----VELFVRFEasqyeypgsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAsdMVKVIDRFKVTHFPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 260 VPriwtkfqmgvyskmpaqkldrllklPILGRIVGR-KVLAGLGLDAVRYALCGAAPVPEALLLWYRRL--GLDVLEVYG 336
Cdd:PLN02574 299 VP-------------------------PILMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlpHVDFIQGYG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 337 MTENS--GYSHVCRPGRQKTGWIGQNSPGVEVRISD-----------EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLR 403
Cdd:PLN02574 354 MTESTavGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwstgcllppgnCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLR 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 404 TGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEG 458
Cdd:PLN02574 434 TGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVLISHPEIIDAAVTAVP 487
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
35-455 |
3.93e-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: 93.27 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFv 114
Cdd:cd17644 24 QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:cd17644 103 ------------------------------------------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLCH--VAERMFVemgSLYGGTTVFFaesldtfvedmkraRPTLLFGVPRIWTKF----Q 268
Cdd:cd17644 135 SHGLIKEYGITSSDRVLQFASIAFdvAAEEIYV---TLLSGATLVL--------------RPEEMRSSLEDFVQYiqqwQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 269 MGVYSKMPA---QKLDRLLKLPILGRIVGRKVLAGlgldavryalcGAAPVPEALLLWYRRLGLDV--LEVYGMTENSGY 343
Cdd:cd17644 198 LTVLSLPPAywhLLVLELLLSTIDLPSSLRLVIVG-----------GEAVQPELVRQWQKNVGNFIqlINVYGPTEATIA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 344 SHVCRPGRQKTGW-----IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFL------ 402
Cdd:cd17644 267 ATVCRLTQLTERNitsvpIGRPIANTQVYILDEnlqpvpvgvpGELHIGGVGLARGYLNRPELTAEKFISHPFNsseser 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 403 --RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd17644 347 lyKTGDLARYLPDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVI 400
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
171-470 |
3.97e-20 |
|
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: 91.56 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAErMFVEMGSLY-GGTTVFfaesLDTF---- 245
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAG-LNLALATFHaGGANVV----MEKFdpae 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 246 -VEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGLDAVRYALcgAAPVPEALLLWY 324
Cdd:cd17637 80 aLELIEEEKVTLMGSFP-------------------------PILSNLLDAAEKSGVDLSSLRHVL--GLDAPETIQRFE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 325 RRLGLDVLEVYGMTENSGYSHVCrPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAE 394
Cdd:cd17637 133 ETTGATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDndrpvpagetGEIVVRGPLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 395 VLTaDGFLRTGDKGEQDAEGNLRLTGRM--KEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG-------EGLSAplgL 465
Cdd:cd17637 212 TFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPG-GENVYPAEVEKVILEHPAIAEVCVIGvpdpkwgEGIKA---V 286
|
....*
gi 489188483 466 CVLSE 470
Cdd:cd17637 287 CVLKP 291
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
18-456 |
6.74e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 93.07 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYLVQPIGggrveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNcaH-WIVtdLAIWMAGHVSVPLYPNLT 96
Cdd:PRK07788 61 RAPDRAALIDERG-----TLTYAELDEQSNALARGLLALGVRAGDGVAVLARN--HrGFV--LALYAAGKVGARIILLNT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 97 AESARQVLEHSE----SAVV----FVGKLDDWPamaPGVPeGIPTVAMPLHPEGRFDRQWSDLQACAPLEGDT--PTAAE 166
Cdd:PRK07788 132 GFSGPQLAEVAAregvKALVyddeFTDLLSALP---PDLG-RLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAplPKPPK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLATLIYTSGTTGVPKGVMHN-FSSFAFAASrgvelfgtreddrMLSYLPLCH-----VAERMFVEMG------SLYGGT 234
Cdd:PRK07788 208 PGGIVILTSGTTGTPKGAPRPePSPLAPLAG-------------LLSRVPFRAgettlLPAPMFHATGwahltlAMALGS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 235 TVFFAESLD--TFVEDMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPilgrivgRKVLAGLGLDAVRY-ALC 311
Cdd:PRK07788 275 TVVLRRRFDpeATLEDIAKHKATALVVVPVM----------------LSRILDLG-------PEVLAKYDTSSLKIiFVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 312 GAAPVPEALLLWYRRLGLDVLEVYGMTENSgYSHVCRPG--RQKTGWIGQNSPGVEVRISDE----------GEVQVRSG 379
Cdd:PRK07788 332 GSALSPELATRALEAFGPVLYNLYGSTEVA-FATIATPEdlAEAPGTVGRPPKGVTVKILDEngnevprgvvGRIFVGNG 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489188483 380 ATMVGYYKEPEKTaevlTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07788 411 FPFEGYTDGRDKQ----IIDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-492 |
9.61e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 --GKLDDWPamapgVPEGIPTvaMPLHPEGrfdrQWSDLQACAPLegdTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFA 192
Cdd:PRK12316 2107 qrHLLERLP-----LPAGVAR--LPLDRDA----EWADYPDTAPA---VQLAGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 193 FAASRGVELFGTREDDRMLSYLPLCH--VAERMFVEM--GS--LYGGTTVFFAESLdtfVEDMKRARPTLLFGVPriwtk 266
Cdd:PRK12316 2173 AHCQAAGERYELSPADCELQFMSFSFdgAHEQWFHPLlnGArvLIRDDELWDPEQL---YDEMERHGVTILDFPP----- 2244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 267 fqmgVYSKMPAQKLDRllklpilgriVGRKVlaglgldAVRYALCGAAPVPEALL-LWYRRLGLDVL-EVYGMTENSGYS 344
Cdd:PRK12316 2245 ----VYLQQLAEHAER----------DGRPP-------AVRVYCFGGEAVPAASLrLAWEALRPVYLfNGYGPTEAVVTP 2303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 --HVCR---PGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGF-------L 402
Cdd:PRK12316 2304 llWKCRpqdPCGAAYVPIGRALGNRRAYILDAdlnllapgmaGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlY 2383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 403 RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVgeGLSAPLGLCVLSEVGRREALNGTRG 482
Cdd:PRK12316 2384 RTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVV--AQDGASGKQLVAYVVPDDAAEDLLA 2460
|
490
....*....|
gi 489188483 483 ALESSLRAHL 492
Cdd:PRK12316 2461 ELRAWLAARL 2470
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
18-446 |
1.27e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 92.08 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYLVQPIGGGRVE----ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYP 93
Cdd:PRK07008 17 AHAARHAGDTEIVSRRVEgdihRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 94 NLTAESARQVLEHSESAVVFVgKLDDWP---AMAPGVPEGIPTVAMPLH---PEGRFDRQ-WSDLQACAPLEGDTPTAAE 166
Cdd:PRK07008 97 RLFPEQIAYIVNHAEDRYVLF-DLTFLPlvdALAPQCPNVKGWVAMTDAahlPAGSTPLLcYETLVGAQDGDYDWPRFDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 167 QLAT-LIYTSGTTGVPKGVMHNFSS---FAFAASRGvELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL 242
Cdd:PRK07008 176 NQASsLCYTSGTTGNPKGALYSHRStvlHAYGAALP-DAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPGPDL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 D--TFVEDMKRARPTLLFGVPRIWtkfqMGVYSKMPAqkldrllklpilgrivgrkvlAGLGLDAVRYALCGAAPVPEAL 320
Cdd:PRK07008 255 DgkSLYELIEAERVTFSAGVPTVW----LGLLNHMRE---------------------AGLRFSTLRRTVIGGSACPPAM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 321 LLWYRR-LGLDVLEVYGMTENSGYSHVCRPG--------------RQKTgwiGQNSPGVEVRISDE------------GE 373
Cdd:PRK07008 310 IRTFEDeYGVEVIHAWGMTEMSPLGTLCKLKwkhsqlpldeqrklLEKQ---GRVIYGVDMKIVGDdgrelpwdgkafGD 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489188483 374 VQVRSGATMVGYYKepeKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVH 446
Cdd:PRK07008 387 LQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENVAVAH 454
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
35-494 |
1.48e-19 |
|
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: 91.28 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVfv 114
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvaMPLHPEgrfdrqwsdlqacaplegdtptaaeQLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:cd17649 89 ---------------------LTHHPR-------------------------QLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLCH--VAERMFVEMgsLYGGTTVFFAESL----DTFVEDMKRARPTLLFGVPRIWTKFq 268
Cdd:cd17649 123 CQATAERYGLTPGDRELQFASFNFdgAHEQLLPPL--ICGACVVLRPDELwasaDELAEMVRELGVTVLDLPPAYLQQL- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 269 mgvyskmpAQKLDRllklpilgriVGRKVLAGLGLdavrYALCGAAPVPEALLLWyrrLGLDVLEV--YGMTEN--SGYS 344
Cdd:cd17649 200 --------AEEADR----------TGDGRPPSLRL----YIFGGEALSPELLRRW---LKAPVRLFnaYGPTEAtvTPLV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVCRPGRQKTGW---IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGF-------LRT 404
Cdd:cd17649 255 WKCEAGAARAGAsmpIGRPLGGRSAYILDAdlnpvpvgvtGELYIGGEGLARGYLGRPELTAERFVPDPFgapgsrlYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 405 GDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGL--CVLSEVGRREAlngtrg 482
Cdd:cd17649 335 GDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLvaYVVLRAAAAQP------ 407
|
490
....*....|..
gi 489188483 483 ALESSLRAHLEQ 494
Cdd:cd17649 408 ELRAQLRTALRA 419
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
37-456 |
2.67e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 91.28 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSR-IAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG 115
Cdd:PRK07867 29 TSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 klDDWPAMAPGVPEGIPTVAMPlhpegrfDRQWSDLqaCAPLEGDTPTA----AEQLATLIYTSGTTGVPKGVMHNFSSF 191
Cdd:PRK07867 109 --SAHAELLDGLDPGVRVINVD-------SPAWADE--LAAHRDAEPPFrvadPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 AFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRarptllFGVpriwtkfqm 269
Cdd:PRK07867 178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRkfSASGFLPDVRR------YGA--------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 270 gVYSKMPAQKLDRLLKLPILG-------RIV-GRKVLAGlglDAVRYAlcgaapvpealllwyRRLGLDVLEVYGMTEnS 341
Cdd:PRK07867 243 -TYANYVGKPLSYVLATPERPddadnplRIVyGNEGAPG---DIARFA---------------RRFGCVVVDGFGSTE-G 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSHVCRPGrQKTGWIGQNSPGVEVRISDEGE----------------------VQVRSGATMVGYYKEPEKTAEVLtAD 399
Cdd:PRK07867 303 GVAITRTPD-TPPGALGPLPPGVAIVDPDTGTecppaedadgrllnadeaigelVNTAGPGGFEGYYNDPEADAERM-RG 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489188483 400 GFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07867 381 GVYWSGDLAYRDADGYAYFAGRLGDWMRVD-GENLGTAPIERILLRYPDATEVAVYA 436
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
32-456 |
7.52e-19 |
|
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: 90.24 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAV 111
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 112 VFV-------GKLDDWPAMAPGVPEGIPTV-----------AMPLHPeGRFdrQWSDLQACAPLEGDTPTAAEQLATLIY 173
Cdd:cd05968 167 LITadgftrrGREVNLKEEADKACAQCPTVekvvvvrhlgnDFTPAK-GRD--LSYDEEKETAGDGAERTESEDPLMIIY 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 174 TSGTTGVPKGVMHNFSSFAF-AASRGVELFGTREDDRMLsylplchvaerMFVEMGSLYGgttvffaesldtfvedmkra 252
Cdd:cd05968 244 TSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLT-----------WFTDLGWMMG-------------------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 253 rPTLLFGvpRIWTKFQMGVYSKMPAQ-KLDRLLKL------------PILGRIV---GRKVLAGLGLDAVRYALCGAAPV 316
Cdd:cd05968 293 -PWLIFG--GLILGATMVLYDGAPDHpKADRLWRMvedheithlglsPTLIRALkprGDAPVNAHDLSSLRVLGSTGEPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 317 -PEALLLWYRRLGLD---VLEVYGMTENSGYSHVCRPGRQ-KTGWIGQNSPGVEVRISDE---------GEVQVRS---G 379
Cdd:cd05968 370 nPEPWNWLFETVGKGrnpIINYSGGTEISGGILGNVLIKPiKPSSFNGPVPGMKADVLDEsgkparpevGELVLLApwpG 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 380 ATMvGYYKEPEKTAEVLTA--DGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05968 450 MTR-GFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDTINVA-GKRVGPAEIESVLNAHPAVLESAAIG 526
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
166-530 |
1.37e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 89.39 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 166 EQLATLIYTSGTTGVPKGVM---HNFSSFAFAASRGvELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL 242
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMlsnKNLYNTVVPLCKH-SIFKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDI 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 DTFVEDMKRARPTLLFGVPRiwtkfqmgVYSKMPAQKLDRLLKLPILGRIVGRKVLA--------GLG--LDAVRYALCG 312
Cdd:PTZ00342 383 NYFSKDIYNSKGNILAGVPK--------VFNRIYTNIMTEINNLPPLKRFLVKKILSlrksnnngGFSkfLEGITHISSK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 313 -------------------AAPVPEALLLWyrrLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQN-SPGVEVRI---- 368
Cdd:PTZ00342 455 ikdkvnpnlevilngggklSPKIAEELSVL---LNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPiSPNTKYKVrtwe 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 369 ----SD---EGEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVAPAPIEN 441
Cdd:PTZ00342 532 tykaTDtlpKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNN 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 442 RLAVHDRIEQvCVV--GEGLSAPLGLC---------------VLSEVGRREA--LNG-TRGALESSLraHLEQVNGA--- 498
Cdd:PTZ00342 612 LYSQISFINF-CVVygDDSMDGPLAIIsvdkyllfkclkddnMLESTGINEKnyLEKlTDETINNNI--YVDYVKGKmle 688
|
410 420 430
....*....|....*....|....*....|....*...
gi 489188483 499 ------LDKHERLVGLVLVQETWAVDNgFLTPTLKIKR 530
Cdd:PTZ00342 689 vykktnLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKR 725
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
35-492 |
1.87e-18 |
|
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: 88.13 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFv 114
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFA-- 192
Cdd:cd17643 90 ------------------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLal 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 193 FAASRGVelFGTREDDRMLsylpLCHVAERMFV--EM-GSL-YGGTTVFF----AESLDTFVEDMKRARPTLLFGVPriw 264
Cdd:cd17643 122 FAATQRW--FGFNEDDVWT----LFHSYAFDFSvwEIwGALlHGGRLVVVpyevARSPEDFARLLRDEGVTVLNQTP--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 TKFqmgvYSKMPAQKLDrllklpilgrivgrkvlaGLGLDAVRYALCGAAPVPEALLL-WYRRLGL---DVLEVYGMTEN 340
Cdd:cd17643 193 SAF----YQLVEAADRD------------------GRDPLALRYVIFGGEALEAAMLRpWAGRFGLdrpQLVNMYGITET 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 341 SGYS--HVCRP---GRQKTGWIGQNSPGVEVRISDE----------GEVQVrSGATMV-GYYKEPEKTAEVLTADGF--- 401
Cdd:cd17643 251 TVHVtfRPLDAadlPAAAASPIGRPLPGLRVYVLDAdgrpvppgvvGELYV-SGAGVArGYLGRPELTAERFVANPFggp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 402 ----LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVcVVGEGLSAPLGLCVLSEVGRREAL 477
Cdd:cd17643 330 gsrmYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDA-AVIVREDEPGDTRLVAYVVADDGA 407
|
490
....*....|....*
gi 489188483 478 NGTRGALESSLRAHL 492
Cdd:cd17643 408 AADIAELRALLKELL 422
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
31-456 |
2.24e-18 |
|
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: 88.40 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESA 110
Cdd:cd17634 79 TSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VVFV-------GKLDDWPAMapgVPEGIPTVAMPLH--------------PEGRfDRQWSDLQACAPLEGDT-PTAAEQL 168
Cdd:cd17634 159 LLITadggvraGRSVPLKKN---VDDALNPNVTSVEhvivlkrtgsdidwQEGR-DLWWRDLIAKASPEHQPeAMNAEDP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVMHNFSSFAFAASRGVE-LFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAESL----- 242
Cdd:cd17634 235 LFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVpnwpt 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 -DTFVEDMKRARPTLLFGVPRIwtkfqmgVYSKMPAqkldrllklpilgrivGRKVLAGLGLDAVRYALCGAAPV-PEAL 320
Cdd:cd17634 315 pARMWQVVDKHGVNILYTAPTA-------IRALMAA----------------GDDAIEGTDRSSLRILGSVGEPInPEAY 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 321 LLWYRRLGLD---VLEVYGMTENSGYSHVCRPGRQ--KTGWIGQNSPGVEVRISD----------EGEVQVRS---GATM 382
Cdd:cd17634 372 EWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDneghpqpggtEGNLVITDpwpGQTR 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 383 VGYYKEPEKTAEVL-TADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd17634 452 TLFGDHERFEQTYFsTFKGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAHPKVAEAAVVG 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-494 |
2.50e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 89.63 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 3 TANRLPLEVFFEREKRHPQRRYLVQPIGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIW 82
Cdd:PRK12316 3049 TAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAIL 3128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 83 MAGHVSVPLYPNLTAESARQVLEHSESAVvfvgkLDDWPAMAPGVPEGIPTVAMplhpegrfDRQWSDLQACAPlegDTP 162
Cdd:PRK12316 3129 KAGGAYVPLDPEYPEERLAYMLEDSGAQL-----LLSQSHLRLPLAQGVQVLDL--------DRGDENYAEANP---AIR 3192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 163 TAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLChvaermfvemgslyggttvFFAESL 242
Cdd:PRK12316 3193 TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS-------------------FDVFVE 3253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 DTFVEDMKRArpTLLFGVPRIWTKFQMGVySKMPAQKLDRLLKLPILGRIVGRKVLAGLGLDAVRYALCGAAPVPEALLL 322
Cdd:PRK12316 3254 ELFWPLMSGA--RVVLAGPEDWRDPALLV-ELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQ 3330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 323 WYrrLGLDVLEVYGMTENS--GYSHVCRPGRQKTGWIGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYKEPE 390
Cdd:PRK12316 3331 VF--AGLPLYNLYGPTEATitVTHWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALgelylggeglARGYHNRPG 3408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 391 KTAEVLTADGF------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLG 464
Cdd:PRK12316 3409 LTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVA 3487
|
490 500 510
....*....|....*....|....*....|
gi 489188483 465 LCVLSEvgrrealngTRGALESSLRAHLEQ 494
Cdd:PRK12316 3488 YVVPED---------EAGDLREALKAHLKA 3508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-492 |
5.11e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 5.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVV-- 112
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLls 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 113 --FVGKLDDwpamapgVPEGIPTVAMPlHPEGRFDRQWSDlqacAPlegDTPTAAEQLATLIYTSGTTGVPKGVMHNFSS 190
Cdd:PRK12316 615 qsHLGRKLP-------LAAGVQVLDLD-RPAAWLEGYSEE----NP---GTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 191 FAFAASRGVELFGTREDDRMLSYLPLC-HVAERMFveMGSLYGGTTVFFAE-----SLDTFVEDMKRARPTLLFGVPRIW 264
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTVLQKTPFSfDVSVWEF--FWPLMSGARLVVAApgdhrDPAKLVELINREGVDTLHFVPSML 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 265 TKFQmgvyskmPAQKLDRLLKLPILgrivgrkvlaglgldavryaLCGAAPVPEALL--LWYRRLGLDVLEVYGMTENS- 341
Cdd:PRK12316 758 QAFL-------QDEDVASCTSLRRI--------------------VCSGEALPADAQeqVFAKLPQAGLYNLYGPTEAAi 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSH-VCRPGRQKTGWIGQNSPGVEVRISD----------EGEVQVRSGATMVGYYKEPEKTAEVLTADGFL------RT 404
Cdd:PRK12316 811 DVTHwTCVEEGGDSVPIGRPIANLACYILDanlepvpvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPFVagermyRT 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 405 GDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAPLGLCVLSEVGrrealNGTRGAL 484
Cdd:PRK12316 891 GDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEG-----GDWREAL 964
|
....*...
gi 489188483 485 ESSLRAHL 492
Cdd:PRK12316 965 KAHLAASL 972
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
129-456 |
8.27e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.10 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 129 EGIPTVAMPLHPEGRFDRQWSDLQACAPLEGDtptaaeqLATLIYTSGTTGVPKGVMhnFSSFAFAASrgvelfGTREDD 208
Cdd:PRK07824 5 RAPALLPVPAQDERRAALLRDALRVGEPIDDD-------VALVVATSGTTGTPKGAM--LTAAALTAS------ADATHD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 209 RM------LSYLPLCHVAErMFVEMGSLYGGTTVFFAESLDTF-VEDMKRARPTLlfGVPRIWTkfqmgvySKMPAQkld 281
Cdd:PRK07824 70 RLggpgqwLLALPAHHIAG-LQVLVRSVIAGSEPVELDVSAGFdPTALPRAVAEL--GGGRRYT-------SLVPMQ--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 282 rLLKlpILGRIVGRKVLAglGLDAVryaLCGAAPVPEALLLWYRRLGLDVLEVYGMTENSG---YShvcrpgrqktgwiG 358
Cdd:PRK07824 137 -LAK--ALDDPAATAALA--ELDAV---LVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGgcvYD-------------G 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 359 QNSPGVEVRISDEgevQVRSGATMV--GYYKEPEKTAevLTADGFLRTGDKGEQDaEGNLRLTGRMKEIFKTSkGKYVAP 436
Cdd:PRK07824 196 VPLDGVRVRVEDG---RIALGGPTLakGYRNPVDPDP--FAEPGWFRTDDLGALD-DGVLTVLGRADDAISTG-GLTVLP 268
|
330 340
....*....|....*....|
gi 489188483 437 APIENRLAVHDRIEQVCVVG 456
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFG 288
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
4-455 |
1.82e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 85.46 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPLE--VFFEREKR-HPQRRYLVqpIGGGRveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA 80
Cdd:PLN03102 9 ANNVPLTpiTFLKRASEcYPNRTSII--YGKTR---FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 81 IWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGKldDWPAMAPGVPEGIPTVAMPLHPEGRFDRQWSDLQACAPLEGD 160
Cdd:PLN03102 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR--SFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEELD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 161 ----------TPTAAEQL---------ATLIYTSGTTGVPKGVM--HNFSSF-AFAASRGVELfGTREddRMLSYLPLCH 218
Cdd:PLN03102 162 yecliqrgepTPSLVARMfriqdehdpISLNYTSGTTADPKGVVisHRGAYLsTLSAIIGWEM-GTCP--VYLWTLPMFH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 219 VAERMFVEMGSLYGGTTVFFAEsldtfvedmkrarptllFGVPRIWTKFQMGVYSKMPAqkldrllkLPILGRIVgrkvL 298
Cdd:PLN03102 239 CNGWTFTWGTAARGGTSVCMRH-----------------VTAPEIYKNIEMHNVTHMCC--------VPTVFNIL----L 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 299 AGLGLDAVR-----YALCGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCR----------------PGRQKTGWI 357
Cdd:PLN03102 290 KGNSLDLSPrsgpvHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEwqdewnrlpenqqmelKARQGVSIL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 358 GQNSPGVEVRISDE---------GEVQVRSGATMVGYYKEPEKTAEVLTaDGFLRTGDKGEQDAEGNLRLTGRMKEIFkT 428
Cdd:PLN03102 370 GLADVDVKNKETQEsvprdgktmGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDII-I 447
|
490 500
....*....|....*....|....*..
gi 489188483 429 SKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:PLN03102 448 SGGENISSVEVENVLYKYPKVLETAVV 474
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
20-492 |
2.24e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 85.32 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 20 PQRRYLVQpigGGRVeeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAES 99
Cdd:PRK07798 17 PDRVALVC---GDRR--LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 100 ARQVLEHSESAVVFVG---------------KLDDWPAMAPGVPEGIPTVAMPlhpegrfdrqWSDLQACAPLEGDTPTA 164
Cdd:PRK07798 92 LRYLLDDSDAVALVYErefaprvaevlprlpKLRTLVVVEDGSGNDLLPGAVD----------YEDALAAGSPERDFGER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 AEQLATLIYTSGTTGVPKGVM--HN---FSSF---AFA-----------ASRGVELFGTReddrMLSYLPLCHVAERMFV 225
Cdd:PRK07798 162 SPDDLYLLYTGGTTGMPKGVMwrQEdifRVLLggrDFAtgepiedeeelAKRAAAGPGMR----RFPAPPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 226 EMGSLYGGTTVFfaESLDTF-----VEDMKRARPTLLFgvpriwtkfqmgvyskmpaqkldrllklpILGRIVGRKVLAG 300
Cdd:PRK07798 238 FAALFSGQTVVL--LPDVRFdadevWRTIEREKVNVIT-----------------------------IVGDAMARPLLDA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 301 LgLDAVRYALC--------GAAPVPEALLLWYRRL-GLDVLEVYGMTEN-SGYSHVCRPGRQKTGW----IGqnsPGVEV 366
Cdd:PRK07798 287 L-EARGPYDLSslfaiasgGALFSPSVKEALLELLpNVVLTDSIGSSETgFGGSGTVAKGAVHTGGprftIG---PRTVV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 367 RISDEGEVQV---------RSGATMVGYYKEPEKTAEVL-TADGfLR---TGDKGEQDAEGNLRLTGRMKEIFKTSkGKY 433
Cdd:PRK07798 363 LDEDGNPVEPgsgeigwiaRRGHIPLGYYKDPEKTAETFpTIDG-VRyaiPGDRARVEADGTITLLGRGSVCINTG-GEK 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188483 434 VAPAPIENRLAVHDRIEQVCVVGeglsAP---LGLCVLSEVGRREALNGTRGALESSLRAHL 492
Cdd:PRK07798 441 VFPEEVEEALKAHPDVADALVVG----VPderWGQEVVAVVQLREGARPDLAELRAHCRSSL 498
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
35-455 |
2.91e-17 |
|
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: 84.23 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNltaesarqvlehsesavvfv 114
Cdd:cd17652 11 ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPA-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplHPEGRFDRQWSDLQACAPLegdtpTAAEQLATLIYTSGTTGVPKGVM---HNFSSF 191
Cdd:cd17652 71 ------------------------YPAERIAYMLADARPALLL-----TTPDNLAYVIYTSGSTGRPKGVVvthRGLANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 AFAAsrgVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFF-AESL---DTFVEDMKRARPTLLFGVPriwtkf 267
Cdd:cd17652 122 AAAQ---IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLApAEELlpgEPLADLLREHRITHVTLPP------ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 268 qmGVYSKMPAQKLdrllkLPILGRIVGrkvlaglgldavryalcGAAPVPEALLLWYRrlGLDVLEVYGMTE---NSGYS 344
Cdd:cd17652 193 --AALAALPPDDL-----PDLRTLVVA-----------------GEACPAELVDRWAP--GRRMINAYGPTEttvCATMA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVCRPGRQKTgwIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGF-------LRTGDK 407
Cdd:cd17652 247 GPLPGGGVPP--IGRPVPGTRVYVLDArlrpvppgvpGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDL 324
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489188483 408 GEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd17652 325 ARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPGVAEAVVV 371
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
165-518 |
4.16e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 84.05 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 AEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLchvaermFVEMGSLYGGTTVffaesldt 244
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPL-------FALFGPALGLTSV-------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 245 fVEDMK-----RARPTLLFGVPRIWtkfqmgvyskmpaqKLDRLLKLPILGRIVGRKVLA-GLGLDAVRYALCGAAPVPE 318
Cdd:cd05910 149 -IPDMDptrpaRADPQKLVGAIRQY--------------GVSIVFGSPALLERVARYCAQhGITLPSLRRVLSAGAPVPI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 319 ALLLWYRRL---GLDVLEVYGMTE----NSGYSHVCR------PGRQKTGWIGQNSPGVEVRI---SDE----------- 371
Cdd:cd05910 214 ALAARLRKMlsdEAEILTPYGATEalpvSSIGSRELLatttaaTSGGAGTCVGRPIPGVRVRIieiDDEpiaewddtlel 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 -----GEVQVRSGATMVGYYKEPEKTAEVLTAD---GFL-RTGDKGEQDAEGNLRLTGRMKEIFKTSKGKYVApAPIENR 442
Cdd:cd05910 294 prgeiGEITVTGPTVTPTYVNRPVATALAKIDDnseGFWhRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYT-EPVERV 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 443 LAVHDRIEQVCVVGEG-LSAPLG-LCVLSEVGRREalngTRGALESSLRAHLEQvngalDKHERLVGLVLVQETWAVD 518
Cdd:cd05910 373 FNTHPGVRRSALVGVGkPGCQLPvLCVEPLPGTIT----PRARLEQELRALAKD-----YPHTQRIGRFLIHPSFPVD 441
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-492 |
5.91e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GK--LDDWPamapgVPEGIPTVAMPlhpegrfdrqwsdlQACAPLEGDTPT------AAEQLATLIYTSGTTGVPKGVM- 185
Cdd:PRK12467 1678 QShlQARLP-----LPDGLRSLVLD--------------QEDDWLEGYSDSnpavnlAPQNLAYVIYTSGSTGRPKGAGn 1738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 186 -HNFSSFAFAASRgvELFGTREDDRMLSYLPLchvAERMFVE--MGSLYGGTTVFFA---ESLD--TFVEDMKRARPTLL 257
Cdd:PRK12467 1739 rHGALVNRLCATQ--EAYQLSAADVVLQFTSF---AFDVSVWelFWPLINGARLVIAppgAHRDpeQLIQLIERQQVTTL 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 258 FGVPRIWTKFqmgvyskmpAQKLDRLLKLPILGRIVgrkvlaglgldavryaLCGAAPVPEALLLWYRRLGLDVL-EVYG 336
Cdd:PRK12467 1814 HFVPSMLQQL---------LQMDEQVEHPLSLRRVV----------------CGGEALEVEALRPWLERLPDTGLfNLYG 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 337 MTENSgySHV----CRPGRQKTGW---IGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTAD 399
Cdd:PRK12467 1869 PTETA--VDVthwtCRRKDLEGRDsvpIGQPIANLSTYILDAslnpvpigvaGELYLGGVGLARGYLNRPALTAERFVAD 1946
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 400 GF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRI-EQVCVVGEGLSA--------PL 463
Cdd:PRK12467 1947 PFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLREQGGVrEAVVIAQDGANGkqlvayvvPT 2025
|
490 500
....*....|....*....|....*....
gi 489188483 464 GLCVLSEVGRREALngtRGALESSLRAHL 492
Cdd:PRK12467 2026 DPGLVDDDEAQVAL---RAILKNHLKASL 2051
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
11-456 |
6.12e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 84.16 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 11 VFFEREKRHPQRRYLvqpIGGGRveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVP 90
Cdd:PRK08279 42 VFEEAAARHPDRPAL---LFEDQ--SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 91 LYPNLTAEsarqVLEHS----ESAVVFVGKlDDWPAMApGVPEGIpTVAMPLHPEGRFDRQ----WSDLQACAPLEGDTP 162
Cdd:PRK08279 117 LNTQQRGA----VLAHSlnlvDAKHLIVGE-ELVEAFE-EARADL-ARPPRLWVAGGDTLDdpegYEDLAAAAAGAPTTN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 163 TA------AEQLATLIYTSGTTGVPK-GVMHNF----SSFAFAAsrgveLFGTREDDRMLSYLPLCHvAERMFVEMGS-L 230
Cdd:PRK08279 190 PAsrsgvtAKDTAFYIYTSGTTGLPKaAVMSHMrwlkAMGGFGG-----LLRLTPDDVLYCCLPLYH-NTGGTVAWSSvL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 231 YGGTTVFFAE--SLDTFVEDMKRARPTLlfgvpriwtkFQ----MGVY-SKMPAQKLDRLLKLpilgrivgrKVLAGLGL 303
Cdd:PRK08279 264 AAGATLALRRkfSASRFWDDVRRYRATA----------FQyigeLCRYlLNQPPKPTDRDHRL---------RLMIGNGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 304 davRyalcgaapvPEALLLWYRRLGLD-VLEVYGMTE-NSGYSHVcrPGRQKTgwIGqNSPG--------VE-------- 365
Cdd:PRK08279 325 ---R---------PDIWDEFQQRFGIPrILEFYAASEgNVGFINV--FNFDGT--VG-RVPLwlahpyaiVKydvdtgep 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 366 VRISD-------EGEV-----QVRSGATMVGyYKEPEKTAEVLTADGF------LRTGDKGEQDAEGNLRLTGRMKEIFK 427
Cdd:PRK08279 388 VRDADgrcikvkPGEVglligRITDRGPFDG-YTDPEASEKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDTFR 466
|
490 500
....*....|....*....|....*....
gi 489188483 428 TsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK08279 467 W-KGENVATTEVENALSGFPGVEEAVVYG 494
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
37-456 |
9.13e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 83.33 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRS-LDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV---PLYP------------------- 93
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVntnPLYTaremrhqfkdsgaralvyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 94 NLTAESARQVLEHSESAVVFVGKLDDWPAMAPG---------VPEGIPTVAMPLH-PEGRFDRQWSDLqACAPLegdtPT 163
Cdd:PRK12492 130 NMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGwlvntvvdkVKKMVPAYHLPQAvPFKQALRQGRGL-SLKPV----PV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 164 AAEQLATLIYTSGTTGVPKGVM--HN---------FSSFAFAASRGVELFgtRE-DDRMLSYLPLCHV----AERMFVeM 227
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKGAMltHGnlvanmlqvRACLSQLGPDGQPLM--KEgQEVMIAPLPLYHIyaftANCMCM-M 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 228 GSlyGGTTVFFAESLDT--FVEDMKRARPTLLFGVPRIWtkfqMGVYSKMPAQKLD-RLLKLPILGrivgrkvlaglgld 304
Cdd:PRK12492 282 VS--GNHNVLITNPRDIpgFIKELGKWRFSALLGLNTLF----VALMDHPGFKDLDfSALKLTNSG-------------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 305 avryalcGAAPVPEALLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQ-KTGWIGQNSPGVEVRISDE----------GE 373
Cdd:PRK12492 342 -------GTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELaRLGTVGIPVPGTALKVIDDdgnelplgerGE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVC 453
Cdd:PRK12492 415 LCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS-GFNVYPNEIEDVVMAHPKVANCA 493
|
...
gi 489188483 454 VVG 456
Cdd:PRK12492 494 AIG 496
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
165-445 |
1.64e-16 |
|
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: 82.15 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 165 AEQLATLIYTSGTTGVPKGVM---HNFSSFAFAASRGVElfgTREDDRMLSYLPLCHvaermfvEMGSLYGGTTVFFAES 241
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMlthENLVHNMFAILNSTE---WKTKDRILSWMPLTH-------DMGLIAFHLAPLIAGM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 LDTFVedmkrarPTLLFGV-PRIWTKfqmgvysKMPAQKLDrLLKLPILG-----RIVGRKVLAGLGLDAVRYALCGAAP 315
Cdd:cd05908 175 NQYLM-------PTRLFIRrPILWLK-------KASEHKAT-IVSSPNFGykyflKTLKPEKANDWDLSSIRMILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 316 VP----EALLLWYRRLGLD---VLEVYGMTENSgySHVCRPGRQKTGW----------IGQNSPGV-------------- 364
Cdd:cd05908 240 IDyelcHEFLDHMSKYGLKrnaILPVYGLAEAS--VGASLPKAQSPFKtitlgrrhvtHGEPEPEVdkkdsecltfvevg 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 365 ------EVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQdAEGNLRLTGRMKEIFKT 428
Cdd:cd05908 318 kpidetDIRICDEdnkilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFV 396
|
330
....*....|....*..
gi 489188483 429 SkGKYVAPAPIEnRLAV 445
Cdd:cd05908 397 N-GQNVYPHDIE-RIAE 411
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
37-456 |
6.68e-16 |
|
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: 80.25 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG- 115
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 ----KLDDWPAMapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqlatLIYTSGTTGVPKGVMHNFSSF 191
Cdd:cd05973 81 anrhKLDSDPFV-----------------------------------------------MMFTSGTTGLPKGVPVPLRAL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 192 AFAASRGVELFGTREDDRMLSylplchvaermFVEMGSLYGgttVFFAesldtFVEDMKRARPTLL----FGVPRIW-TK 266
Cdd:cd05973 114 AAFGAYLRDAVDLRPEDSFWN-----------AADPGWAYG---LYYA-----ITGPLALGHPTILleggFSVESTWrVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 267 FQMGVYSKMPAQKLDRLLklpilgRIVGRKVLAGLGLDAVRYALCGAAPVPEaLLLWYR-RLGLDVLEVYGMTEN----S 341
Cdd:cd05973 175 ERLGVTNLAGSPTAYRLL------MAAGAEVPARPKGRLRRVSSAGEPLTPE-VIRWFDaALGVPIHDHYGQTELgmvlA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSHVCRPGRQktGWIGQNSPGVEVRISDEGEVQVRSGA--------------TMVGYYKEPEKTAevltADGFLRTGDK 407
Cdd:cd05973 248 NHHALEHPVHA--GSAGRAMPGWRVAVLDDDGDELGPGEpgrlaidiansplmWFRGYQLPDTPAI----DGGYYLTGDT 321
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 489188483 408 GEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVI-TMSGYRIGPFDVESALIEHPAVAEAAVIG 369
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
173-457 |
3.02e-15 |
|
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: 76.68 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 173 YTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHvAERMFVEMGSLYGGTTVFFAESLD--TFVEDMK 250
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNpkSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 251 RARPTLLFGVPriwtkfqmgvyskmpaQKLDRLLKlpilgriVGRKVLAglgldaVRYALCGAAPVPEALLLWYRRL--G 328
Cdd:cd17633 86 QYNATVIYLVP----------------TMLQALAR-------TLEPESK------IKSIFSSGQKLFESTKKKLKNIfpK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 329 LDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDE-----GEVQVRSGATMVGYYKEpektaEVLTADGFLR 403
Cdd:cd17633 137 ANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNAdggeiGKIFVKSEMVFSGYVRG-----GFSNPDGWMS 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489188483 404 TGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGE 457
Cdd:cd17633 212 VGDIGYVDEEGYLYLVGRESDMIIIG-GINIFPTEIESVLKAIPGIEEAIVVGI 264
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-456 |
3.05e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 78.65 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 1 MVTANRLPLEVFFEREKRHPQRRYLVQPIGggrveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA 80
Cdd:PRK13382 38 MRREGMGPTSGFAIAAQRCPDRPGLIDELG-----TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 81 IWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVGKlddwpamapgvpEGIPTVAMPLH--PEGRFDRQWSDLQACAPLE 158
Cdd:PRK13382 113 ANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE------------EFSATVDRALAdcPQATRIVAWTDEDHDLTVE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 159 -------GDTPTAAEQLA-TLIYTSGTTGVPKGVMHNFSSFAFAASRgvelfgtreddrMLSYLPLchVAERMFV---EM 227
Cdd:PRK13382 181 vliaahaGQRPEPTGRKGrVILLTSGTTGTPKGARRSGPGGIGTLKA------------ILDRTPW--RAEEPTVivaPM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 228 GSLYGGTTVFFAESL------------DTFVEDMKRARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLP--ILGRIV 293
Cdd:PRK13382 247 FHAWGFSQLVLAASLactivtrrrfdpEATLDLIDRHRATGLAVVPVM----------------FDRIMDLPaeVRNRYS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 294 GRkvlaglgldAVRYALCGAAPV-PEALLLWYRRLGlDVL-EVYGMTEnSGYSHVCRPG--RQKTGWIGQNSPGVEVRIS 369
Cdd:PRK13382 311 GR---------SLRFAAASGSRMrPDVVIAFMDQFG-DVIyNNYNATE-AGMIATATPAdlRAAPDTAGRPAEGTEIRIL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 370 DE-------GEVQ---VRSGATMVGYykEPEKTAEvlTADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPI 439
Cdd:PRK13382 380 DQdfrevptGEVGtifVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEV 454
|
490
....*....|....*..
gi 489188483 440 ENRLAVHDRIEQVCVVG 456
Cdd:PRK13382 455 EKTLATHPDVAEAAVIG 471
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-455 |
9.23e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.19 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 12 FFEREKR-HPQRRYLVQpiggGRVEeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVP 90
Cdd:PLN02479 25 FLERAAVvHPTRKSVVH----GSVR-YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNC 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 91 LYPNLTAESARQVLEHSESAVVFVGK-----LDDWPAMAPGVPEGipTVAMPL---------------HPEGRFDRQWSD 150
Cdd:PLN02479 100 VNIRLNAPTIAFLLEHSKSEVVMVDQefftlAEEALKILAEKKKS--SFKPPLlivigdptcdpkslqYALGKGAIEYEK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 151 -LQACAPLEGDTPTAAE-QLATLIYTSGTTGVPKGV-MHNFSSFAFAASRGVeLFGTREDDRMLSYLPLCHVAERMFVEM 227
Cdd:PLN02479 178 fLETGDPEFAWKPPADEwQSIALGYTSGTTASPKGVvLHHRGAYLMALSNAL-IWGMNEGAVYLWTLPMFHCNGWCFTWT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 228 GSLYGGTTVFFAE-SLDTFVEDMKRARPTLLFGVPRIWTKFqmgvyskMPAQKLDRLLKLPILgrivgrkvlaglgldaV 306
Cdd:PLN02479 257 LAALCGTNICLRQvTAKAIYSAIANYGVTHFCAAPVVLNTI-------VNAPKSETILPLPRV----------------V 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 307 RYALCGAAPvPEALLLWYRRLGLDVLEVYGMTENSGYSHVC--RP--------------GRQKTGWIG---------QNS 361
Cdd:PLN02479 314 HVMTAGAAP-PPSVLFAMSEKGFRVTHTYGLSETYGPSTVCawKPewdslppeeqarlnARQGVRYIGlegldvvdtKTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 362 PGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIEN 441
Cdd:PLN02479 393 KPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLEVEN 470
|
490
....*....|....
gi 489188483 442 RLAVHDRIEQVCVV 455
Cdd:PLN02479 471 VVYTHPAVLEASVV 484
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
34-490 |
1.17e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 76.58 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 34 VEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLyPNLTA--------ESARQVLE 105
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PLPMGfggresyiAQLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 106 HSESAVVFVGklDDWPAMAPGVPEGIPtvamplhpeGRFDRQWSDLQACAPLEGDTPTA-AEQLATLIYTSGTTGVPKGV 184
Cdd:PRK09192 126 SAQPAAIITP--DELLPWVNEATHGNP---------LLHVLSHAWFKALPEADVALPRPtPDDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 185 -------MHNFSsfafAASR-GVELfgtREDDRMLSYLPLCHvaermfvEMGsLYGgttvFFAESLDTFVE-DMkraRPT 255
Cdd:PRK09192 195 iithralMANLR----AISHdGLKV---RPGDRCVSWLPFYH-------DMG-LVG----FLLTPVATQLSvDY---LPT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 256 LLFGV-PRIWTKF---QMGVYSKMPAQKLDrllklpILGRIVGRKVLAGLGLDAVRYALCGAAPV--------------- 316
Cdd:PRK09192 253 RDFARrPLQWLDLisrNRGTISYSPPFGYE------LCARRVNSKDLAELDLSCWRVAGIGADMIrpdvlhqfaeafapa 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 317 ---PEALLLWY--------------------RRLGLDVLEVYGMTENSGyshvCRPGRQKTGWI-GQNSPGVEVRISDE- 371
Cdd:PRK09192 327 gfdDKAFMPSYglaeatlavsfsplgsgivvEEVDRDRLEYQGKAVAPG----AETRRVRTFVNcGKALPGHEIEIRNEa 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 ---------GEVQVRSGATMVGYYKEPEkTAEVLTADGFLRTGDKGEQdAEGNLRLTGRMKEIFkTSKGKYVAPAPIENR 442
Cdd:PRK09192 403 gmplpervvGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLI-IINGRNIWPQDIEWI 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 443 LAVHDRIEQ--VCVVG---EGLSAPLGL--CVLSEVGRREALngtRGALESSLRA 490
Cdd:PRK09192 480 AEQEPELRSgdAAAFSiaqENGEKIVLLvqCRISDEERRGQL---IHALAALVRS 531
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
37-477 |
1.93e-14 |
|
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: 75.68 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVgk 116
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 117 lddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAAS 196
Cdd:cd05974 79 -------------------------------------------DENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 197 RGVELFGTREDDRMLSYLP---LCHVAERMFVEMGSlyGGTTVFFAES---LDTFVEDMKRARPTLLFGVPRIWtkfqmg 270
Cdd:cd05974 116 STMYWIGLKPGDVHWNISSpgwAKHAWSCFFAPWNA--GATVFLFNYArfdAKRVLAALVRYGVTTLCAPPTVW------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 271 vysKMPAQKLDRLLKLPiLGRIVGrkvlAGLGLDavryalcgaapvPEALLLWYRRLGLDVLEVYGMTENS---GYShvc 347
Cdd:cd05974 188 ---RMLIQQDLASFDVK-LREVVG----AGEPLN------------PEVIEQVRRAWGLTIRDGYGQTETTalvGNS--- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 348 rPGRQ-KTGWIGQNSPGVEVRISD-------EGEVQVRSGAT-----MVGYYKEPEKTAEVLtADGFLRTGDKGEQDAEG 414
Cdd:cd05974 245 -PGQPvKAGSMGRPLPGYRVALLDpdgapatEGEVALDLGDTrpvglMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDG 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 415 NLRLTGRMKEIFKTSKGKyVAPAPIENRLAVHDRIEQVCVV----GEGLSAPLGLCVL---SEVGRREAL 477
Cdd:cd05974 323 YLTYVGRADDVFKSSDYR-ISPFELESVLIEHPAVAEAAVVpspdPVRLSVPKAFIVLragYEPSPETAL 391
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-456 |
4.10e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 74.93 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 29 IGGGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSE 108
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVFVGklddwPAMAPGVP-EGIPT------VAMPLHPEGRFDRQWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVP 181
Cdd:PRK04319 146 AKVLITT-----PALLERKPaDDLPSlkhvllVGEDVEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 182 KGVMH--NFSSFAFAASRGVELFgtREDDRM-----------LSY---LPLCHvaermfvemgslyGGTTV-----FFAE 240
Cdd:PRK04319 221 KGVLHvhNAMLQHYQTGKYVLDL--HEDDVYwctadpgwvtgTSYgifAPWLN-------------GATNVidggrFSPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 241 SLDTFVEDMkraRPTLLFGVPriwTKFQMgvyskmpaqkldrLLKlpilgriVGRKVLAGLGLDAVRYALCGAAPV-PEA 319
Cdd:PRK04319 286 RWYRILEDY---KVTVWYTAP---TAIRM-------------LMG-------AGDDLVKKYDLSSLRHILSVGEPLnPEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 320 LLLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQ-KTGWIGQNSPGVEVRISD----------EGEVQVRSG--ATMVGYY 386
Cdd:PRK04319 340 VRWGMKVFGLPIHDNWWMTETGGIMIANYPAMDiKPGSMGKPLPGIEAAIVDdqgnelppnrMGNLAIKKGwpSMMRGIW 419
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 387 KEPEKTAEVLtADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK04319 420 NNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTS-GERVGPFEVESKLMEHPAVAEAGVIG 487
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
10-466 |
7.25e-14 |
|
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: 73.90 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVqpIGGgrvEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:cd17655 1 ELFEEQAEKTPDHTAVV--FED---QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVFVgklddwpamapgvpegiptvamplhpEGRFDRQWSDLQACAPLEGDT-------- 161
Cdd:cd17655 76 PIDPDYPEERIQYILEDSGADILLT--------------------------QSHLQPPIAFIGLIDLLDEDTiyheesen 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 162 ---PTAAEQLATLIYTSGTTGVPKGVM------HNFSSFAfaasrgVELFGTREDDRMLSYLPLCHVA--ERMFVemgSL 230
Cdd:cd17655 130 lepVSKSDDLAYVIYTSGSTGKPKGVMiehrgvVNLVEWA------NKVIYQGEHLRVALFASISFDAsvTEIFA---SL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 231 YGGTTVFF-----AESLDTFVEDMKRARPTLLFGVPriwTKFQMGVYSkmpaqklDRLLKLPILGRIVGrkvlaglglda 305
Cdd:cd17655 201 LSGNTLYIvrketVLDGQALTQYIRQNRITIIDLTP---AHLKLLDAA-------DDSEGLSLKHLIVG----------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 306 vryalcGAAPVPEALLLWYRRLGL--DVLEVYGMTENS--GYSHVCRPGRQKTGWIGQNSPGVEVR--ISDE-------- 371
Cdd:cd17655 260 ------GEALSTELAKKIIELFGTnpTITNAYGPTETTvdASIYQYEPETDQQVSVPIGKPLGNTRiyILDQygrpqpvg 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 --GEVQVRSGATMVGYYKEPEKTAEVLTADGFL------RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRL 443
Cdd:cd17655 334 vaGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRIELGEIEARL 412
|
490 500
....*....|....*....|....
gi 489188483 444 AVHDRI-EQVCVVGEGLSAPLGLC 466
Cdd:cd17655 413 LQHPDIkEAVVIARKDEQGQNYLC 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
171-456 |
1.38e-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: 71.95 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFF----AESLDTFV 246
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVrrvdAEEVLELI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDmKRARPTLLFGvPRIwtkfqmgvySKMPAQKLDRLLKLPilgrivgrkvlaglGLDAVRYALCGAAPVPEALLLWYRR 326
Cdd:cd17636 85 EA-ERCTHAFLLP-PTI---------DQIVELNADGLYDLS--------------SLRSSPAAPEWNDMATVDTSPWGRK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 327 LGLdvlevYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEvL 396
Cdd:cd17636 140 PGG-----YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEdgrevpdgevGEIVARGPTVMAGYWNRPEVNAR-R 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 397 TADGFLRTGDKGEQDAEGNLRLTGRMKEIFKtSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd17636 214 TRGGWHHTNDLGRREPDGSLSFVGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAAVIG 272
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
35-456 |
1.40e-13 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 72.85 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRS-LDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF 113
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 VGklDDWPAMapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeqlatLIYTSGTTGVPKGV-MHNFSSFA 192
Cdd:cd05937 84 VD--PDDPAI-----------------------------------------------LIYTSGTTGLPKAAaISWRRTLV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 193 FAASRGvELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRARPTLLFGV---------- 260
Cdd:cd05937 115 TSNLLS-HDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRkfSASQFWKDVRDSGATIIQYVgelcryllst 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 261 --------------------PRIWTKFQmgvyskmpaqklDRlLKLPILGRIVgRKVLAGLGLDAVRYALCGAAPVPEAL 320
Cdd:cd05937 194 ppspydrdhkvrvawgnglrPDIWERFR------------ER-FNVPEIGEFY-AATEGVFALTNHNVGDFGAGAIGHHG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 321 LLWYRRLGLDVLEVyGMTENSGysHVCRpgRQKTGWIgqnspgVEVRISDEGEVQVR----SGATMVGYYKEPEKTAEVL 396
Cdd:cd05937 260 LIRRWKFENQVVLV-KMDPETD--DPIR--DPKTGFC------VRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKL 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 397 TADGF------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05937 329 VRDVFrkgdiyFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYG 393
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-494 |
2.46e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 73.28 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHS------E 108
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSgiglllS 2291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 109 SAVVF--VGKL----------DDWPAMAPGVPEGIPTVAMPLHpegrfdrqwsdlqacaplegdtptaaeqLATLIYTSG 176
Cdd:PRK05691 2292 DRALFeaLGELpagvarwcleDDAAALAAYSDAPLPFLSLPQH----------------------------QAYLIYTSG 2343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 177 TTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVA--ERMFVEMgsLYGGTTVFFAE---SLDTFVEDMKR 251
Cdd:PRK05691 2344 STGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAasERLLVPL--LCGARVVLRAQgqwGAEEICQLIRE 2421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 252 ARPTLLFGVPRiwtkfqmgvYSKMPAQKL-DRLLKLPILGRIVGRKVLAGLGLDAVRyalcgAAPVPEALllwyrrlgld 330
Cdd:PRK05691 2422 QQVSILGFTPS---------YGSQLAQWLaGQGEQLPVRMCITGGEALTGEHLQRIR-----QAFAPQLF---------- 2477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 331 vLEVYGMTENSGYSHVCR-PGRQKTGW----IGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYKEPEKTAEV 395
Cdd:PRK05691 2478 -FNAYGPTETVVMPLACLaPEQLEEGAasvpIGRVVGARVAYILDADLALVPQGATgelyvggaglAQGYHDRPGLTAER 2556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 396 LTADGF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVGEGLSAP---LGL 465
Cdd:PRK05691 2557 FVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDHQVKI-RGFRIELGEIESRLLEHPAVREAVVLALDTPSGkqlAGY 2635
|
490 500
....*....|....*....|....*....
gi 489188483 466 CVLSEVGRREAlngTRGALESSLRAHLEQ 494
Cdd:PRK05691 2636 LVSAVAGQDDE---AQAALREALKAHLKQ 2661
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
37-493 |
3.11e-13 |
|
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: 71.66 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLP-AGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFvg 115
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 116 klddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFAA 195
Cdd:cd17648 91 -----------------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 196 SRGVELFG--TREDDRMLSYLPLC--HVAERMFveMGSLYGGTTVFFAESL----DTFVEDMKRARPTLLFGVPRIWTKF 267
Cdd:cd17648 124 TSLSERYFgrDNGDEAVLFFSNYVfdFFVEQMT--LALLNGQKLVVPPDEMrfdpDRFYAYINREKVTYLSGTPSVLQQY 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 268 QMGvyskmpaqkldrllKLPILGRIvgrkvlaglglDAVRYALcgAAPVPEALLLWYRRLgldVLEVYGMTENSGYSHVC 347
Cdd:cd17648 202 DLA--------------RLPHLKRV-----------DAAGEEF--TAPVFEKLRSRFAGL---IINAYGPTETTVTNHKR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 348 R--PGRQKTGWIGQNSPGVEVRISDEGEVQVRSGAT----------MVGYYKEPEKTAEVLTADGF-------------- 401
Cdd:cd17648 252 FfpGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVgelylggdgvARGYLNRPELTAERFLPNPFqteqerargrnarl 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 402 LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV-GEGLSAPLGlcvlsevGRREALNG- 479
Cdd:cd17648 332 YKTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALASYPGVRECAVVaKEDASQAQS-------RIQKYLVGy 403
|
490
....*....|....*...
gi 489188483 480 ----TRGALESSLRAHLE 493
Cdd:cd17648 404 ylpePGHVPESDLLSFLR 421
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
39-484 |
4.14e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.72 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 39 WGEVGDQARRAAAWLrsLDLPAGSRIAIISKNCAHWIVTDLAIWMAGhVSVPLYPNLT--------AESA---------R 101
Cdd:PRK05851 34 WPEVHGRAENVAARL--LDRDRPGAVGLVGEPTVELVAAIQGAWLAG-AAVSILPGPVrgaddgrwADATltrfagigvR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 102 QVLEHSEsavvfvgKLDDWPAMAPGVPegIPTVAmplhpegrfdrQWSDLQACAPLegdTPTAAEQLATLIYTSGTTGVP 181
Cdd:PRK05851 111 TVLSHGS-------HLERLRAVDSSVT--VHDLA-----------TAAHTNRSASL---TPPDSGGPAVLQGTAGSTGTP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 182 K-------GVMHNFSsfAFAASRGVelfgTREDDRMLSYLPLCHVAERMFVEMGSLYG-----GTTVFFAESLDTFVEDM 249
Cdd:PRK05851 168 RtailspgAVLSNLR--GLNARVGL----DAATDVGCSWLPLYHDMGLAFLLTAALAGaplwlAPTTAFSASPFRWLSWL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 250 KRARPTLlfgvpriwTKFQMGVYSkmpaqkldrllklpILGRIVGRkvLAGLGLDAVRYALCGAAPVP----EALLLWYR 325
Cdd:PRK05851 242 SDSRATL--------TAAPNFAYN--------------LIGKYARR--VSDVDLGALRVALNGGEPVDcdgfERFATAMA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 326 RLGLD---VLEVYGMTENSGYSHVCRPG---------------RQKTGWIGQNSPGVEVRIS-----------DEGEVQV 376
Cdd:PRK05851 298 PFGFDagaAAPSYGLAESTCAVTVPVPGiglrvdevttddgsgARRHAVLGNPIPGMEVRISpgdgaagvagrEIGEIEI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 377 RSGATMVGYYKEPEktaevLTADGFLRTGDKGEQdAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK05851 378 RGASMMSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAKELI-TVAGRNIFPTEIERVAAQVRGVREGAVVA 450
|
490 500 510
....*....|....*....|....*....|..
gi 489188483 457 EGL---SAPLGLCVLSE-VGRREAlnGTRGAL 484
Cdd:PRK05851 451 VGTgegSARPGLVIAAEfRGPDEA--GARSEV 480
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
10-455 |
4.42e-13 |
|
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: 71.43 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVQpigggRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSV 89
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD-----RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 90 PLYPNLTAESARQVLEHSESAVVFvgklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtpTAAEQLA 169
Cdd:cd17645 77 PIDPDYPGERIAYMLADSSAKILL-------------------------------------------------TNPDDLA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 170 TLIYTSGTTGVPKGVM---HNFSSFAFAASrgvELFGTREDDRMLSYLPLchvaermfvemgslyggttvffaeSLDTFV 246
Cdd:cd17645 108 YVIYTSGSTGLPKGVMiehHNLVNLCEWHR---PYFGVTPADKSLVYASF------------------------SFDASA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 247 EDMkraRPTLLFGVpriwtkfQMGVYSKMPAQKLDRL--------LKLPILGRIVGRKVLAgLGLDAVRYALCGAAPVPE 318
Cdd:cd17645 161 WEI---FPHLTAGA-------ALHVVPSERRLDLDALndyfnqegITISFLPTGAAEQFMQ-LDNQSLRVLLTGGDKLKK 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 319 AlllwyRRLGLDVLEVYGMTENS--GYSHVCRPGRQKTGwIGQNSPGVEVRISDE----------GEVQVRSGATMVGYY 386
Cdd:cd17645 230 I-----ERKGYKLVNNYGPTENTvvATSFEIDKPYANIP-IGKPIDNTRVYILDEalqlqpigvaGELCIAGEGLARGYL 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 387 KEPEKTAEVLTADGFL------RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd17645 304 NRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVL 377
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
35-513 |
1.63e-12 |
|
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: 69.69 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gklddwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaaeQLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:cd05940 82 ----------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRARPTLLFGVPRIwTKFQMgvy 272
Cdd:cd05940 110 GAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKkfSASNFWDDIRKYQATIFQYIGEL-CRYLL--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 273 sKMPAQKLDRLLKLpilgrivgRKVLaGLGLDavryalcgaapvPEallLWYR---RLGL-DVLEVYGMTE-NSGYSHVC 347
Cdd:cd05940 186 -NQPPKPTERKHKV--------RMIF-GNGLR------------PD---IWEEfkeRFGVpRIAEFYAATEgNSGFINFF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 348 RpgrqKTGWIGQNSPGVEVRISDE------------------------GEV-----QVRSGATMVGYYKEPEKTAEVLT- 397
Cdd:cd05940 241 G----KPGAIGRNPSLLRKVAPLAlvkydlesgepirdaegrcikvprGEPgllisRINPLEPFDGYTDPAATEKKILRd 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 398 ----ADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG---EGLSAPLGLCVLSe 470
Cdd:cd05940 317 vfkkGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVYGvqvPGTDGRAGMAAIV- 394
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489188483 471 VGRREALNGtrgaleSSLRAHLEQvngALDKHERLVGLVLVQE 513
Cdd:cd05940 395 LQPNEEFDL------SALAAHLEK---NLPGYARPLFLRLQPE 428
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
35-422 |
3.73e-12 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 68.77 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFv 114
Cdd:PRK04813 26 EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 gKLDDWPAMApgvpEGIPTVamplhpegrfdrQWSDLQAcAPLEGDTPTAAEQL-----ATLIYTSGTTGVPKGVM--H- 186
Cdd:PRK04813 105 -ATEELPLEI----LGIPVI------------TLDELKD-IFATGNPYDFDHAVkgddnYYIIFTSGTTGKPKGVQisHd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 187 NFSSFafaASRGVELFGTREDDRMLSYLPLCHVAERMfvemgSLY-----GGTTVffaeSLD-TFVEDMKR---ARPTLL 257
Cdd:PRK04813 167 NLVSF---TNWMLEDFALPEGPQFLNQAPYSFDLSVM-----DLYptlasGGTLV----ALPkDMTANFKQlfeTLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 258 FGVpriWT---KF-QMGVYSKMPAQKldrllKLPilgrivgrkvlaglglDAVRYALCGAA-PVPEALLLWYRRLGLDVL 332
Cdd:PRK04813 235 INV---WVstpSFaDMCLLDPSFNEE-----HLP----------------NLTHFLFCGEElPHKTAKKLLERFPSATIY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 333 EVYGMTENS---------------------GYshvCRPGrqkTGWIGQNSPGVEVRISDEGEVqVRSGATM-VGYYKEPE 390
Cdd:PRK04813 291 NTYGPTEATvavtsieitdemldqykrlpiGY---AKPD---SPLLIIDEEGTKLPDGEQGEI-VISGPSVsKGYLNNPE 363
|
410 420 430
....*....|....*....|....*....|....*
gi 489188483 391 KTAEVL-TADG--FLRTGDKGEQDaEGNLRLTGRM 422
Cdd:PRK04813 364 KTAEAFfTFDGqpAYHTGDAGYLE-DGLLFYQGRI 397
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
145-427 |
4.64e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 68.58 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 145 DRQWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAfaasRGVELFGTRED----DRMLSYLPLCHVA 220
Cdd:PRK08043 344 DKLWIFAHLLMPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADftpnDRFMSALPLFHSF 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 221 ERMFVEMGSLYGGTTVFFAESLDTF--VEDMKRARP-TLLFGvpriwTKFQMGVYSKMpAQKLDrllklpiLGRivgrkv 297
Cdd:PRK08043 420 GLTVGLFTPLLTGAEVFLYPSPLHYriVPELVYDRNcTVLFG-----TSTFLGNYARF-ANPYD-------FAR------ 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 298 laglgldaVRYALCGAAPVPEAL-LLWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVR------ISD 370
Cdd:PRK08043 481 --------LRYVVAGAEKLQESTkQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARllsvpgIEQ 552
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 371 EGEVQVRSGATMVGYYK-EPEKTAEVLTAD--------GFLRTGDKGEQDAEGNLRLTGRMKEIFK 427
Cdd:PRK08043 553 GGRLQLKGPNIMNGYLRvEKPGVLEVPTAEnargemerGWYDTGDIVRFDEQGFVQIQGRAKRFAK 618
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
171-509 |
4.88e-12 |
|
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: 67.41 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFaFAASRGVELFGTREDD---------------RMLSYLPLCHVAErMFVEMGSLYGGTT 235
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDI-FRMLMGGADFGTGEFTpsedahkaaaaaagtVMFPAPPLMHGTG-SWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 236 VFFAE---SLDTFVEDMKRARPTLLFGVPRIWTKFQMGVYSKMPAQKLDRLLKLPILGRIVGRKVLAGLgLDAVryalcg 312
Cdd:cd05924 86 VVLPDdrfDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGL-LELV------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 313 aapvPEALLLwyrrlgldvlEVYGMTE--NSGYSHVcRPGRQKTGWIGQNSPGVEVRISDEGEVQV---------RSGAT 381
Cdd:cd05924 159 ----PNITLV----------DAFGSSEtgFTGSGHS-AGSGPETGPFTRANPDTVVLDDDGRVVPPgsggvgwiaRRGHI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 382 MVGYYKEPEKTAEVL-TADG--FLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVGEG 458
Cdd:cd05924 224 PLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEALKSHPAVYDVLVVGRP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489188483 459 lSAPLGLCVLSEVGRREALNGTRGALESSLRAHLeqvngALDKHERLVGLV 509
Cdd:cd05924 303 -DERWGQEVVAVVQLREGAGVDLEELREHCRTRI-----ARYKLPKQVVFV 347
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
38-456 |
2.89e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 65.82 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 38 SWGEVGDQARRAAAWLRSLDLPAGS-RIAIISKNcahwiVTDLAIWMA-----GHVSVPLYPNL-TAESARQVLeHSESA 110
Cdd:PRK13388 28 TWREVLAEAAARAAALIALADPDRPlHVGVLLGN-----TPEMLFWLAaaalgGYVLVGLNTTRrGAALAADIR-RADCQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VVFVGklddwpamapgvPEGIPTVAMPLHPEGRF----DRQWSDLQACAP-LEGDTPTAAEQLATLIYTSGTTGVPKGVM 185
Cdd:PRK13388 102 LLVTD------------AEHRPLLDGLDLPGVRVldvdTPAYAELVAAAGaLTPHREVDAMDPFMLIFTSGTTGAPKAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 186 HNFSSFAFAASRGVELFGTREDDRMLSYLPLCH---VAERMFVEMGSlyGGTTVFFAE-SLDTFVEDMKRARPTLLFGVP 261
Cdd:PRK13388 170 CSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHsnaVMAGWAPAVAS--GAAVALPAKfSASGFLDDVRRYGATYFNYVG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 262 RiwtkfqmgvyskmpaqKLDRLLKLPILGRIVGRKVLAGLGLDAVryalcgaapvPEALLLWYRRLGLDVLEVYGMTENS 341
Cdd:PRK13388 248 K----------------PLAYILATPERPDDADNPLRVAFGNEAS----------PRDIAEFSRRFGCQVEDGYGSSEGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYshVCRPGRQKTGWIGQNSPGVE-----------VRISDE-----------GEVQVRSGATM-VGYYKEPEKTAEVLtA 398
Cdd:PRK13388 302 VI--VVREPGTPPGSIGRGAPGVAiynpetltecaVARFDAhgallnadeaiGELVNTAGAGFfEGYYNNPEATAERM-R 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 399 DGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK13388 379 HGMYWSGDLAYRDADGWIYFAGRTADWMRVD-GENLSAAPIERILLRHPAINRVAVYA 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
37-499 |
4.43e-11 |
|
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: 65.41 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 37 LSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV-- 114
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTas 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 -----GK-------LDDWPAMAPGVPEGI-----PTVAM-PLHPEGRFDrqWSDLQA------CAPLEGDTPTaaeqlaT 170
Cdd:cd05967 163 cgiepGKvvpykplLDKALELSGHKPHHVlvlnrPQVPAdLTKPGRDLD--WSELLAkaepvdCVPVAATDPL------Y 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 171 LIYTSGTTGVPKGVMHNFSSFAFAASRGVE-LFGTREDDRMLS--------------YLPLCHvaermfvemgslyGGTT 235
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMRnIYGIKPGDVWWAasdvgwvvghsyivYGPLLH-------------GATT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 236 VFFaESLDTFVED-------MKRARPTLLFGVP---RIWTKFQmgvyskmPAQKLDRLLKLPILGRIvgrkVLAGLGLDA 305
Cdd:cd05967 302 VLY-EGKPVGTPDpgafwrvIEKYQVNALFTAPtaiRAIRKED-------PDGKYIKKYDLSSLRTL----FLAGERLDP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 306 VRYAlcgaapvpealllWYRR-LGLDVLEVYGMTEnSGYSHVCRP-GRQ----KTGWIGQNSPGVEVRISDEGEVQVRSG 379
Cdd:cd05967 370 PTLE-------------WAENtLGVPVIDHWWQTE-TGWPITANPvGLEplpiKAGSPGKPVPGYQVQVLDEDGEPVGPN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 380 A-------------TMVGYYKEPE--KTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLA 444
Cdd:cd05967 436 ElgniviklplppgCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVA-GHRLSTGEMEESVL 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489188483 445 VHDRIEQVCVVG--EGLSA--PLGLCVLsevgrREALNGTRGALESSLRAHLEQVNGAL 499
Cdd:cd05967 515 SHPAVAECAVVGvrDELKGqvPLGLVVL-----KEGVKITAEELEKELVALVREQIGPV 568
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
161-455 |
4.72e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 161 TPTAAEQLATLIYTSGTTGVPKGV--MHNfsSFAFAASRGVELFGTREDDRMLSYLPLCHvaERMFVEMGSL---YGGTT 235
Cdd:PRK10946 177 TPSPADEVAFFQLSGGSTGTPKLIprTHN--DYYYSVRRSVEICGFTPQTRYLCALPAAH--NYPMSSPGALgvfLAGGT 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 236 VFFAESLDtfvedmkrarPTLLFgvPRIwTKFQMGVYSKMPAQKLdrlLKLPILGRIVGRKVLAGLGLDAVryalcGAAP 315
Cdd:PRK10946 253 VVLAPDPS----------ATLCF--PLI-EKHQVNVTALVPPAVS---LWLQAIAEGGSRAQLASLKLLQV-----GGAR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 316 VPEALLlwyRR----LGLDVLEVYGMTE--------NSGYSHVC----RPgrqktgwigqNSPGVEVRISDE-------- 371
Cdd:PRK10946 312 LSETLA---RRipaeLGCQLQQVFGMAEglvnytrlDDSDERIFttqgRP----------MSPDDEVWVADAdgnplpqg 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 --GEVQVRSGATMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLAVHDRI 449
Cdd:PRK10946 379 evGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRG-GEKIAAEEIENLLLRHPAV 457
|
....*.
gi 489188483 450 EQVCVV 455
Cdd:PRK10946 458 IHAALV 463
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
169-423 |
5.84e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.37 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 169 ATLIYTSGTTGVPKGVM--HN--FSSFAFAASRgVElFGTreDDRMLSYLPLCHVaermFvemgSLYGGT---------T 235
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVlsHRnlLANRAQVAAR-ID-FSP--EDKVFNALPVFHS----F----GLTGGLvlpllsgvkV 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 236 VFFAESLDTfvedmkRARP--------TLLFGVpriwTKFQMGvYSKMpAQKLDrllklpilgrivgrkvlaglgLDAVR 307
Cdd:PRK06814 864 FLYPSPLHY------RIIPeliydtnaTILFGT----DTFLNG-YARY-AHPYD---------------------FRSLR 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 308 YALCGAAPVPEALL-LWYRRLGLDVLEVYGMTENSGYSHVCRPGRQKTGWIGQNSPGVEVR------ISDEGEVQVRSGA 380
Cdd:PRK06814 911 YVFAGAEKVKEETRqTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRlepvpgIDEGGRLFVRGPN 990
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489188483 381 TMVGYYKEPEKTAEVLTADGFLRTGDKGEQDAEGNLRLTGRMK 423
Cdd:PRK06814 991 VMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAK 1033
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
35-456 |
6.61e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 64.80 E-value: 6.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDlPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF- 113
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 ----VGKLDDwpamapgvpEGIPTVAMplhpegrfdRQW-SDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNF 188
Cdd:PRK07638 104 erykLNDLPD---------EEGRVIEI---------DEWkRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 189 SSFAFAASRGVELFGTREDDRMLSYLPLCHvAERMFVEMGSLYGGTTVFFAESLDTF--VEDMKRARPTLLFGVPRIWTK 266
Cdd:PRK07638 166 QSWLHSFDCNVHDFHMKREDSVLIAGTLVH-SLFLYGAISTLYVGQTVHLMRKFIPNqvLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 267 FQmgvyskmpaqKLDRLLKLPIlgrivgrKVLAGlgldavryalcGA---APVPEALLLWYRRLGLdvLEVYGMTENS-- 341
Cdd:PRK07638 245 LY----------KENRVIENKM-------KIISS-----------GAkweAEAKEKIKNIFPYAKL--YEFYGASELSfv 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 342 GYSH----------VCRPGRQKTGWIgQNSPGVEVRISDEGEVQVRSGATMVGYYKEPEKTAEvLTADGFLRTGDKGEQD 411
Cdd:PRK07638 295 TALVdeeserrpnsVGRPFHNVQVRI-CNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYED 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 489188483 412 AEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07638 373 EEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
31-456 |
1.41e-10 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 63.81 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESA 110
Cdd:TIGR02188 83 PGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VVFV-------GK-------LDDWPAMAPGVPE--------GIPTVAMPlhpEGRfDRQWSDLQA-----CAPlegdTPT 163
Cdd:TIGR02188 163 LVITadeglrgGKviplkaiVDEALEKCPVSVEhvlvvrrtGNPVVPWV---EGR-DVWWHDLMAkasayCEP----EPM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 164 AAEQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVE-LFGTREDDRML-----------SYL---PLCHvaermfvemg 228
Cdd:TIGR02188 235 DSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKyVFDIKDGDIFWctadvgwitghSYIvygPLAN---------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 229 slyGGTTVFFaESLDT------FVEDMKRARPTLLFGVP---RIWTKfqmgvYSKMPAQKLDrLLKLPILGRiVGRkvla 299
Cdd:TIGR02188 305 ---GATTVMF-EGVPTypdpgrFWEIIEKHKVTIFYTAPtaiRALMR-----LGDEWVKKHD-LSSLRLLGS-VGE---- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 300 glgldavryalcgaaPV-PEALLLWYRRLGLD---VLEVYGMTENSGYSHVCRPG--RQKTGWIGQNSPGVEVRISDEgE 373
Cdd:TIGR02188 370 ---------------PInPEAWMWYYKVVGKErcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVDE-E 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMVGY--------------YKEPEKTAEVL--TADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPA 437
Cdd:TIGR02188 434 GNPVEGPGEGGYlvikqpwpgmlrtiYGDHERFVDTYfsPFPGYYFTGDGARRDKDGYIWITGRVDDVINVS-GHRLGTA 512
|
490
....*....|....*....
gi 489188483 438 PIENRLAVHDRIEQVCVVG 456
Cdd:TIGR02188 513 EIESALVSHPAVAEAAVVG 531
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
35-455 |
6.22e-10 |
|
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: 61.72 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFV 114
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 -GKLDDWPAMapgvpEGIPTvamplHPEgrfdrqWSDLQACAPLEGDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAF 193
Cdd:cd17656 92 qRHLKSKLSF-----NKSTI-----LLE------DPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 194 AASRGVELFGTREDDRMLSY----LPLCHvaERMFVEMgsLYGGTtvffaesLDTFVEDMKRARPTL--LFGVPRIWTKF 267
Cdd:cd17656 156 LLHFEREKTNINFSDKVLQFatcsFDVCY--QEIFSTL--LSGGT-------LYIIREETKRDVEQLfdLVKRHNIEVVF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 268 QMGVYSKMPAQKLDRLLKLPilgRIVGRKVLAGLGLDavryalcgaapVPEALLLWYRRLGLDVLEVYGMTEN---SGYS 344
Cdd:cd17656 225 LPVAFLKFIFSEREFINRFP---TCVKHIITAGEQLV-----------ITNEFKEMLHEHNVHLHNHYGPSEThvvTTYT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 345 HVCRPGRQKTGWIGQNSPGVEVRISDE----------GEVQVrSGATMV-GYYKEPEKTAEVLTADGF------LRTGDK 407
Cdd:cd17656 291 INPEAEIPELPPIGKPISNTWIYILDQeqqlqpqgivGELYI-SGASVArGYLNRQELTAEKFFPDPFdpnermYRTGDL 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 489188483 408 GEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV 455
Cdd:cd17656 370 ARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEAVVL 416
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-455 |
1.83e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 4 ANRLPLEVFFEREKRHPQRRYLVQpiGGGrveELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWM 83
Cdd:PRK05691 1129 AQAWLPELLNEQARQTPERIALVW--DGG---SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILK 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 84 AGHVSVPLYPNLTAESARQVLEHSESAVVFV--GKLDDWPAmapgvPEGIPTVAM-PLHPEGrfdrqWSDLQACAPLEGD 160
Cdd:PRK05691 1204 AGGAYVPLDPDYPAERLAYMLADSGVELLLTqsHLLERLPQ-----AEGVSAIALdSLHLDS-----WPSQAPGLHLHGD 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 161 tptaaeQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPL---CHVAERMFvemgSLYGGTTVF 237
Cdd:PRK05691 1274 ------NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIsfdVSVWECFW----PLITGCRLV 1343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 238 FA---ESLDT--FVEDMKRARPTLLFGVPriwtkfqmgvyskmpaqkldrllklPILGRIVGRKVLAGLGldAVRYALCG 312
Cdd:PRK05691 1344 LAgpgEHRDPqrIAELVQQYGVTTLHFVP-------------------------PLLQLFIDEPLAAACT--SLRRLFSG 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 313 AAPVPEALllwyRRLGLDVL------EVYGMTE---NSGYSHvCRPGRQKTGWIGQNSPGVEVRISDE----------GE 373
Cdd:PRK05691 1397 GEALPAEL----RNRVLQRLpqvqlhNRYGPTEtaiNVTHWQ-CQAEDGERSPIGRPLGNVLCRVLDAelnllppgvaGE 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMVGYYKEPEKTAEVLTADGF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVH 446
Cdd:PRK05691 1472 LCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQARLLAQ 1550
|
....*....
gi 489188483 447 DRIEQVCVV 455
Cdd:PRK05691 1551 PGVAQAAVL 1559
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
310-456 |
3.12e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.24 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 310 LCGAAPVPEALLLWYRRLGLDVLEVYGMTENSgySHVC--RPGRQKTGWI--GQNSPGVEVRI--SDEGEVQVRSGATMV 383
Cdd:PRK07445 236 LLGGAPAWPSLLEQARQLQLRLAPTYGMTETA--SQIAtlKPDDFLAGNNssGQVLPHAQITIpaNQTGNITIQAQSLAL 313
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 384 GYYkePEKTAevltADGFLRTGDKGEQDAEGNLRLTGRM--KEIfktSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK07445 314 GYY--PQILD----SQGIFETDDLGYLDAQGYLHILGRNsqKII---TGGENVYPAEVEAAILATGLVQDVCVLG 379
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
10-213 |
5.67e-09 |
|
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: 58.32 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 10 EVFFEREKRHPQRRYLVQPIGggrveELSWGEVGDQARRAAAWLRSLDLPAGSRIAII---SKncahW-IVTDLAIWMAG 85
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDG-----SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCfekSK----WaVVAMLAVLKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 86 HVSVPLYPNLTAESARQVLEHSESAVVFVGKLDDwpamapgvpegiptvamplhpegrfdrqwsdlqacaplegdtptaa 165
Cdd:cd05918 74 GAFVPLDPSHPLQRLQEILQDTGAKVVLTSSPSD---------------------------------------------- 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489188483 166 eqLATLIYTSGTTGVPKGVM---HNFSSFAFAASRgveLFGTREDDRML---SY 213
Cdd:cd05918 108 --AAYVIFTSGSTGKPKGVViehRALSTSALAHGR---ALGLTSESRVLqfaSY 156
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
31-186 |
1.06e-08 |
|
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: 58.05 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA------IWMAghVSvplyPNLTAESA---- 100
Cdd:cd05943 93 DGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLAtasigaIWSS--CS----PDFGVPGVldrf 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 101 RQV---LEHSESAVVFVGK----LDDWPAMAPGVPEGIPTVAMP-LHPEGRFD-------RQWSDLQA---CAPLEGDTP 162
Cdd:cd05943 167 GQIepkVLFAVDAYTYNGKrhdvREKVAELVKGLPSLLAVVVVPyTVAAGQPDlskiakaLTLEDFLAtgaAGELEFEPL 246
|
170 180
....*....|....*....|....
gi 489188483 163 TAAEQLATLiYTSGTTGVPKGVMH 186
Cdd:cd05943 247 PFDHPLYIL-YSSGTTGLPKCIVH 269
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-555 |
1.00e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 55.17 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSEsavvfV 114
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSG-----V 3193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 115 GKLDDWPAMAPGVPegIPTVAMPLHPEGrfDRQWSDLQACAplegDTPTAAEQLATLIYTSGTTGVPKGVMHNFSSFAFA 194
Cdd:PRK12467 3194 KLLLTQAHLLEQLP--APAGDTALTLDR--LDLNGYSENNP----STRVMGENLAYVIYTSGSTGKPKGVGVRHGALANH 3265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 195 ASRGVELFGTREDDRMLSYLPLchvaermfvemgslyggttvffaeSLDTFVEdmkRARPTLLFGVP------RIWTKFQ 268
Cdd:PRK12467 3266 LCWIAEAYELDANDRVLLFMSF------------------------SFDGAQE---RFLWTLICGGClvvrdnDLWDPEE 3318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 269 MgvYSKMPAQKLDRLLKLP----ILGRIVGRKVLAGLGldavRYALCGAAPVPEALLLWYRRLGLDVL-EVYGMTE---- 339
Cdd:PRK12467 3319 L--WQAIHAHRISIACFPPaylqQFAEDAGGADCASLD----IYVFGGEAVPPAAFEQVKRKLKPRGLtNGYGPTEavvt 3392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 340 ----NSGYSHVCRPGRQKtgwIGQNSPGVEVRISDE----------GEVQVRSGATMVGYYKEPEKTAEVLTADGFL--- 402
Cdd:PRK12467 3393 vtlwKCGGDAVCEAPYAP---IGRPVAGRSIYVLDGqlnpvpvgvaGELYIGGVGLARGYHQRPSLTAERFVADPFSgsg 3469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 403 ----RTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVV---GEGLSAPLGLCVlsevgrre 475
Cdd:PRK12467 3470 grlyRTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVREAVVLardGAGGKQLVAYVV-------- 3540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 476 aLNGTRGALESSLRAHLEqvnGALDKHerlvglvLVQETWAVDNGF-LTPTLKIKRNMVEGAYGSRFHEWV------ERR 548
Cdd:PRK12467 3541 -PADPQGDWRETLRDHLA---ASLPDY-------MVPAQLLVLAAMpLGPNGKVDRKALPDPDAKGSREYVaprsevEQQ 3609
|
....*..
gi 489188483 549 EAVLWHE 555
Cdd:PRK12467 3610 LAAIWAD 3616
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
35-456 |
5.50e-07 |
|
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: 52.29 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 35 EELSWGEVGDQARRAA-AWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF 113
Cdd:cd05938 4 ETYTYRDVDRRSNQAArALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 VGklddwPAMAPGVPEGIPTV-AMPLH----PEGRFDRQWSDLQACAPLEGDTPTAAEQLATL--------IYTSGTTGV 180
Cdd:cd05938 84 VA-----PELQEAVEEVLPALrADGVSvwylSHTSNTEGVISLLDKVDAASDEPVPASLRAHVtikspalyIYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 181 PKGVMHNFSSfAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAE--SLDTFVEDMKRARPTLLF 258
Cdd:cd05938 159 PKAARISHLR-VLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPkfSASQFWDDCRKHNVTVIQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 259 GVPRIwtkfqMGVYSKMPAQKLDRllklpilgrivGRKVLAGLGlDAVRyalcgaAPVPEALLlwyRRLG-LDVLEVYGM 337
Cdd:cd05938 238 YIGEL-----LRYLCNQPQSPNDR-----------DHKVRLAIG-NGLR------ADVWREFL---RRFGpIRIREFYGS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 338 TE------------------NSGYSHVCR------------PGRQKTGWigqnspGVEVRisdEGEV-----QVRSGATM 382
Cdd:cd05938 292 TEgnigffnytgkigavgrvSYLYKLLFPfelikfdvekeePVRDAQGF------CIPVA---KGEPgllvaKITQQSPF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 383 VGYYKEPEKTAEVLTADGFLR------TGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:cd05938 363 LGYAGDKEQTEKKLLRDVFKKgdvyfnTGDLLVQDQQNFLYFHDRVGDTFRW-KGENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
36-185 |
6.51e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.35 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 36 ELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVFVG 115
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 562
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489188483 116 klDDWPAMAPGVPEG-IPTVAMPLHPegrfdrqwsdlQACAPLEGDTPtaaEQLATLIYTSGTTGVPKGVM 185
Cdd:PRK10252 563 --ADQLPRFADVPDLtSLCYNAPLAP-----------QGAAPLQLSQP---HHTAYIIFTSGSTGRPKGVM 617
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-499 |
1.05e-06 |
|
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: 51.41 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESA 110
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 111 VVFV-------GKLDDWPAMAPGVPEGIPTV-----------AMPLHpEGRfDRQWSDLQA-----CAPlegdTPTAAEQ 167
Cdd:cd05966 159 LVITadggyrgGKVIPLKEIVDEALEKCPSVekvlvvkrtggEVPMT-EGR-DLWWHDLMAkqspeCEP----EWMDSED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 168 LATLIYTSGTTGVPKGVMHN---FSSFAFAASRGVelFGTREDDRML-----------SYL---PLCHvaermfvemgsl 230
Cdd:cd05966 233 PLFILYTSGSTGKPKGVVHTtggYLLYAATTFKYV--FDYHPDDIYWctadigwitghSYIvygPLAN------------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 231 yGGTTVFFaESL------DTFVEDMKRARPTLLFGVP---RIWTKFqmgvySKMPAQKLDRlLKLPILGRiVGRkvlagl 301
Cdd:cd05966 299 -GATTVMF-EGTptypdpGRYWDIVEKHKVTIFYTAPtaiRALMKF-----GDEWVKKHDL-SSLRVLGS-VGE------ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 302 gldavryalcgaaPV-PEALLLWYRRLG---LDVLEVYGMTENSGYSHVCRPG--RQKTGWIGQNSPGVEVRISDE--GE 373
Cdd:cd05966 364 -------------PInPEAWMWYYEVIGkerCPIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAILDEegNE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 374 VQVRSGATMV----------GYYKEPEKTAEVLTAD--GFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIEN 441
Cdd:cd05966 431 VEGEVEGYLVikrpwpgmarTIYGDHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVS-GHRLGTAEVES 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489188483 442 RLAVHDRIEQVCVV-------GEGLSAplglCVLSEVGRREAlngtrGALESSLRAHLEQVNGAL 499
Cdd:cd05966 510 ALVAHPAVAEAAVVgrphdikGEAIYA----FVTLKDGEEPS-----DELRKELRKHVRKEIGPI 565
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-489 |
1.83e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 1 MVTANRLPL---EVFFEREKRHPQR---RYLVQPIGGGRVeeLSWGEVGDQARRAAAWLRSLDLPaGSRIAIISKNCAHW 74
Cdd:PRK05691 1 MMDAFELPLtlvQALQRRAAQTPDRlalRFLADDPGEGVV--LSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 75 IVTDLAIWMAGHVSVPLYPnltAESARQvlEHSESAVVFvgklddwpaMAPGVPEGIPTVAMPLHPEGRFDRQWSD---- 150
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYP---PESARR--HHQERLLSI---------IADAEPRLLLTVADLRDSLLQMEELAAAnape 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 151 ------LQACAPLEGDTPT-AAEQLATLIYTSGTTGVPKGVM---HNFSSFAFAASRGvelFG--TREDDRMLSYLPLCH 218
Cdd:PRK05691 144 llcvdtLDPALAEAWQEPAlQPDDIAFLQYTSGSTALPKGVQvshGNLVANEQLIRHG---FGidLNPDDVIVSWLPLYH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 219 vaermfvEMGsLYGGttvfFAESLDTFVEDMKRArPTLLFGVPRIWTKfQMGVYSKMPAQKLDRLLKLpiLGRIVGRKVL 298
Cdd:PRK05691 221 -------DMG-LIGG----LLQPIFSGVPCVLMS-PAYFLERPLRWLE-AISEYGGTISGGPDFAYRL--CSERVSESAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 299 AGLGLDAVRYALCGAAPVPE-ALLLWYRRL---GLD---VLEVYGMTENSGYSHVCRPGR-------------QKTGWIG 358
Cdd:PRK05691 285 ERLDLSRWRVAYSGSEPIRQdSLERFAEKFaacGFDpdsFFASYGLAEATLFVSGGRRGQgipaleldaealaRNRAEPG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 359 QNS---------PGVEVRISDE-----------GEVQVRSGATMVGYYKEPEKTAEVLTA-DG--FLRTGDKGEQdAEGN 415
Cdd:PRK05691 365 TGSvlmscgrsqPGHAVLIVDPqslevlgdnrvGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFL-RDGE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 416 LRLTGRMKEIFkTSKGKYVAPAPIENRLAvhdriEQVCVVGEGLSAPL--------GLCVLSEVGRREALNGTRGALESS 487
Cdd:PRK05691 444 LFVTGRLKDML-IVRGHNLYPQDIEKTVE-----REVEVVRKGRVAAFavnhqgeeGIGIAAEISRSVQKILPPQALIKS 517
|
..
gi 489188483 488 LR 489
Cdd:PRK05691 518 IR 519
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
172-236 |
4.32e-06 |
|
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: 49.35 E-value: 4.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489188483 172 IYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMfVEMGS-LYGGTTV 236
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGI-MGVGQaLLHGSTV 174
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
32-186 |
1.67e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 47.48 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 32 GRVEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLA------IWMAghVSvplyPNLTAESA----R 101
Cdd:PRK03584 110 GPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAtaslgaIWSS--CS----PDFGVQGVldrfG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 102 QVlehsESAVVFV-------GK----LDDWPAMAPGVPEGIPTVAMP-LHPEGRFDRQ-----WSDlqACAPLEGDTPTa 164
Cdd:PRK03584 184 QI----EPKVLIAvdgyrygGKafdrRAKVAELRAALPSLEHVVVVPyLGPAAAAAALpgallWED--FLAPAEAAELE- 256
|
170 180
....*....|....*....|....*..
gi 489188483 165 AEQLAT-----LIYTSGTTGVPKGVMH 186
Cdd:PRK03584 257 FEPVPFdhplwILYSSGTTGLPKCIVH 283
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
18-456 |
1.85e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 47.30 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 18 RHPQRRYLVQPIGGgrveeLSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTA 97
Cdd:PRK13383 47 RWPGRTAIIDDDGA-----LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 98 ESARQVLEHSESAVVFVGklDDWPAMAPGVPEGIPTVamplhpegrfDRQWSDLQACapleGDTPTAAEQLATLIYTSGT 177
Cdd:PRK13383 122 DALAAALRAHHISTVVAD--NEFAERIAGADDAVAVI----------DPATAGAEES----GGRPAVAAPGRIVLLTSGT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 178 TGVPKGVMH--NFSSFAFAASRGVELFGTREDDRMLSYLPLCH-VAERMFVEMGSLyGGTTV----FFAESLdtfVEDMK 250
Cdd:PRK13383 186 TGKPKGVPRapQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHgLGLGMLMLTIAL-GGTVLthrhFDAEAA---LAQAS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 251 RARPTLLFGVPRIwtkfqmgvyskmpaqkLDRLLKLPilGRIVGRKVLAGLgldavRYALCGAAPVPEALLLWYRRLGLD 330
Cdd:PRK13383 262 LHRADAFTAVPVV----------------LARILELP--PRVRARNPLPQL-----RVVMSSGDRLDPTLGQRFMDTYGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 331 VL-EVYGMTEnSGYSHVCRPG--RQKTGWIGQNSPGVEVRISDEGEVQVR---SGATMVG------YYKEPEKTAEVlta 398
Cdd:PRK13383 319 ILyNGYGSTE-VGIGALATPAdlRDAPETVGKPVAGCPVRILDRNNRPVGprvTGRIFVGgelagtRYTDGGGKAVV--- 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489188483 399 DGFLRTGDKGEQDAEGNLRLTGRMKEIFkTSKGKYVAPAPIENRLAVHDRIEQVCVVG 456
Cdd:PRK13383 395 DGMTSTGDMGYLDNAGRLFIVGREDDMI-ISGGENVYPRAVENALAAHPAVADNAVIG 451
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
174-339 |
1.10e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 44.75 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 174 TSGTTGVPKGVMHNFSS---FAFAASRGVELFGTREDDR---MLSY------LPLCHVAERMfvemgslygGTTVFFAES 241
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDldrWAELFARSLRAAGVRPGDRvqnAFGYglftggLGLHYGAERL---------GATVIPAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 242 LDTF--VEDMKRARPTLLFGVPriwtkfqmgvySKmpaqkldrLLKLpilgrivgRKVLAGLGLD----AVRYALCGAAP 315
Cdd:COG1541 162 GNTErqLRLMQDFGPTVLVGTP-----------SY--------LLYL--------AEVAEEEGIDprdlSLKKGIFGGEP 214
|
170 180
....*....|....*....|....*
gi 489188483 316 VPEALLLWY-RRLGLDVLEVYGMTE 339
Cdd:COG1541 215 WSEEMRKEIeERWGIKAYDIYGLTE 239
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
31-184 |
1.14e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 45.12 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 31 GGRVEELSWGEVGDQARRAAAWLRSLDLPaGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLY-PNLT--AESARQVLEHS 107
Cdd:PRK12476 63 AGCAVELTWTQLGVRLRAVGARLQQVAGP-GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFaPELPghAERLDTALRDA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 108 ESAVVFV-----GKLDDWPAMAPGV--PEGIPTVAMPLHPEGRFDRqwsdlqacAPLEGDtptaaeQLATLIYTSGTTGV 180
Cdd:PRK12476 142 EPTVVLTttaaaEAVEGFLRNLPRLrrPRVIAIDAIPDSAGESFVP--------VELDTD------DVSHLQYTSGSTRP 207
|
....
gi 489188483 181 PKGV 184
Cdd:PRK12476 208 PVGV 211
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
148-460 |
1.36e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 148 WSDLQACAPLEGDTP--TAAEQLATLIYTSGTTGVPKGVMhnfssfafaasrgVELFGTREDDrmLSYLPLCHVAERMFV 225
Cdd:PRK05691 3849 WEEVQAGEVASHNPGiySGPDNLAYVIYTSGSTGLPKGVM-------------VEQRGMLNNQ--LSKVPYLALSEADVI 3913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 226 EMGSlyggttvffAESLDTFVEDMkRARPtlLFG-----VPRIWTKFQMGVYSKMPAQKLDRLLKLPILgrIVGRKVLAG 300
Cdd:PRK05691 3914 AQTA---------SQSFDISVWQF-LAAP--LFGarveiVPNAIAHDPQGLLAHVQAQGITVLESVPSL--IQGMLAEDR 3979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 301 LGLDAVRYAL-CGAAPVPEALLLW---YRRLGLdvLEVYGMTENSGYSHVCRPGRQKTGW----IGQNSPGVEVRISDE- 371
Cdd:PRK05691 3980 QALDGLRWMLpTGEAMPPELARQWlqrYPQIGL--VNAYGPAECSDDVAFFRVDLASTRGsylpIGSPTDNNRLYLLDEa 4057
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 372 ---------GEVQVRSGATMVGYYKEPEKTAEVLTADGF-------LRTGDKGEQDAEGNLRLTGRMKEIFKTsKGKYVA 435
Cdd:PRK05691 4058 lelvplgavGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI-RGYRIE 4136
|
330 340
....*....|....*....|....*.
gi 489188483 436 PAPIENRLAVHDRIEQVCV-VGEGLS 460
Cdd:PRK05691 4137 LGEIEARLHEQAEVREAAVaVQEGVN 4162
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
166-499 |
1.58e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 44.42 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 166 EQLATLIYTSGTTGVPKGVMHNFSSFAFAASRGVELFGTREDDRMLSYLPLCHVAERMFVEMGSLYGGTTVFFAES---L 242
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNplyP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 243 DTFVEDMKRARPTLLFGVPRIWTkfqmgvYSKMPAQKLDRllKLPILGRIVgrkvlagLGLDAVRYALCGAAP--VPEAL 320
Cdd:PRK06334 263 KKIVEMIDEAKVTFLGSTPVFFD------YILKTAKKQES--CLPSLRFVV-------IGGDAFKDSLYQEALktFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 321 LlwyrRLGldvlevYGMTEnsgyshvCRP--------GRQKTGWIGQNSPGVEVRI-SDEGEVQVRSGATMV-------- 383
Cdd:PRK06334 328 L----RQG------YGTTE-------CSPvitintvnSPKHESCVGMPIRGMDVLIvSEETKVPVSSGETGLvltrgtsl 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 384 --GYYKEPEKTAEV-LTADGFLRTGDKGEQDAEGNLRLTGRMKEIFKTSkGKYVAPAPIENRLavhdrIEQVCVVGEGLS 460
Cdd:PRK06334 391 fsGYLGEDFGQGFVeLGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESIL-----MEGFGQNAADHA 464
|
330 340 350
....*....|....*....|....*....|....*....
gi 489188483 461 APLGLCVLSevGRREALngtrgALESSLRAHLEQVNGAL 499
Cdd:PRK06334 465 GPLVVCGLP--GEKVRL-----CLFTTFPTSISEVNDIL 496
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
141-186 |
2.05e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 43.98 E-value: 2.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489188483 141 EGRfDRQWSDLQA-----CAPlegdTPTAAEQLATLIYTSGTTGVPKGVMH 186
Cdd:PRK00174 220 EGR-DLWWHELVAgasdeCEP----EPMDAEDPLFILYTSGSTGKPKGVLH 265
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
34-184 |
6.76e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 39.29 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 34 VEELSWGEVGDQARRAAAWLRSLDLPAGSRIAIISKNCAHWIVTDLAIWMAGHVSVPLYPNLTAESARQVLEHSESAVVF 113
Cdd:PLN03052 206 VNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188483 114 V-------GK--------LDDWPAMAPGVPEGIPTVAMPLHpEGrfDRQWSD-LQACAPLE-GDTPTAAEQ----LATLI 172
Cdd:PLN03052 286 TqdvivrgGKsiplysrvVEAKAPKAIVLPADGKSVRVKLR-EG--DMSWDDfLARANGLRrPDEYKAVEQpveaFTNIL 362
|
170
....*....|..
gi 489188483 173 YTSGTTGVPKGV 184
Cdd:PLN03052 363 FSSGTTGEPKAI 374
|
|
| |
