|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
37-344 |
9.28e-57 |
|
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: 190.79 E-value: 9.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:COG0318 1 LADLLRRAAARHPDRPALVF-GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA--VLTldgelpdgvafldegaapdelAVLYYVrkrGG--GL-HGVELTNENILSTIEAVVHA 191
Cdd:COG0318 80 NPRLTAEELAYILEDSGAraLVT---------------------ALILYT---SGttGRpKGVMLTHRNLLANAAAIAAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 192 MDLTaEGARTVLTAPLSTAAGSAVQLLPTLAAGGTVV--------------------------------AAGARGVRVPW 239
Cdd:COG0318 136 LGLT-PGDVVLVALPLFHVFGLTVGLLAPLLAGATLVllprfdpervlelierervtvlfgvptmlarlLRHPEFARYDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 RHLR------ASFPAARCVR-----------GWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLGPA----ADQG 298
Cdd:COG0318 215 SSLRlvvsggAPLPPELLERfeerfgvriveGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDgrelPPGE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2484101036 299 VGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:COG0318 295 VGEIVVRGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLY 340
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
41-346 |
9.99e-47 |
|
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: 163.94 E-value: 9.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 41 LDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTC 120
Cdd:cd17631 1 LRRRARRHPDRTALVFG-GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 121 SDPELEWIADDSGAVLTLDgelpdgvafldegaapdELAVLYYVRKRGGGLHGVELTNENILStiEAVVHAMDLTA-EGA 199
Cdd:cd17631 80 TPPEVAYILADSGAKVLFD-----------------DLALLMYTSGTTGRPKGAMLTHRNLLW--NAVNALAALDLgPDD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 200 RTVLTAPLSTAAGSAVQLLPTLAAGGTVV------------AAGARGVR----VP------WRH----------LR---- 243
Cdd:cd17631 141 VLLVVAPLFHIGGLGVFTLPTLLRGGTVVilrkfdpetvldLIERHRVTsfflVPtmiqalLQHprfattdlssLRaviy 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 244 -ASFPAARCVR-----------GWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLGP----AADQGVGELLCRGP 307
Cdd:cd17631 221 gGAPMPERLLRalqargvkfvqGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPdgreVPPGEVGEIVVRGP 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 2484101036 308 SVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVTPV 346
Cdd:cd17631 301 HVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIV 339
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
41-343 |
6.72e-44 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 156.32 E-value: 6.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 41 LDRSALRHSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTC 120
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 121 SDPELEWIADDSGAV---------------------------------------LTLDGELPDGVAFLDEGAAPDELAVL 161
Cdd:pfam00501 81 PAEELAYILEDSGAKvlitddalkleellealgklevvklvlvldrdpvlkeepLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 162 YY------VRKrggglhGVELTNENILSTIEAVV---HAMDLTAEGARTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGA 232
Cdd:pfam00501 161 IYtsgttgKPK------GVMLTHRNLVANVLSIKrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 233 RGVRVPWRHL----------------------------RASFPAARCVR------------------------GWGVAET 260
Cdd:pfam00501 235 FPALDPAALLelierykvtvlygvptllnmlleagapkRALLSSLRLVLsggaplppelarrfrelfggalvnGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 261 GGIGLL-LPTDQRAAHPRSVGVPFGGMEVALL-----GPAADQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGD 333
Cdd:pfam00501 315 TGVVTTpLPLDEDLRSLGSVGRPLPGTEVKIVddetgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDeDGWYRTGD 394
|
410
....*....|
gi 2484101036 334 QVHIDGDGFV 343
Cdd:pfam00501 395 LGRRDEDGYL 404
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
37-346 |
1.53e-43 |
|
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: 156.18 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM-GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA-VLTLDGELPDGVA-----FLDEGAAPDELAVLYYVrkrGG--GL-HGVELTNENILSTIEA 187
Cdd:cd05936 80 NPLYTPRELEHILNDSGAkALIVAVSFTDLLAagaplGERVALTPEDVAVLQYT---SGttGVpKGAMLTHRNLVANALQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 188 VVHAMDLTAEGARTVLTA-PLSTAAGSAVQLLPTLAAGGTVV---------------------------------AAGAR 233
Cdd:cd05936 157 IKAWLEDLLEGDDVVLAAlPLFHVFGLTVALLLPLALGATIVliprfrpigvlkeirkhrvtifpgvptmyiallNAPEF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 234 GVRVPwRHLR------ASFPAA-----------RCVRGWGVAETGGIGLLLPTDqRAAHPRSVGVPFGGMEVALLGP--- 293
Cdd:cd05936 237 KKRDF-SSLRlcisggAPLPVEvaerfeeltgvPIVEGYGLTETSPVVAVNPLD-GPRKPGSIGIPLPGTEVKIVDDdge 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 294 -AADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVTPV 346
Cdd:cd05936 315 eLPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIV 368
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
37-344 |
2.02e-41 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 152.56 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGNA---LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVP 113
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 114 VLPDPTCSDPELEWIADDSGA-------------VLTLDGELPD--GVAFLDEGAAPDELAVLYY--VRKRGGGLH---- 172
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAkvlfvedqeqldkLLEVRDELPSlrHIVVLDPRGLRDDPRLLSLdeLLALGREVAdpae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 173 ---------------------------GVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAVQLLpTLAAGG 225
Cdd:COG1022 173 learraavkpddlatiiytsgttgrpkGVMLTHRNLLSNARALLERLPLG-PGDRTLSFLPLAHVFERTVSYY-ALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 226 TV------------------------------VAAGAR----------------GVRVPWRHLRA-----SFPAARCVRg 254
Cdd:COG1022 251 TVafaespdtlaedlrevkptfmlavprvwekVYAGIQakaeeagglkrklfrwALAVGRRYARArlagkSPSLLLRLK- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAE-------------------TGG-------------IGLLL-----------------PTDQRaahPRSVGVPFGG 285
Cdd:COG1022 330 HALADklvfsklrealggrlrfavSGGaalgpelarffraLGIPVlegygltetspvitvnrPGDNR---IGTVGPPLPG 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 286 MEVALlgpAADqgvGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:COG1022 407 VEVKI---AED---GEILVRGPNVMKGYYKNPEATAEAFDaDGWLHTGDIGELDEDGFLR 460
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
60-344 |
2.60e-41 |
|
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: 150.05 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 60 NALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVltld 139
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 140 gelpdgVAFLDEgaaPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGS-AVQLL 218
Cdd:cd05907 80 ------ALFVED---PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPAT-EGDRHLSFLPLAHVFERrAGLYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 219 PtLAAGGTV------------------------------VAAGARGVRVPwRHLRASF---PAARC-------------- 251
Cdd:cd05907 150 P-LLAGARIyfassaetllddlsevrptvflavprvwekVYAAIKVKAVP-GLKRKLFdlaVGGRLrfaasggaplpael 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 -----------VRGWGVAETGGIGLL-LPTDQRAAhprSVGVPFGGMEVALlgpAADqgvGELLCRGPSVARRYWNDPES 319
Cdd:cd05907 228 lhffralgipvYEGYGLTETSAVVTLnPPGDNRIG---TVGKPLPGVEVRI---ADD---GEILVRGPNVMLGYYKNPEA 298
|
330 340
....*....|....*....|....*.
gi 2484101036 320 TAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:cd05907 299 TAEALDaDGWLHTGDLGEIDEDGFLH 324
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
45-343 |
4.20e-31 |
|
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: 122.73 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 45 ALRHSARVAAVDRA-GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDP 123
Cdd:cd05904 15 ASAHPSRPALIDAAtGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 124 ELEWIADDSGA-------------------VLTLDGELPDGVAFL------DEGAAP------DELAVLYYVRKRGGGLH 172
Cdd:cd05904 95 EIAKQVKDSGAklafttaelaeklaslalpVVLLDSAEFDSLSFSdllfeaDEAEPPvvvikqDDVAALLYSSGTTGRSK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 173 GVELTNENILSTIEAVVHAMDLTAEGARTVL-TAPLSTAAGSAVQLLPTLAAGGTVV------------AAGARGVR--- 236
Cdd:cd05904 175 GVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLcVLPMFHIYGLSSFALGLLRLGATVVvmprfdleellaAIERYKVThlp 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 -VP----------------------------------WRHLRASFPAARCVRGWGVAETGGIGLL-LPTDQRAAHPRSVG 280
Cdd:cd05904 255 vVPpivlalvkspivdkydlsslrqimsgaaplgkelIEAFRAKFPNVDLGQGYGMTESTGVVAMcFAPEKDRAKYGSVG 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 281 VPFGGMEVALLGPAADQG-----VGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFV 343
Cdd:cd05904 335 RLVPNVEAKIVDPETGESlppnqTGELWIRGPSIMKGYLNNPEATAATIDkEGWLHTGDLCYIDEDGYL 403
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
59-344 |
2.71e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 120.24 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 59 GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG--VPVLPDPTCSdpELEWIADDSGAVL 136
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAiaVPILAEFTAD--EVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 137 TLDGElpdgvafldegaaPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVhAMDLTAEGARTVLTAPLSTAAGSAVQ 216
Cdd:cd05914 83 IFVSD-------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVK-EVVLLGKGDKILSILPLHHIYPLTFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 217 LLPTLAAGGTVV------------AAGAR-----GVRVPW--------------------------------RHL----- 242
Cdd:cd05914 149 LLLPLLNGAHVVfldkipsakiiaLAFAQvtptlGVPVPLviekifkmdiipkltlkkfkfklakkinnrkiRKLafkkv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 ---------------------------RASFPAARcvrGWGVAETGG-IGLLLPTDQRAAhprSVGVPFGGMEVALLGPA 294
Cdd:cd05914 229 heafggnikefviggakinpdveeflrTIGFPYTI---GYGMTETAPiISYSPPNRIRLG---SAGKVIDGVEVRIDSPD 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2484101036 295 ADQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:cd05914 303 PATGEGEIIVRGPNVMKGYYKNPEATAEAFDkDGWFHTGDLGKIDAEGYLY 353
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
48-343 |
5.09e-28 |
|
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: 113.95 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 48 HSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVpVLP-DPTCSDPELE 126
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAV-VAPlNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 127 WIADDSGAVLTL---DGELPDGVAFLDEGAAPDELAVLYYVRKRGGG----------------------------LH--- 172
Cdd:cd05926 80 FYLADLGSKLVLtpkGELGPASRAASKLGLAILELALDVGVLIRAPSaeslsnlladkknaksegvplpddlaliLHtsg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 173 ------GVELTNENILSTIEAVVHAMDLTAEGaRTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGA----------RGVR 236
Cdd:cd05926 160 ttgrpkGVPLTHRNLAASATNITNTYKLTPDD-RTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRfsastfwpdvRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 VPW----------------RHLRASFPAARCVRGWGVA----------ETGGIGLL----------------LPTDQRaa 274
Cdd:cd05926 239 ATWytavptihqillnrpePNPESPPPKLRFIRSCSASlppavlealeATFGAPVLeaygmteaahqmtsnpLPPGPR-- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 275 HPRSVGVPFGgMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAE-TFDDGWFHTGDQVHIDGDGFV 343
Cdd:cd05926 317 KPGSVGKPVG-VEVRILDedgeILPPGVVGEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDADGYL 389
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
53-343 |
5.47e-28 |
|
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: 113.85 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 53 AAVDRA-GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADD 131
Cdd:cd05911 1 AQIDADtGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 132 SGA-------------------------VLTLDGElPDGVAF---LDEGAAPDELAVLYYVRKRGG-------------G 170
Cdd:cd05911 81 SKPkviftdpdglekvkeaakelgpkdkIIVLDDK-PDGVLSiedLLSPTLGEEDEDLPPPLKDGKddtaailyssgttG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 171 L-HGVELTNENILSTIEaVVHAMDLTAEGARTVLTAPLSTAAGSAVQ-LLPTLAAGGTVV-------AAGARGVR----- 236
Cdd:cd05911 160 LpKGVCLSHRNLIANLS-QVQTFLYGNDGSNDVILGFLPLYHIYGLFtTLASLLNGATVIimpkfdsELFLDLIEkykit 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 ----VPW------RH----------------------------LRASFPAARCVRGWGVAETGGIGLLLPTDQraAHPRS 278
Cdd:cd05911 239 flylVPPiaaalaKSplldkydlsslrvilsggaplskelqelLAKRFPNATIKQGYGMTETGGILTVNPDGD--DKPGS 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2484101036 279 VGVPFGGMEVALLGPAADQ-----GVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFV 343
Cdd:cd05911 317 VGRLLPNVEAKIVDDDGKDslgpnEPGEICVRGPQVMKGYYNNPEATKETFDeDGWLHTGDIGYFDEDGYL 387
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
46-344 |
7.09e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 113.74 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 46 LRHSARVA----AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV--PV---Lp 116
Cdd:PRK06187 12 LRHGARKHpdkeAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlhPInirL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 dptcSDPELEWIADDSGA--------------------------VLTLDGELPDGVAFLDE-----GAAPDE-------- 157
Cdd:PRK06187 91 ----KPEEIAYILNDAEDrvvlvdsefvpllaailpqlptvrtvIVEGDGPAAPLAPEVGEyeellAAASDTfdfpdide 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 158 --LAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGaRTVLTAPLSTAAGSAVQLLPTLAaGGTVVAAG---- 231
Cdd:PRK06187 167 ndAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD-VYLVIVPMFHVHAWGLPYLALMA-GAKQVIPRrfdp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 232 ---ARGVR---------VP--W----RHLRASF----------------PAARC-----------VRGWGVAETGGIG-L 265
Cdd:PRK06187 245 enlLDLIEtervtfffaVPtiWqmllKAPRAYFvdfsslrlviyggaalPPALLrefkekfgidlVQGYGMTETSPVVsV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 266 LLPTDQ---RAAHPRSVGVPFGGMEVALLGP-----AADQG-VGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVH 336
Cdd:PRK06187 325 LPPEDQlpgQWTKRRSAGRPLPGVEARIVDDdgdelPPDGGeVGEIIVRGPWLMQGYWNRPEATAETIDGGWLHTGDVGY 404
|
....*...
gi 2484101036 337 IDGDGFVT 344
Cdd:PRK06187 405 IDEDGYLY 412
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
37-346 |
2.63e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 112.31 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVF-GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA--VLTLDGELP------DGVA-------------------------FLDEGA--------AP 155
Cdd:PRK07656 86 NTRYTADEAAYILARGDAkaLFVLGLFLGvdysatTRLPalehvviceteeddphtekmktftdFLAAGDpaerapevDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 156 DELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAVQLLPTLAAGGTVV------- 228
Cdd:PRK07656 166 DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT-EGDRYLAANPFFHVFGYKAGVNAPLMRGATILplpvfdp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 -----AAGARGVRV----P----------------WRHLR------ASFPAARCVR------------GWGVAETGGIGL 265
Cdd:PRK07656 245 devfrLIETERITVlpgpPtmynsllqhpdrsaedLSSLRlavtgaASMPVALLERfeselgvdivltGYGLSEASGVTT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 266 LLPTDQ-RAAHPRSVGVPFGGMEVALLGP----AADQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDG 339
Cdd:PRK07656 325 FNRLDDdRKTVAGTIGTAIAGVENKIVNElgeeVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDaDGWLHTGDLGRLDE 404
|
....*..
gi 2484101036 340 DGFVTPV 346
Cdd:PRK07656 405 EGYLYIV 411
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
173-344 |
6.84e-27 |
|
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: 108.53 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 173 GVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAvQLLPTLAAGGTVV-------AAGARGVR--------- 236
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLT-EGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVllpkfdpEAALELIErekvtillg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 VP--WRHLR-------------------------------ASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPF 283
Cdd:cd04433 95 VPtlLARLLkapesagydlsslralvsggaplppellerfEEAPGIKLVNGYGLTETGGTVATGPPDDDARKPGSVGRPV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2484101036 284 GGMEVALL----GPAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:cd04433 175 PGVEVRIVdpdgGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDEDGYLY 239
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
51-344 |
8.97e-27 |
|
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: 110.07 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDrAGNALTYGQMWSSAARVAGGLLDQG-VGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIA 129
Cdd:cd05941 2 RIAIVD-DGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 130 DDSGAVLTLDGelpdgvafldegaapdelAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGaRTVLTAPLST 209
Cdd:cd05941 81 TDSEPSLVLDP------------------ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDD-VLLHVLPLHH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 210 AAGSAVQLLPTLAAGGTVV------AAGARGVR----------VP--WRHLRASFPA---------ARCVRGWGVAETGG 262
Cdd:cd05941 142 VHGLVNALLCPLFAGASVEflpkfdPKEVAISRlmpsitvfmgVPtiYTRLLQYYEAhftdpqfarAAAAERLRLMVSGS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 263 IGLLLPTDQR----------------------------AAHPRSVGVPFGGMEVALL----GPAADQG-VGELLCRGPSV 309
Cdd:cd05941 222 AALPVPTLEEweaitghtllerygmteigmalsnpldgERRPGTVGMPLPGVQARIVdeetGEPLPRGeVGEIQVRGPSV 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 2484101036 310 ARRYWNDPESTAETF-DDGWFHTGDQVHIDGDGFVT 344
Cdd:cd05941 302 FKEYWNKPEATKEEFtDDGWFKTGDLGVVDEDGYYW 337
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
34-347 |
2.02e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.09 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 34 EPCLAELLDRSALRHSARVAaVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVP 113
Cdd:PRK05605 31 DTTLVDLYDNAVARFGDRPA-LDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 114 VLPDPTCSDPELEWIADDSGA----------------------------------------------------------- 134
Cdd:PRK05605 110 VEHNPLYTAHELEHPFEDHGArvaivwdkvaptverlrrttpletivsvnmiaampllqrlalrlpipalrkaraaltgp 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 135 --------VLTLDGELPDGVAFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTV---- 202
Cdd:PRK05605 190 apgtvpweTLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPERVlaal 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 203 ---------LTAPLSTAAGSAVQLLPT-----------------LAAGGTV---VAAGARGVRVPWRHLRASFPAA---- 249
Cdd:PRK05605 270 pmfhaygltLCLTLAVSIGGELVLLPApdidlildamkkhpptwLPGVPPLyekIAEAAEERGVDLSGVRNAFSGAmalp 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 -------------RCVRGWGVAETGGIGLLLP-TDQRaaHPRSVGVPFGGMEVALLGP------AADQGVGELLCRGPSV 309
Cdd:PRK05605 350 vstvelwekltggLLVEGYGLTETSPIIVGNPmSDDR--RPGYVGVPFPDTEVRIVDPedpdetMPDGEEGELLVRGPQV 427
|
410 420 430
....*....|....*....|....*....|....*...
gi 2484101036 310 ARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVTPVA 347
Cdd:PRK05605 428 FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVD 465
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
37-349 |
1.32e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 107.25 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAgNALTYGQMWSSAARVAGGLLDQ-GVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL 115
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAIITEE-EEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 116 PDPTCSDPELEWIADDSGA-VLTLDGELPDGVAFLD-----------------EGAAPDELA--------VLYYVRKRGG 169
Cdd:PRK06839 83 LNIRLTENELIFQLKDSGTtVLFVEKTFQNMALSMQkvsyvqrvisitslkeiEDRKIDNFVeknesasfIICYTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 170 GLHGVELTNENILSTIEAVVHAMDLTAEGARTVLTaPLSTAAGSAVQLLPTLAAGGTVVAAGA----RGVR--------- 236
Cdd:PRK06839 163 KPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLL-PLFHIGGIGLFAFPTLFAGGVIIVPRKfeptKALSmiekhkvtv 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 ---VPWRH---------LRASFPAARCV-----------------------RGWGVAETGGIGLLLPTDQRAAHPRSVGV 281
Cdd:PRK06839 242 vmgVPTIHqalincskfETTNLQSVRWFynggapcpeelmrefidrgflfgQGFGMTETSPTVFMLSEEDARRKVGSIGK 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 282 PFGGMEVALLGPAADQ----GVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVTPVAVR 349
Cdd:PRK06839 322 PVLFCDYELIDENKNKvevgEVGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGRK 393
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
59-343 |
2.64e-24 |
|
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: 102.75 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 59 GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTL 138
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 139 DgelpdgvafldegaapdELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAVQLL 218
Cdd:cd05934 81 V-----------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG-EDDVYLTVLPLFHINAQAVSVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 219 PTLAAGGTVVAAGARGVRVPWRHLRAS----------------------FPAARCVR----------------------- 253
Cdd:cd05934 143 AALSVGATLVLLPRFSASRFWSDVRRYgatvtnylgamlsyllaqppspDDRAHRLRaaygapnppelheefeerfgvrl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 --GWGVAETGgIGLLLPTDQRAAhPRSVGVPFGGMEVALLG----PAADQGVGELLCR---GPSVARRYWNDPESTAETF 324
Cdd:cd05934 223 leGYGMTETI-VGVIGPRDEPRR-PGSIGRPAPGYEVRIVDddgqELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM 300
|
330
....*....|....*....
gi 2484101036 325 DDGWFHTGDQVHIDGDGFV 343
Cdd:cd05934 301 RNGWFHTGDLGYRDADGFF 319
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
51-341 |
3.12e-24 |
|
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: 102.61 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPtcSDPE--LEWI 128
Cdd:cd05930 3 AVAVVD-GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP--SYPAerLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 129 ADDSGAVLTLdgelpdgvafldegAAPDELAVLYY------VRKrggglhGVELTNENILSTIEAVVHAMDLTAEGaRTV 202
Cdd:cd05930 80 LEDSGAKLVL--------------TDPDDLAYVIYtsgstgKPK------GVMVEHRGLVNLLLWMQEAYPLTPGD-RVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 203 LTAPLSTAAgSAVQLLPTLAAGGTVVAAGARGVRVP------------------------------------WRHL---- 242
Cdd:cd05930 139 QFTSFSFDV-SVWEIFGALLAGATLVVLPEEVRKDPealadllaeegitvlhltpsllrlllqelelaalpsLRLVlvgg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 -----------RASFPAARCVRGWGVAETGGIGLL--LPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCR 305
Cdd:cd05930 218 ealppdlvrrwRELLPGARLVNLYGPTEATVDATYyrVPPDDEEDGRVPIGRPIPNTRVYVLDenlrPVPPGVPGELYIG 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2484101036 306 GPSVARRYWNDPESTAETFDDGWFH-------TGDQVHIDGDG 341
Cdd:cd05930 298 GAGLARGYLNRPELTAERFVPNPFGpgermyrTGDLVRWLPDG 340
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
45-342 |
9.74e-24 |
|
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: 101.17 E-value: 9.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 45 ALRHSARVAaVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG--VPVlpDPTCSD 122
Cdd:cd05945 1 AAANPDRPA-VVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPL--DASSPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 123 PELEWIADDSGAVLTLdgelpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTV 202
Cdd:cd05945 78 ERIREILDAAKPALLI--------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLG-PGDVFL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 203 LTAPLSTAAgSAVQLLPTLAAGGTVVAAG---------------ARGVRVpW------------------------RH-- 241
Cdd:cd05945 143 NQAPFSFDL-SVMDLYPALASGATLVPVPrdatadpkqlfrflaEHGITV-WvstpsfaamcllsptftpeslpslRHfl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 242 -------------LRASFPAARCVRGWGVAETGGI--GLLLPTDQRAAHPR-SVGVPFGGMEVALL----GPAADQGVGE 301
Cdd:cd05945 221 fcgevlphktaraLQQRFPDARIYNTYGPTEATVAvtYIEVTPEVLDGYDRlPIGYAKPGAKLVILdedgRPVPPGEKGE 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2484101036 302 LLCRGPSVARRYWNDPESTAETF--DDG--WFHTGDQVHIDGDGF 342
Cdd:cd05945 301 LVISGPSVSKGYLNNPEKTAAAFfpDEGqrAYRTGDLVRLEADGL 345
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
37-346 |
3.20e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 100.39 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK08316 13 IGDILRRSARRYPDKTALVFG-DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTL--------------------------------DGELPDGVAFLDEGAAP--------D 156
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLvdpalaptaeaalallpvdtlilslvlggreaPGGWLDFADWAEAGSVAepdveladD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 157 ELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGaRTVLTAPLSTAAGSAVQLLPTLAAGGT-VVAAGARGV 235
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADD-IPLHALPLYHCAQLDVFLGPYLYVGATnVILDAPDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 236 RV---------------P--W----RH----------------------------LRASFPAARCVRGWGVAETGGIGLL 266
Cdd:PRK08316 251 LIlrtieaeritsffapPtvWisllRHpdfdtrdlsslrkgyygasimpvevlkeLRERLPGLRFYNCYGQTEIAPLATV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 267 LPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:PRK08316 331 LGPEEHLRRPGSAGRPVLNVETRVVDddgnDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
....
gi 2484101036 343 VTPV 346
Cdd:PRK08316 411 ITVV 414
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-344 |
3.35e-22 |
|
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: 97.44 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:cd05959 5 AATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA-VLTLDGEL------------PDGV------------------AFLDEGAA--------PDE 157
Cdd:cd05959 85 NTLLTPDDYAYYLEDSRArVVVVSGELapvlaaaltkseHTLVvlivsggagpeagalllaELVAAEAEqlkpaathADD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 158 LAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVLTAPLSTAAGSAVQLLPTLAAGGTV---------- 227
Cdd:cd05959 165 PAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTvlmperptpa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 228 -VAAGARGVR------VPwrHLRASFPAAR------------CV-----------RGW----GVAETGGIG------LLL 267
Cdd:cd05959 245 aVFKRIRRYRptvffgVP--TLYAAMLAAPnlpsrdlsslrlCVsagealpaevgERWkarfGLDILDGIGstemlhIFL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 268 PTDQRAAHPRSVGVPFGGMEVALLGPA----ADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:cd05959 323 SNRPGRVRYGTTGKPVPGYEVELRDEDggdvADGEPGELYVRGPSSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFY 402
|
.
gi 2484101036 344 T 344
Cdd:cd05959 403 T 403
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
62-342 |
4.85e-22 |
|
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: 96.39 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTLdge 141
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 142 lpdgvafldEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAeGARTVLTAPLSTAAGSAVQLLPTL 221
Cdd:cd05935 79 ---------VGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP-SDVILACLPLFHVTGFVGSLNTAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 222 AAGGTVVAAG----------------ARGVRVP----------------WRHLR------ASFPAA-----------RCV 252
Cdd:cd05935 149 YVGGTYVLMArwdretaleliekykvTFWTNIPtmlvdllatpefktrdLSSLKvltgggAPMPPAvaekllkltglRFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 253 RGWGVAETGGIGLLLPtdqrAAHPRS--VGVPFGGMEVALLGPAA-----DQGVGELLCRGPSVARRYWNDPESTAETF- 324
Cdd:cd05935 229 EGYGLTETMSQTHTNP----PLRPKLqcLGIP*FGVDARVIDIETgrelpPNEVGEIVVRGPQIFKGYWNRPEETEESFi 304
|
330 340
....*....|....*....|.
gi 2484101036 325 -DDG--WFHTGDQVHIDGDGF 342
Cdd:cd05935 305 eIKGrrFFRTGDLGYMDEEGY 325
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
62-344 |
1.64e-20 |
|
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: 91.75 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTLdge 141
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 142 lpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVLTAPLSTAAGSAVQLLPTL 221
Cdd:cd05919 88 -----------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 222 AAGGTVVAAGAR-------------------GVRVPWRHLRAS-------FPAARCV--------RG--------WGVAE 259
Cdd:cd05919 157 AVGASAVLNPGWptaervlatlarfrptvlyGVPTFYANLLDScagspdaLRSLRLCvsagealpRGlgerwmehFGGPI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 260 TGGIG------LLLPTDQRAAHPRSVGVPFGGMEVALLGPAA----DQGVGELLCRGPSVARRYWNDPESTAETFDDGWF 329
Cdd:cd05919 237 LDGIGatevghIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGhtipPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWY 316
|
330
....*....|....*
gi 2484101036 330 HTGDQVHIDGDGFVT 344
Cdd:cd05919 317 RTGDKFCRDADGWYT 331
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
37-344 |
3.13e-20 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 91.75 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGnALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL- 115
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGER-RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 116 -----------------------PD---------------PTCSDPELEWIADDSGAVLTLDGELPDGVAFLDEGAAPDE 157
Cdd:COG1021 106 lpahrraeishfaeqseavayiiPDrhrgfdyralarelqAEVPSLRHVLVVGDAGEFTSLDALLAAPADLSEPRPDPDD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 158 LAVLyyvrKRGGGLHGV----ELTNENILSTIEAVVHAMDLTAEgarTVLTAPLSTA---AGSAVQLLPTLAAGGTVVAA 230
Cdd:COG1021 186 VAFF----QLSGGTTGLpkliPRTHDDYLYSVRASAEICGLDAD---TVYLAALPAAhnfPLSSPGVLGVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 231 G-----------ARgVRV-----------------PWRH-----LR------ASFP---AARCVRGWGV--------AEt 260
Cdd:COG1021 259 PdpspdtafpliER-ERVtvtalvpplallwldaaERSRydlssLRvlqvggAKLSpelARRVRPALGCtlqqvfgmAE- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 261 ggiGLLL------PTDQRAahpRSVGVPFG-GMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFD-DGW 328
Cdd:COG1021 337 ---GLVNytrlddPEEVIL---TTQGRPISpDDEVRIVDedgnPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTpDGF 410
|
410
....*....|....*.
gi 2484101036 329 FHTGDQVHIDGDGFVT 344
Cdd:COG1021 411 YRTGDLVRRTPDGYLV 426
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
46-344 |
6.76e-20 |
|
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: 90.38 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 46 LRHSARVAA--------VDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPD 117
Cdd:cd12119 2 LEHAARLHGdreivsrtHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 118 PTCSDPELEWIADDSGA-VLTLDGELPDGVAFLDEGAAPDELAVLYYVRKRGGGLHGVELTN------------------ 178
Cdd:cd12119 82 PRLFPEQIAYIINHAEDrVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVLAyeellaaespeydwpdfd 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 179 ENILSTI------------------EAVVHAMDL--------------------------------TAEGARTVLTAPLS 208
Cdd:cd12119 162 ENTAAAIcytsgttgnpkgvvyshrSLVLHAMAAlltdglglsesdvvlpvvpmfhvnawglpyaaAMVGAKLVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 209 TAAgSAVQLL----PTLAAGGTVVAAG------ARGVRVPwrHLR------ASFPAA----------RCVRGWGVAETGG 262
Cdd:cd12119 242 DPA-SLAELIeregVTFAAGVPTVWQGlldhleANGRDLS--SLRrvviggSAVPRSlieafeergvRVIHAWGMTETSP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 263 IG---------LLLPTDQRAAHPRSVGVPFGGMEVALLG------PAADQGVGELLCRGPSVARRYWNDPESTAETFDDG 327
Cdd:cd12119 319 LGtvarppsehSNLSEDEQLALRAKQGRPVPGVELRIVDddgrelPWDGKAVGELQVRGPWVTKSYYKNDEESEALTEDG 398
|
410
....*....|....*..
gi 2484101036 328 WFHTGDQVHIDGDGFVT 344
Cdd:cd12119 399 WLRTGDVATIDEDGYLT 415
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
61-344 |
1.21e-19 |
|
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: 89.36 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 61 ALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTLdg 140
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 eLPDGVAFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAVQLLPT 220
Cdd:cd05903 79 -VPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLG-PGDVFLVASPMAHQTGFVYGFTLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 221 LAAGGTVV-------AAGARGVRV-------------------------PWRHLR------ASFP---AARC-------- 251
Cdd:cd05903 157 LLLGAPVVlqdiwdpDKALALMREhgvtfmmgatpfltdllnaveeagePLSRLRtfvcggATVPrslARRAaellgakv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALL---GPAADQG-VGELLCRGPSVARRYWNDPESTAETFDDG 327
Cdd:cd05903 237 CSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVddtGATLAPGvEGELLSRGPSVFLGYLDRPDLTADAAPEG 316
|
330
....*....|....*..
gi 2484101036 328 WFHTGDQVHIDGDGFVT 344
Cdd:cd05903 317 WFRTGDLARLDEDGYLR 333
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
37-344 |
2.27e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 88.94 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGNAlTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSW-TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTL-DGELPDGVA-----------FLDEGAAPDELAVLYYVRKRGGGLHGVELTNEN---- 180
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMIcHADFPEHAAavraaspdlthVVAIGGARAGLDYEALVARHLGARVANAAVDHDdpcw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 181 --------------ILS--TIEAVV--HAMDL---TAEGARTVLTAPLSTAAGsaVQLLPTLAAGGTVVAAGARGVRVP- 238
Cdd:PRK07470 168 ffftsgttgrpkaaVLThgQMAFVItnHLADLmpgTTEQDASLVVAPLSHGAG--IHQLCQVARGAATVLLPSERFDPAe 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 239 -------WR------------------------H--LR----ASFPAAR-------------CVRGWGVAE-TGGIGLLL 267
Cdd:PRK07470 246 vwalverHRvtnlftvptilkmlvehpavdrydHssLRyviyAGAPMYRadqkralaklgkvLVQYFGLGEvTGNITVLP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 268 PT-----DQRAAHPRSVGVPFGGMEVALLGpaaDQG-------VGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQV 335
Cdd:PRK07470 326 PAlhdaeDGPDARIGTCGFERTGMEVQIQD---DEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLG 402
|
....*....
gi 2484101036 336 HIDGDGFVT 344
Cdd:PRK07470 403 HLDARGFLY 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
32-342 |
2.54e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 88.94 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 32 DLEPcLAELLDRSALRHSARvAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG 111
Cdd:PRK06710 22 DIQP-LHKYVEQMASRYPEK-KALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 112 VPVLPDPTCSDPELEWIADDSGA--VLTLDGELP--------------------DGVAFLDEGAAP-------------- 155
Cdd:PRK06710 100 IVVQTNPLYTERELEYQLHDSGAkvILCLDLVFPrvtnvqsatkiehvivtriaDFLPFPKNLLYPfvqkkqsnlvvkvs 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 156 --------------------------DELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVL------ 203
Cdd:PRK06710 180 esetihlwnsvekevntgvevpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLgvlpff 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 204 -----TA--PLSTAAGSAVQLLP----------------TLAAGGTVV---------------------AAGARGVRVPW 239
Cdd:PRK06710 260 hvygmTAvmNLSIMQGYKMVLIPkfdmkmvfeaikkhkvTLFPGAPTIyiallnspllkeydissiracISGSAPLPVEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 RHLRASFPAARCVRGWGVAETGGI---GLLLptDQRAahPRSVGVPFGGMEVALL----GPAADQG-VGELLCRGPSVAR 311
Cdd:PRK06710 340 QEKFETVTGGKLVEGYGLTESSPVthsNFLW--EKRV--PGSIGVPWPDTEAMIMsletGEALPPGeIGEIVVKGPQIMK 415
|
410 420 430
....*....|....*....|....*....|.
gi 2484101036 312 RYWNDPESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:PRK06710 416 GYWNKPEETAAVLQDGWLHTGDVGYMDEDGF 446
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
34-341 |
2.54e-19 |
|
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: 89.53 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 34 EPCLAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG-- 111
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVF-GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAay 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 112 VPVlpDPTCSDPELEWIADDSGA--VLT---LDGELPDG---VAFLDE-------------GAAPDELAVLYY------V 164
Cdd:COG1020 554 VPL--DPAYPAERLAYMLEDAGArlVLTqsaLAARLPELgvpVLALDAlalaaepatnppvPVTPDDLAYVIYtsgstgR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 165 RKrggglhGVELTNENILSTIEAVVHAMDLTAeGARTVLTAPLSTAAgSAVQLLPTLAAGGTVVAAGARGVR-------- 236
Cdd:COG1020 632 PK------GVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFDA-SVWEIFGALLSGATLVLAPPEARRdpaalael 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 -----------VP-------------------------------WRHLRASFPAARCVRGWGVAETGGIGLLLPTDQRAA 274
Cdd:COG1020 704 larhrvtvlnlTPsllralldaapealpslrlvlvggealppelVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 275 HPRSV--GVPFGGMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETF------DDG--WFHTGDQVHIDGD 340
Cdd:COG1020 784 DGGSVpiGRPIANTRVYVLDahlqPVPVGVPGELYIGGAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPD 863
|
.
gi 2484101036 341 G 341
Cdd:COG1020 864 G 864
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
63-341 |
4.84e-19 |
|
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: 87.32 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 63 TYGQMWSSAARVAGGLLDQ-GVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTL-DG 140
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLtDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 ELPDGVAFL------------------------DEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTa 196
Cdd:TIGR01733 81 ALASRLAGLvlpvilldplelaalddapappppDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 197 EGARTVLTAPLSTAAgSAVQLLPTLAAGGTVVAAGARGVRVP----------------------WRHL------------ 242
Cdd:TIGR01733 160 PDDRVLQFASLSFDA-SVEEIFGALLAGATLVVPPEDEERDDaallaaliaehpvtvlnltpslLALLaaalppalaslr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 -----------------RASFPAARCVRGWGVAETG---GIGLLLPTDQRAAHPRSVGVPFGGMEVALL----GPAADQG 298
Cdd:TIGR01733 239 lvilggealtpalvdrwRARGPGARLINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLdddlRPVPVGV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 299 VGELLCRGPSVARRYWNDPESTAETF---------DDGWFHTGDQVHIDGDG 341
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFvpdpfaggdGARLYRTGDLVRYLPDG 370
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
61-341 |
6.99e-19 |
|
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: 87.41 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 61 ALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTldg 140
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 elpdgvaFLDEGaaPDELAVLYYVRKRGGGLHGVELTNENILSTIE---AVV---------------HAMDLTAE----- 197
Cdd:cd17640 82 -------VVEND--SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRslsDIVppqpgdrflsilpiwHSYERSAEyfifa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 198 -GARTVLTAPLS------------------------------TAAGSAVQ--LLPTLAAGGTVVAAGARGVRVPwRHLRA 244
Cdd:cd17640 153 cGCSQAYTSIRTlkddlkrvkphyivsvprlweslysgiqkqVSKSSPIKqfLFLFFLSGGIFKFGISGGGALP-PHVDT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 245 SFPAA--RCVRGWGVAETGGIGlllpTDQRAAHPR--SVGVPFGGMEVALLGPaaDQGV-------GELLCRGPSVARRY 313
Cdd:cd17640 232 FFEAIgiEVLNGYGLTETSPVV----SARRLKCNVrgSVGRPLPGTEIKIVDP--EGNVvlppgekGIVWVRGPQVMKGY 305
|
330 340
....*....|....*....|....*....
gi 2484101036 314 WNDPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:cd17640 306 YKNPEATSKVLDsDGWFNTGDLGWLTCGG 334
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
61-344 |
3.42e-18 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 85.37 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 61 ALTYGQMWSSAARVAGGLLDQGvGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV---LPDPTCSDPELEWIADDSG--AV 135
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVplpPPTPGRHAERLAAILADAGprVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 136 LTLDGE------------------------LPDGVA--FLDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVV 189
Cdd:cd05931 103 LTTAAAlaavrafaasrpaagtprllvvdlLPDTSAadWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 190 HAMDLTaEGARTV--------------LTAPLstAAGSAVQLLPTLA--------------AGGTVVAA--------GAR 233
Cdd:cd05931 183 RAYGLD-PGDVVVswlplyhdmgliggLLTPL--YSGGPSVLMSPAAflrrplrwlrlisrYRATISAApnfaydlcVRR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 234 GVRVP--------WRHL--------------------RASFPAARCVRGWGVAET--------GGIGLLLPTDQRAAHPR 277
Cdd:cd05931 260 VRDEDlegldlssWRVAlngaepvrpatlrrfaeafaPFGFRPEAFRPSYGLAEAtlfvsggpPGTGPVVLRVDRDALAG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 278 ----------------SVGVPFGGMEVALLGPA-----ADQGVGELLCRGPSVARRYWNDPESTAETF-------DDGWF 329
Cdd:cd05931 340 ravavaaddpaarelvSCGRPLPDQEVRIVDPEtgrelPDGEVGEIWVRGPSVASGYWGRPEATAETFgalaatdEGGWL 419
|
410
....*....|....*.
gi 2484101036 330 HTGD-QVHIDGDGFVT 344
Cdd:cd05931 420 RTGDlGFLHDGELYIT 435
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
39-344 |
4.66e-18 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 85.16 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVA----AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:COG0365 13 NCLDRHAEGRGDKVAliweGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 115 lpdPTCSD---PELEWIADDSGA--VLTLDGELPDGVAFLDEGAAPDELAVLYYVRKR---GGGLHGVELTNEnilSTIE 186
Cdd:COG0365 93 ---PVFPGfgaEALADRIEDAEAkvLITADGGLRGGKVIDLKEKVDEALEELPSLEHVivvGRTGADVPMEGD---LDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 187 AVVHAMDLTAEGARTVLTAPL-----S-----------TAAGSAVQ--------------------------------LL 218
Cdd:COG0365 167 ELLAAASAEFEPEPTDADDPLfilytSgttgkpkgvvhTHGGYLVHaattakyvldlkpgdvfwctadigwatghsyiVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 219 PTLAAGGTVVAAGAR----------------GVRV----P--WRHLRASFPAAR------CVR----------------- 253
Cdd:COG0365 247 GPLLNGATVVLYEGRpdfpdpgrlweliekyGVTVfftaPtaIRALMKAGDEPLkkydlsSLRllgsageplnpevweww 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 ----------GWGVAETGGIgLLLPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCRG--PSVARRYWNDP 317
Cdd:COG0365 327 yeavgvpivdGWGQTETGGI-FISNLPGLPVKPGSMGKPVPGYDVAVVDedgnPVPPGEEGELVIKGpwPGMFRGYWNDP 405
|
410 420 430
....*....|....*....|....*....|
gi 2484101036 318 ESTAETF---DDGWFHTGDQVHIDGDGFVT 344
Cdd:COG0365 406 ERYRETYfgrFPGWYRTGDGARRDEDGYFW 435
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
39-341 |
5.38e-18 |
|
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: 84.56 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVAAVDRAGnALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDP 118
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDR-SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 TCSDPELEWIADDSGAVLTL-DGELPDGVAFL------------------DEGAAPDELAVLYYVRKRGGGLHGVELTNE 179
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLtDRSLAGRAGGLevavvidealdagpagnpAVPVSPDDLAYVMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 180 NILSTieavVHAMDLTAEGARTV--LTAPLSTAAgSAVQLLPTLAAGGTVV---------------AAGARGVRVPW--- 239
Cdd:cd12117 160 GVVRL----VKNTNYVTLGPDDRvlQTSPLAFDA-STFEIWGALLNGARLVlapkgtlldpdalgaLIAEEGVTVLWlta 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 -----------------RHL-----RASFPAARCVR----------GWGVAETGGIGLLLPTDQRAAHPRSV--GVPFGG 285
Cdd:cd12117 235 alfnqladedpecfaglRELltggeVVSPPHVRRVLaacpglrlvnGYGPTENTTFTTSHVVTELDEVAGSIpiGRPIAN 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101036 286 MEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETF-----DDG--WFHTGDQVHIDGDG 341
Cdd:cd12117 315 TRVYVLDedgrPVPPGVPGELYVGGDGLALGYLNRPALTAERFvadpfGPGerLYRTGDLARWLPDG 381
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
37-338 |
9.74e-18 |
|
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: 84.26 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSAR---VAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVP 113
Cdd:cd05906 12 LLELLLRAAERGPTKgitYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 114 ----VLPDPTCSDPELE-------------WIADDSGA-----VLTLDGELPDGVAFLDEG-----------AAPDELAV 160
Cdd:cd05906 92 apltVPPTYDEPNARLRklrhiwqllgspvVLTDAELVaefagLETLSGLPGIRVLSIEELldtaadhdlpqSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 161 LYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAE-------------------------GARTV-------LTAPL- 207
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQdvflnwvpldhvgglvelhlravylGCQQVhvpteeiLADPLr 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 208 ------------STAAGSAVQLLPTLAA-----------------GG--TVVAAGARGVRVPWRH-LRASFPAArcvrGW 255
Cdd:cd05906 252 wldlidryrvtiTWAPNFAFALLNDLLEeiedgtwdlsslrylvnAGeaVVAKTIRRLLRLLEPYgLPPDAIRP----AF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 256 GVAETG-GI--GLLLPTDQRAAHPR--SVGVPFGGMEVALL---GPAADQG-VGELLCRGPSVARRYWNDPESTAETF-D 325
Cdd:cd05906 328 GMTETCsGViySRSFPTYDHSQALEfvSLGRPIPGVSMRIVddeGQLLPEGeVGRLQVRGPVVTKGYYNNPEANAEAFtE 407
|
410
....*....|...
gi 2484101036 326 DGWFHTGDQVHID 338
Cdd:cd05906 408 DGWFRTGDLGFLD 420
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
38-346 |
2.68e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 82.73 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 38 AELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPD 117
Cdd:PRK06188 15 GHLLVSALKRYPDRPALVL-GDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 118 PTCSDPELEWIADDSGA--------------------------VLTLdGELPDGVAFLDEGAA-----------PDELAV 160
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGIstlivdpapfveralallarvpslkhVLTL-GPVPDGVDLLAAAAKfgpaplvaaalPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 161 LYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEgARTVLTAPLSTAAGSAVqlLPTLAAGGTV-VAAG---ARGVR 236
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPAD-PRFLMCTPLSHAGGAFF--LPTLLRGGTViVLAKfdpAEVLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 VPWRH-LRASF------------PA---------------------ARCVRG-----------WGVAETG-GIGLLLPTD 270
Cdd:PRK06188 250 AIEEQrITATFlvptmiyalldhPDlrtrdlssletvyygaspmspVRLAEAierfgpifaqyYGQTEAPmVITYLRKRD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 271 QRAAHPR---SVGVPFGGMEVALLGPA---ADQG-VGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK06188 330 HDPDDPKrltSCGRPTPGLRVALLDEDgreVAQGeVGEICVRGPLVMDGYWNRPEETAEAFRDGWLHTGDVAREDEDGFY 409
|
...
gi 2484101036 344 TPV 346
Cdd:PRK06188 410 YIV 412
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
44-343 |
3.95e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 81.96 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 44 SALRHSARVAAVDRA------GNALTYGQMWSSAARVAGGlldqgVGPADRVVVHYPNGFRWLYAFLGVVLAGgVPVLPD 117
Cdd:PRK07787 2 ASLNPAAVAAAADIAdavrigGRVLSRSDLAGAATAVAER-----VAGARRVAVLATPTLATVLAVVGALIAG-VPVVPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 118 PTCSDP-ELEWIADDSGAVLTLdGELPDGVAFL--------------DEGAAPDELAVLYYVRKRGGGLHGVELTNENIL 182
Cdd:PRK07787 76 PPDSGVaERRHILADSGAQAWL-GPAPDDPAGLphvpvrlharswhrYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 183 STIEAVVHAMDLTAEGArTVLTAPLSTAAGSAVQLLPTLAAGGTVV-------AAGAR----------GVRVPWRHLRAS 245
Cdd:PRK07787 155 ADLDALAEAWQWTADDV-LVHGLPLFHVHGLVLGVLGPLRIGNRFVhtgrptpEAYAQalseggtlyfGVPTVWSRIAAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 246 FPAARCVRG------------------------------WGVAETggiglLLPTDQRAAHPR---SVGVPFGGMEVALLG 292
Cdd:PRK07787 234 PEAARALRGarllvsgsaalpvpvfdrlaaltghrpverYGMTET-----LITLSTRADGERrpgWVGLPLAGVETRLVD 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 293 ------PAADQGVGELLCRGPSVARRYWNDPESTAETF-DDGWFHTGDQVHIDGDGFV 343
Cdd:PRK07787 309 edggpvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFtADGWFRTGDVAVVDPDGMH 366
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
46-343 |
4.23e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 82.40 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 46 LRHSARV----AAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCS 121
Cdd:PRK06178 39 LRAWARErpqrPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 122 DPELEWIADDSGA--VLTLDG--------------------------------ELPDGV--------------------- 146
Cdd:PRK06178 119 EHELSYELNDAGAevLLALDQlapvveqvraetslrhvivtsladvlpaeptlPLPDSLraprlaaagaidllpalract 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 147 -AFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIeAVVHAMDLTAEGARTVLT-APLSTAAGSAVQLLPTLAAG 224
Cdd:PRK06178 199 aPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA-AAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 225 GTVV------------AAGARGV-----------------RVPWRHLRaSFPAARCVR---------------------- 253
Cdd:PRK06178 278 ATLVllarwdavafmaAVERYRVtrtvmlvdnavelmdhpRFAEYDLS-SLRQVRVVSfvkklnpdyrqrwraltgsvla 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 --GWGVAET---GGIGLLLPTDQR--AAHPRSVGVPFGGMEV--------ALLGPAADqgvGELLCRGPSVARRYWNDPE 318
Cdd:PRK06178 357 eaAWGMTEThtcDTFTAGFQDDDFdlLSQPVFVGLPVPGTEFkicdfetgELLPLGAE---GEIVVRTPSLLKGYWNKPE 433
|
410 420
....*....|....*....|....*
gi 2484101036 319 STAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK06178 434 ATAEALRDGWLHTGDIGKIDEQGFL 458
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
56-344 |
5.31e-17 |
|
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: 81.61 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 56 DRAGNALTYGQMWSsAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG-- 133
Cdd:cd05909 2 DTLGTSLTYRKLLT-GAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLT-------------LDGELPDGVAFLDE-------------------------------GAAPDELAVLYYVRKRGG 169
Cdd:cd05909 81 TVLTskqfieklklhhlFDVEYDARIVYLEDlrakiskadkckaflagkfppkwllrifgvaPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 170 GLHGVELTNENILSTIEAVVHAMDLTAEGArtVLTA-PLSTAAGSAVQLLPTLAAGGTV--------------------- 227
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPEDV--VFGAlPFFHSFGLTGCLWLPLLSGIKVvfhpnpldykkipeliydkka 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 228 ---------------------------VAAGARGVRvpwRHLRASFP---AARCVRGWGVAETGGIgLLLPTDQRAAHPR 277
Cdd:cd05909 239 tillgtptflrgyaraahpedfsslrlVVAGAEKLK---DTLRQEFQekfGIRILEGYGTTECSPV-ISVNTPQSPNKEG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 278 SVGVPFGGMEVALLGPA----ADQGV-GELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:cd05909 315 TVGRPLPGMEVKIVSVEtheeVPIGEgGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLT 386
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
39-340 |
7.64e-17 |
|
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: 81.06 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDP 118
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDR-GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 TCSDPELEWIADDSGAVLTLdgelpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEG 198
Cdd:cd17645 81 DYPGERIAYMLADSSAKILL--------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 199 aRTVLTAPLSTAAgSAVQLLPTLAAGGTV-VAAGARGVRVP-------WRHLRASF-PAARC------------------ 251
Cdd:cd17645 147 -KSLVYASFSFDA-SAWEIFPHLTAGAALhVVPSERRLDLDalndyfnQEGITISFlPTGAAeqfmqldnqslrvlltgg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 -------------VRGWGVAETGGIGLLLPTDQRAAHpRSVGVPFGGMEVALLGPA---ADQGV-GELLCRGPSVARRYW 314
Cdd:cd17645 225 dklkkierkgyklVNNYGPTENTVVATSFEIDKPYAN-IPIGKPIDNTRVYILDEAlqlQPIGVaGELCIAGEGLARGYL 303
|
330 340
....*....|....*....|....*.
gi 2484101036 315 NDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:cd17645 304 NRPELTAEKFIVHPFVPGERMYRTGD 329
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
37-343 |
1.04e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 80.95 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK06087 25 LADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA-----------------VLTLDGELP--DGVAFLDEgAAP---------------------- 155
Cdd:PRK06087 105 LPSWREAELVWVLNKCQAkmffaptlfkqtrpvdlILPLQNQLPqlQQIVGVDK-LAPatsslslsqiiadyeplttait 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 156 ---DELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGArTVLTAPLSTAAGSAVQLLPTLAAGGTVV---- 228
Cdd:PRK06087 184 thgDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDV-FMMPAPLGHATGFLHGVTAPFLIGARSVlldi 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 ------AAGARGVRVPW------------RHLRAS---FPAARCVRGWGV---------AETGGIGLLLPTDQRAAHPRS 278
Cdd:PRK06087 263 ftpdacLALLEQQRCTCmlgatpfiydllNLLEKQpadLSALRFFLCGGTtipkkvareCQQRGIKLLSVYGSTESSPHA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 279 V--------------GVPFGGMEVALLG------PAADQgvGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHI 337
Cdd:PRK06087 343 VvnlddplsrfmhtdGYAAAGVEIKVVDearktlPPGCE--GEEASRGPNVFMGYLDEPELTARALDeEGWYYSGDLCRM 420
|
....*.
gi 2484101036 338 DGDGFV 343
Cdd:PRK06087 421 DEAGYI 426
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
51-346 |
1.84e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 80.24 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDRA-GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWI- 128
Cdd:PRK09088 11 RLAAVDLAlGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 129 ---------ADDSGAVLTLDGELPDGVAFLDEGAAPDELA--------VLYYVRKRGGGLHGVELTNENILSTieaVVHA 191
Cdd:PRK09088 91 qdaeprlllGDDAVAAGRTDVEDLAAFIASADALEPADTPsippervsLILFTSGTSGQPKGVMLSERNLQQT---AHNF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 192 MDLTAEGARTVL--TAPLSTAAGSAVQLLPTLAAGGTV-VAAGARGVR-----------------VP------------- 238
Cdd:PRK09088 168 GVLGRVDAHSSFlcDAPMFHIIGLITSVRPVLAVGGSIlVSNGFEPKRtlgrlgdpalgithyfcVPqmaqafraqpgfd 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 239 ---WRHLRASFP-----AARCVRGW-----------GVAETGGI-GLLLPTDQRAAHPRSVGVPFGGMEVALL---GPAA 295
Cdd:PRK09088 248 aaaLRHLTALFTggaphAAEDILGWlddgipmvdgfGMSEAGTVfGMSVDCDVIRAKAGAAGIPTPTVQTRVVddqGNDC 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2484101036 296 DQGV-GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFVTPV 346
Cdd:PRK09088 328 PAGVpGELLLRGPNLSPGYWRRPQATARAFTgDGWFRTGDIARRDADGFFWVV 380
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
54-334 |
2.21e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 80.01 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG--VPVLPD-P------------ 118
Cdd:cd12114 5 AVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDqPaarreailadag 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 -----TCSDPELEWIADDSGAVLTLDGELPDGvAFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMD 193
Cdd:cd12114 85 arlvlTDGPDAQLDVAVFDVLILDLDALAAPA-PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 194 LTAEGaRTVLTAPLSTAAgSAVQLLPTLAAGGTVVAAGARGVRVP--WRHL----------------------------- 242
Cdd:cd12114 164 VGPDD-RVLALSSLSFDL-SVYDIFGALSAGATLVLPDEARRRDPahWAELierhgvtlwnsvpallemlldvleaaqal 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 ----------------------RASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSV--GVPFGGMEVALLGPAA--- 295
Cdd:cd12114 242 lpslrlvllsgdwipldlparlRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPRGrdc 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2484101036 296 -DQGVGELLCRGPSVARRYWNDPESTAETF---DDG--WFHTGDQ 334
Cdd:cd12114 322 pDWVPGELWIGGRGVALGYLGDPELTAARFvthPDGerLYRTGDL 366
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
37-344 |
3.09e-16 |
|
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: 79.29 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:cd05920 17 LGDLLARSAARHPDRIAVVD-GDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTLdgeLPDGVAFLDEGAAPDEL-------AVLyyvrKRGGGLHG----VELTNENILSTI 185
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYI---VPDRHAGFDHRALARELaesipevALF----LLSGGTTGtpklIPRTHNDYAYNV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 186 EAVVHAMDLTAEgarTVLTAPLSTAAGSAVQ---LLPTLAAGGTVVAAG------------ARGVR----VP-------- 238
Cdd:cd05920 169 RASAEVCGLDQD---TVYLAVLPAAHNFPLAcpgVLGTLLAGGRVVLAPdpspdaafplieREGVTvtalVPalvslwld 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 239 ---WRHL-------------RASFPAARCVRG---------WGVAEtggiGLLLPT-----DQRAAHprSVGVPFG-GME 287
Cdd:cd05920 246 aaaSRRAdlsslrllqvggaRLSPALARRVPPvlgctlqqvFGMAE----GLLNYTrlddpDEVIIH--TQGRPMSpDDE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 288 V----ALLGPAADQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:cd05920 320 IrvvdEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTpDGFYRTGDLVRRTPDGYLV 381
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
54-343 |
4.19e-16 |
|
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: 78.95 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG 133
Cdd:cd17649 5 ALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLTLdgelpdgvafldeGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAeGARTVLTAPLSTaAGS 213
Cdd:cd17649 85 AGLLL-------------THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP-GDRELQFASFNF-DGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 214 AVQLLPTLAAGGTVV---------------------------------------AAGARGVRVPWR------------HL 242
Cdd:cd17649 150 HEQLLPPLICGACVVlrpdelwasadelaemvrelgvtvldlppaylqqlaeeaDRTGDGRPPSLRlyifggealspeLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 RASFPAA-RCVRGWGVAETGGIGLL--LPTDQRAAHPRS-VGVPFGGMEVALL----GPAADQGVGELLCRGPSVARRYW 314
Cdd:cd17649 230 RRWLKAPvRLFNAYGPTEATVTPLVwkCEAGAARAGASMpIGRPLGGRSAYILdadlNPVPVGVTGELYIGGEGLARGYL 309
|
330 340 350
....*....|....*....|....*....|....*..
gi 2484101036 315 NDPESTAETF------DDG--WFHTGDQVHIDGDGFV 343
Cdd:cd17649 310 GRPELTAERFvpdpfgAPGsrLYRTGDLARWRDDGVI 346
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-341 |
4.72e-16 |
|
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: 78.89 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVAaVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG--VPVlp 116
Cdd:cd17653 1 DAFERIAAAHPDAVA-VESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAayVPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTLdgelpdgvaFLDegaAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTA 196
Cdd:cd17653 78 DAKLPSARIQAILRTSGATLLL---------TTD---SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 197 eGARTVLTAPLSTAAGSAVqLLPTLAAGGTVVAAGARGvrvPWRHL------------------RASFP----------- 247
Cdd:cd17653 146 -GSRVAQVLSIAFDACIGE-IFSTLCNGGTLVLADPSD---PFAHVartvdalmstpsilstlsPQDFPnlktiflggea 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 248 -----------AARCVRGWGVAETG---GIGLLLPTDqraahPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPSV 309
Cdd:cd17653 221 vppslldrwspGRRLYNAYGPTECTissTMTELLPGQ-----PVTIGKPIPNSTCYILDadlqPVPEGVVGEICISGVQV 295
|
330 340 350
....*....|....*....|....*....|....*....
gi 2484101036 310 ARRYWNDPESTAE-----TFDDGW--FHTGDQVHIDGDG 341
Cdd:cd17653 296 ARGYLGNPALTASkfvpdPFWPGSrmYRTGDYGRWTEDG 334
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
39-341 |
6.97e-16 |
|
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: 78.35 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVA--AVDRAgnaLTYGQMWSSAARVAGGLLDQGVGPADRVVVHypngF---RWLY-AFLGVVLAGGV 112
Cdd:cd05918 3 DLIEERARSQPDAPAvcAWDGS---LTYAELDRLSSRLAHHLRSLGVGPGVFVPLC----FeksKWAVvAMLAVLKAGGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 PVLPDPtcSDPE--LEWIADDSGA--VLTLDgelPDGVAFldegaapdelaVLYY-----VRKrggglhGVELTNENILS 183
Cdd:cd05918 76 FVPLDP--SHPLqrLQEILQDTGAkvVLTSS---PSDAAY-----------VIFTsgstgKPK------GVVIEHRALST 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 184 TIEAVVHAMDLTAEgARTVLTAPLSTAAgSAVQLLPTLAAGGTV-----------VAAGARGVRVPWRHLRASF-----P 247
Cdd:cd05918 134 SALAHGRALGLTSE-SRVLQFASYTFDV-SILEIFTTLAAGGCLcipseedrlndLAGFINRLRVTWAFLTPSVarlldP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 248 A--------------------------ARCVRGWGVAETGgIGLLLPTDQRAAHPRSVGVPFGGM----------EVALL 291
Cdd:cd05918 212 EdvpslrtlvlggealtqsdvdtwadrVRLINAYGPAECT-IAATVSPVVPSTDPRNIGRPLGATcwvvdpdnhdRLVPI 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 292 GpaadqGVGELLCRGPSVARRYWNDPESTAETF--DDGW------------FHTGDQVHIDGDG 341
Cdd:cd05918 291 G-----AVGELLIEGPILARGYLNDPEKTAAAFieDPAWlkqegsgrgrrlYRTGDLVRYNPDG 349
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
54-344 |
7.09e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 78.49 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG 133
Cdd:cd12116 5 AVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLTL-DGELPDGVAF------------------LDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDL 194
Cdd:cd12116 85 PALVLtDDALPDRLPAglpvlllalaaaaaapaaPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 195 TAEGARTVLTAPlsTAAGSAVQLLPTLAAGGTVVAAGARGVRVP---------------------WRHLRASfpaarcvr 253
Cdd:cd12116 165 GPGDRLLAVTTY--AFDISLLELLLPLLAGARVVIAPRETQRDPealarlieahsitvmqatpatWRMLLDA-------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAET-----GGIGL-------LL-----------PTD----------QRAAHPRSVGVPFGGMEVALLGPAAD---Q 297
Cdd:cd12116 235 GWQGRAGltalcGGEALppdlaarLLsrvgslwnlygPTEttiwstaarvTAAAGPIPIGRPLANTQVYVLDAALRpvpP 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101036 298 GV-GELLCRGPSVARRYWNDPESTAETFDDG--------WFHTGDQVHIDGDGFVT 344
Cdd:cd12116 315 GVpGELYIGGDGVAQGYLGRPALTAERFVPDpfagpgsrLYRTGDLVRRRADGRLE 370
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
51-341 |
7.60e-16 |
|
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: 78.12 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIAD 130
Cdd:cd17643 3 AVAVVD-EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 131 DSGAVLTLDgelpdgvafldegaAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAE------------- 197
Cdd:cd17643 82 DSGPSLLLT--------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDdvwtlfhsyafdf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 198 -----------GARTVL-----------TAPLSTAAGSAV---------QLLPTLAAGGT-------VVAAG----ARGV 235
Cdd:cd17643 148 svweiwgallhGGRLVVvpyevarspedFARLLRDEGVTVlnqtpsafyQLVEAADRDGRdplalryVIFGGealeAAML 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 236 RvPWRHlRASFPAARCVRGWGVAETG---GIGLLLPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPS 308
Cdd:cd17643 228 R-PWAG-RFGLDRPQLVNMYGITETTvhvTFRPLDAADLPAAAASPIGRPLPGLRVYVLDadgrPVPPGVVGELYVSGAG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2484101036 309 VARRYWNDPESTAETFDDGWF--------HTGDQVHIDGDG 341
Cdd:cd17643 306 VARGYLGRPELTAERFVANPFggpgsrmyRTGDLARRLPDG 346
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
42-343 |
8.38e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 78.28 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 42 DRSALRHsarvaavdrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCS 121
Cdd:PRK07786 32 DAPALRF---------LGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 122 DPELEWIADDSGA-------------------------VLTLDGELPDGVAFLDE-----GAAP-------DELAVLYYV 164
Cdd:PRK07786 103 PPEIAFLVSDCGAhvvvteaalapvatavrdivpllstVVVAGGSSDDSVLGYEDllaeaGPAHapvdipnDSPALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 165 RKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVLTAPLSTAAGSAvQLLPTLAAGGTVV---------------- 228
Cdd:PRK07786 183 SGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTViyplgafdpgqlldvl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 --------------------AAGARG----VRV-PW----------RHLRASFPAARCVRGWGVAETGGIGLLLPTDQRA 273
Cdd:PRK07786 262 eaekvtgiflvpaqwqavcaEQQARPrdlaLRVlSWgaapasdtllRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDAI 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 274 AHPRSVGVPFGGMEVALLGPAAD---QG-VGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK07786 342 RKLGSVGKVIPTVAARVVDENMNdvpVGeVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYV 415
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
242-341 |
9.08e-16 |
|
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: 78.03 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 242 LRASFpAARCVRGWGVAET-GGIGLLLPTDQRAAHprsVGVPFGGMEVAL-----LG--PAADQGVGELLCRGPSVARRY 313
Cdd:cd05927 294 LRVAL-GCPVLEGYGQTECtAGATLTLPGDTSVGH---VGGPLPCAEVKLvdvpeMNydAKDPNPRGEVCIRGPNVFSGY 369
|
90 100
....*....|....*....|....*....
gi 2484101036 314 WNDPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:cd05927 370 YKDPEKTAEALDeDGWLHTGDIGEWLPNG 398
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
37-341 |
1.07e-15 |
|
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: 77.74 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRAGNaLTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDES-LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTLDGelpdgvafldegaaPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVvhAMDLTA 196
Cdd:cd12115 80 DPAYPPERLRFILEDAQARLVLTD--------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWA--AAAFSA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 197 EGARTVLTAPLSTAAGSAVQLLPTLAAGGTVVAA------------------------------------GARGV----- 235
Cdd:cd12115 144 EELAGVLASTSICFDLSVFELFGPLATGGKVVLAdnvlalpdlpaaaevtlintvpsaaaellrhdalpaSVRVVnlage 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 236 ---RVPWRHLRASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPS 308
Cdd:cd12115 224 plpRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLDralqPVPLGVPGELYIGGAG 303
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2484101036 309 VARRYWNDPESTAETFDDGWFH-------TGDQVHIDGDG 341
Cdd:cd12115 304 VARGYLGRPGLTAERFLPDPFGpgarlyrTGDLVRWRPDG 343
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
36-343 |
1.60e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 77.51 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 36 CLAELLDRSALRHSARVAAVDR-AGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 115 LPDPTCSDPELEWIADDSGA--VLTLDG-ELPDGVAFLDE------GAAPDELA---------VLYY------------- 163
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVrwVICADAfKTSDYHAMLQEllpglaEGQPGALAcerlpelrgVVSLapapppgflawhe 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 164 VRKRGGGLH------------------------------GVELTNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGS 213
Cdd:PRK12583 179 LQARGETVSrealaerqasldrddpiniqytsgttgfpkGATLSHHNILNNGYFVAESLGLT-EHDRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 214 AVQLLPTLAAGGTVV-------------------AAGARGVRV--------PWR------HLRASFPA-ARCVR------ 253
Cdd:PRK12583 258 VLANLGCMTVGACLVypneafdplatlqaveeerCTALYGVPTmfiaeldhPQRgnfdlsSLRTGIMAgAPCPIevmrrv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 -----------GWGVAETGGIGLLL-PTDQRAAHPRSVGVPFGGMEVALLGPAADQ----GVGELLCRGPSVARRYWNDP 317
Cdd:PRK12583 338 mdemhmaevqiAYGMTETSPVSLQTtAADDLERRVETVGRTQPHLEVKVVDPDGATvprgEIGELCTRGYSVMKGYWNNP 417
|
410 420
....*....|....*....|....*..
gi 2484101036 318 ESTAETFD-DGWFHTGDQVHIDGDGFV 343
Cdd:PRK12583 418 EATAESIDeDGWMHTGDLATMDEQGYV 444
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
40-344 |
2.66e-15 |
|
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: 76.80 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 40 LLDRSALR-HSARVAAVDRAGnALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDP 118
Cdd:TIGR02262 9 LLDRNVVEgRGGKTAFIDDIS-SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 TCSDPELEWIADDSGA-VLTLDGEL-----------PDGVAFLDEGAA------------------------PDELAVLY 162
Cdd:TIGR02262 88 LLTADDYAYMLEDSRArVVFVSGALlpvikaalgksPHLEHRVVVGRPeagevqlaellateseqfkpaatqADDPAFWL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 163 YVRKRGGGLHGVELTNENILSTIE-------------AVVHAMDL-------------TAEGARTVLTAPLSTAAGSAVQ 216
Cdd:TIGR02262 168 YSSGSTGMPKGVVHTHSNPYWTAElyarntlgireddVCFSAAKLffayglgnaltfpMSVGATTVLMGERPTPDAVFDR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 217 LL---PTLAAGG-TVVAAGARGVRVPWR---HLRASFPAA---------RCVRGWGVAETGGIG------LLLPTDQRAA 274
Cdd:TIGR02262 248 LRrhqPTIFYGVpTLYAAMLADPNLPSEdqvRLRLCTSAGealpaevgqRWQARFGVDIVDGIGstemlhIFLSNLPGDV 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 275 HPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:TIGR02262 328 RYGTSGKPVPGYRLRLVGdggqDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYT 401
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
71-347 |
3.51e-15 |
|
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: 76.32 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 71 AARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG------VPVlpDPTCSDPELEWIADDSGAVLTLDGE--- 141
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglvfVPL--NPTLKESVLRYLVADAGGRIVLADAgaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 142 ---------LPDGVAFLDEGA-------------APDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGa 199
Cdd:cd05922 81 drlrdalpaSPDPGTVLDADGiraarasapahevSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 200 RTVLTAPLSTAAGSAvQLLPTLAAGGTVV-------------------AAGARGV--------RVPW------------- 239
Cdd:cd05922 160 RALTVLPLSYDYGLS-VLNTHLLRGATLVltndgvlddafwedlrehgATGLAGVpstyamltRLGFdpaklpslryltq 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 ----------RHLRASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALL----GPAADQGVGELLCR 305
Cdd:cd05922 239 aggrlpqetiARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILdddgTPTPPGEPGEIVHR 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2484101036 306 GPSVARRYWNDP-ESTAETFDDGWFHTGDQVHIDGDGFVTPVA 347
Cdd:cd05922 319 GPNVMKGYWNDPpYRRKEGRGGGVLHTGDLARRDEDGFLFIVG 361
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
43-341 |
8.22e-15 |
|
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: 75.07 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 43 RSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSD 122
Cdd:cd17651 3 RQAARTPDAPALVAE-GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 123 PELEWIADDSGAVLTL---------DGELPDGVAFLDEGAA------------PDELAVLYYVRKRGGGLHGVELTNENI 181
Cdd:cd17651 82 ERLAFMLADAGPVLVLthpalagelAVELVAVTLLDQPGAAagadaepdpaldADDLAYVIYTSGSTGRPKGVVMPHRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 182 LSTIEAVVHAMDLTAeGARTVLTAPLSTAAgSAVQLLPTLAAGGTVV--------------------------------- 228
Cdd:cd17651 162 ANLVAWQARASSLGP-GARTLQFAGLGFDV-SVQEIFSTLCAGATLVlppeevrtdppalaawldeqrisrvflptvalr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 ---AAGARGVRVP------------------WRHLRASFPAARCVRGWGVAETGGI-GLLLPTDQrAAHPR--SVGVPFG 284
Cdd:cd17651 240 alaEHGRPLGVRLaalrylltggeqlvltedLREFCAGLPGLRLHNHYGPTETHVVtALSLPGDP-AAWPAppPIGRPID 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 285 GMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWF-------HTGDQVHIDGDG 341
Cdd:cd17651 319 NTRVYVLDaalrPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmyRTGDLARWLPDG 386
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-341 |
1.15e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.58 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 30 YEDLEPCLAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLA 109
Cdd:PRK12467 507 TEYAPDCVHQLIEAQARQHPERPALV-FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKA 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 110 GGVPVLPDPTCSDPELEWIADDSGAVLTLDGE-------LPDGVAFLDEGA-----------------APDELAVLYYVR 165
Cdd:PRK12467 586 GGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQShllaqlpVPAGLRSLCLDEpadllcgysghnpevalDPDNLAYVIYTS 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 166 KRGGGLHGVELTNENILSTIEAVVHAMDLTAEgARTVLTAPLStAAGSAVQLLPTLAAGGTVV----------------- 228
Cdd:PRK12467 666 GSTGQPKGVAISHGALANYVCVIAERLQLAAD-DSMLMVSTFA-FDLGVTELFGALASGATLHllppdcardaeafaalm 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 -----------------------AAGARGVR--------------VPWRHLRasfPAARCVRGWGVAET--GGIGLLLPT 269
Cdd:PRK12467 744 adqgvtvlkivpshlqallqasrVALPRPQRalvcggealqvdllARVRALG---PGARLINHYGPTETtvGVSTYELSD 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 270 DQRAAHPRSVGVPFGGMEV----ALLGPAADQGVGELLCRGPSVARRYWNDPESTAETF------DDG--WFHTGDQVHI 337
Cdd:PRK12467 821 EERDFGNVPIGQPLANLGLyildHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgADGgrLYRTGDLARY 900
|
....
gi 2484101036 338 DGDG 341
Cdd:PRK12467 901 RADG 904
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
62-341 |
1.24e-14 |
|
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: 74.56 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGgvpvLPDPTCSDpelewiaddsgavlTLdGE 141
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN----IPIVTVYA--------------TL-GE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 142 lpDGVAF-LDE--------GAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVV--------------------HAM 192
Cdd:cd17639 67 --DALIHsLNEtecsaiftDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGdrvpellgpddrylaylplaHIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 193 DLTAE------GAR----TVLTAPLSTAAGS---AVQLLPTLAAG-------------------GTV------------V 228
Cdd:cd17639 145 ELAAEnvclyrGGTigygSPRTLTDKSKRGCkgdLTEFKPTLMVGvpaiwdtirkgvlaklnpmGGLkrtlfwtayqskL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 AAGARGV-------RVPWR-------HLRASF-------PAAR-------C--VRGWGVAETGGIG-LLLPTDQRAAhpr 277
Cdd:cd17639 225 KALKEGPgtplldeLVFKKvraalggRLRYMLsggaplsADTQeflnivlCpvIQGYGLTETCAGGtVQDPGDLETG--- 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 278 SVGVPFGGMEVALL-----GPAADQGV--GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:cd17639 302 RVGPPLPCCEIKLVdweegGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDG 373
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
39-340 |
2.56e-14 |
|
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: 73.85 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDP 118
Cdd:cd17646 2 ALVAEQAARTPDAPAVVD-EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 TCSDPELEWIADDSGAVLTLDGE--------LPDGVAFLDEGAA------------PDELAVLYYVRKRGGGLHGVELTN 178
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTAdlaarlpaGGDVALLGDEALAappatpplvpprPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 179 ENILSTIEAVVHAMDLTAeGARTVLTAPLSTAAgSAVQLLPTLAAGGTVVAAGARGVRVP-------------------- 238
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGP-GDRVLQKTPLSFDV-SVWELFWPLVAGARLVVARPGGHRDPaylaalirehgvttchfvps 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 239 -------------WRHLRASF-----------------PAARCVRGWGVAETgGIGLLLPTDQRAAHPRSV--GVPFGGM 286
Cdd:cd17646 239 mlrvflaepaagsCASLRRVFcsgealppelaarflalPGAELHNLYGPTEA-AIDVTHWPVRGPAETPSVpiGRPVPNT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 287 EVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:cd17646 318 RLYVLDdalrPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGD 375
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
37-342 |
2.76e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 73.84 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQ-GVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL 115
Cdd:PRK08314 12 LFHNLEVSARRYPDKTAIV-FYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 116 PDPTCSDPELEWIADDSGA------------VLTLDGEL------------------------------------PDGVA 147
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGArvaivgselapkVAPAVGNLrlrhvivaqysdylpaepeiavpawlraepplqalaPGGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 148 FLDE-----------GAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEgARTVLTAPLSTAAGSAVQ 216
Cdd:PRK08314 171 AWKEalaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPE-SVVLAVLPLFHVTGMVHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 217 LLPTLAAGGTVV-------AAGARGV---RVP-W------------------------RHLR---ASFPAA--------- 249
Cdd:PRK08314 250 MNAPIYAGATVVlmprwdrEAAARLIeryRVThWtniptmvvdflaspglaerdlsslRYIGgggAAMPEAvaerlkelt 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 --RCVRGWGVAETGGIGLLLPTDqraaHPRS--VGVPFGGMEVALLGPAA----DQG-VGELLCRGPSVARRYWNDPEST 320
Cdd:PRK08314 330 glDYVEGYGLTETMAQTHSNPPD----RPKLqcLGIPTFGVDARVIDPETleelPPGeVGEIVVHGPQVFKGYWNRPEAT 405
|
410 420
....*....|....*....|....*.
gi 2484101036 321 AETFD--DG--WFHTGDQVHIDGDGF 342
Cdd:PRK08314 406 AEAFIeiDGkrFFRTGDLGRMDEEGY 431
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-340 |
3.05e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.22 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 33 LEPCLAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:PRK12316 3055 LERGVHRLFEEQVERTPDAVALA-FGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGA 3133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 PVLPDPTCSDPELEWIADDSGAVLTLDGE-----LPDGVAFL-----DEGAA---------PDELAVLYYVRKRGGGLHG 173
Cdd:PRK12316 3134 YVPLDPEYPEERLAYMLEDSGAQLLLSQShlrlpLAQGVQVLdldrgDENYAeanpairtmPENLAYVIYTSGSTGKPKG 3213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 174 VELTNENILSTIEAVVHAMDLTAEGarTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGARGVRVP--------------- 238
Cdd:PRK12316 3214 VGIRHSALSNHLCWMQQAYGLGVGD--RVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPallvelinsegvdvl 3291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 239 ---WRHLRASFPAARCVRGWGVAETGGIGLLLPTDQRAA----------------------------HPRS--VGVPFGG 285
Cdd:PRK12316 3292 hayPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQvfaglplynlygpteatitvthwqcveeGKDAvpIGRPIAN 3371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 286 MEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:PRK12316 3372 RACYILDgslePVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
40-344 |
9.94e-14 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 71.95 E-value: 9.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 40 LLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPT 119
Cdd:cd12118 9 FLERAAAVYPDRTSIVYG-DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 120 CSDPELEWIADDSGA-VLTLDGELpDGVAFLDEGAaPDELA----------VLYYVRKRGGGLHGVELTNENI-LSTIEA 187
Cdd:cd12118 88 LDAEEIAFILRHSEAkVLFVDREF-EYEDLLAEGD-PDFEWippadewdpiALNYTSGTTGRPKGVVYHHRGAyLNALAN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 188 VV-HAMDLtaeGARTVLTAPLSTAAGSAVQLLPTlAAGGTVV----------------------------------AAGA 232
Cdd:cd12118 166 ILeWEMKQ---HPVYLWTLPMFHCNGWCFPWTVA-AVGGTNVclrkvdakaiydliekhkvthfcgaptvlnmlanAPPS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 233 RGVRVPWR---HLRASFPAARCVR-----------GWGVAETGGIGLL---------LPTDQRAAHPRSVGVPFGGME-V 288
Cdd:cd12118 242 DARPLPHRvhvMTAGAPPPAAVLAkmeelgfdvthVYGLTETYGPATVcawkpewdeLPTEERARLKARQGVRYVGLEeV 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2484101036 289 ALLGPAADQGV-------GELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:cd12118 322 DVLDPETMKPVprdgktiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIE 384
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
254-342 |
1.08e-13 |
|
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: 71.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIGLLLPTDQRaahPRSVGVPFGGMEVALL----GPAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWF 329
Cdd:cd17637 142 LYGQTETSGLVTLSPYRER---PGSAGRPGPLVRVRIVddndRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWH 218
|
90
....*....|...
gi 2484101036 330 HTGDQVHIDGDGF 342
Cdd:cd17637 219 HTGDLGRFDEDGY 231
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
250-346 |
1.70e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.39 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 RCVRGWGVAETGGIGLLLPTDQRAaHPRSVGVPFGGMEVALLGpaaDQGV-------GELLCRGPSVARRYWNDPESTAE 322
Cdd:PRK12492 360 TIVEGYGLTETSPVASTNPYGELA-RLGTVGIPVPGTALKVID---DDGNelplgerGELCIKGPQVMKGYWQQPEATAE 435
|
90 100
....*....|....*....|....*
gi 2484101036 323 TFD-DGWFHTGDQVHIDGDGFVTPV 346
Cdd:PRK12492 436 ALDaEGWFKTGDIAVIDPDGFVRIV 460
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
63-344 |
1.78e-13 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 70.94 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 63 TYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTLDGEL 142
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 143 PDGVAF----LDEGAAP-------------DELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTaEGARTVLTA 205
Cdd:TIGR01923 81 LEEKDFqadsLDRIEAAgryetslsasfnmDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFT-EDDNWLLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 206 PLSTAAGSAVqLLPTLAAGGTVVAAGARG--------------VRVP---WRHLRASFPAA--RCVR------------- 253
Cdd:TIGR01923 160 PLYHISGLSI-LFRWLIEGATLRIVDKFNqllemianervthiSLVPtqlNRLLDEGGHNEnlRKILlggsaipapliee 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 ----------GWGVAETGGIGLLLPTDQRAAHPrSVGVPFGGMEVALLGPAAdQGVGELLCRGPSVARRYWNDPESTAET 323
Cdd:TIGR01923 239 aqqyglpiylSYGMTETCSQVTTATPEMLHARP-DVGRPLAGREIKIKVDNK-EGHGEIMVKGANLMKGYLYQGELTPAF 316
|
330 340
....*....|....*....|.
gi 2484101036 324 FDDGWFHTGDQVHIDGDGFVT 344
Cdd:TIGR01923 317 EQQGWFNTGDIGELDGEGFLY 337
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
37-343 |
2.14e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 70.85 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDrAGNALTYGQMwSSAARVAGGLLDQGVG--PADRVVVHYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:PRK08974 25 LVDMFEQAVARYADQPAFIN-MGEVMTFRKL-EERSRAFAAYLQNGLGlkKGDRVALMMPNLLQYPIALFGILRAGMIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 115 LPDPTCSDPELEWIADDSGA-------------------------VLTLDGE-------------------------LPD 144
Cdd:PRK08974 103 NVNPLYTPRELEHQLNDSGAkaivivsnfahtlekvvfktpvkhvILTRMGDqlstakgtlvnfvvkyikrlvpkyhLPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 145 GVAF---LDEG---------AAPDELAVLYYVrkrgGGLHGVE----LTNENILSTIE-AVVHAMDLTAEGARTVLTA-P 206
Cdd:PRK08974 183 AISFrsaLHKGrrmqyvkpeLVPEDLAFLQYT----GGTTGVAkgamLTHRNMLANLEqAKAAYGPLLHPGKELVVTAlP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 207 LSTAAGSAVQLLPTLAAGGT-VVAAGARGV--------RVPWRHL-----------------RASFPAARCVRGWG---- 256
Cdd:PRK08974 259 LYHIFALTVNCLLFIELGGQnLLITNPRDIpgfvkelkKYPFTAItgvntlfnallnneefqELDFSSLKLSVGGGmavq 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 257 --VAE-----TG-----GIGLLLPTDQRAAHPR-------SVGVPFGGMEVALL---GPAADQG-VGELLCRGPSVARRY 313
Cdd:PRK08974 339 qaVAErwvklTGqylleGYGLTECSPLVSVNPYdldyysgSIGLPVPSTEIKLVdddGNEVPPGePGELWVKGPQVMLGY 418
|
410 420 430
....*....|....*....|....*....|
gi 2484101036 314 WNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK08974 419 WQRPEATDEVIKDGWLATGDIAVMDEEGFL 448
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
39-340 |
3.26e-13 |
|
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: 70.43 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 39 ELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDP 118
Cdd:cd17655 1 ELFEEQAEKTPDHTAVV-FEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 119 TCSDPELEWIADDSGA-VLTLDGELPDGVAF------LDEGAA-------------PDELAVLYYVRKRGGGLHGVELTN 178
Cdd:cd17655 80 DYPEERIQYILEDSGAdILLTQSHLQPPIAFiglidlLDEDTIyheesenlepvskSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 179 ENILSTIEAVVHAMDLTaEGARTVLTAPLSTAAgSAVQLLPTLAAGGTVV------------------------------ 228
Cdd:cd17655 160 RGVVNLVEWANKVIYQG-EHLRVALFASISFDA-SVTEIFASLLSGNTLYivrketvldgqaltqyirqnritiidltpa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 229 -----AAGARGVRVPWRHLRASFPA--ARCVRGW--------------GVAET---GGIGLLLPTDQRAAHPrSVGVPFG 284
Cdd:cd17655 238 hlkllDAADDSEGLSLKHLIVGGEAlsTELAKKIielfgtnptitnayGPTETtvdASIYQYEPETDQQVSV-PIGKPLG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 285 GMEVALLgpaaDQ-------GV-GELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:cd17655 317 NTRIYIL----DQygrpqpvGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGD 376
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
43-346 |
4.59e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 69.90 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 43 RSALRHSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVpVLP------ 116
Cdd:PRK07514 10 RAAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAV-FLPlntayt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 -----------DPT---CSDPELEW---IADDSGA--VLTLD----GELPDGVA-----FLDEGAAPDELAVLYYVRKRG 168
Cdd:PRK07514 89 laeldyfigdaEPAlvvCDPANFAWlskIAAAAGAphVETLDadgtGSLLEAAAaapddFETVPRGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 169 GGLHGVELTNENILSTIEAVVHAMDLTAEgarTVLTAPL--------------STAAGSAVQLLPTLAAGgTVVAAGAR- 233
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPD---DVLIHALpifhthglfvatnvALLAGASMIFLPKFDPD-AVLALMPRa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 234 ----GV--------------RVPWRHLR----ASFP-AARCVRGW------------GVAETGGI------GlllptDQR 272
Cdd:PRK07514 245 tvmmGVptfytrllqeprltREAAAHMRlfisGSAPlLAETHREFqertghaileryGMTETNMNtsnpydG-----ERR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 273 AAhprSVGVPFGGMEVALLGPAADQ-----GVGELLCRGPSVARRYWNDPESTAETF-DDGWFHTGDQVHIDGDGFVTPV 346
Cdd:PRK07514 320 AG---TVGFPLPGVSLRVTDPETGAelppgEIGMIEVKGPNVFKGYWRMPEKTAEEFrADGFFITGDLGKIDERGYVHIV 396
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-324 |
7.77e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 69.99 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 33 LEPCLAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:PRK12316 4549 ATRCVHQLVAERARMTPDAVAVV-FDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGA 4627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 PVLPDPTCSDPELEWIADDSGAVLTLDGE-------LPDGVAFLD-------EG---------AAPDELAVLYYVRKRGG 169
Cdd:PRK12316 4628 YVPLDPEYPRERLAYMMEDSGAALLLTQShllqrlpIPDGLASLAldrdedwEGfpahdpavrLHPDNLAYVIYTSGSTG 4707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 170 GLHGVELTNENILSTIEAVVHAMDLTAEGaRTVLTAPLSTaAGSAVQLLPTLAAGGTVVAAGArGVRVPWRHLR------ 243
Cdd:PRK12316 4708 RPKGVAVSHGSLVNHLHATGERYELTPDD-RVLQFMSFSF-DGSHEGLYHPLINGASVVIRDD-SLWDPERLYAeihehr 4784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 244 ----------------------------------------------ASFPAARCVRGWGVAETGGIGLL---LPTDQRAA 274
Cdd:PRK12316 4785 vtvlvfppvylqqlaehaerdgeppslrvycfggeavaqasydlawRALKPVYLFNGYGPTETTVTVLLwkaRDGDACGA 4864
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 275 HPRSVGVPFGGMEVALL----GPAADQGVGELLCRGPSVARRYWNDPESTAETF 324
Cdd:PRK12316 4865 AYMPIGTPLGNRSGYVLdgqlNPLPVGVAGELYLGGEGVARGYLERPALTAERF 4918
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
268-344 |
9.24e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.07 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 268 PTDQRAAhprSVGVPFGGMEVALLGPAADQGV-----GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:PRK08315 365 PLEKRVT---TVGRALPHLEVKIVDPETGETVprgeqGELCTRGYSVMKGYWNDPEKTAEAIDaDGWMHTGDLAVMDEEG 441
|
...
gi 2484101036 342 FVT 344
Cdd:PRK08315 442 YVN 444
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
255-343 |
1.06e-12 |
|
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: 68.53 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLGP-AADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGD 333
Cdd:cd05912 220 YGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDgQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGD 299
|
90
....*....|
gi 2484101036 334 QVHIDGDGFV 343
Cdd:cd05912 300 IGYLDEEGFL 309
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
9-343 |
1.10e-12 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 68.93 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 9 SCAAGWFRDERVSrrldgvlryEDLEPCLAELLDRSALrhsarVAAVDRAGNA--LTYGQMWSSAARVAGGLLDQGVGPA 86
Cdd:PRK13295 15 SIAAGHWHDRTIN---------DDLDACVASCPDKTAV-----TAVRLGTGAPrrFTYRELAALVDRVAVGLARLGVGRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 87 DRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGA------------------------------VL 136
Cdd:PRK13295 81 DVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESkvlvvpktfrgfdhaamarrlrpelpalrhVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 137 TLDGELPDGVAFL----------DEGA-------APDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAE-- 197
Cdd:PRK13295 161 VVGGDGADSFEALlitpaweqepDAPAilarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADdv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 198 -----------------------GARTVL--------------TAPLSTAAGS---AVQLLPTLAAGGTVVA-------A 230
Cdd:PRK13295 241 ilmaspmahqtgfmyglmmpvmlGATAVLqdiwdparaaelirTEGVTFTMAStpfLTDLTRAVKESGRPVSslrtflcA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 231 GARGVRVPWRHLRASFpAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLGP-----AADQgVGELLCR 305
Cdd:PRK13295 321 GAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDAdgaplPAGQ-IGRLQVR 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 2484101036 306 GPSVARRYWNDPESTAeTFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK13295 399 GCSNFGGYLKRPQLNG-TDADGWFDTGDLARIDADGYI 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
45-343 |
1.32e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 68.37 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 45 ALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPE 124
Cdd:PRK06145 12 ARRTPDRAALVYR-DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 125 LEWIADDSGA-VLTLDGELPDGVAF------LDEGA--------------------APDELAVLYYVRKRGGGLHGVELT 177
Cdd:PRK06145 91 VAYILGDAGAkLLLVDEEFDAIVALetpkivIDAAAqadsrrlaqggleippqaavAPTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 178 NENILSTIEAVVHAMDLTAEgARTVLTAPLSTAAGSAVQLLPTLAAGG-----------TVVAAGAR------------- 233
Cdd:PRK06145 171 YGNLHWKSIDHVIALGLTAS-ERLLVVGPLYHVGAFDLPGIAVLWVGGtlrihrefdpeAVLAAIERhrltcawmapvml 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 234 -----------------------GVRVPWRHLRA---SFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGME 287
Cdd:PRK06145 250 srvltvpdrdrfdldslawciggGEKTPESRIRDftrVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVE 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 288 VALLG------PAADQGvgELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK06145 330 IRIADgagrwlPPNMKG--EICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGFL 389
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
278-342 |
2.77e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 67.29 E-value: 2.77e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 278 SVGVPFGGMEVAL---LGPAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:PRK03640 308 SAGKPLFPCELKIekdGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIGYLDEEGF 375
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
49-340 |
2.99e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 67.31 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 49 SARVAAVDRA-GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEW 127
Cdd:PLN02246 37 SDRPCLIDGAtGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 128 IADDSGA-----------------------VLTLDGElPDGVAFL------DEGA------APDELAVLYYVRKRGGGLH 172
Cdd:PLN02246 117 QAKASGAkliitqscyvdklkglaeddgvtVVTIDDP-PEGCLHFseltqaDENElpeveiSPDDVVALPYSSGTTGLPK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 173 GVELT---------------NENILSTIEAVV-------HAMDLTaegarTVLTAPLStaAGSAVQLLP----------- 219
Cdd:PLN02246 196 GVMLThkglvtsvaqqvdgeNPNLYFHSDDVIlcvlpmfHIYSLN-----SVLLCGLR--VGAAILIMPkfeigalleli 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 -----TLAA-GGTVVAAGARGVRVPWRHL---------------------RASFPAARCVRGWGVAETG---GIGLLLPT 269
Cdd:PLN02246 269 qrhkvTIAPfVPPIVLAIAKSPVVEKYDLssirmvlsgaaplgkeledafRAKLPNAVLGQGYGMTEAGpvlAMCLAFAK 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 270 DQRAAHPRSVGVPFGGMEVALLGPaaDQGV-------GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGD 340
Cdd:PLN02246 349 EPFPVKSGSCGTVVRNAELKIVDP--ETGAslprnqpGEICIRGPQIMKGYLNDPEATANTIDkDGWLHTGDIGYIDDD 425
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
54-340 |
3.04e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 68.06 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG 133
Cdd:PRK12316 2021 AVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG 2100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLTLDGE-------LPDGVAFLD----------------EGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEA--- 187
Cdd:PRK12316 2101 AALLLTQRhllerlpLPAGVARLPldrdaewadypdtapaVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAage 2180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 188 ---------VVHAMDLTAEGARTVLTAPLSTAA----------------------GSAVQLLP----------------- 219
Cdd:PRK12316 2181 ryelspadcELQFMSFSFDGAHEQWFHPLLNGArvlirddelwdpeqlydemerhGVTILDFPpvylqqlaehaerdgrp 2260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 ----TLAAGGTVVAAGarGVRVPWRHLRasfpAARCVRGWGVAETGGIGLLL---PTDQRAAHPRSVGVPFGGMEVALLG 292
Cdd:PRK12316 2261 pavrVYCFGGEAVPAA--SLRLAWEALR----PVYLFNGYGPTEAVVTPLLWkcrPQDPCGAAYVPIGRALGNRRAYILD 2334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2484101036 293 ----PAADQGVGELLCRGPSVARRYWNDPESTAETF-DDGWFHTGDQVHIDGD 340
Cdd:PRK12316 2335 adlnLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvPDPFSASGERLYRTGD 2387
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-344 |
4.32e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 66.15 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 268 PTDQRAahpRSVGVPFGGMEVALLGPAADQ----GV-GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:cd05917 168 SIEKRV---NTVGRIMPHTEAKIVDPEGGIvppvGVpGELCIRGYSVMKGYWNDPEKTAEAIDgDGWLHTGDLAVMDEDG 244
|
...
gi 2484101036 342 FVT 344
Cdd:cd05917 245 YCR 247
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
240-344 |
4.42e-12 |
|
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: 65.99 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 RHLRASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRSVGVPFGGMEVALLGPaadqgvGELLCRGPSVARRYWNDPES 319
Cdd:cd17638 133 RRMRSELGFETVLTAYGLTEAGVATMCRPGDDAETVATTCGRACPGFEVRIADD------GEVLVRGYNVMQGYLDDPEA 206
|
90 100
....*....|....*....|....*.
gi 2484101036 320 TAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:cd17638 207 TAEAIDaDGWLHTGDVGELDERGYLR 232
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
58-344 |
6.74e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.59 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 58 AGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLT 137
Cdd:PRK06060 27 AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 138 L-DGELPDGVA---------FLDEGA----------APDELAVLYYVRKRGGGLHGVELTNENILSTIEAVV-HAMDLT- 195
Cdd:PRK06060 107 VtSDALRDRFQpsrvaeaaeLMSEAArvapggyepmGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTp 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 196 ------------AEGARTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGAR-----GV-----RVPWRHLRASFPAARCVR 253
Cdd:PRK06060 187 edtglcsarmyfAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGpsvlyGVpnffaRVIDSCSPDSFRSLRCVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWG------VAET-----GGIGLL---------------LPTDQRAAHPRSVGVPFGGMEVALLGPAADQGV-GELLCRG 306
Cdd:PRK06060 267 SAGealelgLAERlmeffGGIPILdgigstevgqtfvsnRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVeGDLWVRG 346
|
330 340 350
....*....|....*....|....*....|....*...
gi 2484101036 307 PSVARRYWNDPESTAEtfDDGWFHTGDQVHIDGDGFVT 344
Cdd:PRK06060 347 PAIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVT 382
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
35-346 |
9.05e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 66.20 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 35 PCLAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFIC-MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 115 LPDPTCSDPELEWIADDSGA--------------------------------VLTLDG-----------------ELPDG 145
Cdd:PRK07059 102 NVNPLYTPRELEHQLKDSGAeaivvlenfattvqqvlaktavkhvvvasmgdLLGFKGhivnfvvrrvkkmvpawSLPGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 146 VAF---LDEGA---------APDELAVLYYVrkrgGGLHGVE----LTNENILSTieavVHAMDLTAEGAR--------- 200
Cdd:PRK07059 182 VRFndaLAEGArqtfkpvklGPDDVAFLQYT----GGTTGVSkgatLLHRNIVAN----VLQMEAWLQPAFekkprpdql 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 201 -TVLTAPLSTAAGSAVQLLPTLAAGGT-VVAAGARGV--------------------------------RVPWRHLRASF 246
Cdd:PRK07059 254 nFVCALPLYHIFALTVCGLLGMRTGGRnILIPNPRDIpgfikelkkyqvhifpavntlynallnnpdfdKLDFSKLIVAN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 247 --------PAAR-------C--VRGWGVAETGGIGLLLPTDQrAAHPRSVGVPFGGMEVALlgpAADQG-------VGEL 302
Cdd:PRK07059 334 gggmavqrPVAErwlemtgCpiTEGYGLSETSPVATCNPVDA-TEFSGTIGLPLPSTEVSI---RDDDGndlplgePGEI 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2484101036 303 LCRGPSVARRYWNDPESTAE-TFDDGWFHTGDQVHIDGDGFVTPV 346
Cdd:PRK07059 410 CIRGPQVMAGYWNRPDETAKvMTADGFFRTGDVGVMDERGYTKIV 454
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
255-341 |
9.48e-12 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 65.91 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAETGGIGLLLPTDQraAHPRSVGVPFGGMEVALlgpaadQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGD 333
Cdd:cd17641 355 YGQTELAGAYTVHRDGD--VDPDTVGVPFPGTEVRI------DEVGEILVRSPGVFVGYYKNPEATAEDFDeDGWLHTGD 426
|
....*...
gi 2484101036 334 QVHIDGDG 341
Cdd:cd17641 427 AGYFKENG 434
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
63-342 |
1.17e-11 |
|
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: 65.58 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 63 TYGQMWSSAARVAGGLLDQGVG-PADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG-AVLTLDG 140
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARiTVALCAH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 ELpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEA-VVHAMDLTaEGARTVLTAPLSTAAGSAVQLLP 219
Cdd:cd05958 92 AL----------TASDDICILAFTSGTTGAPKATMHFHRDPLASADRyAVNVLRLR-EDDRFVGSPPLAFTFGLGGVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 TLAAGGTVVAAGAR----------------------GVRVPWRHLRASFPAARCVR---------------GW----GVA 258
Cdd:cd05958 161 PFGVGASGVLLEEAtpdlllsaiarykptvlftaptAYRAMLAHPDAAGPDLSSLRkcvsagealpaalhrAWkeatGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 259 ETGGIG------LLLPTDQRAAHPRSVGVPFGGMEVALL----GPAADQGVGELLCRGPSVARryWNDPESTAETFDDGW 328
Cdd:cd05958 241 IIDGIGstemfhIFISARPGDARPGATGKPVPGYEAKVVddegNPVPDGTIGRLAVRGPTGCR--YLADKRQRTYVQGGW 318
|
330
....*....|....
gi 2484101036 329 FHTGDQVHIDGDGF 342
Cdd:cd05958 319 NITGDTYSRDPDGY 332
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
216-342 |
1.23e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 65.80 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 216 QLLPTLAAGGTVVAA-------GARGVRVPWRHLRASfpAARCVRGWGVAETGGIGLLLPTDQRAA---HPRSVGVPFGG 285
Cdd:PRK05857 273 KLVSELKSANATVPSlrlvgygGSRAIAADVRFIEAT--GVRTAQVYGLSETGCTALCLPTDDGSIvkiEAGAVGRPYPG 350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101036 286 MEVALL-----GPAADQGV-----GELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:PRK05857 351 VDVYLAatdgiGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGF 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-343 |
2.81e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 65.19 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 33 LEPCLAELLDRSALRhSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:PRK05691 2186 LDQTLHGLFAAQAAR-TPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 PVLPDPTCSDPELEWIADDSGAVLTLD--------GELPDGVA---FLDEGAA--------------PDELAVLYYVRKR 167
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLLSdralfealGELPAGVArwcLEDDAAAlaaysdaplpflslPQHQAYLIYTSGS 2344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 168 GGGLHGVELTNENILSTIEAVVHAMDLTAE------------------------GARTVLTAPLSTAAGSAVQL------ 217
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADdcelhfysinfdaaserllvpllcGARVVLRAQGQWGAEEICQLireqqv 2424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 218 --LPTLAAGGTVVAA--GARGVRVP---------------WRHLRASFPAARCVRGWGVAETggigLLLPTDQRAAHPRS 278
Cdd:PRK05691 2425 siLGFTPSYGSQLAQwlAGQGEQLPvrmcitggealtgehLQRIRQAFAPQLFFNAYGPTET----VVMPLACLAPEQLE 2500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 279 VG---VPFG---GMEVAL-----LGPAADQGVGELLCRGPSVARRYWNDPESTAETF-------DDG-WFHTGDQVHIDG 339
Cdd:PRK05691 2501 EGaasVPIGrvvGARVAYildadLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFvadpfaaDGGrLYRTGDLVRLRA 2580
|
....
gi 2484101036 340 DGFV 343
Cdd:PRK05691 2581 DGLV 2584
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-343 |
5.48e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.03 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 33 LEPCLAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:PRK12467 3093 SERLVHQLIEAQVARTPEAPALV-FGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGA 3171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 PVLPDPTCSDPELEWIADDSGA--------------------VLTLDGELPDGVA--FLDEGAAPDELAVLYYVRKRGGG 170
Cdd:PRK12467 3172 YVPLDPEYPRERLAYMIEDSGVkllltqahlleqlpapagdtALTLDRLDLNGYSenNPSTRVMGENLAYVIYTSGSTGK 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 171 LHGVELTNENILSTIEAVVHAMDLTAeGARTVLTAPLSTaAGSAVQLLPTLAAGGTVVAAGARgVRVPWRH--------- 241
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYELDA-NDRVLLFMSFSF-DGAQERFLWTLICGGCLVVRDND-LWDPEELwqaihahri 3328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 242 ------------------------------------------LRASFPAARCVRGWGVAETGGIGLLLPTDQRAAHPRS- 278
Cdd:PRK12467 3329 siacfppaylqqfaedaggadcasldiyvfggeavppaafeqVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPy 3408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 279 --VGVPFGGMEVALL----GPAADQGVGELLCRGPSVARRYWNDPESTAETF------DDG--WFHTGDQVHIDGDGFV 343
Cdd:PRK12467 3409 apIGRPVAGRSIYVLdgqlNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFvadpfsGSGgrLYRTGDLARYRADGVI 3487
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
35-343 |
8.96e-11 |
|
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: 62.91 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 35 PCLAELLDRSALRHSARVAAVD-RAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVP 113
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 114 VLPDPTCSDPEL---------------------EWIADDSGAVLTLDGELPDGVA------FLDEGAAPDELAVLYYVRK 166
Cdd:cd05923 81 ALINPRLKAAELaeliergemtaaviavdaqvmDAIFQSGVRVLALSDLVGLGEPesagplIEDPPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 167 RGGGLHGVELTNENILSTIEAVVH-AMDLTAEGARTVLTAPLSTAAGSAVQLLPTLAAGGT--VVAAGARGVRVPW---- 239
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTqAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTyvVVEEFDPADALKLieqe 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 -----------------------------RHLR---ASFPAA------RCVRGWGVAETGGIGLLLPTDQRAAHPRSVG- 280
Cdd:cd05923 241 rvtslfatpthldalaaaaefaglklsslRHVTfagATMPDAvlervnQHLPGEKVNIYGTTEAMNSLYMRDARTGTEMr 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 281 ---------VPFGGMEVALLGPAADqgvGELLCRGPSVA--RRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:cd05923 321 pgffsevriVRIGGSPDEALANGEE---GELIVAAAADAafTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDV 391
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
252-343 |
1.64e-10 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 62.20 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAETGGIGLLLPTDQRAaHPRSVGVPFGGMEVAL---LGPAADQG-VGELLCRGPSVARRYWNDPESTAETFD-D 326
Cdd:PRK08751 358 VEAYGLTETSPAACINPLTLKE-YNGSIGLPIPSTDACIkddAGTVLAIGeIGELCIKGPQVMKGYWKRPEETAKVMDaD 436
|
90
....*....|....*..
gi 2484101036 327 GWFHTGDQVHIDGDGFV 343
Cdd:PRK08751 437 GWLHTGDIARMDEQGFV 453
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
254-342 |
2.30e-10 |
|
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: 61.36 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIgLLLPTDQRAAHPRSVGVPFGGMEVAL----LGPAADQGVGELLCRG--PSVARRYWNDPESTAETFDDG 327
Cdd:cd05969 238 TWWQTETGSI-MIANYPCMPIKPGSMGKPLPGVKAAVvdenGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDG 316
|
90
....*....|....*
gi 2484101036 328 WFHTGDQVHIDGDGF 342
Cdd:cd05969 317 WYLTGDLAYRDEDGY 331
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
252-341 |
2.68e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 61.53 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAET---GGIglllptdQRAA--HPRSVGVPFGGMEVALLG-----------PAadqgvGELLCRGPSVARRYWN 315
Cdd:PTZ00216 456 IQGWGLTETvccGGI-------QRTGdlEPNAVGQLLKGVEMKLLDteeykhtdtpePR-----GEILLRGPFLFKGYYK 523
|
90 100
....*....|....*....|....*..
gi 2484101036 316 DPESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:PTZ00216 524 QEELTREVLDeDGWFHTGDVGSIAANG 550
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
54-341 |
3.23e-10 |
|
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: 61.11 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG 133
Cdd:cd17652 5 AVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLTLdgelpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAeGARTVLTAPLSTAAgS 213
Cdd:cd17652 85 PALLL--------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGP-GSRVLQFASPSFDA-S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 214 AVQLLPTLAAGGTVVAAGaRGVRVPWRHLRASF-----------PAA--------------------------------- 249
Cdd:cd17652 149 VWELLMALLAGATLVLAP-AEELLPGEPLADLLrehrithvtlpPAAlaalppddlpdlrtlvvageacpaelvdrwapg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 -RCVRGWGVAETgGIGLLLPTDQRAAHPRSVGVPFGGMEVALLG----PAADQGVGELLCRGPSVARRYWNDPESTAETF 324
Cdd:cd17652 228 rRMINAYGPTET-TVCATMAGPLPGGGVPPIGRPVPGTRVYVLDarlrPVPPGVPGELYIAGAGLARGYLNRPGLTAERF 306
|
330 340
....*....|....*....|....*
gi 2484101036 325 ------DDG--WFHTGDQVHIDGDG 341
Cdd:cd17652 307 vadpfgAPGsrMYRTGDLARWRADG 331
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
32-343 |
3.85e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.72 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 32 DLEPCLAELLDRSAlRHSARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG 111
Cdd:PRK12467 1571 PLARLVHQLIEDQA-AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGG 1649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 112 VPVLPDPTCSDPELEWIADDSGAVLTLDGE-------LPDGVA--FLDEG---------------AAPDELAVLYYVRKR 167
Cdd:PRK12467 1650 AYVPLDPEYPRERLAYMIEDSGIELLLTQShlqarlpLPDGLRslVLDQEddwlegysdsnpavnLAPQNLAYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 168 GGGLHGVELTNENILSTIEAVVHAMDLTAE------------------------GARTVLTAPlsTAAGSAVQLLPTLAA 223
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAAdvvlqftsfafdvsvwelfwplinGARLVIAPP--GAHRDPEQLIQLIER 1807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 224 GGTVVA-----------------AGARGVRV-----------PWRHLRASFPAARCVRGWGVAETGGIGLLLPTDQ---- 271
Cdd:PRK12467 1808 QQVTTLhfvpsmlqqllqmdeqvEHPLSLRRvvcggealeveALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRkdle 1887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 272 -RAAHPrsVGVPFGGMEV----ALLGPAADQGVGELLCRGPSVARRYWNDPESTAETF--------DDGWFHTGDQVHID 338
Cdd:PRK12467 1888 gRDSVP--IGQPIANLSTyildASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtvGSRLYRTGDLARYR 1965
|
....*
gi 2484101036 339 GDGFV 343
Cdd:PRK12467 1966 ADGVI 1970
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
34-341 |
5.27e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 60.53 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 34 EPCLAELLDRSALRHSARVAAVDRAGnALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLG-------- 105
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDR-PLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAcarlgatv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 106 -----------------------VVLAGG------VPVLPD-PTCSDPELEWIA--DDSGA----------VLTLDGELP 143
Cdd:PRK06164 88 iavntryrshevahilgrgrarwLVVWPGfkgidfAAILAAvPPDALPPLRAIAvvDDAADatpapapgarVQLFALPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 144 DGVAFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENIL---STIEAVVHAMDltaEGARTVLTAPLSTAAGSAVqLLPT 220
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLlrhARAIARAYGYD---PGAVLLAALPFCGVFGFST-LLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 221 LAAGGTVV-------AAGAR------------------------GVRVPWRHLR----ASF-PAARCVRGW----GVAET 260
Cdd:PRK06164 244 LAGGAPLVcepvfdaARTARalrrhrvthtfgndemlrrildtaGERADFPSARlfgfASFaPALGELAALararGVPLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 261 GGIG----LLLPTDQRAAHPRSVGVPFGGM------EVALLGP-----AADQGVGELLCRGPSVARRYWNDPESTAETF- 324
Cdd:PRK06164 324 GLYGssevQALVALQPATDPVSVRIEGGGRpaspeaRVRARDPqdgalLPDGESGEIEIRAPSLMRGYLDNPDATARALt 403
|
410
....*....|....*..
gi 2484101036 325 DDGWFHTGDQVHIDGDG 341
Cdd:PRK06164 404 DDGYFRTGDLGYTRGDG 420
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-343 |
7.47e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 60.16 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIGLLLPTDqrAAHPRSVGVPFGGMEVALLGPAADQ----GVGELLCRGPSVARRYWNDPESTAETFD-DGW 328
Cdd:PRK05677 357 GYGMTETSPVVSVNPSQ--AIQVGTIGIPVPSTLCKVIDDDGNElplgEVGELCVKGPQVMKGYWQRPEATDEILDsDGW 434
|
90
....*....|....*
gi 2484101036 329 FHTGDQVHIDGDGFV 343
Cdd:PRK05677 435 LKTGDIALIQEDGYM 449
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
44-343 |
9.15e-10 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 59.86 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 44 SALRHSARVAAVDRA-GNALTYGQMWSSAARVAGGLLDQ-GVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCS 121
Cdd:PLN02574 48 SHHNHNGDTALIDSStGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 122 DPEL-EWIADDSGAVLTLDGE--------------LPDGVAFlDEGA------------------AP----DELAVLYYV 164
Cdd:PLN02574 128 LGEIkKRVVDCSVGLAFTSPEnveklsplgvpvigVPENYDF-DSKRiefpkfyelikedfdfvpKPvikqDDVAAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 165 RKRGGGLHGVELTNENILSTIEAVV--HAMDLTAEGARTVLTA--PLSTAAGSAVQLLPTLAAGGTVVAA----GARGVR 236
Cdd:PLN02574 207 SGTTGASKGVVLTHRNLIAMVELFVrfEASQYEYPGSDNVYLAalPMFHIYGLSLFVVGLLSLGSTIVVMrrfdASDMVK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 VPWRHLRASFP----------------AARC-------------------------------VRGWGVAETGGIGLLLPT 269
Cdd:PLN02574 287 VIDRFKVTHFPvvppilmaltkkakgvCGEVlkslkqvscgaaplsgkfiqdfvqtlphvdfIQGYGMTESTAVGTRGFN 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 270 DQRAAHPRSVGVPFGGMEV--------ALLGPAadqGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGD 340
Cdd:PLN02574 367 TEKLSKYSSVGLLAPNMQAkvvdwstgCLLPPG---NCGELWIQGPGVMKGYLNNPKATQSTIDkDGWLRTGDIAYFDED 443
|
...
gi 2484101036 341 GFV 343
Cdd:PLN02574 444 GYL 446
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
37-341 |
9.89e-10 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 59.61 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDRA-GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL 115
Cdd:PLN02330 30 LPDFVLQDAELYADKVAFVEAVtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 116 PDPTCSDPELEWIADDSGAVLTLDG----------ELP----------DGVAFLDEGAAPD--------------ELAVL 161
Cdd:PLN02330 110 ANPTALESEIKKQAEAAGAKLIVTNdtnygkvkglGLPvivlgeekieGAVNWKELLEAADragdtsdneeilqtDLCAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 162 YYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVL-TAPLSTAAGSAVQLLPTLAAGGTVVAAGARGVR---- 236
Cdd:PLN02330 190 PFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMIGQVVTLgLIPFFHIYGITGICCATLRNKGKVVVMSRFELRtfln 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 237 ------------VP------------------------------------WRHLRASFPAARCVRGWGVAETGGIGLLLP 268
Cdd:PLN02330 270 alitqevsfapiVPpiilnlvknpiveefdlsklklqaimtaaaplapelLTAFEAKFPGVQVQEAYGLTEHSCITLTHG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 269 TDQRA---AHPRSVGVPFGGMEVALLGPAADQGV-----GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDG 339
Cdd:PLN02330 350 DPEKGhgiAKKNSVGFILPNLEVKFIDPDTGRSLpkntpGELCVRSQCVMQGYYNNKEETDRTIDeDGWLHTGDIGYIDD 429
|
..
gi 2484101036 340 DG 341
Cdd:PLN02330 430 DG 431
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
246-342 |
1.00e-09 |
|
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: 59.20 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 246 FPAARCVRGWGVAETGGIgLLLPTDQRAAHPRSVGVPFGGMEVALL----GPAADQGVGELLCRGPSVARRYWNDPESTA 321
Cdd:cd17635 140 TGLTNTAQVYGLSETGTA-LCLPTDDDSIEINAVGRPYPGVDVYLAatdgIAGPSASFGTIWIKSPANMLGYWNNPERTA 218
|
90 100
....*....|....*....|.
gi 2484101036 322 ETFDDGWFHTGDQVHIDGDGF 342
Cdd:cd17635 219 EVLIDGWVNTGDLGERREDGF 239
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
254-344 |
1.13e-09 |
|
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: 59.40 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIGLL-LPTDQRAAhprSVGVPFGGMEVALlgpaADQGvgELLCRGPSVARRYWNDPESTAETF-DDGWFHT 331
Cdd:cd05932 305 AYGMTENFAYSHLnYPGRDKIG---TVGNAGPGVEVRI----SEDG--EILVRSPALMMGYYKDPEATAEAFtADGFLRT 375
|
90
....*....|...
gi 2484101036 332 GDQVHIDGDGFVT 344
Cdd:cd05932 376 GDKGELDADGNLT 388
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
32-341 |
1.78e-09 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 58.74 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 32 DLEPCLAELLDRSALRH---SARVAAVDRAgnALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVL 108
Cdd:PRK05852 13 DFGPRIADLVEVAATRLpeaPALVVTADRI--AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 109 AGGVPVLPDPTCSDPELEWIADDSGAVLTLDGEL---------------------------------------PDGVAFL 149
Cdd:PRK05852 91 ADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADgphdraepttrwwpltvnvggdsgpsggtlsvhldaatePTPATST 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 150 DEGAAPDELAVLYYvrkrgGGLHG----VELTNENILSTIEAVVHAMDLTAEGArTVLTAPLSTAAGSAVQLLPTLAAGG 225
Cdd:PRK05852 171 PEGLRPDDAMIMFT-----GGTTGlpkmVPWTHANIASSVRAIITGYRLSPRDA-TVAVMPLYHGHGLIAALLATLASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 226 TVV-----------------AAGA----------------------RGVRVPWRHLRA-SFP-------------AARCV 252
Cdd:PRK05852 245 AVLlpargrfsahtfwddikAVGAtwytavptihqilleraatepsGRKPAALRFIRScSAPltaetaqalqtefAAPVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 253 RGWGVAE------TGGIGLLLPTDQRAAHPRSVGVPfGGMEVALLGPAADQ----GVGELLCRGPSVARRYWNDPESTAE 322
Cdd:PRK05852 325 CAFGMTEathqvtTTQIEGIGQTENPVVSTGLVGRS-TGAQIRIVGSDGLPlpagAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410
....*....|....*....
gi 2484101036 323 TFDDGWFHTGDQVHIDGDG 341
Cdd:PRK05852 404 NFTDGWLRTGDLGSLSAAG 422
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
37-344 |
2.26e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 58.62 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVDrAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF-GGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 117 DPTCSDPELEWIADDSGA-VLTLDGELPDGVAFLDEGAAP---------------------------------------D 156
Cdd:PRK06155 102 NTALRGPQLEHILRNSGArLLVVEAALLAALEAADPGDLPlpavwlldapasvsvpagwstaplppldapapaaavqpgD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 157 ELAVLYYVRKRGG--------------GLHGVE---LTNENILSTIEAVVHAMDLTA------EGARTVLTAPLST---- 209
Cdd:PRK06155 182 TAAILYTSGTTGPskgvccphaqfywwGRNSAEdleIGADDVLYTTLPLFHTNALNAffqallAGATYVLEPRFSAsgfw 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 210 ----AAGSAV-----QLLPTLAAGGTVVAAGARGVRVPW-----RHLRASFpAARC----VRGWGVAETGGIGLLLPTDQ 271
Cdd:PRK06155 262 pavrRHGATVtyllgAMVSILLSQPARESDRAHRVRVALgpgvpAALHAAF-RERFgvdlLDGYGSTETNFVIAVTHGSQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 272 RaahPRSVGVPFGGMEVALLG----PAADQGVGELLCRGP---SVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:PRK06155 341 R---PGSMGRLAPGFEARVVDehdqELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFR 417
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
278-343 |
2.45e-09 |
|
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: 58.52 E-value: 2.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101036 278 SVGVPFGGMEVALLGPAADqGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFV 343
Cdd:cd05933 372 SCGKALPGCKTKIHNPDAD-GIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFL 437
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
20-335 |
3.73e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 57.97 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 20 VSRRLDGVLR------YEDLEPCLAELLDRSALRHSARVAAVDRAGNA----LTYGQMWSSAARVAGGLLDQGVGPADRV 89
Cdd:PRK08180 18 VERRADGTIYlrsaepLGDYPRRLTDRLVHWAQEAPDRVFLAERGADGgwrrLTYAEALERVRAIAQALLDRGLSAERPL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 90 VVHYPNGFRWLYAFLGVVLAGgVPVLPdptcSDPELEWIADDSGAVLTLDGELPDGVAFLDEGAA---------PDELAV 160
Cdd:PRK08180 98 MILSGNSIEHALLALAAMYAG-VPYAP----VSPAYSLVSQDFGKLRHVLELLTPGLVFADDGAAfaralaavvPADVEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 161 LYYVRKRGGGLHgveLTNENILSTIE--AVVHAMDLTAEG--ARTVLTAPlSTAAGSAV---------------QLLP-- 219
Cdd:PRK08180 173 VAVRGAVPGRAA---TPFAALLATPPtaAVDAAHAAVGPDtiAKFLFTSG-STGLPKAVinthrmlcanqqmlaQTFPfl 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 -------------------------TLAAGGTV-------VAAG-ARGVR------------VP--WRHLR--------- 243
Cdd:PRK08180 249 aeeppvlvdwlpwnhtfggnhnlgiVLYNGGTLyiddgkpTPGGfDETLRnlreisptvyfnVPkgWEMLVpalerdaal 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 244 ---------------ASFPAA-----------------RCVRGWGVAETGGIGLLlpTDQRAAHPRSVGVPFGGMEVALL 291
Cdd:PRK08180 329 rrrffsrlkllfyagAALSQDvwdrldrvaeatcgeriRMMTGLGMTETAPSATF--TTGPLSRAGNIGLPAPGCEVKLV 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2484101036 292 gPAADQGvgELLCRGPSVARRYWNDPESTAETFDD-GWFHTGDQV 335
Cdd:PRK08180 407 -PVGGKL--EVRVKGPNVTPGYWRAPELTAEAFDEeGYYRSGDAV 448
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
267-343 |
4.29e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.65 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 267 LPTDQRAAHPRSVGVPFGGME-VALLGPAADQGV-------GELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHID 338
Cdd:PRK08162 348 LPLDERAQLKARQGVRYPLQEgVTVLDPDTMQPVpadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLH 427
|
....*
gi 2484101036 339 GDGFV 343
Cdd:PRK08162 428 PDGYI 432
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
61-343 |
1.42e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 56.25 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 61 ALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGA-VLT-- 137
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGArVLIah 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 138 ------LDGELPDGVAFLdEGAAPDELAVLY--------------------------------------YVRKRGGGLHG 173
Cdd:PRK12406 91 adllhgLASALPAGVTVL-SVPTPPEIAAAYrispalltppagaidwegwlaqqepydgppvpqpqsmiYTSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 174 VEL---TNENILSTIEAVVHAMDLTaEGARTVLTAPLSTAA-----------GSAVQLLPTLAAGGT------------- 226
Cdd:PRK12406 170 VRRaapTPEQAAAAEQMRALIYGLK-PGIRALLTGPLYHSApnayglragrlGGVLVLQPRFDPEELlqlierhrithmh 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 227 -VVAAGARGVRVPwRHLRASF----------PAARCVRG----------------WGVAETGGIGLLLPtDQRAAHPRSV 279
Cdd:PRK12406 249 mVPTMFIRLLKLP-EEVRAKYdvsslrhvihAAAPCPADvkramiewwgpviyeyYGSTESGAVTFATS-EDALSHPGTV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 280 GVPFGGMEVALLG----PAADQGVGELLCRGPSVAR-RYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK12406 327 GKAAPGAELRFVDedgrPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEIDRGGFITSGDVGYLDADGYL 395
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
243-341 |
1.89e-08 |
|
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: 55.61 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 RASFPAARcvRGWGVAETGGIGLLLP-TDQRaahPRSVG--VPFGGMEVALLGPAADQGV---GELLCRGPSVARRYWND 316
Cdd:cd17642 324 RFKLPGIR--QGYGLTETTSAILITPeGDDK---PGAVGkvVPFFYAKVVDLDTGKTLGPnerGELCVKGPMIMKGYVNN 398
|
90 100
....*....|....*....|....*.
gi 2484101036 317 PESTAETFD-DGWFHTGDQVHIDGDG 341
Cdd:cd17642 399 PEATKALIDkDGWLHSGDIAYYDEDG 424
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
271-344 |
3.72e-08 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 55.32 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 271 QRAAHPRSVGVPFGGMEVALLGPAADQ--GVGE---LLCRGPSVARRYWNDPESTAETFDD----GWFHTGDQVHIDGDG 341
Cdd:PRK08633 954 QTGSKEGSVGMPLPGVAVRIVDPETFEelPPGEdglILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDG 1033
|
...
gi 2484101036 342 FVT 344
Cdd:PRK08633 1034 FLT 1036
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
255-342 |
6.51e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 54.13 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAETGGIgLLLPTDQRAAHPRSVGVPFGGMEVALLGPAADQG----VGEL-LCRG-PSVARRYWNDPESTAETFDDGW 328
Cdd:PRK04319 355 WWMTETGGI-MIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELppnrMGNLaIKKGwPSMMRGIWNNPEKYESYFAGDW 433
|
90
....*....|....
gi 2484101036 329 FHTGDQVHIDGDGF 342
Cdd:PRK04319 434 YVSGDSAYMDEDGY 447
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
57-114 |
7.69e-08 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 53.89 E-value: 7.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 57 RAGNALTYGQMWSSAARVAGGLLDQ-GVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:cd05905 10 KEATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPI 68
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
247-345 |
9.29e-08 |
|
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: 53.07 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 247 PAARCVRGWGVAETGGIGLLLPTDQRAAHprSVGVPFGGMEVALLGPA----ADQGVGELLCRGPSVARRYWNDPESTAE 322
Cdd:cd17636 135 PWGRKPGGYGQTEVMGLATFAALGGGAIG--GAGRPSPLVQVRILDEDgrevPDGEVGEIVARGPTVMAGYWNRPEVNAR 212
|
90 100
....*....|....*....|....*.
gi 2484101036 323 TFDDGWFHTGDQVHIDGDG---FVTP 345
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGslsFVGP 238
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
280-344 |
1.35e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 1.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 280 GVPFGGMEVALLGPA----ADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVH-IDGDGFVT 344
Cdd:PRK09192 388 GKALPGHEIEIRNEAgmplPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYlLDGYLYIT 457
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
267-343 |
1.72e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 52.92 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 267 LPTDQRAAHPRSVGVPFGGME--------VALLGPAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHID 338
Cdd:PLN02479 362 LPPEEQARLNARQGVRYIGLEgldvvdtkTMKPVPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKH 441
|
....*
gi 2484101036 339 GDGFV 343
Cdd:PLN02479 442 PDGYI 446
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
16-333 |
2.17e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 52.36 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 16 RDERVSRRLDGVLRY------EDLEPCLAELLDRSALRHSARVAAVDRAGNA-----LTYGQMWSSAARVAGGLLDQGVG 84
Cdd:PRK12582 24 PDISVERRADGSIVIksrhplGPYPRSIPHLLAKWAAEAPDRPWLAQREPGHgqwrkVTYGEAKRAVDALAQALLDLGLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 85 PADRVVVHYPNGFRWLYAFLGVVLAgGVPVLPdptcSDPELEWIADDSGAVLTLDGELPDGVAFLDEGAAPDE-LAVLyy 163
Cdd:PRK12582 104 PGRPVMILSGNSIEHALMTLAAMQA-GVPAAP----VSPAYSLMSHDHAKLKHLFDLVKPRVVFAQSGAPFARaLAAL-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 164 vrkrggGLHGVELTNENILSTIEAVVHAMDLTAegartvlTAPLSTAAGSAVQLLPTLAA------GGT----------- 226
Cdd:PRK12582 177 ------DLLDVTVVHVTGPGEGIASIAFADLAA-------TPPTAAVAAAIAAITPDTVAkylftsGSTgmpkavintqr 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 227 ---VVAAGARGVR--------------VPWRH------------------------------------------------ 241
Cdd:PRK12582 244 mmcANIAMQEQLRprepdppppvsldwMPWNHtmggnanfngllwgggtlyiddgkplpgmfeetirnlreisptvygnv 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 242 ----------------LRASF---------------------PAARCVR----------GWGVAETGGI--GLLLPTDQr 272
Cdd:PRK12582 324 pagyamlaeamekddaLRRSFfknlrlmayggatlsddlyerMQALAVRttghripfytGYGATETAPTttGTHWDTER- 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 273 aahPRSVGVPFGGMEVALLgPAADQgvGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGD 333
Cdd:PRK12582 403 ---VGLIGLPLPGVELKLA-PVGDK--YEVRVKGPNVTPGYHKDPELTAAAFDeEGFYRLGD 458
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
255-344 |
2.68e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 52.06 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAETGGIGLL---------LPTDQRAAHPRSVGVPFGGMEVALLGPAAD------QGVGELLCRGPSVARRYWndpES 319
Cdd:PRK06018 325 WGMTEMSPLGTLaalkppfskLPGDARLDVLQKQGYPPFGVEMKITDDAGKelpwdgKTFGRLKVRGPAVAAAYY---RV 401
|
90 100
....*....|....*....|....*.
gi 2484101036 320 TAETFD-DGWFHTGDQVHIDGDGFVT 344
Cdd:PRK06018 402 DGEILDdDGFFDTGDVATIDAYGYMR 427
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
12-114 |
3.07e-07 |
|
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: 52.11 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 12 AGWFRDERVSrrldgvLRYEDLEPCLAELLDRSALRHSARvaavDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVV 91
Cdd:cd05968 52 AAWFVGGRMN------IVEQLLDKWLADTRTRPALRWEGE----DGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGI 121
|
90 100
....*....|....*....|...
gi 2484101036 92 HYPNGFRWLYAFLGVVLAGGVPV 114
Cdd:cd05968 122 YLPMIPEIVPAFLAVARIGGIVV 144
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
250-342 |
3.82e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 51.63 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 RCVRGWGVAETGGIGLL---------LPTDQRAAHPRSVGVPFGGMEVALLGPAADQ----GV--GELLCRGPSVARRYW 314
Cdd:PRK07008 320 EVIHAWGMTEMSPLGTLcklkwkhsqLPLDEQRKLLEKQGRVIYGVDMKIVGDDGRElpwdGKafGDLQVRGPWVIDRYF 399
|
90 100
....*....|....*....|....*...
gi 2484101036 315 ndpESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:PRK07008 400 ---RGDASPLVDGWFPTGDVATIDADGF 424
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
255-342 |
3.84e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 51.61 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 255 WGVAET--GGIGLLlPTDQRaaHPRSVGVPFGGMEVALL---GPAADQG-VGELLCRG---PSVARRYWNDPESTAETFD 325
Cdd:PRK08008 319 YGMTETivGIIGDR-PGDKR--RWPSIGRPGFCYEAEIRddhNRPLPAGeIGEICIKGvpgKTIFKEYYLDPKATAKVLE 395
|
90
....*....|....*...
gi 2484101036 326 -DGWFHTGDQVHIDGDGF 342
Cdd:PRK08008 396 aDGWLHTGDTGYVDEEGF 413
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
252-343 |
5.13e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 51.35 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAET-GGIGLLLPTDQRAAHprSVGVPFGGMEVAL-----LG--PAADQGVGELLCRGPSVARRYWNDPESTAET 323
Cdd:PLN02430 412 VQGYGLTETlGPTTLGFPDEMCMLG--TVGAPAVYNELRLeevpeMGydPLGEPPRGEICVRGKCLFSGYYKNPELTEEV 489
|
90 100
....*....|....*....|
gi 2484101036 324 FDDGWFHTGDQVHIDGDGFV 343
Cdd:PLN02430 490 MKDGWFHTGDIGEILPNGVL 509
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
42-147 |
6.42e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 51.04 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 42 DRSALRHSARVaavdragnaLTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCS 121
Cdd:PRK07798 18 DRVALVCGDRR---------LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100
....*....|....*....|....*..
gi 2484101036 122 DPELEWIADDSGAV-LTLDGELPDGVA 147
Cdd:PRK07798 89 EDELRYLLDDSDAVaLVYEREFAPRVA 115
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-138 |
6.69e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 51.32 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 37 LAELLDRSALRHSARVAAVdRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLP 116
Cdd:PRK05691 1133 LPELLNEQARQTPERIALV-WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100
....*....|....*....|..
gi 2484101036 117 DPTCSDPELEWIADDSGAVLTL 138
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELLL 1233
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
295-343 |
7.04e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 50.83 E-value: 7.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2484101036 295 ADQGVGELL-CRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK07867 348 ADEAIGELVnTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYA 397
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
62-342 |
7.28e-07 |
|
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: 50.41 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVpVLPDPTCSDPE-LEWIADDSGAVLTLDG 140
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAV-YVPLTTLLGPKdIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 ElpdgvafldegaapDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLT-------------AEGARTVLTAPL 207
Cdd:cd05972 80 A--------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRpddihwniadpgwAKGAWSSFFGPW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 208 STAAGSAVQLLPTLAAGGTVVAAGARGVRV------PWRHLRASFPAAR-------CV---------------------- 252
Cdd:cd05972 146 LLGATVFVYEGPRFDAERILELLERYGVTSfcgpptAYRMLIKQDLSSYkfshlrlVVsageplnpeviewwraatglpi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 253 -RGWGVAETGG-IGLLLPTDqraAHPRSVGVPFGGMEVALLG------PAADQGVGELLCRGPSVARRYWNDPESTAETF 324
Cdd:cd05972 226 rDGYGQTETGLtVGNFPDMP---VKPGSMGRPTPGYDVAIIDddgrelPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASI 302
|
330
....*....|....*...
gi 2484101036 325 DDGWFHTGDQVHIDGDGF 342
Cdd:cd05972 303 RGDYYLTGDRAYRDEDGY 320
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
243-344 |
7.35e-07 |
|
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: 50.41 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 243 RASFPAARCVRGWGVAETGGIGLLLPTDQRAAhpRSVGVPFGGMEVALLGPaadqgvGELLCRGPSVARRYWNdPESTAE 322
Cdd:cd17630 130 RAADRGIPLYTTYGMTETASQVATKRPDGFGR--GGVGVLLPGRELRIVED------GEIWVGGASLAMGYLR-GQLVPE 200
|
90 100
....*....|....*....|..
gi 2484101036 323 TFDDGWFHTGDQVHIDGDGFVT 344
Cdd:cd17630 201 FNEDGWFTTKDLGELHADGRLT 222
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
248-343 |
7.71e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.80 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 248 AARCVRGWGVAETGGIGLLLPtdqrAAHPRSVGVPFGGME-----------VALLGPA-----ADQGVGELL-CRGPSVA 310
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREP----GTPPGSIGRGAPGVAiynpetltecaVARFDAHgallnADEAIGELVnTAGAGFF 363
|
90 100 110
....*....|....*....|....*....|...
gi 2484101036 311 RRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PRK13388 364 EGYYNNPEATAERMRHGMYWSGDLAYRDADGWI 396
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
51-342 |
1.41e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 49.90 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIAD 130
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 131 DSGA------------VLTLDGELPDGVAFL--DEGAAP----------DELAVLYYVRKRGGGLH----------GV-- 174
Cdd:PRK08276 81 DSGAkvlivsaaladtAAELAAELPAGVPLLlvVAGPVPgfrsyeealaAQPDTPIADETAGADMLyssgttgrpkGIkr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 175 ELTN----ENILSTIEAVVHAMDLTAeGARTVLTAPLSTAA----GSAVQLLptlaaGGTVV------AAGA-------- 232
Cdd:PRK08276 161 PLPGldpdEAPGMMLALLGFGMYGGP-DSVYLSPAPLYHTAplrfGMSALAL-----GGTVVvmekfdAEEAlalieryr 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 233 ------------RGVRVPwRHLRASF----------PAARC--------VRGWG------VAETGGIGL-LLPTDQRAAH 275
Cdd:PRK08276 235 vthsqlvptmfvRMLKLP-EEVRARYdvsslrvaihAAAPCpvevkramIDWWGpiiheyYASSEGGGVtVITSEDWLAH 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2484101036 276 PRSVGVPFGGmEVALLGPAADQ----GVGELLCRGPSVARRYWNDPESTAETF-DDGWFHTGDQVHIDGDGF 342
Cdd:PRK08276 314 PGSVGKAVLG-EVRILDEDGNElppgEIGTVYFEMDGYPFEYHNDPEKTAAARnPHGWVTVGDVGYLDEDGY 384
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
274-342 |
1.47e-06 |
|
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: 49.80 E-value: 1.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 274 AHPRSVGVPFGGMEVALL---GPAADQG-VGELLCR---GPSVA--RRYWNDPESTAETFDDGWFHTGDQVHIDGDGF 342
Cdd:cd05970 350 PKPGSMGKPAPGYEIDLIdreGRSCEAGeEGEIVIRtskGKPVGlfGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGY 427
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
240-344 |
2.09e-06 |
|
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: 48.94 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 RHLRASFPAARCVRGWGVAETGGIGLLLPtdQRAAHPRSVGVPFGGMEVALLGpAADQGVGELLCRGPSVARRYWNDPES 319
Cdd:cd17633 128 KKLKNIFPKANLIEFYGTSELSFITYNFN--QESRPPNSVGRPFPNVEIEIRN-ADGGEIGKIFVKSEMVFSGYVRGGFS 204
|
90 100
....*....|....*....|....*
gi 2484101036 320 TAetfdDGWFHTGDQVHIDGDGFVT 344
Cdd:cd17633 205 NP----DGWMSVGDIGYVDEEGYLY 225
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
54-340 |
2.31e-06 |
|
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: 49.00 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSG 133
Cdd:cd17650 5 AVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 134 AVLTLdgelpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVLTAPLSTAAgS 213
Cdd:cd17650 85 AKLLL--------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDV-F 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 214 AVQLLPTLAAGGTVV----------------------------AAGARGV--RVPWRHLRASF----------------- 246
Cdd:cd17650 150 AGDFARSLLNGGTLVicpdevkldpaalydlilksritlmestPALIRPVmaYVYRNGLDLSAmrllivgsdgckaqdfk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 247 -------PAARCVRGWGVAETGGIGLLLPTDqRAAHPRS----VGVPFGGMEVALLGPAAD---QGV-GELLCRGPSVAR 311
Cdd:cd17650 230 tlaarfgQGMRIINSYGVTEATIDSTYYEEG-RDPLGDSanvpIGRPLPNTAMYVLDERLQpqpVGVaGELYIGGAGVAR 308
|
330 340
....*....|....*....|....*....
gi 2484101036 312 RYWNDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:cd17650 309 GYLNRPELTAERFVENPFAPGERMYRTGD 337
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
63-343 |
2.43e-06 |
|
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: 48.97 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 63 TYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVlPDPTCSDPE-LEW-IADDSGAVLTLDG 140
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAV-PLFALFGPEaLEYrLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 elpdgvafldegaaPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEGARTVLT-APLSTAAGSAVQLLP 219
Cdd:cd05971 87 --------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTpADWAWIGGLLDVLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 TLAAGGTVVAAGAR--------------GVRV--------------------PWRHLRASF----PAARCVRGWG----- 256
Cdd:cd05971 153 SLYFGVPVLAHRMTkfdpkaaldlmsryGVTTaflpptalkmmrqqgeqlkhAQVKLRAIAtggeSLGEELLGWAreqfg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 257 --VAE----------TGGIGLLLPTDqraahPRSVGVPFGGMEVALLG----PAADQGVGELLCRGP-SVAR-RYWNDPE 318
Cdd:cd05971 233 veVNEfygqtecnlvIGNCSALFPIK-----PGSMGKPIPGHRVAIVDdngtPLPPGEVGEIAVELPdPVAFlGYWNNPS 307
|
330 340
....*....|....*....|....*
gi 2484101036 319 STAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:cd05971 308 ATEKKMAGDWLLTGDLGRKDSDGYF 332
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
36-228 |
2.67e-06 |
|
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: 48.97 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 36 CLAELLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL 115
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFE-DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 116 PDPTCSDPELEWIADDSGAVLTLdgelpdgvafldegAAPDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLT 195
Cdd:cd17644 80 LDPNYPQERLTYILEDAQISVLL--------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT 145
|
170 180 190
....*....|....*....|....*....|...
gi 2484101036 196 AEgARTVLTAPLSTAAgSAVQLLPTLAAGGTVV 228
Cdd:cd17644 146 SS-DRVLQFASIAFDV-AAEEIYVTLLSGATLV 176
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
228-344 |
4.51e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.42 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 228 VAAGARGVRVPWRHLRASFPAARCVRGWGVAETG-GIGLLLPTDQRAAhprSVGVPFGGMEVALLG-PAADQGvGELLCR 305
Cdd:PRK06814 912 VFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApVIALNTPMHNKAG---TVGRLLPGIEYRLEPvPGIDEG-GRLFVR 987
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2484101036 306 GPSVARRYWN-DPESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:PRK06814 988 GPNVMLGYLRaENPGVLEPPADGWYDTGDIVTIDEEGFIT 1027
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-344 |
5.04e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.63 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 221 LAAGGTVVAAGARGVRVPWRHLRASFPAArcvrgwGVAETGGIGLLLptdqraahprSVGVPFGGMEVALLGPA-----A 295
Cdd:PRK05691 330 LAEATLFVSGGRRGQGIPALELDAEALAR------NRAEPGTGSVLM----------SCGRSQPGHAVLIVDPQslevlG 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 296 DQGVGELLCRGPSVARRYWNDPESTAETF--DDG--WFHTGDQVHI-DGDGFVT 344
Cdd:PRK05691 394 DNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFLrDGELFVT 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
51-324 |
7.79e-06 |
|
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: 47.39 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDRAgNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRW-LYAFLGVVLAGGVPVLPDPTCSDPELEWIA 129
Cdd:cd17648 3 RVAVVYGD-KRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELmIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 130 DDSGA--VLTLDGEL------------PDGVAFLDEGAAP--DELAVLYYVRKRGGGL----------HGVE-----LTN 178
Cdd:cd17648 82 EDTGArvVITNSTDLayaiytsgttgkPKGVLVEHGSVVNlrTSLSERYFGRDNGDEAvlffsnyvfdFFVEqmtlaLLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 179 ENILSTI--EAVVHAMDLTAEGARTVLTApLStAAGSAVQL-----LPTLAaggTVVAAGARGVRVPWRHLRASFPAaRC 251
Cdd:cd17648 162 GQKLVVPpdEMRFDPDRFYAYINREKVTY-LS-GTPSVLQQydlarLPHLK---RVDAAGEEFTAPVFEKLRSRFAG-LI 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 252 VRGWGVAETG--GIGLLLPTDQRAAhpRSVGVPFGGMEVALLGPAADQ----GVGELLCRGPSVARRYWNDPESTAETF 324
Cdd:cd17648 236 INAYGPTETTvtNHKRFFPGDQRFD--KSLGRPVRNTKCYVLNDAMKRvpvgAVGELYLGGDGVARGYLNRPELTAERF 312
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
62-341 |
7.99e-06 |
|
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: 47.46 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPEL--------------EW 127
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLkqclqeaepdafigIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 128 IADDSGAVLTLDGEL--PDGVAFLDE--GAAPDELAVLYYVRKRGGGLHGVELTNE-NILSTIEAVVHAMDLTAE----- 197
Cdd:cd05910 83 KADEPAAILFTSGSTgtPKGVVYRHGtfAAQIDALRQLYGIRPGEVDLATFPLFALfGPALGLTSVIPDMDPTRParadp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 198 ----------GARTVLTAP----LSTAAGSAVQL-LPTL----AAGGTVVAAGARGVRvpwrhlRASFPAARCVRGWGVA 258
Cdd:cd05910 163 qklvgairqyGVSIVFGSPalleRVARYCAQHGItLPSLrrvlSAGAPVPIALAARLR------KMLSDEAEILTPYGAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 259 ETGGIGLLLPTDQRAAHPRS--------VGVPFGGMEVALL----GPAA---------DQGVGELLCRGPSVARRYWNDP 317
Cdd:cd05910 237 EALPVSSIGSRELLATTTAAtsggagtcVGRPIPGVRVRIIeiddEPIAewddtlelpRGEIGEITVTGPTVTPTYVNRP 316
|
330 340
....*....|....*....|....*....
gi 2484101036 318 ESTAET-FDDG----WFHTGDQVHIDGDG 341
Cdd:cd05910 317 VATALAkIDDNsegfWHRMGDLGYLDDEG 345
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
62-340 |
8.95e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.64 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGAVLTLDGE 141
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 142 -------LPDG--VAFLDEGAA---------------PDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAe 197
Cdd:PRK12316 617 hlgrklpLAAGvqVLDLDRPAAwlegyseenpgtelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGV- 695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 198 gARTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGARGVRVPWR------------------HLRASFPAAR--------- 250
Cdd:PRK12316 696 -GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKlvelinregvdtlhfvpsMLQAFLQDEDvasctslrr 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 251 -CVRG----WGVAE--------TGGIGLLLPTD-----------QRAAHPRSVGVPFGGMEV----ALLGPAADQGVGEL 302
Cdd:PRK12316 775 iVCSGealpADAQEqvfaklpqAGLYNLYGPTEaaidvthwtcvEEGGDSVPIGRPIANLACyildANLEPVPVGVLGEL 854
|
330 340 350
....*....|....*....|....*....|....*...
gi 2484101036 303 LCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGD 340
Cdd:PRK12316 855 YLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGD 892
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
254-335 |
1.19e-05 |
|
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: 47.04 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIGLLlpTDQRAAHPRSVGVPFGGMEVALLgPAADQGvgELLCRGPSVARRYWNDPESTAETFD-DGWFHTG 332
Cdd:cd05921 327 GLGATETAPTATF--THWPTERSGLIGLPAPGTELKLV-PSGGKY--EVRVKGPNVTPGYWRQPELTAQAFDeEGFYCLG 401
|
...
gi 2484101036 333 DQV 335
Cdd:cd05921 402 DAA 404
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
254-344 |
1.24e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 47.02 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 254 GWGVAETGGIglLLPTDQRAAHPRSVGVPFGgmevallgPAADQGV--------------GELLCRGPSVARRYWNDPES 319
Cdd:PTZ00342 492 GYGLTETTGP--IFVQHADDNNTESIGGPIS--------PNTKYKVrtwetykatdtlpkGELLIKSDSIFSGYFLEKEQ 561
|
90 100
....*....|....*....|....*.
gi 2484101036 320 TAETF-DDGWFHTGDQVHIDGDGFVT 344
Cdd:PTZ00342 562 TKNAFtEDGYFKTGDIVQINKNGSLT 587
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
293-346 |
1.57e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.52 E-value: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2484101036 293 PAADQGVGELLCRGPSVARRYWNDPESTAETFD-DGWFHTGDQVHIDGDGFVTPV 346
Cdd:PRK10946 374 PLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDaNGFYCSGDLVSIDPDGYITVV 428
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
242-333 |
1.84e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.63 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 242 LRASFpAARCVRGWGVAETGG-IGLLLPTDQRAAHprsVGVPFGGMEVALLG------PAADQGV--GELLCRGPSVARR 312
Cdd:PLN02736 396 LRICF-GGRVLEGYGMTETSCvISGMDEGDNLSGH---VGSPNPACEVKLVDvpemnyTSEDQPYprGEICVRGPIIFKG 471
|
90 100
....*....|....*....|..
gi 2484101036 313 YWNDPESTAETFD-DGWFHTGD 333
Cdd:PLN02736 472 YYKDEVQTREVIDeDGWLHTGD 493
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
252-344 |
2.54e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.93 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAETGGIGLL------LPTDQRAAHPRSVGVPFGGMEVALLG-----PAADQGVGELLCRGPSVARRYWNDPEST 320
Cdd:PRK05620 327 VHVWGMTETSPVGTVarppsgVSGEARWAYRVSQGRFPASLEYRIVNdgqvmESTDRNEGEIQVRGNWVTASYYHSPTEE 406
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2484101036 321 ----AETF-------------DDGWFHTGDQVHIDGDGFVT 344
Cdd:PRK05620 407 gggaASTFrgedvedandrftADGWLRTGDVGSVTRDGFLT 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
293-343 |
2.96e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 45.78 E-value: 2.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2484101036 293 PAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQVHIDGDGFV 343
Cdd:PLN03102 386 PRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHV 436
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
36-341 |
3.24e-05 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 45.56 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 36 CLAELldrSALRHSARVAAvdrAGNALTYGQMWSSAAR-VAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV-- 112
Cdd:PLN02860 12 CLTRL---ATLRGNAVVTI---SGNRRRTGHEFVDGVLsLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIva 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 113 -------------------PVL--PDPTCSD----------PELEW-----IADDSGAVLTLDGELPD-------GVAFL 149
Cdd:PLN02860 86 plnyrwsfeeaksamllvrPVMlvTDETCSSwyeelqndrlPSLMWqvfleSPSSSVFIFLNSFLTTEmlkqralGTTEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 150 DEGAAPDELAVLYYVRKRGGGLHGVELTNENI----LSTIEAVVHA-MDLTAEGARTVLTAPLSTA-----AGSAVQLLP 219
Cdd:PLN02860 166 DYAWAPDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAIVGYGeDDVYLHTAPLCHIGGLSSAlamlmVGACHVLLP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 220 TLAAGG--------------TVVA---------------AGARGVR--------VPWRHLRAS---FPAARCVRGWGVAE 259
Cdd:PLN02860 246 KFDAKAalqaikqhnvtsmiTVPAmmadlisltrksmtwKVFPSVRkilngggsLSSRLLPDAkklFPNAKLFSAYGMTE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 260 TGG----IGLLLPTDQRAAHPRS-----------------VGVPFGGMEVALLGPAADQgVGELLCRGPSVARRYWNDPE 318
Cdd:PLN02860 326 ACSsltfMTLHDPTLESPKQTLQtvnqtksssvhqpqgvcVGKPAPHVELKIGLDESSR-VGRILTRGPHVMLGYWGQNS 404
|
410 420
....*....|....*....|....
gi 2484101036 319 STAETF-DDGWFHTGDQVHIDGDG 341
Cdd:PLN02860 405 ETASVLsNDGWLDTGDIGWIDKAG 428
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
63-334 |
3.68e-05 |
|
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: 45.56 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 63 TYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVlpdPTCSDPELEWIAddsgAVLTLDGEL 142
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAV---PVSIGSNEEHKL----KLNKVWNTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 143 PDGVAFLDEGA---APDELAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAEgaRTVLT-APLSTAAG-SAVQL 217
Cdd:cd05908 90 KNPYLITEEEVlceLADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK--DRILSwMPLTHDMGlIAFHL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 218 LPTLAAGGTVVAAGARGVRVP--W------------------------------------RHLRA--------------S 245
Cdd:cd05908 168 APLIAGMNQYLMPTRLFIRRPilWlkkasehkativsspnfgykyflktlkpekandwdlSSIRMilngaepidyelchE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 246 FPAARCVRG---------WGVAEtGGIGLLLP---------------------------TDQRAAHPRSVGVPFGGMEVA 289
Cdd:cd05908 248 FLDHMSKYGlkrnailpvYGLAE-ASVGASLPkaqspfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIR 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2484101036 290 LLGPA----ADQGVGELLCRGPSVARRYWNDPESTAETF-DDGWFHTGDQ 334
Cdd:cd05908 327 ICDEDnkilPDGYIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDL 376
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
247-333 |
4.44e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.22 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 247 PAARCVRGWGVAETGGiGLLLPTDQRAAHPRSVGVPFGGMEVAL-----LGPAADQGV--GELLCRGPSVARRYWNDPES 319
Cdd:PLN02861 407 SCSVLSQGYGLTESCG-GCFTSIANVFSMVGTVGVPMTTIEARLesvpeMGYDALSDVprGEICLRGNTLFSGYHKRQDL 485
|
90
....*....|....
gi 2484101036 320 TAETFDDGWFHTGD 333
Cdd:PLN02861 486 TEEVLIDGWFHTGD 499
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
54-340 |
4.54e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.27 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 54 AVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGG--VPVlpDpTCSDPE-LEWIAD 130
Cdd:PRK04813 20 AYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHayIPV--D-VSSPAErIEMIIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 131 DSGAVLTLD-GELPDGVAFLD------------EGAAPDELAVL-----YYVRKRGG--GL-HGVELTNENILSTIEAVV 189
Cdd:PRK04813 97 VAKPSLIIAtEELPLEILGIPvitldelkdifaTGNPYDFDHAVkgddnYYIIFTSGttGKpKGVQISHDNLVSFTNWML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 190 HAMDLtAEGARTVLTAPLSTAAgSAVQLLPTLAAGGTVVAA---------------GARGVRVpW--------------- 239
Cdd:PRK04813 177 EDFAL-PEGPQFLNQAPYSFDL-SVMDLYPTLASGGTLVALpkdmtanfkqlfetlPQLPINV-Wvstpsfadmclldps 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 240 ------------------------RHLRASFPAARCVRGWGVAE-TGGIGLLLPTDQR-AAHPR-SVGVPFGGMEVALLG 292
Cdd:PRK04813 254 fneehlpnlthflfcgeelphktaKKLLERFPSATIYNTYGPTEaTVAVTSIEITDEMlDQYKRlPIGYAKPDSPLLIID 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101036 293 ----PAADQGVGELLCRGPSVARRYWNDPESTAETF--DDGW--FHTGDQVHIDGD 340
Cdd:PRK04813 334 eegtKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFftFDGQpaYHTGDAGYLEDG 389
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
42-341 |
5.92e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 44.89 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 42 DRSALRH-SARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNG---FRWLYAFLGvvlAGGVPVLPD 117
Cdd:PRK09274 21 DQLAVAVpGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSlefFALTFALFK---AGAVPVLVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 118 P--------TC---SDPE--------------LEWIADDSGAVLTLDGELPDGVAFLDE-------------GAAPDELA 159
Cdd:PRK09274 98 PgmgiknlkQClaeAQPDafigipkahlarrlFGWGKPSVRRLVTVGGRLLWGGTTLATllrdgaaapfpmaDLAPDDMA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 160 VLYYVRKRGGGLHGVELTNENILSTIEAVVHA-------MDL----------TAEGARTVL-----TAPLS--------- 208
Cdd:PRK09274 178 AILFTSGSTGTPKGVVYTHGMFEAQIEALREDygiepgeIDLptfplfalfgPALGMTSVIpdmdpTRPATvdpaklfaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 209 -------------------TAAGSAVQL-LPTLAaggTVVAAGARGVRVPWRHLRASFPA-ARCVRGWG------VAETG 261
Cdd:PRK09274 258 ierygvtnlfgspallerlGRYGEANGIkLPSLR---RVISAGAPVPIAVIERFRAMLPPdAEILTPYGatealpISSIE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 262 GIGLLLPTDQRAAHPRS--VGVPFGGMEVALLG-------------PAADQGVGELLCRGPSVARRYWNDPESTAET-FD 325
Cdd:PRK09274 335 SREILFATRAATDNGAGicVGRPVDGVEVRIIAisdapipewddalRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkIP 414
|
410 420
....*....|....*....|
gi 2484101036 326 DG----WFHTGDQVHIDGDG 341
Cdd:PRK09274 415 DGqgdvWHRMGDLGYLDAQG 434
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
56-244 |
2.06e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 56 DRAGNA--LTYGQMwSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPV-LPDPtcSDP----ELEWI 128
Cdd:PRK07769 48 ERDGVArdLTWSQF-GARNRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVpLFDP--AEPghvgRLHAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 129 ADDS--GAVLTLDGE------------------------LPDGVAFLDEGAAPDE--LAVLYYVRKRGGGLHGVELTNEN 180
Cdd:PRK07769 125 LDDCtpSAILTTTDSaegvrkffrarpakerprviavdaVPDEVGATWVPPEANEdtIAYLQYTSGSTRIPAGVQITHLN 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 181 ILSTIEAVVHAMDLTaEGARTVLTAPLSTAAGSAVQLLPTLAAGGTVVAAGARGVRVPWRHLRA 244
Cdd:PRK07769 205 LPTNVLQVIDALEGQ-EGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPGRWIRE 267
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
250-344 |
2.82e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 RCVRGWGVAETGGI-GLLLPTdqrAAHPRSVGVPFGGMEVALLG-PAADQGvGELLCRGPSVARRYW--NDP-------- 317
Cdd:PRK08043 506 RILEGYGVTECAPVvSINVPM---AAKPGTVGRILPGMDARLLSvPGIEQG-GRLQLKGPNIMNGYLrvEKPgvlevpta 581
|
90 100
....*....|....*....|....*..
gi 2484101036 318 ESTAETFDDGWFHTGDQVHIDGDGFVT 344
Cdd:PRK08043 582 ENARGEMERGWYDTGDIVRFDEQGFVQ 608
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
14-94 |
3.08e-04 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 42.69 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 14 WFRDERVSRRLDGVLRYedlepCLAELLDRSALRHsarVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHY 93
Cdd:cd05967 43 WFVGGRLNTCYNALDRH-----VEAGRGDQIALIY---DSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYM 114
|
.
gi 2484101036 94 P 94
Cdd:cd05967 115 P 115
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
51-186 |
3.41e-04 |
|
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: 42.46 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 51 RVAAVDRAgNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIAD 130
Cdd:cd17656 4 AVAVVFEN-QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101036 131 DSGA-VLTLDGELPDGVAF-------------------LDEGAAPDELAVLYYVRKRGGGLHGVELTNENILSTIE 186
Cdd:cd17656 83 DSGVrVVLTQRHLKSKLSFnkstilledpsisqedtsnIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
256-343 |
3.90e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 42.25 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 256 GVAETGGIGLLLP-TDQRAAHPRSVGvpfggmevALLGPAADQGVGELLCRGPSVARRYWNDPESTAETFDDGWFHTGDQ 334
Cdd:PRK07529 381 GERRIGSVGLRLPyQRVRVVILDDAG--------RYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDL 452
|
....*....
gi 2484101036 335 VHIDGDGFV 343
Cdd:PRK07529 453 GRIDADGYF 461
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
62-341 |
6.31e-04 |
|
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: 41.35 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVLPDPTCSDPELEWIADDSGA-VLTLDG 140
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGArLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 elpDGVAFLDEGaapdeLAVLYYVRKRGGGLHGVELTNENILSTIEAVVHAMDLTAE-------------GARTVLTAPL 207
Cdd:cd05973 81 ---ANRHKLDSD-----PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEdsfwnaadpgwayGLYYAITGPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 208 ST-------AAGSAVQL---------LPTLAAGGTV----VAAGARGVRVPWRHLR----ASFPAARCVRGWGVAETGG- 262
Cdd:cd05973 153 ALghptillEGGFSVEStwrvierlgVTNLAGSPTAyrllMAAGAEVPARPKGRLRrvssAGEPLTPEVIRWFDAALGVp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 263 ---------IGLLLPTDQRAAHP---RSVGVPFGGMEVALLGPAADQ-GVGELLCRGPSVARR-------YWNDPEStae 322
Cdd:cd05973 233 ihdhygqteLGMVLANHHALEHPvhaGSAGRAMPGWRVAVLDDDGDElGPGEPGRLAIDIANSplmwfrgYQLPDTP--- 309
|
330
....*....|....*....
gi 2484101036 323 TFDDGWFHTGDQVHIDGDG 341
Cdd:cd05973 310 AIDGGYYLTGDTVEFDPDG 328
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
12-94 |
6.68e-04 |
|
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: 41.41 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 12 AGWFRDERVSrrldgvLRYEDLEPCLAELLDRSALRHSARVAAVDRAgnaLTYGQMWSSAARVAGGLLDQGVGPADRVVV 91
Cdd:cd17634 44 IKWFEDATLN------LAANALDRHLRENGDRTAIIYEGDDTSQSRT---ISYRELHREVCRFAGTLLDLGVKKGDRVAI 114
|
...
gi 2484101036 92 HYP 94
Cdd:cd17634 115 YMP 117
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
62-346 |
6.68e-04 |
|
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: 41.40 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 62 LTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVpVLPDPTCSDP-ELEWIADDSGAVltldg 140
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV-VIPATTLLTPdDLRDRVDRGGAV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 141 elpdgVAFLDEGAAPDELAVLYYVRKRGGGLHGVELTNENI----LSTIEAV------VHaMDLTAEG----ARTVLTAP 206
Cdd:cd05974 75 -----YAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWIglkpgdVH-WNISSPGwakhAWSCFFAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 207 LStaAGSAVQL-------------------LPTLAAGGTV----VAAGARGVRVPWRHLRASFPA------ARCVRGWGV 257
Cdd:cd05974 149 WN--AGATVFLfnyarfdakrvlaalvrygVTTLCAPPTVwrmlIQQDLASFDVKLREVVGAGEPlnpeviEQVRRAWGL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 258 AETGGIGLLLPTDQRAAHPR------SVGVPFGGMEVALLGP---AADQGVGELL---CRGPSVARRYWNDPESTAETFD 325
Cdd:cd05974 227 TIRDGYGQTETTALVGNSPGqpvkagSMGRPLPGYRVALLDPdgaPATEGEVALDlgdTRPVGLMKGYAGDPDKTAHAMR 306
|
330 340
....*....|....*....|.
gi 2484101036 326 DGWFHTGDQVHIDGDGFVTPV 346
Cdd:cd05974 307 GGYYRTGDIAMRDEDGYLTYV 327
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
246-341 |
6.87e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 41.34 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 246 FPAARCVRGWGVAETGGIgLLLPTDQRAAHPRSVGVPFGGMEVALLG-----PAADQGVGELLCRGPSVARRYW-NDP-E 318
Cdd:PRK06334 323 FPHIQLRQGYGTTECSPV-ITINTVNSPKHESCVGMPIRGMDVLIVSeetkvPVSSGETGLVLTRGTSLFSGYLgEDFgQ 401
|
90 100
....*....|....*....|...
gi 2484101036 319 STAETFDDGWFHTGDQVHIDGDG 341
Cdd:PRK06334 402 GFVELGGETWYVTGDLGYVDRHG 424
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
295-344 |
7.21e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.25 E-value: 7.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 295 ADQGVGELLCRGPSVARRYWNDPESTAETF------------------DDGWFHTGD-QVHIDGDGFVT 344
Cdd:PRK07769 414 PDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapdDALWVRTGDyGVYFDGELYIT 482
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
82-342 |
9.23e-04 |
|
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: 40.82 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 82 GVGPADRVVVHYPNGFRWLYA--FLGVVLAGGVPVLPD-PTCSDPE--------LEWIADDSGAVLTLDGELPDGVAFLD 150
Cdd:cd05929 38 GVWIADGVYIYLINSILTVFAaaAAWKCGACPAYKSSRaPRAEACAiieikaaaLVCGLFTGGGALDGLEDYEAAEGGSP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 151 EGAAPDELAVLYYVRKRG--GGLHGVELTNENILSTIEAVVHAMDLT--AEGARTVLTAPLSTAAGSAVQLLpTLAAGGT 226
Cdd:cd05929 118 ETPIEDEAAGWKMLYSGGttGRPKGIKRGLPGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRWSMT-ALFMGGT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 227 VV------AAGA-RGV---RVPW------------------RH------LRASFPAA---------RCVRGWG------V 257
Cdd:cd05929 197 LVlmekfdPEEFlRLIeryRVTFaqfvptmfvrllklpeavRNaydlssLKRVIHAAapcppwvkeQWIDWGGpiiweyY 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 258 AETGGIGL-LLPTDQRAAHPRSVGVPFGGmEVALLGPAADQ----GVGELLCRGPSvARRYWNDPESTAETFD-DGWFHT 331
Cdd:cd05929 277 GGTEGQGLtIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEvppgEIGEVYFANGP-GFEYTNDPEKTAAARNeGGWSTL 354
|
330
....*....|.
gi 2484101036 332 GDQVHIDGDGF 342
Cdd:cd05929 355 GDVGYLDEDGY 365
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
279-339 |
1.06e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 40.63 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2484101036 279 VGVPFGGMEVALLGpaadqgvGELLCRGPSVARRYWNDPESTAETFDDGWFHT-------GDQVHIDG 339
Cdd:PRK09029 291 VGSPLPGREVKLVD-------GEIWLRGASLALGYWRQGQLVPLVNDEGWFATrdrgewqNGELTILG 351
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
250-342 |
1.41e-03 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 40.62 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 250 RC--VRGWGVAETGGIGLL-LP--TDQRaahPRSVGVPFGGMEVALLGP---AADQGVGELLCRG---PSVARRYWNDPE 318
Cdd:cd05966 381 RCpiVDTWWQTETGGIMITpLPgaTPLK---PGSATRPFFGIEPAILDEegnEVEGEVEGYLVIKrpwPGMARTIYGDHE 457
|
90 100
....*....|....*....|....*..
gi 2484101036 319 STAETF---DDGWFHTGDQVHIDGDGF 342
Cdd:cd05966 458 RYEDTYfskFPGYYFTGDGARRDEDGY 484
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
45-112 |
1.74e-03 |
|
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: 40.33 E-value: 1.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2484101036 45 ALRHS------ARVAAVDRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:cd05943 76 LLRHAdaddpaAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAI 149
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
59-115 |
2.21e-03 |
|
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: 39.64 E-value: 2.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101036 59 GNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGVPVL 115
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAAL 57
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
226-343 |
2.27e-03 |
|
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: 39.87 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 226 TVVAAGARGVRVPWRHLRASFPAARC--VRGWGVAETGGiglLLPTDQRAAHPRSVG---VPFGGMEVALLG----PAAD 296
Cdd:cd17634 358 ILGSVGEPINPEAYEWYWKKIGKEKCpvVDTWWQTETGG---FMITPLPGAIELKAGsatRPVFGVQPAVVDneghPQPG 434
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2484101036 297 QGVGELLCRG--PSVARRYWNDPESTAET----FDDGWFHtGDQVHIDGDGFV 343
Cdd:cd17634 435 GTEGNLVITDpwPGQTRTLFGDHERFEQTyfstFKGMYFS-GDGARRDEDGYY 486
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-343 |
2.38e-03 |
|
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: 39.39 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2484101036 252 VRGWGVAETGGIGLLLPTDqRAAHPRSVGVPFGGMEV---------ALLGPAADQGVGELLCRGPSVARRYWNDPESTAE 322
Cdd:cd05944 150 VEGYGLTEATCLVAVNPPD-GPKRPGSVGLRLPYARVrikvldgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNA 228
|
90 100
....*....|....*....|.
gi 2484101036 323 TFDDGWFHTGDQVHIDGDGFV 343
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYL 249
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
37-112 |
2.71e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 39.47 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2484101036 37 LAELLDRSALRHSARVAAVDRaGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPNGFRWLYAFLGVVLAGGV 112
Cdd:PRK08279 39 LGDVFEEAAARHPDRPALLFE-DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
278-343 |
3.85e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 39.21 E-value: 3.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2484101036 278 SVGVPFGGMEVALLG----PAADQGVGELLCRGPSVARRYwNDPESTAETFD-DGWFHTGDQVHIDGDGFV 343
Cdd:PRK07768 361 TLGPPLPGLEVRVVDedgqVLPPRGVGVIELRGESVTPGY-LTMDGFIPAQDaDGWLDTGDLGYLTEEGEV 430
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
296-344 |
4.77e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 38.95 E-value: 4.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2484101036 296 DQGVGELLCRGPSVARRYWNDPESTAETF-------------------DDGWFHTGD-QVHIDGDGFVT 344
Cdd:PRK12476 426 DGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgaadDGTWLRTGDlGVYLDGELYIT 494
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
45-95 |
5.22e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 38.62 E-value: 5.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2484101036 45 ALRHSA--RVAAV----DRAGNALTYGQMWSSAARVAGGLLDQGVGPADRVVVHYPN 95
Cdd:PRK03584 92 LLRHRRddRPAIIfrgeDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPN 148
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
300-333 |
7.45e-03 |
|
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: 38.21 E-value: 7.45e-03
10 20 30
....*....|....*....|....*....|....*
gi 2484101036 300 GELLCRGPSVARRYWNDPESTAETFD-DGWFHTGD 333
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDeDGFYRTGD 470
|
|
| |
