|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
6-438 |
0e+00 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 554.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 6 NQKYWDPqLETQSRAEWDALKLGLLKDHLKHAYDNSPYYRSSFDAAGVKPEDLKTLADLQRFPTIDKKILRERQeakPLl 85
Cdd:COG1541 1 SEMYWNP-IETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNY---PF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 86 gDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFWSSGLRPEDRYAHSLNFSLFIGGPCV-LGAQKLGA 164
Cdd:COG1541 76 -GLFAVPLEEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLhYGAERLGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 165 LSIHAGTVPSERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDPKkDLAVKRIFVAGEPGGsiPETRARIEALWGAEV 244
Cdd:COG1541 155 TVIPAGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPR-DLSLKKGIFGGEPWS--EEMRKEIEERWGIKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 245 YDYYGLSDIFGSCAGMCEEKDGLHWAEDHILVEVLDPETGEAVAPGERGEMVLTTLKKRARPLIRFRTGDIVSFTDEPCA 324
Cdd:COG1541 232 YDIYGLTEVGPGVAYECEAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 325 CGRTSQRLLGVHGRRDDMLIVRGVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTIEVERAAGFqgTADALADRLA 404
Cdd:COG1541 312 CGRTHPRIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGA--SLEALAEAIA 389
|
410 420 430
....*....|....*....|....*....|....
gi 500090113 405 HRVKAITGVGAHIAVLDPDTLPRATHKAKRVEDR 438
Cdd:COG1541 390 AALKAVLGLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
12-439 |
0e+00 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 535.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 12 PQLETQSRAEWDALKLGLLKDHLKHAYDNSPYYRSSFDAAGVKPEDLKTLADLQRFPTIDKKILRERQEAKPLlgdlaAV 91
Cdd:cd05913 1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLF-----AV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 92 PERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFWSSGLRPEDRYAHSLNFSLFIGG-PCVLGAQKLGALSIHAG 170
Cdd:cd05913 76 PREKVVRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGlGFHYGAERLGALVIPAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 171 TVPSERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDPKKdLAVKRIFVAGEPGGSipETRARIEALWGAEVYDYYGL 250
Cdd:cd05913 156 GGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRE-LSLKVGIFGAEPWTE--EMRKRIERRLGIKAYDIYGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 251 SDIFGSCAGM-CEEKDGLHWAEDHILVEVLDPETGEAVAPGERGEMVLTTLKKRARPLIRFRTGDIVSFTDEPCACGRTS 329
Cdd:cd05913 233 TEIIGPGVAFeCEEKDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 330 QRLLGVHGRRDDMLIVRGVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTIEVERAAGFQGTA--DALADRLAHRV 407
Cdd:cd05913 313 RRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEADDDEklEALKQRLERHI 392
|
410 420 430
....*....|....*....|....*....|..
gi 500090113 408 KAITGVGAHIAVLDPDTLPRATHKAKRVEDRR 439
Cdd:cd05913 393 KSVLGVTVEVELVEPGSLPRSEGKAKRVIDKR 424
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
347-439 |
4.66e-31 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 114.50 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 347 GVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTIEVERAAGF---QGTADALADRLAHRVKAITGVGAHIAVLDPD 423
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFsdeIKDLEALEKRIAKELKSVLGVSVKVELVEPG 80
|
90
....*....|....*.
gi 500090113 424 TLPRATHKAKRVEDRR 439
Cdd:pfam14535 81 TLPRSEGKAKRVIDLR 96
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
95-361 |
6.62e-30 |
|
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: 118.54 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 95 DVVYVSASSGSTGVPTVSPFTQQDfddWIDYEARQFWSSGLRPEDRYAHSLNFSLFIGGPCVLGAQKLGALSIHAGTVPS 174
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN---LLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 175 ERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDpkkDLAVKRIFVAGEPGGsiPETRARIEALWGAEVYDYYGLSDIF 254
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYD---LSSLRALVSGGAPLP--PELLERFEEAPGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 255 GSCAGMCEEKDGLHWAE-----DHILVEVLDPETGEaVAPGERGEMVLTT-------LKKRARPL-----IRFRTGDIVS 317
Cdd:cd04433 153 GTVATGPPDDDARKPGSvgrpvPGVEVRIVDPDGGE-LPPGEIGELVVRGpsvmkgyWNNPEATAavdedGWYRTGDLGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 500090113 318 FTDEPCacgrtsqrlLGVHGRRDDMLIVRGVNIFPSDVEAIVRK 361
Cdd:cd04433 232 LDEDGY---------LYIVGRLKDMIKSGGENVYPAEVEAVLLG 266
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
102-436 |
2.27e-24 |
|
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: 104.89 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 102 SSGSTGVPTVSPFTQQDFDDWIDYEARQFwssGLRPEDRYA------HSLNFSLFIGGPCVLGAQklgaLSIHAGTVPsE 175
Cdd:COG0318 108 TSGTTGRPKGVMLTHRNLLANAAAIAAAL---GLTPGDVVLvalplfHVFGLTVGLLAPLLAGAT----LVLLPRFDP-E 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 176 RLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDPKkdlAVKRIFVAGEPggsIP-ETRARIEALWGAEVYDYYGLSDIF 254
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLS---SLRLVVSGGAP---LPpELLERFEERFGVRIVEGYGLTETS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 255 GSCAGMCEEKDGLHWAE-----DHILVEVLDPEtGEAVAPGERGEMVL----TTL------KKRARPLIR--FRTGDIVS 317
Cdd:COG0318 254 PVVTVNPEDPGERRPGSvgrplPGVEVRIVDED-GRELPPGEVGEIVVrgpnVMKgywndpEATAEAFRDgwLRTGDLGR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 318 FTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVE------------AIVRKDHDFSGEYRLVIeridhldrltie 385
Cdd:COG0318 333 LDED----GY-----LYIVGRKKDMIISGGENVYPAEVEevlaahpgvaeaAVVGVPDEKWGERVVAF------------ 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 500090113 386 VERAAGFQGTADALADRLAHRVkAITGVGAHIAVLdpDTLPR-ATHKAKRVE 436
Cdd:COG0318 392 VVLRPGAELDAEELRAFLRERL-ARYKVPRRVEFV--DELPRtASGKIDRRA 440
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
49-346 |
1.46e-14 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 75.04 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 49 DAAGVKPEDLKTLADLQRFPTIDKKILRERQE-AKPLLGDLAAVPERDVVYVSASSGSTGVP-----TVSPFTQQDFDDW 122
Cdd:pfam00501 109 LEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKpADVPPPPPPPPDPDDLAYIIYTSGTTGKPkgvmlTHRNLVANVLSIK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 123 IDYEarqfWSSGLRPEDRYAHSLNFSlFIGG--PCVLGAQKLGA---LSIHAGTVPSERLLAILRQFQATAIWTTPSYAW 197
Cdd:pfam00501 189 RVRP----RGFGLGPDDRVLSTLPLF-HDFGlsLGLLGPLLAGAtvvLPPGFPALDPAALLELIERYKVTVLYGVPTLLN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 198 YLgetAQKEGIDPKKDLAVKRIFVAGEPGGsiPETRARIEALWGAEVYDYYGLSDifGSCAGMCEEKDGLHWAED----- 272
Cdd:pfam00501 264 ML---LEAGAPKRALLSSLRLVLSGGAPLP--PELARRFRELFGGALVNGYGLTE--TTGVVTTPLPLDEDLRSLgsvgr 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 273 ---HILVEVLDPETGEAVAPGERGEMV---------------LTtlKKRARPLIRFRTGDIVSFTDEpcacGRtsqrlLG 334
Cdd:pfam00501 337 plpGTEVKIVDDETGEPVPPGEPGELCvrgpgvmkgylndpeLT--AEAFDEDGWYRTGDLGRRDED----GY-----LE 405
|
330
....*....|..
gi 500090113 335 VHGRRDDMLIVR 346
Cdd:pfam00501 406 IVGRKKDQIKLG 417
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-359 |
5.15e-14 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 73.99 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 52 GVKPEDLKTLAD--LQRFPTIDKKILRER-QEAKPLLGDL-------AAVPERDVVYVSA--------SSGSTGVP--TV 111
Cdd:COG0365 124 GGKVIDLKEKVDeaLEELPSLEHVIVVGRtGADVPMEGDLdwdellaAASAEFEPEPTDAddplfilyTSGTTGKPkgVV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 112 spFTQQDFDDWIDYEARqfWSSGLRPEDRY----------AHS--LNFSLFIGGPCVLgaqklgalsiHAGTV--PS-ER 176
Cdd:COG0365 204 --HTHGGYLVHAATTAK--YVLDLKPGDVFwctadigwatGHSyiVYGPLLNGATVVL----------YEGRPdfPDpGR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 177 LLAILRQFQATAIWTTPsyawylgeTA----QKEGIDPKK--DL-AVKRIFVAGEPggsI-PETRARIEALWGAEVYDYY 248
Cdd:COG0365 270 LWELIEKYGVTVFFTAP--------TAiralMKAGDEPLKkyDLsSLRLLGSAGEP---LnPEVWEWWYEAVGVPIVDGW 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 249 GLSD---IFGSCAGMCEEKDG------LHWAedhilVEVLDpETGEAVAPGERGEMVLttlkKRARP-LIR--------- 309
Cdd:COG0365 339 GQTEtggIFISNLPGLPVKPGsmgkpvPGYD-----VAVVD-EDGNPVPPGEEGELVI----KGPWPgMFRgywndpery 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090113 310 -----------FRTGDIVSFTDEpcacgrtsqrllG---VHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:COG0365 409 retyfgrfpgwYRTGDGARRDED------------GyfwILGRSDDVINVSGHRIGTAEIESAL 460
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
276-429 |
4.72e-13 |
|
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: 70.73 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 276 VEVLDPETGEAVAPGERGEM---------------VLTTLKKRARPLIR----FRTGDIvsftdepcacGRTSQRLLGVH 336
Cdd:cd05931 366 VRIVDPETGRELPDGEVGEIwvrgpsvasgywgrpEATAETFGALAATDeggwLRTGDL----------GFLHDGELYIT 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 337 GRRDDMLIVRGVNIFPSDVEAIVRKDHDFSGEYRLVIERI--DHLDRLTIEVERAAGFQGTAD-ALADRLAHRVKAITGV 413
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVpdDGEERLVVVAEVERGADPADLaAIAAAIRAAVAREHGV 515
|
170
....*....|....*..
gi 500090113 414 GAH-IAVLDPDTLPRAT 429
Cdd:cd05931 516 APAdVVLVRPGSIPRTS 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
95-438 |
2.63e-12 |
|
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: 68.26 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 95 DVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFWssGLRPEDR------------YAHSLNFSLFIGGPCVLgaqkl 162
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAL--GLTPGDRvfssakmffgygLGNSLWFPLAVGASAVL----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 163 galsiHAGTVPSERLLAILRQFQATAIWTTPS-YAwylgeTAQKEGIDPKKDLAVKRIFV-AGEPggsIPETRA-RIEAL 239
Cdd:cd05919 165 -----NPGWPTAERVLATLARFRPTVLYGVPTfYA-----NLLDSCAGSPDALRSLRLCVsAGEA---LPRGLGeRWMEH 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 240 WGAEVYDYYGLSDIF-------------GSCAGMceekdgLHWAEdhilVEVLDPEtGEAVAPGERGEMVLTT------- 299
Cdd:cd05919 232 FGGPILDGIGATEVGhiflsnrpgawrlGSTGRP------VPGYE----IRLVDEE-GHTIPPGEEGDLLVRGpsaavgy 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 300 LKKRARPLIRF-----RTGDIVSFTDEPCAcgrtsqrllgVH-GRRDDMLIVRGVNIFPSDVE-AIVRkdHDFSGEYRLV 372
Cdd:cd05919 301 WNNPEKSRATFnggwyRTGDKFCRDADGWY----------THaGRADDMLKVGGQWVSPVEVEsLIIQ--HPAVAEAAVV 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500090113 373 -IERIDHLDRLTIEVERAAGF---QGTADALADRLAHRVkAITGVGAHIAVLdpDTLPR-ATHKAKRVEDR 438
Cdd:cd05919 369 aVPESTGLSRLTAFVVLKSPAapqESLARDIHRHLLERL-SAHKVPRRIAFV--DELPRtATGKLQRFKLR 436
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
102-430 |
9.08e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 66.77 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 102 SSGSTGVPTVSPFTQQDFDDWIDYearQFWSSGLRPEDRY--------AHSLNFSlfIGGPCVLGAQKLgalsIHAGTVP 173
Cdd:cd05973 96 TSGTTGLPKGVPVPLRALAAFGAY---LRDAVDLRPEDSFwnaadpgwAYGLYYA--ITGPLALGHPTI----LLEGGFS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 174 SERLLAILRQFQATAIWTTPSYawYLGETAQKEGIDPKKDLAVKRIFVAGEPggSIPETRARIEALWGAEVYDYYGLSDI 253
Cdd:cd05973 167 VESTWRVIERLGVTNLAGSPTA--YRLLMAAGAEVPARPKGRLRRVSSAGEP--LTPEVIRWFDAALGVPIHDHYGQTEL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 254 fgscaGMCEEKdglHWAEDHIL-------------VEVLDpETGEAVAPGERGEMvltTLKKRARPLIRF---------- 310
Cdd:cd05973 243 -----GMVLAN---HHALEHPVhagsagrampgwrVAVLD-DDGDELGPGEPGRL---AIDIANSPLMWFrgyqlpdtpa 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 311 ------RTGDIVSFTDEpcacGRTSqrllgVHGRRDDMLIVRGVNIFPSDVEAIVRKdHDFSGEYRlVIERIDHLDRLTI 384
Cdd:cd05973 311 idggyyLTGDTVEFDPD----GSFS-----FIGRADDVITMSGYRIGPFDVESALIE-HPAVAEAA-VIGVPDPERTEVV 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 500090113 385 E--VERAAGFQGTADaLADRLAHRVKaiTGVGAHiavldpdTLPRATH 430
Cdd:cd05973 380 KafVVLRGGHEGTPA-LADELQLHVK--KRLSAH-------AYPRTIH 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
93-438 |
8.72e-11 |
|
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: 63.51 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 93 ERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEArqFWSsGLRPEDRY--------AHSLNFSLFigGPCVLGAQklgA 164
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA--YWL-GLRPDDIHwniadpgwAKGAWSSFF--GPWLLGAT---V 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 165 LSIHAGTVPSERLLAILRQFQATAIWTTPSyAWYLgetAQKEGIDPKKDLAVKRIFVAGEPGGsiPETRARIEALWGAEV 244
Cdd:cd05972 152 FVYEGPRFDAERILELLERYGVTSFCGPPT-AYRM---LIKQDLSSYKFSHLRLVVSAGEPLN--PEVIEWWRAATGLPI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 245 YDYYGLSDIfGSCAGMCeekdglHWAEDH----------ILVEVLDPEtGEAVAPGERGEMVLTTL-----------KKR 303
Cdd:cd05972 226 RDGYGQTET-GLTVGNF------PDMPVKpgsmgrptpgYDVAIIDDD-GRELPPGEEGDIAIKLPppglflgyvgdPEK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 304 ARPLIR---FRTGDIVSFTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVE-AIVrkdhdfsgEYRLVIER--ID 377
Cdd:cd05972 298 TEASIRgdyYLTGDRAYRDED----GY-----FWFVGRADDIIKSSGYRIGPFEVEsALL--------EHPAVAEAavVG 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500090113 378 HLDRLTIEVERA-----AGFQGTaDALADRLAHRVKAITGVGAHIAVLD-PDTLPR-ATHKAKRVEDR 438
Cdd:cd05972 361 SPDPVRGEVVKAfvvltSGYEPS-EELAEELQGHVKKVLAPYKYPREIEfVEELPKtISGKIRRVELR 427
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
70-430 |
2.62e-10 |
|
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: 62.16 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 70 IDKKILRERQEAkpLLGDLAA----VPERDVVYVSASSGSTGVP-TVsPFTQQDFDDWIDYEARQFwssGLRPEDRYAHS 144
Cdd:cd05930 67 LDPSYPAERLAY--ILEDSGAklvlTDPDDLAYVIYTSGSTGKPkGV-MVEHRGLVNLLLWMQEAY---PLTPGDRVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 145 LNFS-----------LFIGGPCVLgAQKLGALSIhagtvpsERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDPkkd 213
Cdd:cd05930 141 TSFSfdvsvweifgaLLAGATLVV-LPEEVRKDP-------EALADLLAEEGITVLHLTPSLLRLLLQELELAALPS--- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 214 laVKRIFVAGEPGGsiPETRARI-EALWGAEVYDYYGLSDIFGSCAGMCEEKDGLHWAE-------DHILVEVLDPEtGE 285
Cdd:cd05930 210 --LRLVLVGGEALP--PDLVRRWrELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRvpigrpiPNTRVYVLDEN-LR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 286 AVAPGERGEMVLT--------------TLKK----RARPLIR-FRTGDIVSftdepcacgRTSQRLLGVHGRRDDMLIVR 346
Cdd:cd05930 285 PVPPGVPGELYIGgaglargylnrpelTAERfvpnPFGPGERmYRTGDLVR---------WLPDGNLEFLGRIDDQVKIR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 347 GVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTIEVERAAGFQGTADALADRLAHRVKAITgVGAHIAVLdpDTLP 426
Cdd:cd05930 356 GYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYM-VPSAFVVL--DALP 432
|
....
gi 500090113 427 RATH 430
Cdd:cd05930 433 LTPN 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
80-359 |
5.72e-09 |
|
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: 58.01 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 80 EAKPLLGDLAAVperdvVYvsaSSGSTGVPTVSPFTQqdfDDWIDYEARQFWSSGLRPEDRYAHSLnfSLF----IGGPC 155
Cdd:cd17631 92 GAKVLFDDLALL-----MY---TSGTTGRPKGAMLTH---RNLLWNAVNALAALDLGPDDVLLVVA--PLFhiggLGVFT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 156 VLGAQKLGALSIHAGTVPsERLLAILRQFQATAIWTTPSyAWYLgeTAQKEGIDPKKDLAVKRIFVAGEPggsIPETRAR 235
Cdd:cd17631 159 LPTLLRGGTVVILRKFDP-ETVLDLIERHRVTSFFLVPT-MIQA--LLQHPRFATTDLSSLRAVIYGGAP---MPERLLR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 236 IEALWGAEVYDYYGLSDIfGSCAGMCEEKDglhwAEDHIL----------VEVLDPEtGEAVAPGERGEMVLTTLKKRA- 304
Cdd:cd17631 232 ALQARGVKFVQGYGMTET-SPGVTFLSPED----HRRKLGsagrpvffveVRIVDPD-GREVPPGEVGEIVVRGPHVMAg 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500090113 305 ---RP-----LIR---FRTGDIVSFTDEPCacgrtsqrlLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd17631 306 ywnRPeataaAFRdgwFHTGDLGRLDEDGY---------LYIVDRKKDMIISGGENVYPAEVEDVL 362
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
75-406 |
8.78e-09 |
|
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: 57.30 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 75 LRERQEAKPLLGDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFwssGLRPEDRYAHSLNFSLFIGGP 154
Cdd:cd12116 107 LALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERL---GLGPGDRLLAVTTYAFDISLL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 155 CVLGAQKLGALSIHAG---TVPSERLLAILRQFQATAIWTTPSyAWYLGETAQKEGidpkkdLAVKRIFVAGEPggsIPE 231
Cdd:cd12116 184 ELLLPLLAGARVVIAPretQRDPEALARLIEAHSITVMQATPA-TWRMLLDAGWQG------RAGLTALCGGEA---LPP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 232 TRARIEALWGAEVYDYYGLSD--IFGSCAGMCEEKDGLHWAE--DHILVEVLDpETGEAVAPGERGEMVLTT-------L 300
Cdd:cd12116 254 DLAARLLSRVGSLWNLYGPTEttIWSTAARVTAAAGPIPIGRplANTQVYVLD-AALRPVPPGVPGELYIGGdgvaqgyL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 301 KKRARPLIRF-------------RTGDIVsftdepcaCGRTSQRLLgVHGRRDDMLIVRGVNIFPSDVEAIVRKdHDFSG 367
Cdd:cd12116 333 GRPALTAERFvpdpfagpgsrlyRTGDLV--------RRRADGRLE-YLGRADGQVKIRGHRIELGEIEAALAA-HPGVA 402
|
330 340 350
....*....|....*....|....*....|....*....
gi 500090113 368 EYRLVIERIDHLDRLTIEVERAAGFQGTADALADRLAHR 406
Cdd:cd12116 403 QAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRAT 441
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
81-356 |
1.76e-08 |
|
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: 56.69 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 81 AKPLLGDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFddwiDYEARQfwSS---GLRPEDRYAHSL----NFSLfiGG 153
Cdd:COG1021 171 AAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY----LYSVRA--SAeicGLDADTVYLAALpaahNFPL--SS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 154 PCVLGAqklgalsIHAG-TV-----PS-ERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIDPKkdlAVKRIFVagepG 226
Cdd:COG1021 243 PGVLGV-------LYAGgTVvlapdPSpDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLS---SLRVLQV----G 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 227 GS--IPETRARIEALWGAevydyyGLSDIFgscaGMCEekdGL------HWAEDHIL------------VEVLDPEtGEA 286
Cdd:COG1021 309 GAklSPELARRVRPALGC------TLQQVF----GMAE---GLvnytrlDDPEEVILttqgrpispddeVRIVDED-GNP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 287 VAPGERGEmvLTTlkkRARPLIR------------------FRTGDIVSFTDEpcacgrtsqRLLGVHGRRDDMlIVR-G 347
Cdd:COG1021 375 VPPGEVGE--LLT---RGPYTIRgyyrapehnaraftpdgfYRTGDLVRRTPD---------GYLVVEGRAKDQ-INRgG 439
|
....*....
gi 500090113 348 VNIFPSDVE 356
Cdd:COG1021 440 EKIAAEEVE 448
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
73-359 |
2.75e-08 |
|
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: 55.56 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 73 KILRERQEAKPLLGDlAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFWssGLRPEDRYAHS--LNFSLF 150
Cdd:cd05958 77 YILDKARITVALCAH-ALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVL--RLREDDRFVGSppLAFTFG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 151 IGG----PCVLGAqklgALSIHAGTVPSErLLAILRQFQATAIWTTP-SYAWYLGETAQKEgidpkKDLAVKRIFV-AGE 224
Cdd:cd05958 154 LGGvllfPFGVGA----SGVLLEEATPDL-LLSAIARYKPTVLFTAPtAYRAMLAHPDAAG-----PDLSSLRKCVsAGE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 225 --PggsiPETRARIEALWGAEVYDYYGLSD---IFGSCAgmceekdglhwaEDHILV------------EVLDPEtGEAV 287
Cdd:cd05958 224 alP----AALHRAWKEATGIPIIDGIGSTEmfhIFISAR------------PGDARPgatgkpvpgyeaKVVDDE-GNPV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 288 APGERGEMVLTT-------LKKRARPLIR---FRTGDIVSftdepcacgRTSQRLLGVHGRRDDMLIVRGVNIFPSDVEA 357
Cdd:cd05958 287 PDGTIGRLAVRGptgcrylADKRQRTYVQggwNITGDTYS---------RDPDGYFRHQGRSDDMIVSGGYNIAPPEVED 357
|
..
gi 500090113 358 IV 359
Cdd:cd05958 358 VL 359
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
95-359 |
4.08e-08 |
|
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: 54.99 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 95 DVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFwssGLRPEDRYAHSLnfSLFIGGPCVLGAqkLGALSiHAGTvps 174
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF---GLGEDDVYLTVL--PLFHINAQAVSV--LAALS-VGAT--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 175 erlLAILRQFQATAIW-----TTPSYAWYLGET-----AQKEGIDPKkDLAVKRIFVAGEPggsiPETRARIEALWGAEV 244
Cdd:cd05934 151 ---LVLLPRFSASRFWsdvrrYGATVTNYLGAMlsyllAQPPSPDDR-AHRLRAAYGAPNP----PELHEEFEERFGVRL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 245 YDYYGLSDIFGSCAGMCEEKDGlhW-----AEDHILVEVLDPEtGEAVAPGERGEMVLttlkKRARPLIR---------- 309
Cdd:cd05934 223 LEGYGMTETIVGVIGPRDEPRR--PgsigrPAPGYEVRIVDDD-GQELPAGEPGELVI----RGLRGWGFfkgyynmpea 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 500090113 310 ---------FRTGDIVSFTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd05934 296 taeamrngwFHTGDLGYRDAD----GF-----FYFVDRKKDMIRRRGENISSAEVERAI 345
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
81-361 |
4.53e-08 |
|
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: 54.95 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 81 AKPllgDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFwssGLRPEDRYAH----SLNFSLFIGGPCV 156
Cdd:cd05945 87 AKP---ALLIADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDF---PLGPGDVFLNqapfSFDLSVMDLYPAL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 157 LGAQKLGALSiHAGTVPSERLLAILRQFQATaIWT-TPSYAWYLgetAQKEGIDPKKDLAVKRIFVAGEPGgSIPETRAR 235
Cdd:cd05945 161 ASGATLVPVP-RDATADPKQLFRFLAEHGIT-VWVsTPSFAAMC---LLSPTFTPESLPSLRHFLFCGEVL-PHKTARAL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 236 IEALWGAEVYDYYGLSDIFGSCAGMceekdglHWAEDHIL---------------VEVLDpETGEAVAPGERGEMVLT-- 298
Cdd:cd05945 235 QQRFPDARIYNTYGPTEATVAVTYI-------EVTPEVLDgydrlpigyakpgakLVILD-EDGRPVPPGEKGELVISgp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 299 -------------------TLKKRArplirFRTGDIVSFTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd05945 307 svskgylnnpektaaaffpDEGQRA-----YRTGDLVRLEAD----GL-----LFYRGRLDFQVKLNGYRIELEEIEAAL 372
|
..
gi 500090113 360 RK 361
Cdd:cd05945 373 RQ 374
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
66-361 |
9.94e-08 |
|
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: 53.81 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 66 RFPTIDKKILRERQEAKPLLGDLAAVPERDVV-------YVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFwssGLRPE 138
Cdd:TIGR01733 85 RLAGLVLPVILLDPLELAALDDAPAPPPPDAPsgpddlaYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY---GLDPD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 139 DRYA--HSLNFSLF---IGGPCVLGAQKLGALSIHAGTVPSErLLAILRQFQATAIWTTPSYAWYLGETaqkegiDPKKD 213
Cdd:TIGR01733 162 DRVLqfASLSFDASveeIFGALLAGATLVVPPEDEERDDAAL-LAALIAEHPVTVLNLTPSLLALLAAA------LPPAL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 214 LAVKRIFVAGEPGGsiPETRARIEALWG-AEVYDYYGLSDIFGSCAGMCEEKDGLHWAE--------DHILVEVLDPEtG 284
Cdd:TIGR01733 235 ASLRLVILGGEALT--PALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAPRESpvpigrplANTRLYVLDDD-L 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 285 EAVAPGERGEMVLT--------------------TLKKRARPLIRF-RTGDIVSFTDEpcacgrtsqRLLGVHGRRDDML 343
Cdd:TIGR01733 312 RPVPVGVVGELYIGgpgvargylnrpeltaerfvPDPFAGGDGARLyRTGDLVRYLPD---------GNLEFLGRIDDQV 382
|
330
....*....|....*...
gi 500090113 344 IVRGVNIFPSDVEAIVRK 361
Cdd:TIGR01733 383 KIRGYRIELGEIEAALLR 400
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-439 |
2.14e-07 |
|
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: 52.82 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 175 ERLLAILRQFQATAIWTTPSYAWYLgeTAQKEGIDPKkDLAVKRIFVAGEPGGSIPETRARiEALwGAEVYDYYGLSD-- 252
Cdd:cd05971 171 KAALDLMSRYGVTTAFLPPTALKMM--RQQGEQLKHA-QVKLRAIATGGESLGEELLGWAR-EQF-GVEVNEFYGQTEcn 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 253 -IFGSCAGMCEEKDGL--HWAEDHIlVEVLDPEtGEAVAPGERGEMVL----------------TTLKKRARPLirFRTG 313
Cdd:cd05971 246 lVIGNCSALFPIKPGSmgKPIPGHR-VAIVDDN-GTPLPPGEVGEIAVelpdpvaflgywnnpsATEKKMAGDW--LLTG 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 314 DIVSftdepcacgRTSQRLLGVHGRRDDMLIVRGVNIFPSDVE------------AIVRKDHDFSGEyrlVIERIDHLdr 381
Cdd:cd05971 322 DLGR---------KDSDGYFWYVGRDDDVITSSGYRIGPAEIEecllkhpavlmaAVVGIPDPIRGE---IVKAFVVL-- 387
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500090113 382 ltieverAAGFqGTADALADRLAHRVKAItgVGAH---IAVLDPDTLPR-ATHKAKRVEDRR 439
Cdd:cd05971 388 -------NPGE-TPSDALAREIQELVKTR--LAAHeypREIEFVNELPRtATGKIRRRELRA 439
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
335-427 |
3.42e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 52.31 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 335 VHGRRDDMLIVRGVNIFPSDVEAIVRKDHDF-SGEY-RLVIERIDHlDRLTIEVERAAGFQGTADALADRLAHRVKAITG 412
Cdd:PRK09192 456 ITGRAKDLIIINGRNIWPQDIEWIAEQEPELrSGDAaAFSIAQENG-EKIVLLVQCRISDEERRGQLIHALAALVRSEFG 534
|
90
....*....|....*
gi 500090113 413 VGAHIAVLDPDTLPR 427
Cdd:PRK09192 535 VEAAVELVPPHSLPR 549
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
95-361 |
6.69e-07 |
|
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: 50.87 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 95 DVVYVSASSGSTGVPTV---------SPFTQQDFDDWIDYEARQFWSSGLrpedryAHSLN-----FSLFIGGpCVLGAQ 160
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAyyrserswiESFVCNEDLFNISGEDAILAPGPL------SHSLFlygaiSALYLGG-TFIGQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 161 KLGALSihagtvpserLLAILRQFQATAIWTTPSYAWYLGETAQKEgidpkkdLAVKRIFVAGEPggSIPETRARIEALW 240
Cdd:cd17633 74 KFNPKS----------WIRKINQYNATVIYLVPTMLQALARTLEPE-------SKIKSIFSSGQK--LFESTKKKLKNIF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 241 -GAEVYDYYG---LSDIFGSCAGMCEEKDGLHWAEDHILVEVLDPETGEAVAPGERGEMVLT--TLKKRARPLIRFRTGD 314
Cdd:cd17633 135 pKANLIEFYGtseLSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKIFVKSEMVFSgyVRGGFSNPDGWMSVGD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 500090113 315 IvSFTDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAIVRK 361
Cdd:cd17633 215 I-GYVDE--------EGYLYLVGRESDMIIIGGINIFPTEIESVLKA 252
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
276-358 |
1.36e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 50.42 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 276 VEVLDPETGEAVAPGERGEMVLTT---LK----KRA--RPLIR---FRTGDIVSFTDEPCacgrtsqrllgVH--GRRDD 341
Cdd:PRK06178 398 FKICDFETGELLPLGAEGEIVVRTpslLKgywnKPEatAEALRdgwLHTGDIGKIDEQGF-----------LHylGRRKE 466
|
90
....*....|....*..
gi 500090113 342 MLIVRGVNIFPSDVEAI 358
Cdd:PRK06178 467 MLKVNGMSVFPSEVEAL 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
92-359 |
2.83e-06 |
|
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: 49.30 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 92 PERDVVYVSASSGSTGVPTvspFTQQDFD-DWIDYEARQFWSSGLRP--EDRYAHSLnfSLFIGGP--CVLGAQKLGALS 166
Cdd:cd05929 123 DEAAGWKMLYSGGTTGRPK---GIKRGLPgGPPDNDTLMAAALGFGPgaDSVYLSPA--PLYHAAPfrWSMTALFMGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 167 IHAGTVPSERLLAILRQFQATAIWTTPSY---AWYLGETAQKegidpKKDLA-VKRIFVAGEPggSIPETRARIEALWGA 242
Cdd:cd05929 198 VLMEKFDPEEFLRLIERYRVTFAQFVPTMfvrLLKLPEAVRN-----AYDLSsLKRVIHAAAP--CPPWVKEQWIDWGGP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 243 EVYDYYGLSDIFGSCAGMCEEkdglhW------------AEDHILvevldPETGEAVAPGERGEM--------------V 296
Cdd:cd05929 271 IIWEYYGGTEGQGLTIINGEE-----WlthpgsvgravlGKVHIL-----DEDGNEVPPGEIGEVyfangpgfeytndpE 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500090113 297 LTTLKKRARPlirFRT-GDiVSFTDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd05929 341 KTAAARNEGG---WSTlGD-VGYLDE--------DGYLYLTDRRSDMIISGGVNIYPQEIENAL 392
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
92-364 |
7.15e-06 |
|
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: 48.36 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 92 PERDVVYVSASSGSTGVP-----------TVSPFTQQDFDDWIDYEARQ------FWSSGLrpedryaHSLNFSLFIGGP 154
Cdd:cd05911 144 GKDDTAAILYSSGTTGLPkgvclshrnliANLSQVQTFLYGNDGSNDVIlgflplYHIYGL-------FTTLASLLNGAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 155 CVlgaqklgalsihagTVP---SERLLAILRQFQATAIWTTPSYAWYLgetaQKEGIDPKKDLA-VKRIFVAGEPGGSip 230
Cdd:cd05911 217 VI--------------IMPkfdSELFLDLIEKYKITFLYLVPPIAAAL----AKSPLLDKYDLSsLRVILSGGAPLSK-- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 231 ETRARIEALWGAEVYDY-YGLSDifgSCAGMCEEKDGLHWAED------HILVEVLDPETGEAVAPGERGEMvlttlkkr 303
Cdd:cd05911 277 ELQELLAKRFPNATIKQgYGMTE---TGGILTVNPDGDDKPGSvgrllpNVEAKIVDDDGKDSLGPNEPGEI-------- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 304 arpLIR------------------------FRTGDIVSFtDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd05911 346 ---CVRgpqvmkgyynnpeatketfdedgwLHTGDIGYF-DE--------DGYLYIVDRKKELIKYKGFQVAPAELEAVL 413
|
....*
gi 500090113 360 RKdHD 364
Cdd:cd05911 414 LE-HP 417
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
62-429 |
1.99e-05 |
|
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: 46.95 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 62 ADLQRFPTIDKKILRERQEAKPLLGDLAAVPERD---VVYVSASSGSTGVP---TVSPFTQQDFDDWidyEARQFwssGL 135
Cdd:cd17651 101 ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDaddLAYVIYTSGSTGRPkgvVMPHRSLANLVAW---QARAS---SL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 136 RPEDRYAH--SLNF---------SLFIGGPCVLGAQKLGalsihagtVPSERLLAILRQFQATAIWTTPSYAWYLGETAQ 204
Cdd:cd17651 175 GPGARTLQfaGLGFdvsvqeifsTLCAGATLVLPPEEVR--------TDPPALAAWLDEQRISRVFLPTVALRALAEHGR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 205 KEGIDPkkdLAVKRIFVAGEPGGSIPETRARIEALWGAEVYDYYGLSDIFGSCAGMCEEkDGLHWAE--------DHILV 276
Cdd:cd17651 247 PLGVRL---AALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPG-DPAAWPApppigrpiDNTRV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 277 EVLDP--------ETGE------AVAPGERGEMVLTTLKKRARPLIR----FRTGDIVSFTDEpcacGRtsqrlLGVHGR 338
Cdd:cd17651 323 YVLDAalrpvppgVPGElyiggaGLARGYLNRPELTAERFVPDPFVPgarmYRTGDLARWLPD----GE-----LEFLGR 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 339 RDDMLIVRGVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTIEVERAAGFQGTADALADRLAHRVKAITgVGAHIA 418
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYM-VPSAFV 472
|
410
....*....|.
gi 500090113 419 VLdpDTLPRAT 429
Cdd:cd17651 473 LL--DALPLTP 481
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
312-439 |
2.52e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.53 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 312 TGDIVSFTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVE--------------AIVRKDHDFSGE-YRLVIERI 376
Cdd:PRK07768 418 TGDLGYLTEE----GE-----VVVCGRVKDVIIMAGRNIYPTDIEraaarvegvrpgnaVAVRLDAGHSREgFAVAVESN 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500090113 377 DHLDrlTIEVERaagfqgtadaLADRLAHRVKAITGVGAH-IAVLDPDTLPRATH-KAKRVEDRR 439
Cdd:PRK07768 489 AFED--PAEVRR----------IRHQVAHEVVAEVGVRPRnVVVLGPGSIPKTPSgKLRRANAAE 541
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
75-358 |
3.55e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 46.05 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 75 LRERQEAKPLlgDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIdYEARQFWssGLRPEDRYAHSLN-FSLFigG 153
Cdd:PRK09274 157 LLRDGAAAPF--PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQI-EALREDY--GIEPGEIDLPTFPlFALF--G 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 154 PCvlgaqkLGALSI-------HAGTVPSERLLAILRQFQATAIWTTPSYAWYLGETAQKEGIdpkKDLAVKRIFVAGEPg 226
Cdd:PRK09274 230 PA------LGMTSVipdmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGI---KLPSLRRVISAGAP- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 227 gSIPETRARIEALW--GAEVYDYYG-----------LSDIFGSCAGMCEEKDGL----------------------HWAE 271
Cdd:PRK09274 300 -VPIAVIERFRAMLppDAEILTPYGatealpissieSREILFATRAATDNGAGIcvgrpvdgvevriiaisdapipEWDD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 272 DHILvevldpETGEAvapGE---RGEMVL---------TTLKK--RARPLIRFRTGDiVSFTDEPCA---CGRTSQRLLG 334
Cdd:PRK09274 379 ALRL------ATGEI---GEivvAGPMVTrsyynrpeaTRLAKipDGQGDVWHRMGD-LGYLDAQGRlwfCGRKAHRVET 448
|
330 340
....*....|....*....|....
gi 500090113 335 VHGRrddmlivrgvnIFPSDVEAI 358
Cdd:PRK09274 449 AGGT-----------LYTIPCERI 461
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
68-356 |
5.32e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 45.30 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 68 PTIDKKIlrERQEAKPLlgdlaAVPERDVVYVSASSGSTGVP------TVSPFT-QQDFDDWIDYEARQ--------FWS 132
Cdd:PRK07788 188 ETLDDLI--AGSSTAPL-----PKPPKPGGIVILTSGTTGTPkgaprpEPSPLApLAGLLSRVPFRAGEttllpapmFHA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 133 SGlrpedrYAHsLNFSLFIGGPCVLgAQKLGAlsihagtvpsERLLAILRQFQATAIWTTPSYAWYLGETAQKegIDPKK 212
Cdd:PRK07788 261 TG------WAH-LTLAMALGSTVVL-RRRFDP----------EATLEDIAKHKATALVVVPVMLSRILDLGPE--VLAKY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 213 DL-AVKRIFVAGEPGGsiPETRARIEALWGAEVYDYYGLSDI-FGSCAGMCEekdglhWAED---------HILVEVLDp 281
Cdd:PRK07788 321 DTsSLKIIFVSGSALS--PELATRALEAFGPVLYNLYGSTEVaFATIATPED------LAEApgtvgrppkGVTVKILD- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 282 ETGEAVAPGERGEM-VLTTL----------KKRARPLIRfrTGDIVSFTDEPcacgrtsqrLLGVHGRRDDMLIVRGVNI 350
Cdd:PRK07788 392 ENGNEVPRGVVGRIfVGNGFpfegytdgrdKQIIDGLLS--SGDVGYFDEDG---------LLFVDGRDDDMIVSGGENV 460
|
....*.
gi 500090113 351 FPSDVE 356
Cdd:PRK07788 461 FPAEVE 466
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
310-440 |
1.94e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 43.60 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 310 FRTGDIVSFTDEPcacgrtsqrlLGVHGRRDDMLIVRGVNIFPSDVEAI------VRK-------DHDFSGEYRLVIeri 376
Cdd:PRK05851 398 FPTGDLGYLVDGG----------LVVCGRAKELITVAGRNIFPTEIERVaaqvrgVREgavvavgTGEGSARPGLVI--- 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500090113 377 dhldrltieverAAGFQGTADALA-DRLAHRVKAITG-VGAHIAVLDPDTLPRATH-KAKRVEDRRS 440
Cdd:PRK05851 465 ------------AAEFRGPDEAGArSEVVQRVASECGvVPSDVVFVAPGSLPRTSSgKLRRLAVKRS 519
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
333-427 |
2.09e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 333 LGVHGRRDDMLIVRGVNIFPSDVEAIVRKDHDFSGEYRLVIERIDHLDRLTI----EVERAAGFQGTADALADRLAHRV- 407
Cdd:PRK05691 444 LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGRVAAFAVNHQGEEGIgiaaEISRSVQKILPPQALIKSIRQAVa 523
|
90 100
....*....|....*....|
gi 500090113 408 KAITGVGAHIAVLDPDTLPR 427
Cdd:PRK05691 524 EACQEAPSVVLLLNPGALPK 543
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
276-430 |
4.21e-04 |
|
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: 42.69 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 276 VEVLDpETGEAVAPGERGEMVLTT-------LKKRARPLIRF------------RTGDIVSFTDEpcacGRtsqrlLGVH 336
Cdd:cd12115 279 AYVLD-RALQPVPLGVPGELYIGGagvargyLGRPGLTAERFlpdpfgpgarlyRTGDLVRWRPD----GL-----LEFL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 337 GRRDDMLIVRGVNIFPSDVEAIVRkDHDFSGEYRLV-IERIDHLDRLTIEVERAAGFQGTADALADRLAHRVKAITgVGA 415
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALR-SIPGVREAVVVaIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYM-VPS 426
|
170
....*....|....*
gi 500090113 416 HIAVLdpDTLPRATH 430
Cdd:cd12115 427 RFVRL--DALPLTPN 439
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
227-364 |
5.05e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 42.33 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 227 GSIP---ETRARIEALWGAEVYDYYGLSDIFG-SCAGMCEEKD-----GLHWAEDHILVEVLdpETGEAVAPGERGEMVL 297
Cdd:PRK06710 331 GSAPlpvEVQEKFETVTGGKLVEGYGLTESSPvTHSNFLWEKRvpgsiGVPWPDTEAMIMSL--ETGEALPPGEIGEIVV 408
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500090113 298 TTLK---------KRARPLIR---FRTGDiVSFTDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAIVRkDHD 364
Cdd:PRK06710 409 KGPQimkgywnkpEETAAVLQdgwLHTGD-VGYMDE--------DGFFYVKDRKKDMIVASGFNVYPREVEEVLY-EHE 477
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
49-360 |
7.42e-04 |
|
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: 41.73 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 49 DAAGVKPEDLKTLADLQRFPTIDKkiLRERQEAKPLLGDLAAVPERDVvYVSASSGSTGVPTVSPFTQQDFDDWIDYEAR 128
Cdd:cd05923 108 VDAQVMDAIFQSGVRVLALSDLVG--LGEPESAGPLIEDPPREPEQPA-FVFYTSGTTGLPKGAVIPQRAAESRVLFMST 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 129 QfwsSGLRPEDryaHSLNFSLF-----IGGPCVLgaqkLGALSIHAGTVPSE-----RLLAILRQFQATAIWTTPSYAWY 198
Cdd:cd05923 185 Q---AGLRHGR---HNVVLGLMplyhvIGFFAVL----VAALALDGTYVVVEefdpaDALKLIEQERVTSLFATPTHLDA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 199 LGETAQKEGIDPKkdlAVKRIFVAGepgGSIPET-RARIEALWGAEVYDYYGLSDIFGS-----CAGMCEEKDGLHwaeD 272
Cdd:cd05923 255 LAAAAEFAGLKLS---SLRHVTFAG---ATMPDAvLERVNQHLPGEKVNIYGTTEAMNSlymrdARTGTEMRPGFF---S 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 273 HILVEVLDPETGEAVAPGERGEMVLT-----TLKKRARPL------IRF---RTGDIVSFTDEpcacGRtsqrlLGVHGR 338
Cdd:cd05923 326 EVRIVRIGGSPDEALANGEEGELIVAaaadaAFTGYLNQPeatakkLQDgwyRTGDVGYVDPS----GD-----VRILGR 396
|
330 340
....*....|....*....|..
gi 500090113 339 RDDMLIVRGVNIFPSDVEAIVR 360
Cdd:cd05923 397 VDDMIISGGENIHPSEIERVLS 418
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
89-359 |
8.67e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 41.41 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 89 AAVPERDVVYVSASSGSTGVPTvspFTQQDFDDWIDYEARQFWSSGLRPEDRyahslnfsLFIGGPCV-LGAQKLGALSI 167
Cdd:PRK06145 144 AAVAPTDLVRLMYTSGTTDRPK---GVMHSYGNLHWKSIDHVIALGLTASER--------LLVVGPLYhVGAFDLPGIAV 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 168 --HAGTVPSER------LLAILRQFQATAIWTTPSYAwylgeTAQKEGIDPKK-DLAVKRIFVAGepGGSIPETRAR--I 236
Cdd:PRK06145 213 lwVGGTLRIHRefdpeaVLAAIERHRLTCAWMAPVML-----SRVLTVPDRDRfDLDSLAWCIGG--GEKTPESRIRdfT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 237 EALWGAEVYDYYGLSDifgSCAG--MCE-----EKDG-LHWAEDHILVEVLDpETGEAVAPGERGEMVLTTLK------- 301
Cdd:PRK06145 286 RVFTRARYIDAYGLTE---TCSGdtLMEagreiEKIGsTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKvtkgywk 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500090113 302 ---KRARPLIR--FRTGDiVSFTDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:PRK06145 362 dpeKTAEAFYGdwFRSGD-VGYLDE--------EGFLYLTDRKKDMIISGGENIASSEVERVI 415
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
76-359 |
9.90e-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: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 76 RERQEAKPLLGDLAAVPERDVVYVSASSGSTGVPTVSPFTQQDFDDWIDYEARQFWSSGlrPEDRYAHSLNFSLFIGGPC 155
Cdd:cd17634 214 RDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYG--PGDIYWCTADVGWVTGHSY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 156 VL-GAQKLGALSIHAGTVP----SERLLAILRQFQATAIWTTPSYAWYLgetaQKEGID--PKKDLAVKRI-FVAGEPGG 227
Cdd:cd17634 292 LLyGPLACGATTLLYEGVPnwptPARMWQVVDKHGVNILYTAPTAIRAL----MAAGDDaiEGTDRSSLRIlGSVGEPIN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 228 siPETRA---RIEALWGAEVYDYYGLSDIFGSCA----GMCEEKDGLHW-AEDHILVEVLDPEtGEAVAPGERGEMVLT- 298
Cdd:cd17634 368 --PEAYEwywKKIGKEKCPVVDTWWQTETGGFMItplpGAIELKAGSATrPVFGVQPAVVDNE-GHPQPGGTEGNLVITd 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 299 TLKKRARPLIR---------FRTGDIVSFTDEpcACGRTSQRLLGVHGRRDDMLIVRGVNIFPSDVEAIV 359
Cdd:cd17634 445 PWPGQTRTLFGdherfeqtyFSTFKGMYFSGD--GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVL 512
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
310-357 |
2.91e-03 |
|
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: 39.62 E-value: 2.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 500090113 310 FRTGDIVSFTDEpcacGRtsqrlLGVHGRRDDMLIVRGVNIFPSDVEA 357
Cdd:cd17630 207 FTTKDLGELHAD----GR-----LTVLGRADNMIISGGENIQPEEIEA 245
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
276-361 |
5.92e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 39.07 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500090113 276 VEVLDPETGEaVAPGERGEM------VLTTLKKRARPL---IR---FRTGDIVSFTDEPCACgrtsqrllgVHGRRDDML 343
Cdd:PRK06839 328 YELIDENKNK-VEVGEVGELlirgpnVMKEYWNRPDATeetIQdgwLCTGDLARVDEDGFVY---------IVGRKKEMI 397
|
90
....*....|....*...
gi 500090113 344 IVRGVNIFPSDVEAIVRK 361
Cdd:PRK06839 398 ISGGENIYPLEVEQVINK 415
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
310-358 |
6.37e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 38.79 E-value: 6.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500090113 310 FRTGDIvSFTDEpcacgrtsQRLLGVHGRRDDMLIVRGVNIFPSDVEAI 358
Cdd:PRK03640 362 FKTGDI-GYLDE--------EGFLYVLDRRSDLIISGGENIYPAEIEEV 401
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
273-295 |
8.48e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 38.64 E-value: 8.48e-03
|
| |
