|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
37-480 |
0e+00 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 808.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 37 KLACARPLCPPLYAEDP---CCTASAAAVRVRScwpqlglptlVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLL 113
Cdd:cd05938 53 KLGCPVAFLNTNIRSKSllhCFRCCGAKVLVVA----------PELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 114 SEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLG 193
Cdd:cd05938 123 DKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 IVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP 273
Cdd:cd05938 203 IGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPF 353
Cdd:cd05938 283 IRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05938 363 LGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 755503902 434 TVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05938 443 TVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQ 489
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
134-480 |
3.10e-176 |
|
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: 505.35 E-value: 3.10e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05940 80 VVDAALYIYTSGTTGLPKAAIISHRRAWRgGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd05940 160 SNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKdKLLKDVF 372
Cdd:cd05940 240 FGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAATEK-KILRDVF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 373 WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPP 452
Cdd:cd05940 319 KKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPN 398
|
330 340
....*....|....*....|....*...
gi 755503902 453 QALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:cd05940 399 EEFDLSALAAHLEKNLPGYARPLFLRLQ 426
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
76-482 |
6.02e-170 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 495.16 E-value: 6.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 76 LVEFLESLEPDLPALRAmglhLWATGPETNVA--GISNLLSEAADQVDEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPK 151
Cdd:PRK08279 144 LVEAFEEARADLARPPR----LWVAGGDTLDDpeGYEDLAAAAAGAPTTN----PASRSGVTakDTAFYIYTSGTTGLPK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AARISHLKVLQC-QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYI 230
Cdd:PRK08279 216 AAVMSHMRWLKAmGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 231 GELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR-ASWLYKhi 309
Cdd:PRK08279 296 GELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRvPLWLAH-- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 310 fPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAgAPELAKDKLLKDVFWSGDVFFNTGDLLVCDE 389
Cdd:PRK08279 374 -PYAIVKYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYT-DPEASEKKILRDVFKKGDAWFNTGDLMRDDG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 390 QGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLP 469
Cdd:PRK08279 452 FGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLP 531
|
410
....*....|...
gi 755503902 470 PYARPRFLRLQVT 482
Cdd:PRK08279 532 AYAVPLFVRLVPE 544
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
131-479 |
9.95e-144 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 423.76 E-value: 9.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNIMDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd05939 100 DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRiAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVAT 289
Cdd:cd05939 180 FSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSP---FLGYAGAPELAKdK 366
Cdd:cd05939 260 VNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGATNK-K 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAA 446
Cdd:cd05939 339 IARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAA 418
|
330 340 350
....*....|....*....|....*....|...
gi 755503902 447 LAlRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05939 419 IV-DPERKVDLDRFSAVLAKSLPPYARPQFIRL 450
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
136-479 |
2.59e-119 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 360.98 E-value: 2.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05937 88 DPAILIYTSGTTGLPKAAAISWRRTLVtSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY-T 293
Cdd:cd05937 168 FWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 G--RQGAVGRASWLYKHIF--PFSLIRYDVMTGEPIR-NAQGHCMTTSPGEPGLLVA--PVSQQSPFLGYAGAPELAKDK 366
Cdd:cd05937 248 GdfGAGAIGHHGLIRRWKFenQVVLVKMDPETDDPIRdPKTGFCVRAPVGEPGEMLGrvPFKNREAFQGYLHNEDATESK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAA 446
Cdd:cd05937 328 LVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAA 407
|
330 340 350
....*....|....*....|....*....|....*..
gi 755503902 447 LALR----PPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05937 408 ITLEessaVPTEFTKSLLASLARKNLPSYAVPLFLRL 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-479 |
2.19e-74 |
|
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: 242.97 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05934 80 VVDPASILYTSGTTGPPKGVVITHANLTfAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFN- 291
Cdd:cd05934 160 SRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGp 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 --YTGRQGAVGRASWLYKhifpfslIRydvmtgepIRNAQGHcmTTSPGEPG-LLVAPVSQQSPFLGYAGAPElAKDKLL 368
Cdd:cd05934 239 rdEPRRPGSIGRPAPGYE-------VR--------IVDDDGQ--ELPAGEPGeLVIRGLRGWGFFKGYYNMPE-ATAEAM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 KdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGR-AGMAAL 447
Cdd:cd05934 301 R------NGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA--VPDEVGEdEVKAVV 372
|
330 340 350
....*....|....*....|....*....|..
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05934 373 VLRPGETLDPEELFAFCEGQLAYFKVPRYIRF 404
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
137-479 |
3.22e-66 |
|
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: 222.38 E-value: 3.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 137 TCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:COG0318 102 TALILYTSGTTGRPKGVMLTHRNLLaNAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGN-VATFN- 291
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFGV-RIVEGYGLTETSpVVTVNp 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 ---YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLl 368
Cdd:COG0318 261 edpGERRPGSVGRP-------LPGVEVR--------IVDEDGR--ELPPGEVGEIV--VRGPNVMKGYWNDPEATAEAF- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 kdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALA 448
Cdd:COG0318 321 ------RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVV 393
|
330 340 350
....*....|....*....|....*....|.
gi 755503902 449 LRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:COG0318 394 LRPGAELDAEELRAFLRERLARYKVPRRVEF 424
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
136-478 |
7.00e-64 |
|
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: 212.53 E-value: 7.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLaAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPlQILETYGMTEGNVATFNY 292
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsgGAPLPPELLERFEEAPGI-KLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TG-----RQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKL 367
Cdd:cd04433 159 PPdddarKPGSVGRP-------VPGVEVR--------IVDPDGG--ELPPGEIGELV--VRGPSVMKGYWNNPEATAAVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 447
Cdd:cd04433 220 -------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDP-EWGERVVAVV 291
|
330 340 350
....*....|....*....|....*....|.
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd04433 292 VLRPGADLDAEELRAHVRERLAPYKVPRRVV 322
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
75-480 |
8.86e-52 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 185.73 E-value: 8.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 75 TLVEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAAR 154
Cdd:PRK06155 127 ALLAALEAADPGDLPLP----AVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPG---DTAAILYTSGTTGPSKGVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 155 ISHLKvlqcqgFY-------HLCGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF 227
Cdd:PRK06155 200 CPHAQ------FYwwgrnsaEDLEIGADDVLYTTLPLFHTN-ALNAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 QYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNV--ATFNYTGRQGAVGRaswl 305
Cdd:PRK06155 273 YLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLDGYGSTETNFviAVTHGSQRPGSMGR---- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 ykhifpfslirydVMTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFL---GYAGAPElakdkllKDVFWSGDVFFNTG 382
Cdd:PRK06155 348 -------------LAPGFEARVVDEHDQELPDGEPGELL--LRADEPFAfatGYFGMPE-------KTVEAWRNLWFHTG 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 383 DLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRPPQALNLVQLYS 462
Cdd:PRK06155 406 DRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVR 484
|
410
....*....|....*...
gi 755503902 463 HVSENLPPYARPRFLRLQ 480
Cdd:PRK06155 485 HCEPRLAYFAVPRYVEFV 502
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
135-479 |
3.99e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 175.60 E-value: 3.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 135 MDTCLYIFTSGTTGLPKAARISHLKVLQCQgfYHLC---GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFS 211
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAG--RALTerfGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFS 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVA-TF 290
Cdd:PRK13388 228 ASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIvVR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYTGRQGAVGRAswlykhiFPfSLIRYDVMTGEPirnaqghCMTTSPGEPGLLVAP-------VSQQ--SPFLGYAGAPE 361
Cdd:PRK13388 307 EPGTPPGSIGRG-------AP-GVAIYNPETLTE-------CAVARFDAHGALLNAdeaigelVNTAgaGFFEGYYNNPE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDVFWSGDVFFNtgdllvcDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGR 441
Cdd:PRK13388 372 ATAERMRHGMYWSGDLAYR-------DADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE-RVGD 443
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755503902 442 AGMAALALRPPQALNLVQL--YSHVSENLPPYARPRFLRL 479
Cdd:PRK13388 444 QVMAALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRI 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
135-479 |
7.13e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 174.87 E-value: 7.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 135 MDTCLYIFTSGTTGLPKAARISHLKV-----LQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:PRK07867 152 DDLFMLIFTSGTSGDPKAVRCTHRKVasagvMLAQRF----GLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRK 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVAt 289
Cdd:PRK07867 228 FSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIARFARRFG-CVVVDGFGSTEGGVA- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYT--GRQGAVGRAswlykhifPFSLIRYDVMTGEPIRNAQ--GHCMTTSPGEPGLLVApVSQQSPFLGYAGAPELAKD 365
Cdd:PRK07867 306 ITRTpdTPPGALGPL--------PPGVAIVDPDTGTECPPAEdaDGRLLNADEAIGELVN-TAGPGGFEGYYNDPEADAE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLLKDVFWSGDVFFntgdllvCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMA 445
Cdd:PRK07867 377 RMRGGVYWSGDLAY-------RDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP-VVGDQVMA 448
|
330 340 350
....*....|....*....|....*....|....*.
gi 755503902 446 ALALRPPQALNLVQL--YSHVSENLPPYARPRFLRL 479
Cdd:PRK07867 449 ALVLAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRV 484
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
56-406 |
7.46e-43 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 158.63 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 56 TASAAAVRVRSCWPQLGLPTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPgylsaPQNIM 135
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPP-----PPDPD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHL----KVLQCQGFYHLC-GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF 210
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRnlvaNVLSIKRVRPRGfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 211 SA---SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVR--LAVGSGLRPDTWERFLRRFGPlQILETYGMTEG 285
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlvLSGGAPLPPELARRFRELFGG-ALVNGYGLTET 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNY------TGRQGAVGRaswlykhifPFSLIRY---DVMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLGY 356
Cdd:pfam00501 315 TGVVTTPlpldedLRSLGSVGR---------PLPGTEVkivDDETGEPVP----------PGEPGELC--VRGPGVMKGY 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAkdkllKDVFWSGDvFFNTGDLLVCDEQGFLHFHDRTGDTFRWK 406
Cdd:pfam00501 374 LNDPELT-----AEAFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
129-479 |
1.33e-39 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 150.13 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 129 SAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK 207
Cdd:cd05941 83 SEPSLVLDPALILYTSGTTGRPKGVVLTHANLAaNVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQ-----YIGELCRYLVNQPPSK---AECDHKVRLAV-GSG-LRPDTWERFLRRFGpLQIL 277
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMgvptiYTRLLQYYEAHFTDPQfarAAAAERLRLMVsGSAaLPVPTLEEWEAITG-HTLL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTEGNVATFN-YTG--RQGAVGRAswlykhiFPFSLIR-YDVMTGEPirnaqghcmtTSPGEPG-LLVApvsqqSP 352
Cdd:cd05941 242 ERYGMTEIGMALSNpLDGerRPGTVGMP-------LPGVQARiVDEETGEP----------LPRGEVGeIQVR-----GP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 --FLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTG-DTFRWKGENVATTEVAEVLETLDFLQEVN 429
Cdd:cd05941 300 svFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECA 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755503902 430 IYGVTVPGHeGRAGMAALALRPP-QALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05941 374 VIGVPDPDW-GERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLIL 423
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
136-475 |
6.00e-38 |
|
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: 145.78 E-value: 6.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFS 211
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHrnlvANALQIKAWLEDLLEG-DDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQ-----YIGelcryLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTE 284
Cdd:cd05936 205 PIGVLKEIRKHRVTIFPgvptmYIA-----LLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG-VPIVEGYGLTE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 -GNVATFN-YTG--RQGAVGraswlykHIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAP 360
Cdd:cd05936 279 tSPVVAVNpLDGprKPGSIG-------IPLPGTEVK--------IVDDDGE--ELPPGEVGELW--VRGPQVMKGYWNRP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 361 ElAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEG 440
Cdd:cd05936 340 E-ETAEAFVD----G--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDP-YSG 411
|
330 340 350
....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05936 412 EAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPR 446
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
106-471 |
1.07e-35 |
|
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: 139.66 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 106 VAGISNLLSEAADQVDEPVPGYLSAPQNimDTCLYIFTSGTTGLPKAARISH----LKVLQCQGFYHLCgVHQEDVIYLA 181
Cdd:cd05911 119 VLSIEDLLSPTLGEEDEDLPPPLKDGKD--DTAAILYSSGTTGLPKGVCLSHrnliANLSQVQTFLYGN-DGSNDVILGF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 182 LPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLAVGSG-L 259
Cdd:cd05911 196 LPLYHIYG-LFTTLASLLNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPlLDKYDLSSLRVILSGGApL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 260 RPDTWERFLRRFGPLQILETYGMTEGNVATF---NYTGRQGAVGRaswlykhIFPFSLIRYDVMTGepiRNAQGhcmtts 336
Cdd:cd05911 275 SKELQELLAKRFPNATIKQGYGMTETGGILTvnpDGDDKPGSVGR-------LLPNVEAKIVDDDG---KDSLG------ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 337 PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVA 416
Cdd:cd05911 339 PNEPGEIC--VRGPQVMKGYYNNPEATKETFDED----G--WLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELE 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 417 EVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPY 471
Cdd:cd05911 411 AVLLEHPGVADAAVIGIPDE-VSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
96-486 |
1.72e-35 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 139.82 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 96 HLWATGP----ETNVAGISNLLSEAADQVDEPVPgyLSAPqnimDTCLYIFTSGTTGLPKAARISHLKvLQCQGFYHL-- 169
Cdd:PRK08008 136 HICLTRValpaDDGVSSFTQLKAQQPATLCYAPP--LSTD----DTAEILFTSGTTSRPKGVVITHYN-LRFAGYYSAwq 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 170 CGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDH 249
Cdd:PRK08008 209 CALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQH 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 250 KVR-----LAVGSGLRPDtwerFLRRFGpLQILETYGMTEGNVATFNYTG----RQGAVGRASWLYKhifpfslirydvm 320
Cdd:PRK08008 289 CLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYGMTETIVGIIGDRPgdkrRWPSIGRPGFCYE------------- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 321 tgEPIRNAQGHCMttSPGEPG-LLVAPVSQQSPFLGYAGAPElAKDKLLkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRT 399
Cdd:PRK08008 351 --AEIRDDHNRPL--PAGEIGeICIKGVPGKTIFKEYYLDPK-ATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRR 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 400 GDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEgRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK08008 421 CNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRD-EAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEI 499
|
....*...
gi 755503902 480 QVT-SRSC 486
Cdd:PRK08008 500 RKDlPRNC 507
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
134-478 |
3.16e-34 |
|
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: 134.66 E-value: 3.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 134 IMDTCLYIFTSGTTGLPKAARISHLKVLqcqGFYHLCGVHQ----EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd17631 97 FDDLALLMYTSGTTGRPKGAMLTHRNLL---WNAVNALAALdlgpDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVF-----QYigelcrYLVNQPPSKAECDH-KVR-LAVGSGLRPDTWERFLRRFGPlQILETYGM 282
Cdd:cd17631 174 FDPETVLDLIERHRVTSFflvptMI------QALLQHPRFATTDLsSLRaVIYGGAPMPERLLRALQARGV-KFVQGYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TE-GNVATFNYTGRQ----GAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLG 355
Cdd:cd17631 247 TEtSPGVTFLSPEDHrrklGSAGRPV-------FFVEVR--------IVDPDGR--EVPPGEVGEIVV----RGPhvMAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtV 435
Cdd:cd17631 306 YWNRPEATAAAF-------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG--V 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755503902 436 PgHE--GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd17631 377 P-DEkwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
136-475 |
1.87e-32 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 130.51 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqCQGFYHLCGVHQ---EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNL--AASATNITNTYKltpDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAEC-DHKVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTEgnvAT 289
Cdd:cd05926 228 STFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTE---AA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQ--------GAVGRASwlykhifpfslirydvmtGEPIR--NAQGHCMTtsPGEPGLLVapVSQQSPFLGYAGA 359
Cdd:cd05926 304 HQMTSNPlppgprkpGSVGKPV------------------GVEVRilDEDGEILP--PGVVGEIC--LRGPNVTRGYLNN 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHE 439
Cdd:cd05926 362 PEANAEAAFKD----G--WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE-KY 434
|
330 340 350
....*....|....*....|....*....|....*.
gi 755503902 440 GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05926 435 GEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPK 470
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
100-475 |
8.95e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 129.46 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 100 TGPETNVAGISNLLSEAADQVDEPVPGYLSApqniMDTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHLcGVHQED 176
Cdd:COG0365 153 TGADVPMEGDLDWDELLAAASAEFEPEPTDA----DDPLFILYTSGTTGKPKGVVHTHggyLVHAATTAKYVL-DLKPGD 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 177 VIYLALPLYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFqyigelC------RYLVNQPPSKAE 246
Cdd:COG0365 228 VFWCTADIGWATGHSYIVYGPLLNGATVVLyegRPDFpDPGRLWELIEKYGVTVF------FtaptaiRALMKAGDEPLK 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 247 cDH---KVRLA--VGSGLRPDTWERFLRRFGpLQILETYGMTE--GNVATFNYTG--RQGAVGRaswlykhifPFSLIRY 317
Cdd:COG0365 302 -KYdlsSLRLLgsAGEPLNPEVWEWWYEAVG-VPIVDGWGQTEtgGIFISNLPGLpvKPGSMGK---------PVPGYDV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 318 DVM--TGEPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGDLLVCDEQGFL 393
Cdd:COG0365 371 AVVdeDGNPVP----------PGEEGELVIKGPWPGMFRGYWNDPE-----RYRETYFGrfPGWYR-TGDGARRDEDGYF 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 394 HFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVT-VPgHEGRaGMAALA---LRPPQALN--LVQ-LYSHVSE 466
Cdd:COG0365 435 WILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA---AVVgVP-DEIR-GQVVKAfvvLKPGVEPSdeLAKeLQAHVRE 509
|
....*....
gi 755503902 467 NLPPYARPR 475
Cdd:COG0365 510 ELGPYAYPR 518
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
74-475 |
1.36e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 128.38 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 74 PTLVEFLESLEPDLPALRamglHLWATGPETN------VAGISNLLSEAADQVDEPVPGylsapqnIMDTCLYIFTSGTT 147
Cdd:PRK06187 111 SEFVPLLAAILPQLPTVR----TVIVEGDGPAaplapeVGEYEELLAAASDTFDFPDID-------ENDAAAMLYTSGTT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 148 GLPKAARISH----LKVLQCQGFYHLcgvHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHR 223
Cdd:PRK06187 180 GHPKGVVLSHrnlfLHSLAVCAWLKL---SRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPENLLDLIETER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 224 VTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY-------- 292
Cdd:PRK06187 256 VTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTEtSPVVSVLPpedqlpgq 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGHCMTTSPGEPGLLVApvsqQSPFL--GYAGAPELAKDKLLKD 370
Cdd:PRK06187 335 WTKRRSAGRP-------LPGVEAR--------IVDDDGDELPPDGGEVGEIIV----RGPWLmqGYWNRPEATAETIDGG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 371 vfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR 450
Cdd:PRK06187 396 --W-----LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDE-KWGERPVAVVVLK 467
|
410 420
....*....|....*....|....*
gi 755503902 451 PPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06187 468 PGATLDAKELRAFLRGRLAKFKLPK 492
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
71-478 |
1.25e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 125.40 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 71 LGLPTLVEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSE----AADQVDEPVPGYlsAPQNIMDTclyIFTSGT 146
Cdd:PRK07656 107 FVLGLFLGVDYSATTRLPALE----HVVICETEEDDPHTEKMKTFtdflAAGDPAERAPEV--DPDDVADI---LFTSGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 147 TGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT 225
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSnAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERIT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 226 VFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGN-VATFNYTGRQ-----G 297
Cdd:PRK07656 258 VLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtgAASMPVALLERFESELGVDIVLTGYGLSEASgVTTFNRLDDDrktvaG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 298 AVGRAswlykhifpfslirydvMTGEPIRNAQGHCMTTSPGEPG-LLVapvsqQSP--FLGYAGAPELAKDKLlkdvfwS 374
Cdd:PRK07656 338 TIGTA-----------------IAGVENKIVNELGEEVPVGEVGeLLV-----RGPnvMKGYYDDPEATAAAI------D 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 375 GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRPPQ 453
Cdd:PRK07656 390 ADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG--VPDERlGEVGKAYVVLKPGA 467
|
410 420
....*....|....*....|....*
gi 755503902 454 ALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:PRK07656 468 ELTEEELIAYCREHLAKYKVPRSIE 492
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
176-478 |
6.41e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 112.89 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 176 DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV 255
Cdd:PRK07868 647 DTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFI 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 256 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTG-RQGAVGRAswlykhiFPFS----LIRYDVMTGEPIRNAQG 330
Cdd:PRK07868 727 GSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSGaKIGSKGRP-------LPGAgrveLAAYDPEHDLILEDDRG 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 331 HCMTTSPGEPGLLvapvsqqspfLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:PRK07868 800 FVRRAEVNEVGVL----------LARARGPIDPTASVKRGVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPV 869
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTVPGHEgrAGMAALALRPPQALNLVQLYSHVSEnLPPYARPRFLR 478
Cdd:PRK07868 870 YTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAAITAADLTEALAS-LPVGLGPDIVH 934
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
87-475 |
1.25e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 110.86 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 87 LPALRAMGLHLwaTGPETNVAGISNLLSEAA----DQVDEPVPgylsAPQnimDTCLYIFTSGTTGLPKAARISH--LKV 160
Cdd:PRK05605 176 IPALRKARAAL--TGPAPGTVPWETLVDAAIggdgSDVSHPRP----TPD---DVALILYTSGTTGKPKGAQLTHrnLFA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 161 LQCQGFYHLCGV-HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 239
Cdd:PRK05605 247 NAAQGKAWVPGLgDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 240 QPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFGPLqILETYGMTE------GNvaTFNYTGRQGAVGRAswlykhiF 310
Cdd:PRK05605 327 AAEERGVDLSGVRNAF-SGamaLPVSTVELWEKLTGGL-LVEGYGLTEtspiivGN--PMSDDRRPGYVGVP-------F 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 PFSLIRydvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAKDKLLKDvfWsgdvfFNTGDLLVCDEQ 390
Cdd:PRK05605 396 PDTEVR--------IVDPEDPDETMPDGEEGELLVRGPQV--FKGYWNRPEETAKSFLDG--W-----FRTGDVVVMEED 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 391 GFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHEGRAGM-AALALRPPQALNLVQLYSHVSENLP 469
Cdd:PRK05605 459 GFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVG--LPREDGSEEVvAAVVLEPGAALDPEGLRAYCREHLT 536
|
....*.
gi 755503902 470 PYARPR 475
Cdd:PRK05605 537 RYKVPR 542
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
136-475 |
1.90e-24 |
|
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: 105.88 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHlcGVHQEDVIY-LALP--LYHMSGSLLGIvgcLGIGATVVL--K 207
Cdd:cd05972 82 DPALIYFTSGTTGLPKGVLHTHsypLGHIPTAAYWL--GLRPDDIHWnIADPgwAKGAWSSFFGP---WLLGATVFVyeG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHkVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG 285
Cdd:cd05972 157 PRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLVVSAGepLNPEVIEWWRAATG-LPIRDGYGQTET 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTG---RQGAVGRASWLYKhifpFSLIRYDvmtGEPIrnaqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPEl 362
Cdd:cd05972 235 GLTVGNFPDmpvKPGSMGRPTPGYD----VAIIDDD---GREL----------PPGEEGDIAIKLPPPGLFLGYVGDPE- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 aKDKllkdVFWSGDVFFnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQ--EVNIYGVTVPGHEG 440
Cdd:cd05972 297 -KTE----ASIRGDYYL-TGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL-----LEhpAVAEAAVVGSPDPV 365
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755503902 441 RAGM--AALALR----PPQALNLvQLYSHVSENLPPYARPR 475
Cdd:cd05972 366 RGEVvkAFVVLTsgyePSEELAE-ELQGHVKKVLAPYKYPR 405
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-477 |
2.49e-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.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 104.28 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQcQGFY--HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSA 212
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVN-NGYFigERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQ-----YIGELCRylvnqpPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:cd05917 82 LAVLEAIEKEKCTALHgvptmFIAELEH------PDFDKFDlSSLRTGImaGAPCPPELMKRVIEVMNMKDVTIAYGMTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 GNVATFNYTG------RQGAVGRaswlykhIFPFSLIRYDVMTG--EPIRNAQGHCMTTspgepGLLVapvsqqspFLGY 356
Cdd:cd05917 156 TSPVSTQTRTddsiekRVNTVGR-------IMPHTEAKIVDPEGgiVPPVGVPGELCIR-----GYSV--------MKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVP 436
Cdd:cd05917 216 WNDPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VP 287
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 755503902 437 GHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd05917 288 DERyGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYV 329
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-475 |
1.46e-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: 101.29 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 78 EFLESLEPDLPALRAMGLHLWATGPETNVAGISNLlseaADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH 157
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLL----AELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 158 lkvlqcQGFYHLC--------GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SASQFWDDCQKHRVTVFQ 228
Cdd:cd05959 186 ------ADIYWTAelyarnvlGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRPTVFF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 229 YIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTE-GNVATFNYTG--RQGAVGRAS 303
Cdd:cd05959 260 GVPTLYAAMLAAPNLPSRDLSSLRLCVSAGeaLPAEVGERWKARFG-LDILDGIGSTEmLHIFLSNRPGrvRYGTTGKPV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 304 WLYKhifpfslIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvfWsgdvfFNTGD 383
Cdd:cd05959 339 PGYE-------VE--------LRDEDGG--DVADGEPGELY--VRGPSSATMYWNNRDKTRDTFQGE--W-----TRTGD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 384 LLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAgMAALALRP---PQALNLVQL 460
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KAFVVLRPgyeDSEALEEEL 471
|
410
....*....|....*
gi 755503902 461 YSHVSENLPPYARPR 475
Cdd:cd05959 472 KEFVKDRLAPYKYPR 486
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
136-475 |
1.90e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 100.89 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqcqGFY---HLC----GVHQEDVIYLALPLYHMSG--SLLGIVGclgiGATVVL 206
Cdd:PRK07470 164 DPCWFFFTSGTTGRPKAAVLTHGQM----AFVitnHLAdlmpGTTEQDASLVVAPLSHGAGihQLCQVAR----GAATVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KP--KFSASQFWDDCQKHRVTVFQYIGELCRYLVnQPPSKAECDH-KVRLAVGSG---LRPDTwERFLRRFGPLqILETY 280
Cdd:PRK07470 236 LPseRFDPAEVWALVERHRVTNLFTVPTILKMLV-EHPAVDRYDHsSLRYVIYAGapmYRADQ-KRALAKLGKV-LVQYF 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 281 GMTEgnvATFNYT--------------GRQGAVGRASwlykhifpfslirydvmTGE--PIRNAQGHCMttSPGEPGLLV 344
Cdd:PRK07470 313 GLGE---VTGNITvlppalhdaedgpdARIGTCGFER-----------------TGMevQIQDDEGREL--PPGETGEIC 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 345 apVSQQSPFLGYAGAPElAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:PRK07470 371 --VIGPAVFAGYYNNPE-ANAKAFRD-GW-----FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPA 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755503902 425 LQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07470 442 VSEVAVLGVPDPVW-GEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
141-479 |
2.18e-22 |
|
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: 99.91 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHlkvlqcQGFYHLCGVHQEDV------IYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FS 211
Cdd:cd05930 99 IYTSGSTGKPKGVMVEH------RGLVNLLLWMQEAYpltpgdRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEevrKD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNV-A 288
Cdd:cd05930 173 PEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGeaLPPDLVRRWRELLPGARLVNLYGPTEATVdA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFnytgrqgavgraswlykHIFPFSLIRYDVMT-GEPIRNAQ-----GHCMTTSPGEPGLLVapVSQQSPFLGYAGAPEL 362
Cdd:cd05930 251 TY-----------------YRVPPDDEEDGRVPiGRPIPNTRvyvldENLRPVPPGVPGELY--IGGAGLARGYLNRPEL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDT-----FRwkgenVATTEVAEVLETLDFLQEVniygVTVPG 437
Cdd:cd05930 312 TAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQvkirgYR-----IELGEIEAALLAHPGVREA----AVVAR 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 755503902 438 HEGRAGM---AALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd05930 383 EDGDGEKrlvAYVVPDEGGELDEEELRAHLAERLPDYMVPsAFVVL 428
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
110-419 |
2.83e-22 |
|
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: 100.39 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 110 SNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLK-VLQCQGF--YHLCGVHQEDVIYLALPLYH 186
Cdd:cd05904 133 FDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNlIAMVAQFvaGEGSNSDSEDVFLCVLPMFH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 187 MSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFqyigelcrYLVnqPP-----SKAECDHKVRLA----VGS 257
Cdd:cd05904 213 IYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHL--------PVV--PPivlalVKSPIVDKYDLSslrqIMS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 258 G---LRPDTWERFLRRFGPLQILETYGMTE-GNVATFNYT-----GRQGAVGR--ASWLYKHIfpfsliryDVMTGEPIr 326
Cdd:cd05904 283 GaapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApekdrAKYGSVGRlvPNVEAKIV--------DPETGESL- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 327 naqghcmttSPGEPG-LLVapvsqQSPFL--GYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFHDRTGDTF 403
Cdd:cd05904 354 ---------PPNQTGeLWI-----RGPSImkGYLNNPEATAATIDKE----G--WLHTGDLCYIDEDGYLFIVDRLKELI 413
|
330
....*....|....*.
gi 755503902 404 RWKGENVATTEVAEVL 419
Cdd:cd05904 414 KYKGFQVAPAELEALL 429
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
136-451 |
1.17e-21 |
|
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: 97.55 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAaNALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEG-NVATFN 291
Cdd:cd05935 165 ALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQgavgRASWLYKHIFPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDv 371
Cdd:cd05935 244 PPLRP----KLQCLGIP*FGVDARVIDIETGREL----------PPNEVGEIV--VRGPQIFKGYWNRPEETEESFIEI- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 372 fwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALR 450
Cdd:cd05935 307 --KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV--ISVPDERvGEEVKAFIVLR 382
|
.
gi 755503902 451 P 451
Cdd:cd05935 383 P 383
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
112-479 |
3.42e-21 |
|
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: 96.74 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 112 LLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSG- 189
Cdd:cd05922 97 LDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNLLaNARSIAEYLGITADDRALTVLPLSYDYGl 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 190 SLLGIvgCLGIGATVVLKPKFSASQ-FWDDCQKHRVTVFQ---YIGELCRYLVNQPpskAECDHKVRLAVGSGLRPDTWE 265
Cdd:cd05922 174 SVLNT--HLLRGATLVLTNDGVLDDaFWEDLREHGATGLAgvpSTYAMLTRLGFDP---AKLPSLRYLTQAGGRLPQETI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 266 RFLRRFGPL-QILETYGMTEgnvATFNYT--------GRQGAVGRAswlykhiFP---FSLIRYDvmtGEPirnaqghcm 333
Cdd:cd05922 249 ARLRELLPGaQVYVMYGQTE---ATRRMTylpperilEKPGSIGLA-------IPggeFEILDDD---GTP--------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 334 tTSPGEPGLLVApvsqQSPF--LGYAGAP-ELAKDKLLKDVFWsgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:cd05922 307 -TPPGEPGEIVH----RGPNvmKGYWNDPpYRRKEGRGGGVLH-------TGDLARRDEDGFLFIVGRRDRMIKLFGNRI 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTVPGHEgraGMAALALRPPQaLNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPDPLGE---KLALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRV 439
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
136-478 |
9.04e-21 |
|
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: 93.72 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLAL-PLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIInPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd17638 81 ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtgAATVPVELVRRMRSELGFETVLTAYGLTEAGVATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TGRqgavgraswlykhifPFSLIRYDVmtGEPIRNAQGHCmttspGEPGLLVapVSQQSPFLGYAGAPELAKDKLlkdvf 372
Cdd:cd17638 161 PGD---------------DAETVATTC--GRACPGFEVRI-----ADDGEVL--VRGYNVMQGYLDDPEATAEAI----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 373 wSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-GRAGMAALALRP 451
Cdd:cd17638 212 -DADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKAFVVARP 288
|
330 340
....*....|....*....|....*..
gi 755503902 452 PQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd17638 289 GVTLTEEDVIAWCRERLANYKVPRFVR 315
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
139-475 |
1.09e-20 |
|
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: 93.24 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAARISH---LKVLQCQGfyHLCGVHQEDVIYLALPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17633 3 FYIgFTSGTTGLPKAYYRSErswIESFVCNE--DLFNISGEDAILAPGPLSH-SLFLYGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQppskAECDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNVATFNY 292
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGqkLFESTKKKLKNIFPKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 TG---RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGhcmttspGEPGLLVApvsqQSP--FLGYAGAPELAKDKl 367
Cdd:cd17633 156 NQesrPPNSVGR-------PFPNVEIE--------IRNADG-------GEIGKIFV----KSEmvFSGYVRGGFSNPDG- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHEGRaGMAAL 447
Cdd:cd17633 209 -----W-----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP---DARF-GEIAV 274
|
330 340
....*....|....*....|....*...
gi 755503902 448 ALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd17633 275 ALYSGDKLTYKQLKRFLKQKLSRYEIPK 302
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
77-475 |
1.39e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 95.38 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 77 VEFLESLEPDLPALRAMGLHlwATGPETNVAGISNLLSEAADQVDEPVPgylSAPQNimdTCLYIFTSGTTGLPKAARIS 156
Cdd:PRK07788 157 TDLLSALPPDLGRLRAWGGN--PDDDEPSGSTDETLDDLIAGSSTAPLP---KPPKP---GGIVILTSGTTGTPKGAPRP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 157 HLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCR 235
Cdd:PRK07788 229 EPSPLApLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLS 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 236 YLVNQPP---SKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATFnyTGRQ------GAVGRaswl 305
Cdd:PRK07788 308 RILDLGPevlAKYDTSSlKIIFVSGSALSPELATRALEAFGPV-LYNLYGSTEVAFATI--ATPEdlaeapGTVGR---- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 ykhifPFSLIR---YDvMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGapelAKDKLLKDVFWSgdvffnTG 382
Cdd:PRK07788 381 -----PPKGVTvkiLD-ENGNEV----------PRGVVGRIF--VGNGFPFEGYTD----GRDKQIIDGLLS------SG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 383 DLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP--GHEGRagmAALALRPPQALNLVQL 460
Cdd:PRK07788 433 DVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEefGQRLR---AFVVKAPGAALDEDAI 509
|
410
....*....|....*
gi 755503902 461 YSHVSENLPPYARPR 475
Cdd:PRK07788 510 KDYVRDNLARYKVPR 524
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-475 |
1.77e-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: 94.07 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLK-VLQCQGF-YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKF-SA 212
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDpLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYGMTEgNVATF 290
Cdd:cd05919 172 ERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATE-VGHIF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 --NYTG--RQGAVGRaswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDK 366
Cdd:cd05919 250 lsNRPGawRLGSTGR-------PVPGYEIR--------LVDEEGH--TIPPGEEGDLL--VRGPSAAVGYWNNPEKSRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvPGHEGRAGMAA 446
Cdd:cd05919 311 FN-------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAF 382
|
330 340 350
....*....|....*....|....*....|..
gi 755503902 447 LALRPPQALNLV---QLYSHVSENLPPYARPR 475
Cdd:cd05919 383 VVLKSPAAPQESlarDIHRHLLERLSAHKVPR 414
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
136-419 |
1.84e-20 |
|
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: 93.98 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHntLSASIRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQ----YIGELCRYLVNQPPskAECDHKVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVAT 289
Cdd:cd05903 173 KALALMREHGVTFMMgatpFLTDLLNAVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGAK-VCSAYGSTECPGAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTgrQGAVGRASWLYKHIFPfslirydvmtGEPIRNAQGHCMTTSPGEPGLLVApvsqQSP--FLGYAGAPELAKDKL 367
Cdd:cd05903 250 TSIT--PAPEDRRLYTDGRPLP----------GVEIKVVDDTGATLAPGVEGELLS----RGPsvFLGYLDRPDLTADAA 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755503902 368 lkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:cd05903 314 -------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
131-475 |
3.13e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 94.33 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNimDTCLYIFTSGTTGLPKAARISHLKVLQCQgfyhLCGVH-------QEDVIYLALPLYHMSGslLGIVGCLGI--G 201
Cdd:PRK06710 204 PEN--DLALLQYTGGTTGFPKGVMLTHKNLVSNT----LMGVQwlynckeGEEVVLGVLPFFHVYG--MTAVMNLSImqG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 202 ATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV-GSGLRP-DTWERFLRRFGPlQILET 279
Cdd:PRK06710 276 YKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACIsGSAPLPvEVQEKFETVTGG-KLVEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 280 YGMTEGNVAT---FNYTGR-QGAVGrASWLYKHIFPFSLirydvMTGEPIRnaqghcmttsPGEPGLLVapVSQQSPFLG 355
Cdd:PRK06710 355 YGLTESSPVThsnFLWEKRvPGSIG-VPWPDTEAMIMSL-----ETGEALP----------PGEIGEIV--VKGPQIMKG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTV 435
Cdd:PRK06710 417 YWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPD 489
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755503902 436 PgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06710 490 P-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPK 528
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
107-419 |
5.09e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 93.87 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 107 AGISNLLSEAADQvdePVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDVIYLALPL 184
Cdd:PRK07529 187 ARILDFDAELARQ---PGDRLFSGRPiGPDDVAAYFHTGGTTGMPKLAQHTHGnEVANAWLGALLLGLGPGDTVFCGLPL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 185 YHMSGSLLGIVGCLGIGATVVLKPKFSA------SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDhKVRLAV--G 256
Cdd:PRK07529 264 FHVNALLVTGLAPLARGAHVVLATPQGYrgpgviANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS-SLRYALcgA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 257 SGLRPDTWERFLRRFGpLQILETYGMTEGN-VATFNYTG---RQGAVGRAswlykhiFPFSLIRydVMTGEPIRNAQGHC 332
Cdd:PRK07529 343 APLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPDgerRIGSVGLR-------LPYQRVR--VVILDDAGRYLRDC 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 333 mttSPGEPGLLVapVSQQSPFLGYAgapELAKDKLLkdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVAT 412
Cdd:PRK07529 413 ---AVDEVGVLC--IAGPNVFSGYL---EAAHNKGL----WLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDP 480
|
....*..
gi 755503902 413 TEVAEVL 419
Cdd:PRK07529 481 AAIEEAL 487
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
136-478 |
1.97e-19 |
|
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: 91.00 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGF-YHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLAsADRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMTEGNVATFN 291
Cdd:cd05958 178 LLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGeaLPAALHRAWKEATG-IPIIDGIGSTEMFHIFIS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQGAVGRaswlykhifpfslirydvmTGEP-------IRNAQGHcmTTSPGEPGLLVApvsqQSPfLGYAGapeLAk 364
Cdd:cd05958 257 ARPGDARPGA-------------------TGKPvpgyeakVVDDEGN--PVPDGTIGRLAV----RGP-TGCRY---LA- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DKLLKDVFwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGhEGRAGM 444
Cdd:cd05958 307 DKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDES-RGVVVK 383
|
330 340 350
....*....|....*....|....*....|....*..
gi 755503902 445 AALALRP---PQALNLVQLYSHVSENLPPYARPRFLR 478
Cdd:cd05958 384 AFVVLRPgviPGPVLARELQDHAKAHIAPYKYPRAIE 420
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-474 |
2.39e-19 |
|
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: 91.11 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPA--LRAM-------------GLHLWATGPETNVagisnLLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTT 147
Cdd:cd12117 77 LDPELPAerLAFMladagakvlltdrSLAGRAGGLEVAV-----VIDEALDAGPAGNPAVPVSPD---DLAYVMYTSGST 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 148 GLPKAARISHLKVLQ-CQGFYHLcGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHR 223
Cdd:cd12117 149 GRPKGVAVTHRGVVRlVKNTNYV-TLGPDDRVLQTSPL-AFDASTFEIWGALLNGARLVLAPKgtlLDPDALGALIAEEG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 224 VTVFQYIGELCRYLVNQPPskaECDHKVR--LAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGR 301
Cdd:cd12117 227 VTVLWLTAALFNQLADEDP---ECFAGLRelLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 302 ASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSqqspfLGYAGAPELAKDKLLKDVFW 373
Cdd:cd12117 304 GS---------------IPIGRPIANTRVYVLDEDgrpvpPGVPGELYvggDGLA-----LGYLNRPALTAERFVADPFG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 374 SGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVpgHEGRAGMAALA--LRP 451
Cdd:cd12117 364 PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREA---VVVV--REDAGGDKRLVayVVA 438
|
410 420
....*....|....*....|...
gi 755503902 452 PQALNLVQLYSHVSENLPPYARP 474
Cdd:cd12117 439 EGALDAAELRAFLRERLPAYMVP 461
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
141-475 |
4.32e-19 |
|
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: 89.71 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAarishlkVLQCQG--FYHL------CGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd05912 83 MYTSGTTGKPKG-------VQQTFGnhWWSAigsalnLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMTVYLVDKFDA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPlqILETYGMTE--GNVATF 290
Cdd:cd05912 155 EQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCILLGGGPAPKPLLEQCKEKGIP--VYQSYGMTEtcSQIVTL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYT---GRQGAVGRASwlykhiFPFSLirydvmtgePIRNAQGhcmttSPGEPG--LLVAP-VSQqspflGYAGAPELAK 364
Cdd:cd05912 233 SPEdalNKIGSAGKPL------FPVEL---------KIEDDGQ-----PPYEVGeiLLKGPnVTK-----GYLNRPDATE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHE----G 440
Cdd:cd05912 288 E-----SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL-----LSHPAIKEAGVVGIPddkwG 355
|
330 340 350
....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPqaLNLVQLYSHVSENLPPYARPR 475
Cdd:cd05912 356 QVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPK 388
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
125-490 |
9.33e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 89.56 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 125 PGYLSAPQNIMDtclYIFTSGTTGLPKAARISHLKVlQCQGFYHLC--GVHQEDVIYLALPLYHMSGSLLGIVGCLGIGA 202
Cdd:PRK06145 142 PQAAVAPTDLVR---LMYTSGTTDRPKGVMHSYGNL-HWKSIDHVIalGLTASERLLVVGPLYHVGAFDLPGIAVLWVGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 203 TVVLKPKFSASQFWDDCQKHRVTVFQYIG-ELCRYLVNQPPSKAECDhKVRLAVGSGLRpdTWERFLRRFGPL----QIL 277
Cdd:PRK06145 218 TLRIHREFDPEAVLAAIERHRLTCAWMAPvMLSRVLTVPDRDRFDLD-SLAWCIGGGEK--TPESRIRDFTRVftraRYI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTE---GNvaTFNYTGRQ----GAVGRAswlYKHIfpfslirydvmtgePIRNAQGHCMTTSPGEPG--LLVAPVS 348
Cdd:PRK06145 295 DAYGLTEtcsGD--TLMEAGREiekiGSTGRA---LAHV--------------EIRIADGAGRWLPPNMKGeiCMRGPKV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 349 QQspflGYAGAPELAKDKLLKDVFWSGDVFFntgdllvCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEV 428
Cdd:PRK06145 356 TK----GYWKDPEKTAEAFYGDWFRSGDVGY-------LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEA 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 429 NIYGVtvpgHEGRAG---MAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQvtsRSCP-NPS 490
Cdd:PRK06145 425 AVIGV----HDDRWGeriTAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVR---DELPrNPS 483
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
106-474 |
1.24e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 88.87 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 106 VAGISNLLSEAADQVDEPVPgyLSAPQNIMDTCLYIFTSGTTGLPKAarishlkVLQCQGfYHL---------CGVHQED 176
Cdd:PRK03640 114 IPGISVKFAELMNGPKEEAE--IQEEFDLDEVATIMYTSGTTGKPKG-------VIQTYG-NHWwsavgsalnLGLTEDD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 177 VIYLALPLYHMSG-SLLgiVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPsKAECDHKVR-LA 254
Cdd:PRK03640 184 CWLAAVPIFHISGlSIL--MRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLERLG-EGTYPSSFRcML 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 255 VGSGLRP-DTWERFLRRFGPlqILETYGMTE--GNVATFNYTGRQGAVGRASwlyKHIFPFSL-IRYDVMTGEPirNAQG 330
Cdd:PRK03640 261 LGGGPAPkPLLEQCKEKGIP--VYQSYGMTEtaSQIVTLSPEDALTKLGSAG---KPLFPCELkIEKDGVVVPP--FEEG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 331 HCMTTSPGepgllVAPvsqqspflGYagapeLAKDKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENV 410
Cdd:PRK03640 334 EIVVKGPN-----VTK--------GY-----LNREDATRETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 411 ATTEVAEVLETLDFLQEVNIYGVTvpghEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK03640 394 YPAEIEEVLLSHPGVAEAGVVGVP----DDKWGQVPVAfVVKSGEVTEEELRHFCEEKLAKYKVP 454
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
75-456 |
2.75e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 88.01 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 75 TLVE---FLESLEPDL--------PALRAMGLHLWATGPET-NVAGISNLLSEAADQVDEPVPgylsAPQNIMDTCLYIF 142
Cdd:PRK07514 88 TLAEldyFIGDAEPALvvcdpanfAWLSKIAAAAGAPHVETlDADGTGSLLEAAAAAPDDFET----VPRGADDLAAILY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 143 TSGTTGLPKAARISH------LKVL-QCQGFyhlcgvHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:PRK07514 164 TSGTTGRSKGAMLSHgnllsnALTLvDYWRF------TPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDdcQKHRVTVFQ-----YIgelcRYLVNQPPSKAECDHkVRLAV-GSG-LRPDTWERFLRRFGpLQILETYGMTEGNVA 288
Cdd:PRK07514 238 LA--LMPRATVMMgvptfYT----RLLQEPRLTREAAAH-MRLFIsGSApLLAETHREFQERTG-HAILERYGMTETNMN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFN-YTG--RQGAVGraswlykhiFPF---SLIRYDVMTGEPIrnaqghcmttSPGEPGLLvaPVSQQSPFLGYAGAPEL 362
Cdd:PRK07514 310 TSNpYDGerRAGTVG---------FPLpgvSLRVTDPETGAEL----------PPGEIGMI--EVKGPNVFKGYWRMPEK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRA 442
Cdd:PRK07514 369 TAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF-GEG 441
|
410
....*....|....
gi 755503902 443 GMAALALRPPQALN 456
Cdd:PRK07514 442 VTAVVVPKPGAALD 455
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
142-433 |
3.78e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 87.80 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSllgIVGCL-----GIGATVVLKPKfSA 212
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHrnmlANLEQAKAAYGPLLHPGKELVVTALPLYHIFAL---TVNCLlfielGGQNLLITNPR-DI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKaECD-HKVRLAVGSGLR-----PDTWERFLRRFgplqILETYGMTEGN 286
Cdd:PRK08974 289 PGFVKELKKYPFTAITGVNTLFNALLNNEEFQ-ELDfSSLKLSVGGGMAvqqavAERWVKLTGQY----LLEGYGLTECS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 ----VATFNYTGRQGAVGraswlykhiFPFSlirydvMTGEPIRNAQGHcmTTSPGEPGLLVAPVSQQspFLGYAGAPEl 362
Cdd:PRK08974 364 plvsVNPYDLDYYSGSIG---------LPVP------STEIKLVDDDGN--EVPPGEPGELWVKGPQV--MLGYWQRPE- 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 363 AKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:PRK08974 424 ATDEVIKDGWLA------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
78-460 |
4.62e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.42 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 78 EFLESLEPDLPALRamglHLWATGPETNVaGISNLLSEAADQVDEPVPGYLSAPQ-NIMDTCLYIFTSGTTGLPKAARIS 156
Cdd:PRK13295 144 AMARRLRPELPALR----HVVVVGGDGAD-SFEALLITPAWEQEPDAPAILARLRpGPDDVTQLIYTSGTTGEPKGVMHT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 157 HLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTvFQ-----YI 230
Cdd:PRK13295 219 ANTLMANIVPYaERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT-FTmastpFL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 231 GELCRYLVNQPPSKAECdhKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGNVATFNYTGRqgAVGRASWLYKHIF 310
Cdd:PRK13295 298 TDLTRAVKESGRPVSSL--RTFLCAGAPIPGALVERARAALG-AKIVSAWGMTENGAVTLTKLDD--PDERASTTDGCPL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 PFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDkllkdvfwSGDVFFNTGDLLVCDEQ 390
Cdd:PRK13295 373 PGVEVR--------VVDADGA--PLPAGQIGRLQ--VRGCSNFGGYLKRPQLNGT--------DADGWFDTGDLARIDAD 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 391 GFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPghEGRAGMAALA---LRPPQALNLVQL 460
Cdd:PRK13295 433 GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI--VAYP--DERLGERACAfvvPRPGQSLDFEEM 501
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
74-475 |
5.84e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 86.91 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 74 PTLVEFLESLEPDLPALRAMGLHLWATG-PETNVAGISNLLSEAADQVDEPVPgylsapqNIMDTCLYIFTSGTTGLPKA 152
Cdd:PRK08316 116 PALAPTAEAALALLPVDTLILSLVLGGReAPGGWLDFADWAEAGSVAEPDVEL-------ADDDLAQILYTSGTESLPKG 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 153 ARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVF---- 227
Cdd:PRK08316 189 AMLTHRALIaEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAERITSFfapp 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 -QYIGelcryLVNQPpskaECDhKVRLavgSGLR---------P-DTWERFLRRFGPLQILETYGMTE-GNVATF----N 291
Cdd:PRK08316 269 tVWIS-----LLRHP----DFD-TRDL---SSLRkgyygasimPvEVLKELRERLPGLRFYNCYGQTEiAPLATVlgpeE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTGRQGAVGRASwlykhIFPFSLIRYDvmTGEPIrnaqghcmttSPGEPGLLVApvsqQSPFL--GYAGAPELAKDkllk 369
Cdd:PRK08316 336 HLRRPGSAGRPV-----LNVETRVVDD--DGNDV----------APGEVGEIVH----RSPQLmlGYWDDPEKTAE---- 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 370 dVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALAL 449
Cdd:PRK08316 391 -AFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP-KWIEAVTAVVVP 466
|
410 420
....*....|....*....|....*.
gi 755503902 450 RPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK08316 467 KAGATVTEDELIAHCRARLAGFKVPK 492
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
129-398 |
1.37e-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: 85.85 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 129 SAPQNIMDTCLYIFTSGTTGLPKAARISHLKVL----QCQGFYHLcgvHQEDVIYLALPLYHMSGSLLGIVGCLGIGATV 204
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanveQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 VLKPK-FSASQFWDDCQKHRVTVFQYIGELCRYLVNQppSKAECDHKVRLAV--GSGLRPDTWERFLRRFGpLQILETYG 281
Cdd:cd05909 218 VFHPNpLDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEG----NVATFNYTGRQGAVGRaswlykhifPFSLIRY---DVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFL 354
Cdd:cd05909 295 TTECspviSVNTPQSPNKEGTVGR---------PLPGMEVkivSVETHEEV----------PIGEGGLLL--VRGPNVML 353
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755503902 355 GYAGAPElakdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDR 398
Cdd:cd05909 354 GYLNEPE-------LTSFAFGDGWYDTGDIGKIDGEGFLTITGR 390
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
136-447 |
3.00e-17 |
|
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: 84.57 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPkfSASQ 214
Cdd:cd05907 88 DLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAET 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHK---VRLAVGSGLR----------PDTwERFLRRFGpLQILETYG 281
Cdd:cd05907 166 LLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKrklFDLAVGGRLRfaasggaplpAEL-LHFFRALG-IPVYEGYG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTE-GNVATFNYTGRQ--GAVGRaswlykhifpfslirydVMTGEPIR-NAQGHCMTTSPgepgllvapvsqqSPFLGYA 357
Cdd:cd05907 244 LTEtSAVVTLNPPGDNriGTVGK-----------------PLPGVEVRiADDGEILVRGP-------------NVMLGYY 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 358 GAPELAKDKLLKDVfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATTEVAEVLETLDFLQEVNIYGvtvp 436
Cdd:cd05907 294 KNPEATAEALDADG-W-----LHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVIG---- 363
|
330
....*....|.
gi 755503902 437 ghEGRAGMAAL 447
Cdd:cd05907 364 --DGRPFLVAL 372
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
102-477 |
3.01e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 84.83 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 102 PETNVAGISNLLSEAADQVdEPVPGYLSAPQNIMdtclyiFTSGTTGLPKAARISHLKvLQCQGFYHLCGVH---QEDVI 178
Cdd:PRK07786 148 SDDSVLGYEDLLAEAGPAH-APVDIPNDSPALIM------YTSGTTGRPKGAVLTHAN-LTGQAMTCLRTNGadiNSDVG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 179 YLALPLYHMSGslLGIVGC-LGIGATVVLKP--KFSASQFWDDCQKHRVT-VFQYIGELCRYLVNQPPSKAECDHKVrLA 254
Cdd:PRK07786 220 FVGVPLFHIAG--IGSMLPgLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQARPRDLALRV-LS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 255 VGSGLRPDTwerFLRR----FGPLQILETYGMTEGNVATFNYTG-----RQGAVGRaswlykhIFPFSLIRY--DVMTGE 323
Cdd:PRK07786 297 WGAAPASDT---LLRQmaatFPEAQILAAFGQTEMSPVTCMLLGedairKLGSVGK-------VIPTVAARVvdENMNDV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 324 PirnaqghcmttsPGEPGLLV--APVSQQspflGYAGAPELAkdkllKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGD 401
Cdd:PRK07786 367 P------------VGEVGEIVyrAPTLMS----GYWNNPEAT-----AEAFAGG--WFHSGDLVRQDEEGYVWVVDRKKD 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 402 TFRWKGENVATTEVAEVLETLDFLQEVNIYGVTvpgHE--GRAGMAALALRPPQA-LNLVQLYSHVSENLPPYARPRFL 477
Cdd:PRK07786 424 MIISGGENIYCAEVENVLASHPDIVEVAVIGRA---DEkwGEVPVAVAAVRNDDAaLTLEDLAEFLTDRLARYKHPKAL 499
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
141-477 |
3.25e-17 |
|
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: 83.09 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQ-GFYHLCGVHQEDVIYLALPLYHMSG-SLLGIVGCLGiGATVVLkPKFSASQFWDD 218
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIAANlQLIHAMGLTEADVYLNMLPLFHIAGlNLALATFHAG-GANVVM-EKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 219 CQKHRVTVFqyiGELcrylvnqPP---SKAECDHKVRLAVGSgLR-------PDTWERFLRRfGPLQILETYGMTE-GNV 287
Cdd:cd17637 84 IEEEKVTLM---GSF-------PPilsNLLDAAEKSGVDLSS-LRhvlgldaPETIQRFEET-TGATFWSLYGQTEtSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFN-YTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIRnaqghcmttsPGEPGLLVApvsqQSP--FLGYAGAPELAK 364
Cdd:cd17637 152 VTLSpYRERPGSAGRPG-------PLVRVRIVDDNDRPVP----------AGETGEIVV----RGPlvFQGYWNLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWK--GENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRA 442
Cdd:cd17637 211 Y-----TFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIGVPDP-KWGEG 282
|
330 340 350
....*....|....*....|....*....|....*
gi 755503902 443 GMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17637 283 IKAVCVLKPGATLTADELIEFVGSRIARYKKPRYV 317
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
136-477 |
4.00e-17 |
|
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: 84.47 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH---LKVLQCQGFYHLCgvhQEDVIYLALP----LYHMSGSLLG--IVGClgigATVVL 206
Cdd:cd05970 186 DILLVYFSSGTTGMPKMVEHDFtypLGHIVTAKYWQNV---REGGLHLTVAdtgwGKAVWGKIYGqwIAGA----AVFVY 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 K-PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDhKVRLAVGSG--LRPDTWERFLRRFGpLQILETYGMT 283
Cdd:cd05970 259 DyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLS-SLRYCTTAGeaLNPEVFNTFKEKTG-IKLMEGFGQT 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 284 EGNVATFNYTG---RQGAVGRASWLYkhifPFSLIRYD---VMTGEpirnaQGH-CMTTSPGEP-GLlvapvsqqspFLG 355
Cdd:cd05970 337 ETTLTIATFPWmepKPGSMGKPAPGY----EIDLIDREgrsCEAGE-----EGEiVIRTSKGKPvGL----------FGG 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDkllkdVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTV 435
Cdd:cd05970 398 YYKDAEKTAE-----VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPD 470
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 755503902 436 PgHEGRAGMAALAL----RPPQALNlVQLYSHVSENLPPYARPRFL 477
Cdd:cd05970 471 P-IRGQVVKATIVLakgyEPSEELK-KELQDHVKKVTAPYKYPRIV 514
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-472 |
4.93e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 82.91 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL------KP 208
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSnEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN-V 287
Cdd:cd05944 83 PGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVELRARFEDATG-LPVVEGYGLTEATcL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTG---RQGAVGRAswlykhiFPFSLIRYDVMTGEPirNAQGHCmttSPGEpgllVAPVSQQSPflgyaGAPELAK 364
Cdd:cd05944 162 VAVNPPDgpkRPGSVGLR-------LPYARVRIKVLDGVG--RLLRDC---APDE----VGEICVAGP-----GVFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 365 DKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGM 444
Cdd:cd05944 221 YTEGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDA-HAGELPV 299
|
330 340
....*....|....*....|....*...
gi 755503902 445 AALALRPPQALNLVQLYSHVSENLPPYA 472
Cdd:cd05944 300 AYVQLKPGAVVEEEELLAWARDHVPERA 327
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
38-475 |
5.60e-17 |
|
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: 84.17 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 38 LACAR--PLCPPLYAEdpcCTASAAAVRVRSCWPQLgLPTLVEFLESLEP-DLPALRAMGLHLWATGPETNVA----GIS 110
Cdd:cd17634 127 LACARigAVHSVIFGG---FAPEAVAGRIIDSSSRL-LITADGGVRAGRSvPLKKNVDDALNPNVTSVEHVIVlkrtGSD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 111 NLLSEAAD-----QVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLCGVHQEDVIYLALP 183
Cdd:cd17634 203 IDWQEGRDlwwrdLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTAD 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 184 LYHMSGSLLGIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE----CDHKVRLAV 255
Cdd:cd17634 283 VGWVTGHSYLLYGPLACGATTLLyegVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrSSLRILGSV 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 256 GSGLRPDTWERFLRRFGPLQ--ILETYGMTEgnVATFNYTGRQGAVGRASWlyKHIFPFSLIRYDVMtgepirNAQGHcm 333
Cdd:cd17634 363 GEPINPEAYEWYWKKIGKEKcpVVDTWWQTE--TGGFMITPLPGAIELKAG--SATRPVFGVQPAVV------DNEGH-- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 334 TTSPGEPGLLVAPVSQQSPFLGYAGAPelakDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATT 413
Cdd:cd17634 431 PQPGGTEGNLVITDPWPGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTA 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 414 EVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALR----PPQALNlVQLYSHVSENLPPYARPR 475
Cdd:cd17634 507 EIESVLVAHPKVAEAAVVGIPHA-IKGQAPYAYVVLNhgvePSPELY-AELRNWVRKEIGPLATPD 570
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
112-395 |
1.32e-16 |
|
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: 81.93 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 112 LLSEAADQVDEPVPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGS 190
Cdd:TIGR01733 100 ELAALDDAPAPPPPDAPSGPD---DLAYVIYTSGSTGRPKGVVVTHRSLVNlLAWLARRYGLDPDDRV-LQFASLSFDAS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 191 LLGIVGCLGIGATVVL------KPKFSASQFWDDcqKHRVTVFQ---YIGELCrylvnqPPSKAECDHKVRLAVGSG--L 259
Cdd:TIGR01733 176 VEEIFGALLAGATLVVppedeeRDDAALLAALIA--EHPVTVLNltpSLLALL------AAALPPALASLRLVILGGeaL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 260 RPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWlykhifpfslirydVMTGEPIRNAQ-----GHCMT 334
Cdd:TIGR01733 248 TPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPRESP--------------VPIGRPLANTRlyvldDDLRP 313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 335 TSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGD--VFFNTGDLLVCDEQGFLHF 395
Cdd:TIGR01733 314 VPVGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEF 374
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
136-434 |
2.76e-16 |
|
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: 80.38 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANktffavPDILQKEGL----NWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRP-DTWERFLRRFGPLQILETYGMTEGNVA 288
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiAADVRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFNYTGRQ----GAVGraswlykHIFP---FSLIRYDVMTGepIRNAQGHCMTTSPGEpgllvapvsqqspFLGYAGAPE 361
Cdd:cd17635 158 LCLPTDDDsieiNAVG-------RPYPgvdVYLAATDGIAG--PSASFGTIWIKSPAN-------------MLGYWNNPE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 362 LAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVT 434
Cdd:cd17635 216 RTAEVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS 281
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
38-474 |
7.94e-16 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 80.32 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 38 LACAR------PLCPPLYAEDPCCTASAAAVRVrscwpqlglpTLVEFLESLEPDLPALRAMGLHLWATGPETNVAGIsn 111
Cdd:PRK05852 86 LAASRadlvvvPLDPALPIAEQRVRSQAAGARV----------VLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGT-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 112 lLSEAADQVDEPVPgYLSAPQNIM-DTCLYIFTSGTTGLPKAARISHLKVLQ-----CQGFyhlcGVHQEDVIYLALPLY 185
Cdd:PRK05852 154 -LSVHLDAATEPTP-ATSTPEGLRpDDAMIMFTGGTTGLPKMVPWTHANIASsvraiITGY----RLSPRDATVAVMPLY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 186 HMSGSLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA--ECDHKVRL--AVGSGL 259
Cdd:PRK05852 228 HGHGLIAALLATLASGGAVLLpaRGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPsgRKPAALRFirSCSAPL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 260 RPDTWERFLRRFGPlQILETYGMTEG--NVATFNYTGRQ---------GAVGRAswlykhifpfslirydvmTGEPIRNA 328
Cdd:PRK05852 308 TAETAQALQTEFAA-PVVCAFGMTEAthQVTTTQIEGIGqtenpvvstGLVGRS------------------TGAQIRIV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 329 QGHCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:PRK05852 369 GSDGLPLPAGAVGEVW--LRGTTVVRGYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGE 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 409 NVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVFGVPDQLY-GEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIP 504
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
136-433 |
8.85e-16 |
|
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: 80.25 E-value: 8.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH-------LKVLQCQGFYHlcGVHqEDVIYLaLPLYHMSGSLLGIVGCLGIGATVVLKP 208
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQraaesrvLFMSTQAGLRH--GRH-NVVLGL-MPLYHVIGFFAVLVAALALDGTYVVVE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDDCQKHRVTVFQYIGELCRYLVN---QPPSKAECDHKVRLAvGSGLrPDTWERFLRRFGPLQILETYGMTEG 285
Cdd:cd05923 227 EFDPADALKLIEQERVTSLFATPTHLDALAAaaeFAGLKLSSLRHVTFA-GATM-PDAVLERVNQHLPGEKVNIYGTTEA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTGRQGAVGRASWlykhifpFSLIRYDVMTGEPIRNAqghcmttSPGEPGLLVAPVSQQSPFLGYAGAPELAKD 365
Cdd:cd05923 305 MNSLYMRDARTGTEMRPGF-------FSEVRIVRIGGSPDEAL-------ANGEEGELIVAAAADAAFTGYLNQPEATAK 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 366 KLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV 433
Cdd:cd05923 371 KLQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
142-479 |
2.01e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 79.05 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVLQCQGFY-HLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSASQFWDDC 219
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILNNGYFVaESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYpNEAFDPLATLQAV 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 QKHRVTVFQ-----YIGELcrylvnQPPSKAECD-HKVRLAV--GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFN 291
Cdd:PRK12583 288 EEERCTALYgvptmFIAEL------DHPQRGNFDlSSLRTGImaGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQ 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 YTG------RQGAVGRaswlykhifpfSLIRYDVmtgePIRNAQGHcmTTSPGEPGLLVapVSQQSPFLGYAGAPELAKD 365
Cdd:PRK12583 362 TTAaddlerRVETVGR-----------TQPHLEV----KVVDPDGA--TVPRGEIGELC--TRGYSVMKGYWNNPEATAE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMA 445
Cdd:PRK12583 423 SI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKY-GEEIVA 495
|
330 340 350
....*....|....*....|....*....|....
gi 755503902 446 ALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK12583 496 WVRLHPGHAASEEELREFCKARIAHFKVPRYFRF 529
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
136-398 |
2.02e-15 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 79.97 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMsgslLGIVG------CLGIGATVVLKP 208
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILsNIEQISDVFNLRNDDVILSSLPFFHS----FGLTVtlwlplLEGIKVVYHPDP 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 kFSASQFWDDCQKHRVTVFQYIGELCR-YLVNQPPSKAECDhKVRLAVgSG---LRPDTWERFLRRFGpLQILETYGMTE 284
Cdd:PRK08633 859 -TDALGIAKLVAKHRATILLGTPTFLRlYLRNKKLHPLMFA-SLRLVV-AGaekLKPEVADAFEEKFG-IRILEGYGATE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 GN-VATFN-----------YTG-RQGAVGRAswlykhiFPFSLIR-YDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQ 350
Cdd:PRK08633 935 TSpVASVNlpdvlaadfkrQTGsKEGSVGMP-------LPGVAVRiVDPETFEEL----------PPGEDGLIL--IGGP 995
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755503902 351 SPFLGYAGAPELAKdKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDR 398
Cdd:PRK08633 996 QVMKGYLGDPEKTA-EVIKDIDGIG--WYVTGDKGHLDEDGFLTITDR 1040
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
141-475 |
2.04e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 79.03 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKvlqcqGFYHLCGV------HQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:PRK13382 202 LLTSGTTGTPKGARRSGPG-----GIGTLKAIldrtpwRAEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRRRFDPEA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPP---SKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTE-GNVAT 289
Cdd:PRK13382 276 TLDLIDRHRATGLAVVPVMFDRIMDLPAevrNRYSGRSlRFAAASGSRMRPDVVIAFMDQFGDV-IYNNYNATEaGMIAT 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNYTGRQGA---VGRASwlykhifpfslirydvmTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFLGYagAPELAKDk 366
Cdd:PRK13382 355 ATPADLRAApdtAGRPA-----------------EGTEIRILDQDFREVPTGEVGTIF--VRNDTQFDGY--TSGSTKD- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 llkdvFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAA 446
Cdd:PRK13382 413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQY-GQRLAAF 484
|
330 340
....*....|....*....|....*....
gi 755503902 447 LALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK13382 485 VVLKPGASATPETLKQHVRDNLANYKVPR 513
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
128-474 |
6.05e-15 |
|
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: 77.10 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 128 LSAPQNIMDTCLYIFTSGTTGLPKAARISH-------LKVLQCQGFYhlcgvhQEDVIYLALPLYHMSGslLGIV-GCLG 199
Cdd:TIGR01923 104 LSASFNMDQIATLMFTSGTTGKPKAVPHTFrnhyasaVGSKENLGFT------EDDNWLLSLPLYHISG--LSILfRWLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPKFSasQFWDDCQKHRVTVFQYI-GELCRYLvnQPPSKAECDHKVRLavGSGLRPDTWERFLRRFGpLQILE 278
Cdd:TIGR01923 176 EGATLRIVDKFN--QLLEMIANERVTHISLVpTQLNRLL--DEGGHNENLRKILL--GGSAIPAPLIEEAQQYG-LPIYL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 279 TYGMTE--GNVATFN--YTGRQGAVGRASwlykhifPFSLIRYDVmtgePIRNAQGHCMTTSPGepgllvapvsqqsPFL 354
Cdd:TIGR01923 249 SYGMTEtcSQVTTATpeMLHARPDVGRPL-------AGREIKIKV----DNKEGHGEIMVKGAN-------------LMK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 355 GYAGAPELAkdKLLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniygVT 434
Cdd:TIGR01923 305 GYLYQGELT--PAFEQQGW-----FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEA----VV 373
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755503902 435 VPGHEGRAGMAALA-LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:TIGR01923 374 VPKPDAEWGQVPVAyIVSESDISQAKLIAYLTEKLAKYKVP 414
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
82-419 |
1.69e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 76.32 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 82 SLEPDLPALRAMGLhLWATGPETNVAGISNLLSEAadqvdEPvpgyLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLK 159
Cdd:PRK06087 142 PLQNQLPQLQQIVG-VDKLAPATSSLSLSQIIADY-----EP----LTTAITTHgdELAAVLFTSGTEGLPKGVMLTHNN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 160 VLQCQGFYhLCGVH--QEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVT----VFQYIGEL 233
Cdd:PRK06087 212 ILASERAY-CARLNltWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTcmlgATPFIYDL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 234 CRYLVNQPPSKAECdhKVRLAVGSGLRPDTWERFLRRfgPLQILETYGMTEGNVATF----NYTGRQGAV-GRAswlykh 308
Cdd:PRK06087 291 LNLLEKQPADLSAL--RFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESSPHAVvnldDPLSRFMHTdGYA------ 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 309 ifpfslirydvMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQspFLGYAGAPELAkDKLLKDVFWsgdvfFNTGDLLVCD 388
Cdd:PRK06087 361 -----------AAGVEIKVVDEARKTLPPGCEGEEASRGPNV--FMGYLDEPELT-ARALDEEGW-----YYSGDLCRMD 421
|
330 340 350
....*....|....*....|....*....|.
gi 755503902 389 EQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK06087 422 EAGYIKITGRKKDIIVRGGENISSREVEDIL 452
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
142-480 |
1.81e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 76.07 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQE--DVIYLALPLYHM----SGSL--LGIVGClgigATVVLKPK 209
Cdd:PRK08751 215 YTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTGKLEEgcEVVITALPLYHIfaltANGLvfMKIGGC----NHLISNPR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 fSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpSKAECDH---KVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTEGN 286
Cdd:PRK08751 291 -DMPGFVKELKKTRFTAFTGVNTLFNGLLNTP-GFDQIDFsslKMTLGGGMAVQRSVAERWKQVTG-LTLVEAYGLTETS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 VATFnytgrqgavgraswlykhIFPFSLIRYDVMTGEPI-------RNAQGHCMTTspGEPGLLVAPVSQQspFLGYAGA 359
Cdd:PRK08751 368 PAAC------------------INPLTLKEYNGSIGLPIpstdaciKDDAGTVLAI--GEIGELCIKGPQV--MKGYWKR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE 439
Cdd:PRK08751 426 PEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEK 497
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755503902 440 GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:PRK08751 498 SGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFR 538
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
128-476 |
3.24e-14 |
|
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: 75.16 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 128 LSAPQNImdtcLY-IFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQEdvIYLALPLYHMSGSLLG-------IVGCLG 199
Cdd:cd17644 102 LTQPENL----AYvIYTSGSTGKPKGVMIEHQSLVN-----LSHGLIKE--YGITSSDRVLQFASIAfdvaaeeIYVTLL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPK---FSASQFWDDCQKHRVTVFQYIGELCRYLVNQ-PPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGP 273
Cdd:cd17644 171 SGATLVLRPEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLElLLSTIDLPSSLRLVIvgGEAVQPELVRQWQKNVGN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 L-QILETYGMTEGNVATFnytgrqgavgraswLYKHIFPFSLIRYDVMTGEPIRNAQGHCM-----TTSPGEPG-LLVAP 346
Cdd:cd17644 251 FiQLINVYGPTEATIAAT--------------VCRLTQLTERNITSVPIGRPIANTQVYILdenlqPVPVGVPGeLHIGG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 347 VSQQSpflGYAGAPELAKDKLLKDVFWS--GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd17644 317 VGLAR---GYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 425 LQEvniygVTVPGHEGRAG----MAALALRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17644 394 VKT-----AVVIVREDQPGnkrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSA 444
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
136-411 |
6.29e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 74.75 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGiVGCLGIGATVVlkpkFSAS- 213
Cdd:COG1022 184 DLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLSFLPLAHVFERTVS-YYALAAGATVA----FAESp 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 -QFWDDCQKHRVTVF-------------------------------------QYIgelCRYLVNQPPSKAE------CD- 248
Cdd:COG1022 259 dTLAEDLREVKPTFMlavprvwekvyagiqakaeeagglkrklfrwalavgrRYA---RARLAGKSPSLLLrlkhalADk 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 249 ---HKVRLAVG-------SG---LRPDTwERFLRRFGpLQILETYGMTE-GNVATFNYTGRQ--GAVGRAswlykhiFPF 312
Cdd:COG1022 336 lvfSKLREALGgrlrfavSGgaaLGPEL-ARFFRALG-IPVLEGYGLTEtSPVITVNRPGDNriGTVGPP-------LPG 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 313 SLIRydvmtgepIrnaqghcmttspGEPG-LLVapvsqQSP--FLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDE 389
Cdd:COG1022 407 VEVK--------I------------AEDGeILV-----RGPnvMKGYYKNPEATAEAFDAD----G--WLHTGDIGELDE 455
|
330 340
....*....|....*....|....*
gi 755503902 390 QGFLHFHDRTGDTFrwK---GENVA 411
Cdd:COG1022 456 DGFLRITGRKKDLI--VtsgGKNVA 478
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
139-479 |
6.73e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 74.07 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWD 217
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQtAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 DCQKHRVTVFQYIG--ELCRYLVNQPP-SKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNVATFNY- 292
Cdd:PRK09088 219 RLGDPALGITHYFCvpQMAQAFRAQPGfDAAALRHLTALFTGGAPHAAEDILGWLDDG-IPMVDGFGMSEaGTVFGMSVd 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 293 ----TGRQGAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPG--LLVAPvsqqSPFLGYAGAPELAKDK 366
Cdd:PRK09088 298 cdviRAKAGAAGIPT-------PTVQTR--------VVDDQGN--DCPAGVPGelLLRGP----NLSPGYWRRPQATARA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 367 LlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAA 446
Cdd:PRK09088 357 F------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADA-QWGEVGYLA 429
|
330 340 350
....*....|....*....|....*....|...
gi 755503902 447 LALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:PRK09088 430 IVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL 462
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
130-480 |
8.25e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 130 APQNImdtclyIFTSGTTGLPKAARISHLKVLQCQGF----YHLCGVHQEDVIYLALPLYHMSGSLLGIVGcLGIGATVV 205
Cdd:PRK12406 153 QPQSM------IYTSGTTGHPKGVRRAAPTPEQAAAAeqmrALIYGLKPGIRALLTGPLYHSAPNAYGLRA-GRLGGVLV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 LKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPskaecdhKVRLAVG-SGLR----------PDTWERFLRRFGPL 274
Cdd:PRK12406 226 LQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPE-------EVRAKYDvSSLRhvihaaapcpADVKRAMIEWWGPV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 275 qILETYGMTEGNVATF----NYTGRQGAVGRASwlykhifPFSLIRYDVMTGEPIrnaqghcmttSPGEPGLLVAPVSQQ 350
Cdd:PRK12406 299 -IYEYYGSTESGAVTFatseDALSHPGTVGKAA-------PGAELRFVDEDGRPL----------PQGEIGEIYSRIAGN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 351 SPFLgYAGAPElAKDKLLKDVF-WSGDVffntGDLlvcDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVN 429
Cdd:PRK12406 361 PDFT-YHNKPE-KRAEIDRGGFiTSGDV----GYL---DADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCA 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 755503902 430 IYGvtVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQ 480
Cdd:PRK12406 432 VFG--IPDAEfGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
84-398 |
8.37e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 74.23 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 84 EPDLPALRAMGLHLWatgpetnvagisnllSEAADQVDEPvPGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-Q 162
Cdd:PRK08314 158 EPPLQALAPGGVVAW---------------KEALAAGLAP-PPHTAGPD---DLAVLPYTSGTTGVPKGCMHTHRTVMaN 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 CQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqfWD-----DC-QKHRVTVFQYIGELCRY 236
Cdd:PRK08314 219 AVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------WDreaaaRLiERYRVTHWTNIPTMVVD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 237 LVNQPPSKAECDHKVRLAVGSGLR-PD-TWERFLRRFGpLQILETYGMTE------GN-----------VATFNYTGRqg 297
Cdd:PRK08314 293 FLASPGLAERDLSSLRYIGGGGAAmPEaVAERLKELTG-LDYVEGYGLTEtmaqthSNppdrpklqclgIPTFGVDAR-- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 298 avgraswlykhifpfsLIryDVMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKdvfWSGDV 377
Cdd:PRK08314 370 ----------------VI--DPETLEEL----------PPGEVGEIV--VHGPQVFKGYWNRPEATAEAFIE---IDGKR 416
|
330 340
....*....|....*....|.
gi 755503902 378 FFNTGDLLVCDEQGFLHFHDR 398
Cdd:PRK08314 417 FFRTGDLGRMDEEGYFFITDR 437
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
141-475 |
9.38e-14 |
|
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: 73.44 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQcqgFY-HLCG---VHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSAS 213
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVS---FTnWMLSdfpLGPGDVF-LNQAPFSFDLSVMDLYPALASGATLVPVPRdatADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVF---QYIGELCR----YLVNQPPSkaecdhkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:cd05945 179 QLFRFLAEHGITVWvstPSFAAMCLlsptFTPESLPS-------LRHFLFCGevLPHKTARALQQRFPDARIYNTYGPTE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 GNVATfnytgrqgavgraswLYKHIFPFSLIRYDVMT-GEP-------IRNAQGHCMttSPGEPGLLVapVSQQSPFLGY 356
Cdd:cd05945 252 ATVAV---------------TYIEVTPEVLDGYDRLPiGYAkpgaklvILDEDGRPV--PPGEKGELV--ISGPSVSKGY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVP 436
Cdd:cd05945 313 LNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKY 387
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755503902 437 GHEGRAGMAA-LALRPP-QALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05945 388 KGEKVTELIAfVVPKPGaEAGLTKAIKAELAERLPPYMIPR 428
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
118-475 |
1.06e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.66 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 118 DQVDEPVPGYLSAP---QNIMDTCLYI-FTSGTTGLPKA---ARISHLKVLQCQGfyHLCGVHQEDVIYLALPLYHmSGS 190
Cdd:PRK07638 122 DEWKRMIEKYLPTYapiENVQNAPFYMgFTSGSTGKPKAflrAQQSWLHSFDCNV--HDFHMKREDSVLIAGTLVH-SLF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 191 LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQppsKAECDHKVRLaVGSGLRpdtW-----E 265
Cdd:PRK07638 199 LYGAISTLYVGQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKI-ISSGAK---WeaeakE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 266 RFLRRFGPLQILETYGMTEGNVATF----NYTGRQGAVGRaswlykhifPFSLIRYDvmtgepIRNAQGHcmTTSPGEPG 341
Cdd:PRK07638 272 KIKNIFPYAKLYEFYGASELSFVTAlvdeESERRPNSVGR---------PFHNVQVR------ICNEAGE--EVQKGEIG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLVApvsqQSP--FLGYAGAPELAKDklLKDVFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK07638 335 TVYV----KSPqfFMGYIIGGVLARE--LNADGW-----MTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVL 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 420 ETLDFLQEVNIYGVTVPghegRAGMAALALRPPQAlNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07638 404 HEHPAVDEIVVIGVPDS----YWGEKPVAIIKGSA-TKQQLKSFCLQRLSSFKIPK 454
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
73-475 |
1.50e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 73.01 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 73 LPTLVEFLESLEPDLPALRAMGlhlwatGPETNVAGISNLLSEAADQ-VDEPVPGYLsapqniMdtcLYifTSGTTGLPK 151
Cdd:PRK08276 94 ADTAAELAAELPAGVPLLLVVA------GPVPGFRSYEEALAAQPDTpIADETAGAD------M---LY--SSGTTGRPK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AAR--ISHLKVLQCQG------FYHLCGVhqEDVIYLA-LPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKH 222
Cdd:PRK08276 157 GIKrpLPGLDPDEAPGmmlallGFGMYGG--PDSVYLSpAPLYH-TAPLRFGMSALALGGTVVVMEKFDAEEALALIERY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 223 RVTVFQYIGELCRYLVNQPPS-KAECD---HKVRLAVGSGLRPDTWERFLRRFGPLqILETYGMTEGNVATF----NYTG 294
Cdd:PRK08276 234 RVTHSQLVPTMFVRMLKLPEEvRARYDvssLRVAIHAAAPCPVEVKRAMIDWWGPI-IHEYYASSEGGGVTVitseDWLA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 295 RQGAVGRAsWLYK-HIFPfslirydvMTGEPIrnaqghcmttSPGEPGLLVapVSQQSPFLGYAGAPELAKDKllkdvfW 373
Cdd:PRK08276 313 HPGSVGKA-VLGEvRILD--------EDGNEL----------PPGEIGTVY--FEMDGYPFEYHNDPEKTAAA------R 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 374 SGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGV--------------TVPGHE 439
Cdd:PRK08276 366 NPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdeemgervkavvqPADGAD 445
|
410 420 430
....*....|....*....|....*....|....*.
gi 755503902 440 GRAGMAAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:PRK08276 446 AGDALAA------------ELIAWLRGRLAHYKCPR 469
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-475 |
1.80e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 72.97 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 131 PQNIMDTCLYIFTSGTTGLPKAARIShlkvlQCQGFYHlcGVHQ--------EDVIYLALPLYHMSGSLLGIVGCLGIGA 202
Cdd:PRK06839 145 EKNESASFIICYTSGTTGKPKGAVLT-----QENMFWN--ALNNtfaidltmHDRSIVLLPLFHIGGIGLFAFPTLFAGG 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 203 TVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSG------LRPDTWERFLrRFGplqi 276
Cdd:PRK06839 218 VIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpeeLMREFIDRGF-LFG---- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 lETYGMTEGNVATF-----NYTGRQGAVGRaswlykhifPFSLIRYDVmtgepIRNAQGHcmtTSPGEPGLLVapVSQQS 351
Cdd:PRK06839 293 -QGFGMTETSPTVFmlseeDARRKVGSIGK---------PVLFCDYEL-----IDENKNK---VEVGEVGELL--IRGPN 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 PFLGYAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIY 431
Cdd:PRK06839 353 VMKEYWNRPDATEETI-------QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVV 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755503902 432 GVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PRK06839 426 GRQHV-KWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
136-477 |
1.92e-13 |
|
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: 72.50 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQEDVIY--LALPLYHMSGSLLGI-------VGCLGIGATVVL 206
Cdd:cd17650 94 DLAYVIYTSGTTGKPKGVMVEH------RNVAHA--AHAWRREYelDSFPVRLLQMASFSFdvfagdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KP---KFSASQFWDDCQKHRVTVFQYIGELCRYLVnqppskAECD-HKVR------LAVGSGLRPDTWERFL-RRFGP-L 274
Cdd:cd17650 166 CPdevKLDPAALYDLILKSRITLMESTPALIRPVM------AYVYrNGLDlsamrlLIVGSDGCKAQDFKTLaARFGQgM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 275 QILETYGMTEGNVATFNYTGRQGAVGRASwlykhifpfsliryDVMTGEPIRNAQGHCMTTS----P----GEPGLLVAP 346
Cdd:cd17650 240 RIINSYGVTEATIDSTYYEEGRDPLGDSA--------------NVPIGRPLPNTAMYVLDERlqpqPvgvaGELYIGGAG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 347 VSQqspflGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQ 426
Cdd:cd17650 306 VAR-----GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQL-----AR 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 755503902 427 EVNIYGVTVPGHEGRAGMAALA--LRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17650 376 HPAIDEAVVAVREDKGGEARLCayVVAAATLNTAELRAFLAKELPSYMIPSYY 428
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
136-475 |
2.16e-13 |
|
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: 72.53 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ--CQGFYHLcGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL-KPKFSA 212
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVyEGRFDA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVTVF----QYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE-GNV 287
Cdd:cd05969 169 ESWYGIIERVKVTVWytapTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTG---RQGAVGRaswlykhifPFSLIRYDVMT--GEPIRnaqghcmttsPGEPGLLVAPVSQQSPFLGYAGAPEl 362
Cdd:cd05969 248 MIANYPCmpiKPGSMGK---------PLPGVKAAVVDenGNELP----------PGTKGILALKPGWPSMFRGIWNDEE- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 akdkLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRA 442
Cdd:cd05969 308 ----RYKNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGEI 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 755503902 443 GMAALALR----PPQALNlVQLYSHVSENLPPYARPR 475
Cdd:cd05969 381 IKAFISLKegfePSDELK-EEIINFVRQKLGAHVAPR 416
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-475 |
2.26e-13 |
|
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: 72.56 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVlqCQGFYH------LCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPK 209
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNI--VARFSHardpifGNQIIPDTAILTVIPFHHGFG-MFTTLGYLICGFRVVLMYK 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLAVGSG-LRPDTWERFLRRFGPLQILETYGMTEGNV 287
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETTS 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 A---TFNYTGRQGAVGRaswlykhIFPFSLIRY-DVMTGEpirnaqghcmTTSPGEPGLLVApvsqQSPFL--GYAGAPE 361
Cdd:cd17642 342 AiliTPEGDDKPGAVGK-------VVPFFYAKVvDLDTGK----------TLGPNERGELCV----KGPMImkGYVNNPE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGR 441
Cdd:cd17642 401 ATKALIDKD-GW-----LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDE-DAGE 473
|
330 340 350
....*....|....*....|....*....|....
gi 755503902 442 AGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd17642 474 LPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
127-480 |
2.49e-13 |
|
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: 71.96 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 127 YLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHL---CGVHQEDVIYLALPLyhmSGSLLGIVGCLGIGAT 203
Cdd:cd17653 100 TTDSPD---DLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPArldVGPGSRVAQVLSIAF---DACIGEIFSTLCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 204 VVLK-PKFSASQFWDDC----------QKHRVTVFQYIGELcrYLVNQPPSKAecdhkvrLAvgsglrpDTWeRFLRRFg 272
Cdd:cd17653 174 LVLAdPSDPFAHVARTVdalmstpsilSTLSPQDFPNLKTI--FLGGEAVPPS-------LL-------DRW-SPGRRL- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 273 plqiLETYGMTEGNVATfnytgrqgavgraswLYKHIFPfsliRYDVMTGEPIRNA-----QGHCMTTSPGEPGLLVapV 347
Cdd:cd17653 236 ----YNAYGPTECTISS---------------TMTELLP----GQPVTIGKPIPNStcyilDADLQPVPEGVVGEIC--I 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 348 SQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDflQE 427
Cdd:cd17653 291 SGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ--PE 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 755503902 428 VNIYGVTVpgHEGRagmaALALRPPQALNLVQLYSHVSENLPPYARP-RFLRLQ 480
Cdd:cd17653 369 VTQAAAIV--VNGR----LVAFVTPETVDVDGLRSELAKHLPSYAVPdRIIALD 416
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
122-437 |
3.37e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.14 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 122 EPVPGYLSAPQNIMDTClyiFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMsGSLLGIVGCLGI 200
Cdd:PLN02860 162 TTELDYAWAPDDAVLIC---FTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHI-GGLSSALAMLMV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKA--ECDHKVR--LAVGSGLRPDTWERFLRRFGPLQI 276
Cdd:PLN02860 238 GACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMtwKVFPSVRkiLNGGGSLSSRLLPDAKKLFPNAKL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTEG-NVATFN--YTGRQGAVGRASWLYKHIFPFSLIRYD-VMTGEPIRNAQ-GHCMTTSPGEPGLLVapvsqQS 351
Cdd:PLN02860 318 FSAYGMTEAcSSLTFMtlHDPTLESPKQTLQTVNQTKSSSVHQPQgVCVGKPAPHVElKIGLDESSRVGRILT-----RG 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 P--FLGYAG-APELAKDKllkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEV 428
Cdd:PLN02860 393 PhvMLGYWGqNSETASVL-------SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVL-----SQHP 460
|
....*....
gi 755503902 429 NIYGVTVPG 437
Cdd:PLN02860 461 GVASVVVVG 469
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
117-479 |
3.64e-13 |
|
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: 72.14 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 117 ADQVDEPVPGYlsAPQNIMDTCLYIFTSGTTGLPKAARISH----LKVlqCQGFYHLCGVHQEDVIYLALPLYHMSGSLL 192
Cdd:cd05968 220 DEEKETAGDGA--ERTESEDPLMIIYTSGTTGKPKGTVHVHagfpLKA--AQDMYFQFDLKPGDLLTWFTDLGWMMGPWL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 193 gIVGCLGIGATVVL---KPKF-SASQFWDDCQKHRVTVFQYIGELCRYLV--NQPPSKAECDHKVRLAVGSG--LRPDTW 264
Cdd:cd05968 296 -IFGGLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGepWNPEPW 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 265 ERFLRRFGplqiletygmtEGNVATFNYTG----RQGAVGraSWLYKHIFPFSL------IRYDVM--TGEPIRNAQGHC 332
Cdd:cd05968 375 NWLFETVG-----------KGRNPIINYSGgteiSGGILG--NVLIKPIKPSSFngpvpgMKADVLdeSGKPARPEVGEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 333 MTTSPGePGLlvapvsqQSPFLGyagapelaKDKLLKDVFWSG-DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVA 411
Cdd:cd05968 442 VLLAPW-PGM-------TRGFWR--------DEDRYLETYWSRfDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVG 505
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 412 TTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRP---PQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:cd05968 506 PAEIESVLNAHPAVLESAAIGVPHP-VKGEAIVCFVVLKPgvtPTEALAEELMERVADELGKPLSPERILF 575
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
142-477 |
6.83e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.20 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFY---HLCGVHQEDVIYL-ALPLYHMSGslLGIVGCLGI--GATVVLKPK-F 210
Cdd:PRK07059 211 YTGGTTGVSKGATLLHrnivANVLQMEAWLqpaFEKKPRPDQLNFVcALPLYHIFA--LTVCGLLGMrtGGRNILIPNpR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPP-SKAECDhKVRLAVGSGL---RPdTWERFLRRFGpLQILETYGMTEGN 286
Cdd:PRK07059 289 DIPGFIKELKKYQVHIFPAVNTLYNALLNNPDfDKLDFS-KLIVANGGGMavqRP-VAERWLEMTG-CPITEGYGLSETS 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 -VATFNytgrqgavgraswlykhifPFSLIRYDVMTGEP-------IRNAQGHCMttSPGEPGLLVAPVSQQSPflGYAG 358
Cdd:PRK07059 366 pVATCN-------------------PVDATEFSGTIGLPlpstevsIRDDDGNDL--PLGEPGEICIRGPQVMA--GYWN 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 359 AP-ELAKdkllkdvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 437
Cdd:PRK07059 423 RPdETAK-------VMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDE- 494
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755503902 438 HEGRAgMAALALRPPQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:PRK07059 495 HSGEA-VKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
141-479 |
7.91e-13 |
|
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: 70.80 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ----CQgfyHLCGVHQEDVIYlalpLYHMSG---SLLGIVGCLGIGATVVLKPKF--- 210
Cdd:cd17643 99 IYTSGSTGRPKGVVVSHANVLAlfaaTQ---RWFGFNEDDVWT----LFHSYAfdfSVWEIWGALLHGGRLVVVPYEvar 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLRRFGPL--QILETYGMTEGN 286
Cdd:cd17643 172 SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDrpQLVNMYGITETT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 V-ATFNYTGRQGAVGRASwlykhifpfSLIrydvmtGEPIRNAQGHCMTTS-----PGEPGLLVAPVSQQSPflGYAGAP 360
Cdd:cd17643 252 VhVTFRPLDAADLPAAAA---------SPI------GRPLPGLRVYVLDADgrpvpPGVVGELYVSGAGVAR--GYLGRP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 361 ELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVpgHE 439
Cdd:cd17643 315 ELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDA---AVIV--RE 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 755503902 440 GRAG----MAALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd17643 390 DEPGdtrlVAYVVADDGAAADIAELRALLKELLPDYMVPaRYVPL 434
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-477 |
1.18e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 70.15 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAA------RISHLKVLQcqgFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL--K 207
Cdd:cd05971 89 DPALIIYTSGTTGPPKGAlhahrvLLGHLPGVQ---FPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 208 PKFSASQFWDDCQKHRVT-VFQYIGELcRYLVNQPPSKAECDHKVRlAVGSGLRPD-----TWERflRRFGpLQILETYG 281
Cdd:cd05971 166 TKFDPKAALDLMSRYGVTtAFLPPTAL-KMMRQQGEQLKHAQVKLR-AIATGGESLgeellGWAR--EQFG-VEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEGNVATFN----YTGRQGAVGRAswlykhiFPFSLIRydvmtgepIRNAQGhcMTTSPGEPGLLVAPVSQQSPFLGYA 357
Cdd:cd05971 241 QTECNLVIGNcsalFPIKPGSMGKP-------IPGHRVA--------IVDDNG--TPLPPGEVGEIAVELPDPVAFLGYW 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 358 GAPELAKDKLLKDvfwsgdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPg 437
Cdd:cd05971 304 NNPSATEKKMAGD-------WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDP- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755503902 438 HEGRAGMAALALRP----PQALNlVQLYSHVSENLPPYARPRFL 477
Cdd:cd05971 376 IRGEIVKAFVVLNPgetpSDALA-REIQELVKTRLAAHEYPREI 418
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-475 |
1.92e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 69.87 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQE----DVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPK 209
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIaMVELFVRFEASQYEypgsDNVYLAaLPMFHIYGLSLFVVGLLSLGSTIVVMRR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGELCRYLVNQP-PSKAECDHKVRLaVGSGLRP---DTWERFLRRFGPLQILETYGMTEG 285
Cdd:PLN02574 279 FDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQ-VSCGAAPlsgKFIQDFVQTLPHVDFIQGYGMTES 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NvatfnytgrqgAVGRASWLYKHIFPFSLIRYDV--MTGEPIRNAQGHCMttSPGEPGLLVApvsqQSPFL--GYAGAPE 361
Cdd:PLN02574 358 T-----------AVGTRGFNTEKLSKYSSVGLLApnMQAKVVDWSTGCLL--PPGNCGELWI----QGPGVmkGYLNNPK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 LAKDKLLKDVfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGvtVPGHE-G 440
Cdd:PLN02574 421 ATQSTIDKDG-W-----LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA--VPDKEcG 492
|
330 340 350
....*....|....*....|....*....|....*
gi 755503902 441 RAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:PLN02574 493 EIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVR 527
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
137-479 |
2.02e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.25 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 137 TCLYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQF 215
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLSRRAIAADlDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRV------TVFQYIGElcrylvnqPPSKAECDHKVRLAV-GSGLRPDT-WERFLRRFGpLQILETYGMTEG-- 285
Cdd:PRK07787 210 AQALSEGGTlyfgvpTVWSRIAA--------DPEAARALRGARLLVsGSAALPVPvFDRLAALTG-HRPVERYGMTETli 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVAT-FNYTGRQGAVGRAswlykhiFPFSLIRYDVMTGEPIrnaqghcmtTSPGEPgllVAPVSQQSP--FLGYAGAPEL 362
Cdd:PRK07787 281 TLSTrADGERRPGWVGLP-------LAGVETRLVDEDGGPV---------PHDGET---VGELQVRGPtlFDGYLNRPDA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 363 AKDKllkdvfWSGDVFFNTGDLLVCDEQGFLHFHDRTG-DTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGR 441
Cdd:PRK07787 342 TAAA------FTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQR 415
|
330 340 350
....*....|....*....|....*....|....*...
gi 755503902 442 AGMAALALRPPQALNLVQlysHVSENLPPYARPRFLRL 479
Cdd:PRK07787 416 IVAYVVGADDVAADELID---FVAQQLSVHKRPREVRF 450
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
81-475 |
2.17e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 69.33 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 81 ESLEPDLPALRamgLHLWATGPETnVAGISNLLSEAADQVDEPVPGylsapQNIMDTCLYifTSGTTGLPKAAR--ISHL 158
Cdd:PRK13391 111 RALLKQCPGVR---HRLVLDGDGE-LEGFVGYAEAVAGLPATPIAD-----ESLGTDMLY--SSGTTGRPKGIKrpLPEQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 159 KVLQCQGFYHLCGV---HQEDVIYLA-LPLYHmSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELC 234
Cdd:PRK13391 180 PPDTPLPLTAFLQRlwgFRSDMVYLSpAPLYH-SAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 235 RYLVNQPpskaecdHKVRLAVG-SGLR----------PDTWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAV 299
Cdd:PRK13391 259 SRMLKLP-------EEVRDKYDlSSLEvaihaaapcpPQVKEQMIDWWGPI-IHEYYAATEGLGFTAcdseEWLAHPGTV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 300 GRAswlykhifpfslirydvMTGEP-IRNAQGHCMttSPGEPGLLVapVSQQSPFlGYAGAPELAKDKLLKDVFWSgdvf 378
Cdd:PRK13391 331 GRA-----------------MFGDLhILDDDGAEL--PPGEPGTIW--FEGGRPF-EYLNDPAKTAEARHPDGTWS---- 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 379 fNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETL--------------DFLQEVNIYGVTVPGHEGRAGM 444
Cdd:PRK13391 385 -TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHpkvadaavfgvpneDLGEEVKAVVQPVDGVDPGPAL 463
|
410 420 430
....*....|....*....|....*....|.
gi 755503902 445 AAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:PRK13391 464 AA------------ELIAFCRQRLSRQKCPR 482
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-475 |
2.27e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 69.08 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARIShLKVLQCQGFY--HLCGVHQEDVIY-LALP-----LYHmsgsllGIVGCLGIG-ATVVL 206
Cdd:cd05973 89 DPFVMMFTSGTTGLPKGVPVP-LRALAAFGAYlrDAVDLRPEDSFWnAADPgwaygLYY------AITGPLALGhPTILL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSkAECDHKVRLAV----GSGLRPDTWERFLRRFGpLQILETYGM 282
Cdd:cd05973 162 EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRvssaGEPLTPEVIRWFDAALG-VPIHDHYGQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TEGNVATFNYTG-----RQGAVGRAswlykhiFP-FSLIRYDVMTGEPirnaqghcmttSPGEPGLLVAPVSQqSP---F 353
Cdd:cd05973 240 TELGMVLANHHAlehpvHAGSAGRA-------MPgWRVAVLDDDGDEL-----------GPGEPGRLAIDIAN-SPlmwF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 354 LGYAGAPELAKDkllkdvfwsGDvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYG- 432
Cdd:cd05973 301 RGYQLPDTPAID---------GG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGv 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 433 -------------VTVPGHEGRAGMAAlalrppqalnlvQLYSHVSENLPPYARPR 475
Cdd:cd05973 371 pdpertevvkafvVLRGGHEGTPALAD------------ELQLHVKKRLSAHAYPR 414
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
141-480 |
2.87e-12 |
|
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: 68.91 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVL-----QCQGFyhlcGVHQED-VIYLALPLYHMsgSLLGIVGCLGIGATVVLKP---KFS 211
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLAnlvawQARAS----SLGPGArTLQFAGLGFDV--SVQEIFSTLCAGATLVLPPeevRTD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 212 ASQFWDDCQKHRVT-------VFQYIGELCRYLVNQPPSKAE-CDHKVRLAVGSGLRpdtweRFLRRFGPLQILETYGMT 283
Cdd:cd17651 216 PPALAAWLDEQRISrvflptvALRALAEHGRPLGVRLAALRYlLTGGEQLVLTEDLR-----EFCAGLPGLRLHNHYGPT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 284 EGNVATfnytgrqgavgraswlyKHIFPFSLIRYD--VMTGEPIRNAQGHCMTTS-----PGEPG-LLVAPVSQQSpflG 355
Cdd:cd17651 291 ETHVVT-----------------ALSLPGDPAAWPapPPIGRPIDNTRVYVLDAAlrpvpPGVPGeLYIGGAGLAR---G 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLdflqeVNIYGVTV 435
Cdd:cd17651 351 YLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH-----PGVREAVV 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALA----LRPPQALNLVQLYSHVSENLPPYARP-RFLRLQ 480
Cdd:cd17651 426 LAREDRPGEKRLVayvvGDPEAPVDAAELRAALATHLPEYMVPsAFVLLD 475
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
83-474 |
3.85e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.80 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPA------LRAMGLHLWATGPETNV-----AGISNL-LSEAADQVD---EPVPGYLSAPQNImdtCLYIFTSGTT 147
Cdd:PRK12467 592 LDPEYPQdrlaymLDDSGVRLLLTQSHLLAqlpvpAGLRSLcLDEPADLLCgysGHNPEVALDPDNL---AYVIYTSGST 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 148 GLPKAARISHLKVLQcqgfyHLCGVHQE-----DVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDC 219
Cdd:PRK12467 669 GQPKGVAISHGALAN-----YVCVIAERlqlaaDDSMLMVSTFAFDLGVTELFGALASGATLHLLPPdcaRDAEAFAALM 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 QKHRVTVFQYIGELCRYLVnQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGP-LQILETYGMTEGNVATFNYT-GRQG 297
Cdd:PRK12467 744 ADQGVTVLKIVPSHLQALL-QASRVALPRPQRALVCGGEALQVDLLARVRALGPgARLINHYGPTETTVGVSTYElSDEE 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 298 AVGRASWLYKHIFPFSLIRYDvmtgepirnaqgHCMTTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSG 375
Cdd:PRK12467 823 RDFGNVPIGQPLANLGLYILD------------HYLNPVPvGVVGELY--IGGAGLARGYHRRPALTAERFVPDPFgADG 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 376 DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAAL--ALRP-- 451
Cdd:PRK12467 889 GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV--LAQPGDAGLQLVAYLvpAAVAdg 966
|
410 420
....*....|....*....|....*
gi 755503902 452 --PQALNLvQLYSHVSENLPPYARP 474
Cdd:PRK12467 967 aeHQATRD-ELKAQLRQVLPDYMVP 990
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
83-479 |
4.36e-12 |
|
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: 68.16 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPALRamgLHLWATGpetnvAGISNLLSEAADQvdepvPGYLsapqnimdtclyIFTSGTTGLPKAARISHLKVLQ 162
Cdd:cd17649 67 LDPEYPAER---LRYMLED-----SGAGLLLTHHPRQ-----LAYV------------IYTSGSTGTPKGVAVSHGPLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 -CQGFYHLCGVHQEDVIylaLPLYHMS--GSLLGIVGCLGIGATVVLKPKfsasQFWDDCQ-------KHRVTVFQ---- 228
Cdd:cd17649 122 hCQATAERYGLTPGDRE---LQFASFNfdGAHEQLLPPLICGACVVLRPD----ELWASADelaemvrELGVTVLDlppa 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 229 YIGELCRYLVNQPPSKAEcdhKVRLAV--GSGLRPDTWERFLRrfGPLQILETYGMTEGNVATFNYTGRQGAvgRASWLY 306
Cdd:cd17649 195 YLQQLAEEADRTGDGRPP---SLRLYIfgGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGA--ARAGAS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 307 KHIfpfslirYDVMTGEPIRNAQGHCMTTSPGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFW-SGDVFFNTGDLL 385
Cdd:cd17649 268 MPI-------GRPLGGRSAYILDADLNPVPVGVTGELY--IGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 386 VCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVS 465
Cdd:cd17649 339 RWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALR 418
|
410
....*....|....*
gi 755503902 466 ENLPPYARP-RFLRL 479
Cdd:cd17649 419 ASLPDYMVPaHLVFL 433
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
142-483 |
4.37e-12 |
|
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: 68.48 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHlkvlqcQGFY-------HLCGVHQEDViYL-ALPLYHMSGsLLGIVGCLGIGATVVLKPKFSAS 213
Cdd:cd12118 140 YTSGTTGRPKGVVYHH------RGAYlnalaniLEWEMKQHPV-YLwTLPMFHCNG-WCFPWTVAAVGGTNVCLRKVDAK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE-CDHKVRLAVGSGLRPdtwERFLRRFGPL--QILETYGMTEG-NVAT 289
Cdd:cd12118 212 AIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARpLPHRVHVMTAGAPPP---AAVLAKMEELgfDVTHVYGLTETyGPAT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 290 FNY----------------TGRQGavgraswlykhifpfslIRYDVMTGEPIRNAQGhcMTTSP------GE---PGLLV 344
Cdd:cd12118 289 VCAwkpewdelpteerarlKARQG-----------------VRYVGLEEVDVLDPET--MKPVPrdgktiGEivfRGNIV 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 345 ApvsqqspfLGYAGAPElAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd12118 350 M--------KGYLKNPE-ATAEAFRG-GW-----FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755503902 425 LQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR---FLRLQVTS 483
Cdd:cd12118 415 VLEAAVVARPDE-KWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKtvvFGELPKTS 475
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
141-284 |
6.13e-12 |
|
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: 68.73 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLyhmS--GSLLGIVGCLGIGATVVLKPK---FSASQ 214
Cdd:COG1020 623 IYTSGSTGRPKGVMVEHRALVNlLAWMQRRYGLGPGDRVLQFASL---SfdASVWEIFGALLSGATLVLAPPearRDPAA 699
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 215 FWDDCQKHRVTVFQ----YIGELCRYLVNQPPSkaecdhkVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:COG1020 700 LAELLARHRVTVLNltpsLLRALLDAAPEALPS-------LRLVLVGGeaLPPELVRRWRARLPGARLVNLYGPTE 768
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
136-475 |
6.33e-12 |
|
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: 66.97 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLLSLPLYHVGG-LAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 fwddcQKHRVTVFQYIG----ELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLqiLETYGMTE--GNVA 288
Cdd:cd17630 80 -----EDLAPPGVTHVSlvptQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPL--YTTYGMTEtaSQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 289 TFNYTG-RQGAVGRaswlykhifPFSLIRYDVmtgepirnaqghcmtTSPGEpgLLVAPVSQQSPFLGYAGAPELAKDKl 367
Cdd:cd17630 153 TKRPDGfGRGGVGV---------LLPGRELRI---------------VEDGE--IWVGGASLAMGYLRGQLVPEFNEDG- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 368 lkdvfWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAAL 447
Cdd:cd17630 206 -----W-----FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDE-ELGQRPVAVI 274
|
330 340
....*....|....*....|....*...
gi 755503902 448 ALRPPqaLNLVQLYSHVSENLPPYARPR 475
Cdd:cd17630 275 VGRGP--ADPAELRAWLKDKLARFKLPK 300
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
64-474 |
8.39e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 67.76 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 64 VRSCWPQLGLPT-LVEFLESLEPDLPALRAMGLHlwaTGPETNVAGISNLLS-EAADQVDEPVP-GYLSAPQNIMdtcly 140
Cdd:PRK06178 144 VEQVRAETSLRHvIVTSLADVLPAEPTLPLPDSL---RAPRLAAAGAIDLLPaLRACTAPVPLPpPALDALAALN----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 iFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLA-LPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDD 218
Cdd:PRK06178 216 -YTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSfLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFMAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 219 CQKHRVTVfqyigelCRYLVNQP------PSKAECDHKVRLAVGS-----GLRPDTWERFLRRFGPLQILETYGMTEGNV 287
Cdd:PRK06178 295 VERYRVTR-------TVMLVDNAvelmdhPRFAEYDLSSLRQVRVvsfvkKLNPDYRQRWRALTGSVLAEAAWGMTETHT 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 A-TFNyTGRQgaVGRASWLYKHIF-----PFSLIRY-DVMTGEPIrnaqghcmttsP-GEPGLLVapVSQQSPFLGYAGA 359
Cdd:PRK06178 368 CdTFT-AGFQ--DDDFDLLSQPVFvglpvPGTEFKIcDFETGELL-----------PlGAEGEIV--VRTPSLLKGYWNK 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 360 PELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVaEVLetldFLQEVNIYGVTVPG-- 437
Cdd:PRK06178 432 PEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEV-EAL----LGQHPAVLGSAVVGrp 499
|
410 420 430
....*....|....*....|....*....|....*....
gi 755503902 438 --HEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK06178 500 dpDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP 538
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
141-475 |
1.27e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 66.96 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAAR--ISHLKVLQ--------CQGFYhlcGVHQEDVIYLALPLYHMSG-SLLGIVGCLGigATVVLKPK 209
Cdd:PRK13390 154 LYSSGTTGFPKGIQpdLPGRDVDApgdpivaiARAFY---DISESDIYYSSAPIYHAAPlRWCSMVHALG--GTVVLAKR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHRVTVFQYIGEL-CRYLVNQPPSKAECDHKVRLAVGSGLRP---DTWERFLRRFGPLqILETYGMTEG 285
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvDVKHAMIDWLGPI-VYEYYSSTEA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 286 NVATFNYTGR----QGAVGRAswlykhifpfslirydVMTGEPIRNAQGHCMTTspGEPGlLVAPVSQQSPFlGYAGAPE 361
Cdd:PRK13390 308 HGMTFIDSPDwlahPGSVGRS----------------VLGDLHICDDDGNELPA--GRIG-TVYFERDRLPF-RYLNDPE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 362 -LAKDKLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP--GH 438
Cdd:PRK13390 368 kTAAAQHPAHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemGE 442
|
330 340 350
....*....|....*....|....*....|....*...
gi 755503902 439 EGRAGMAALA-LRPPQALNLvQLYSHVSENLPPYARPR 475
Cdd:PRK13390 443 QVKAVIQLVEgIRGSDELAR-ELIDYTRSRIAHYKAPR 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
141-479 |
1.88e-11 |
|
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: 66.53 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHL----KVLQCQGFYhlcGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVL-------KPK 209
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAgivnRLLWMQDEY---PLGPGDRVLQKTPL-SFDVSVWELFWPLVAGARLVVarpgghrDPA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFwddcQKHRVTVFQYIGELCRYLVNQPpsKAECDHKVRLAVGSG--LRPDTWERFLRRFG-PLQILetYGMTEgn 286
Cdd:cd17646 220 YLAALI----REHGVTTCHFVPSMLRVFLAEP--AAGSCASLRRVFCSGeaLPPELAARFLALPGaELHNL--YGPTE-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 287 vATFNYTGRQ--GAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSQqspflGY 356
Cdd:cd17646 290 -AAIDVTHWPvrGPAETPS---------------VPIGRPVPNTRLYVLDDAlrpvpVGVPGELYlggVQLAR-----GY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDflqEVNiyGVTVP 436
Cdd:cd17646 349 LGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHP---AVT--HAVVV 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755503902 437 GHEGRAGMAAL-----ALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd17646 424 ARAAPAGAARLvgyvvPAAGAAGPDTAALRAHLAERLPEYMVPaAFVVL 472
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
136-475 |
2.22e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 65.48 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISH--LKVLQCQGFYHLCGVHQED-------------VIYLALPLYHMSGSLLGIVGCLGI 200
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedIFRMLMGGADFGTGEFTPSedahkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVLKPKFSASQFWDDCQKHRVTVFQYIGE-LCRYLVNQPPSKAECDHKVRLAVGSG---LRPDTWERFLRRFGPLQI 276
Cdd:cd05924 84 QTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTEGNVATFNYTGRQGAVGRaswlykhifPFSLIRYDVMTGEPirnaQGHCMTTSPGEPGLL----VAPvsqqsp 352
Cdd:cd05924 164 VDAFGSSETGFTGSGHSAGSGPETG---------PFTRANPDTVVLDD----DGRVVPPGSGGVGWIarrgHIP------ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 fLGYAGAPELAKD--KLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETldflqEVNI 430
Cdd:cd05924 225 -LGYYGDEAKTAEtfPEVDGVRYA-----VPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKS-----HPAV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 755503902 431 YGVTVPGHE----GRAGMAALALRPPQALNLVQLYSHVSENLPPYARPR 475
Cdd:cd05924 294 YDVLVVGRPderwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPK 342
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
110-411 |
2.24e-11 |
|
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: 66.34 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 110 SNLLSEAADQVDEPVPGylsaPQNIMDTclyIFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMS 188
Cdd:cd05932 119 DDLIAQHPPLEERPTRF----PEQLATL---IYTSGTTGQPKGVMLTFGSfAWAAQAGIEHIGTEENDRMLSYLPLAHVT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 189 GSLLGIVGCLgIGATVVLKPKfSASQFWDDCQKHRVTVFQYIGELC-----RYLVNQPPSK-----------AECDHKV- 251
Cdd:cd05932 192 ERVFVEGGSL-YGGVLVAFAE-SLDTFVEDVQRARPTLFFSVPRLWtkfqqGVQDKIPQQKlnlllkipvvnSLVKRKVl 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 252 --------RLAV-GSGLRPDTWERFLRRFGpLQILETYGMTEG-NVATFNYTGRQ--GAVGRASwlykhifPFSLIRYDv 319
Cdd:cd05932 270 kglgldqcRLAGcGSAPVPPALLEWYRSLG-LNILEAYGMTENfAYSHLNYPGRDkiGTVGNAG-------PGVEVRIS- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 320 mtgepirnAQGHCMTTSPGEpgllvapvsqqspFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRT 399
Cdd:cd05932 341 --------EDGEILVRSPAL-------------MMGYYKDPEATAEAF------TADGFLRTGDKGELDADGNLTITGRV 393
|
330
....*....|...
gi 755503902 400 GDTFRW-KGENVA 411
Cdd:cd05932 394 KDIFKTsKGKYVA 406
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
133-482 |
2.49e-11 |
|
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: 65.88 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 133 NIMDTCLYIFTSGTTGLPKAARISHLKVLQCQ----GFYHLCGVHQEDVIYLA-----LPLYHMSGSLLGivgclgiGAT 203
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRtslsERYFGRDNGDEAVLFFSnyvfdFFVEQMTLALLN-------GQK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 204 VVLKP---KFSASQFWDDCQKHRVTvfqyigelcrYLvNQPPSK------AECDH-KVRLAVGSGLRPDTWERFLRRFgP 273
Cdd:cd17648 165 LVVPPdemRFDPDRFYAYINREKVT----------YL-SGTPSVlqqydlARLPHlKRVDAAGEEFTAPVFEKLRSRF-A 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEGNVATfnytgrqgavgraswlYKHIFPFSLiRYDVMTGEPIRNAQ----GHCMTTSP----GE---PGL 342
Cdd:cd17648 233 GLIINAYGPTETTVTN----------------HKRFFPGDQ-RFDKSLGRPVRNTKcyvlNDAMKRVPvgavGElylGGD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 343 LVAPvsqqspflGYAGAPELAKDKLLKDVFWSGD--------VFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTE 414
Cdd:cd17648 296 GVAR--------GYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 415 VAEVLETLDFLQE---VNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP----RFLRLQVT 482
Cdd:cd17648 368 VEAALASYPGVREcavVAKEDASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVParlvRLEGIPVT 442
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
77-419 |
3.83e-11 |
|
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: 65.55 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 77 VEFLESLEPDLPALRamglHLWATGPETNVAGISNLLSEAADqVDEPVPgylsAPQnimDTCLYIFTSGTTGLPK----- 151
Cdd:COG1021 138 RALARELQAEVPSLR----HVLVVGDAGEFTSLDALLAAPAD-LSEPRP----DPD---DVAFFQLSGGTTGLPKliprt 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 ----------AARIshlkvlqcqgfyhlCGVHQEDViYL-ALPLYH-MSGSLLGIVGCLGIGATVVLKPKFSAsqfwDDC 219
Cdd:COG1021 206 hddylysvraSAEI--------------CGLDADTV-YLaALPAAHnFPLSSPGVLGVLYAGGTVVLAPDPSP----DTA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 ----QKHRVTVfqyIGelcryLVnqPP-------SKAECDHKVR-LAV----GSGLRPDTWERFLRRFGP-LQilETYGM 282
Cdd:COG1021 267 fpliERERVTV---TA-----LV--PPlallwldAAERSRYDLSsLRVlqvgGAKLSPELARRVRPALGCtLQ--QVFGM 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 283 TEGNVatfNYTG-------RQGAVGRAswlykhIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--F 353
Cdd:COG1021 335 AEGLV---NYTRlddpeevILTTQGRP------ISPDDEVR--------IVDEDGN--PVPPGEVGELLT----RGPytI 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 354 LGYAGAPEL-AKdkllkdVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:COG1021 392 RGYYRAPEHnAR------AF-TPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-474 |
4.18e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 130 APQNImdtCLYIFTSGTTGLPKAARISHLKVLQcqgfyHLCGVHQE-----DVIYLALPLYHMSGSLLGIVGCLGIGATV 204
Cdd:PRK12316 4692 HPDNL---AYVIYTSGSTGRPKGVAVSHGSLVN-----HLHATGERyeltpDDRVLQFMSFSFDGSHEGLYHPLINGASV 4763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 VLKPkfsaSQFWDDCQ------KHRVTVFQYIGELCRYLVNQPPSKAECDH-KVRLAVGSGLRPDTWERFLRRFGPLQIL 277
Cdd:PRK12316 4764 VIRD----DSLWDPERlyaeihEHRVTVLVFPPVYLQQLAEHAERDGEPPSlRVYCFGGEAVAQASYDLAWRALKPVYLF 4839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTEGNVATFNYTGRQGAVGRASwlYKHIfpfslirydvmtGEPIRNAQGHCMTTSpGEPgllvAPVSQQSPFL--- 354
Cdd:PRK12316 4840 NGYGPTETTVTVLLWKARDGDACGAA--YMPI------------GTPLGNRSGYVLDGQ-LNP----LPVGVAGELYlgg 4900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 355 -----GYAGAPELAKDKLLKDVFWS-GDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEv 428
Cdd:PRK12316 4901 egvarGYLERPALTAERFVPDPFGApGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE- 4979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 429 niygVTVPGHEGRAGMAALALRPPQALNLV-----------QLYSHVSENLPPYARP 474
Cdd:PRK12316 4980 ----AVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelrdELKAALRERLPEYMVP 5032
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
90-475 |
5.89e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.00 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 90 LRAMGLHLWATGPETNVAGIS-NLLSEAADQVdepvpGYLSAPQNIM--DTCLYIFTSGTTGLPKAARISHLKVLQ--CQ 164
Cdd:PLN02330 141 VKGLGLPVIVLGEEKIEGAVNwKELLEAADRA-----GDTSDNEEILqtDLCALPFSSGTTGISKGVMLTHRNLVAnlCS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 165 GFYhlcGVHQE---DVIYLAL-PLYHMSGsLLGIV-GCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVN 239
Cdd:PLN02330 216 SLF---SVGPEmigQVVTLGLiPFFHIYG-ITGICcATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 240 QPPSKAECDHKVRL----AVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASwlyKHIFPFSLI 315
Cdd:PLN02330 292 NPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHGIAK---KNSVGFILP 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 316 RYDVMTGEPiRNAQGHCMTTsPGEpgllvAPVSQQSPFLGYAGAPElAKDKLLKDVFWsgdvfFNTGDLLVCDEQGFLHF 395
Cdd:PLN02330 369 NLEVKFIDP-DTGRSLPKNT-PGE-----LCVRSQCVMQGYYNNKE-ETDRTIDEDGW-----LHTGDIGYIDDDGDIFI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 396 HDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTVPGHE-GRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PLN02330 436 VDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKESEEDILNFVAANVAHYKKV 513
|
.
gi 755503902 475 R 475
Cdd:PLN02330 514 R 514
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
80-480 |
7.33e-11 |
|
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: 64.62 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 80 LESLEPDL----PALRAmGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLsapqnimdtclyIFTSGTTGLPKAARI 155
Cdd:cd12116 80 LEDAEPALvltdDALPD-RLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYV------------IYTSGSTGRPKGVVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 156 SHLKVL-QCQGFYHLCGVHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWDDCQKHRVTVFQYIG 231
Cdd:cd12116 147 SHRNLVnFLHSMRERLGLGPGDRL-LAVTTYAFDISLLELLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVMQATP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 232 ELCRYLVNQPPSKAEcdhKVRLAVG-SGLRPDTWERFLRRFGPLQILetYGMTEGNVATfnytgrqgAVGRASWLYKHIf 310
Cdd:cd12116 226 ATWRMLLDAGWQGRA---GLTALCGgEALPPDLAARLLSRVGSLWNL--YGPTETTIWS--------TAARVTAAAGPI- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 311 pfslirydvMTGEPIRNAQGHC-----MTTSPGEPG-LLVA--PVSQqspflGYAGAPELAKDKLLKDVFW-SGDVFFNT 381
Cdd:cd12116 292 ---------PIGRPLANTQVYVldaalRPVPPGVPGeLYIGgdGVAQ-----GYLGRPALTAERFVPDPFAgPGSRLYRT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 382 GDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVniyGVTVPGHEGRAGMAALALRP-PQALNLVQL 460
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA---AVVVREDGGDRRLVAYVVLKaGAAPDAAAL 434
|
410 420
....*....|....*....|.
gi 755503902 461 YSHVSENLPPYARP-RFLRLQ 480
Cdd:cd12116 435 RAHLRATLPAYMVPsAFVRLD 455
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
136-466 |
7.55e-11 |
|
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: 64.66 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHlkvlqcQGFYH-------LCGVHQEDVIYLALPLYH---MSGSllGIVGCLGIGATVV 205
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTH------NDYAYnvrasaeVCGLDQDTVYLAVLPAAHnfpLACP--GVLGTLLAGGRVV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 LKPKFSASQFWDDCQKHRVT--------VFQYIGELCRYlVNQPPSkaecdHKVRLAVGSGLRPDTWERFLRRFGPlQIL 277
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTvtalvpalVSLWLDAAASR-RADLSS-----LRLLQVGGARLSPALARRVPPVLGC-TLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 278 ETYGMTEGNVatfNYT----------GRQGavgraswlyKHIFPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApv 347
Cdd:cd05920 285 QVFGMAEGLL---NYTrlddpdeviiHTQG---------RPMSPDDEIR--------VVDEEGN--PVPPGEEGELLT-- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 348 sqQSP--FLGYAGAPEL-AKdkllkdVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDF 424
Cdd:cd05920 341 --RGPytIRGYYRAPEHnAR------AF-TPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPA 411
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755503902 425 LQEVNIygVTVPGHE-GRAGMAALALRPPQaLNLVQLYSHVSE 466
Cdd:cd05920 412 VHDAAV--VAMPDELlGERSCAFVVLRDPP-PSAAQLRRFLRE 451
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
128-479 |
2.86e-10 |
|
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: 62.73 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 128 LSAPQNIMDTCLYIFTSGTTGLPKAARISHlkvlqcQGFYHLcgVHQ-EDVIYLA----LPLY---HMSGSLLGIVGCLG 199
Cdd:cd17655 130 LEPVSKSDDLAYVIYTSGSTGKPKGVMIEH------RGVVNL--VEWaNKVIYQGehlrVALFasiSFDASVTEIFASLL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPKFSASQFWDDCQ---KHRVTVfqyigelcrylVNQPPS----------KAECDHKVRLAVGSGLRPDTWER 266
Cdd:cd17655 202 SGNTLYIVRKETVLDGQALTQyirQNRITI-----------IDLTPAhlklldaaddSEGLSLKHLIVGGEALSTELAKK 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 267 FLRRFGP-LQILETYGMTEGNV--ATFNYTGrqgavgraSWLYKHIFPFslirydvmtGEPIRNAQGHCMTTS----P-G 338
Cdd:cd17655 271 IIELFGTnPTITNAYGPTETTVdaSIYQYEP--------ETDQQVSVPI---------GKPLGNTRIYILDQYgrpqPvG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 339 EPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEV 418
Cdd:cd17655 334 VAGELY--IGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEAR 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755503902 419 LETLDFLQEVNIygVTVPGHEGRAGMAA-LALRPPqaLNLVQLYSHVSENLPPYARPR-FLRL 479
Cdd:cd17655 412 LLQHPDIKEAVV--IARKDEQGQNYLCAyIVSEKE--LPVAQLREFLARELPDYMIPSyFIKL 470
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
116-437 |
4.21e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 62.45 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 116 AADQVDEPVPGYLSAPQNIMDTCLYIFT-SGTTGLPKAARISHLKVLQcqgfyH------LCGVHQEDVIYLALPlyhMS 188
Cdd:PRK06164 161 LFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLR-----HaraiarAYGYDPGAVLLAALP---FC 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 189 GS--LLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGS---GLRpDT 263
Cdd:PRK06164 233 GVfgFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASfapALG-EL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 264 WERFLRRFGPLQILetYGMTE------GNVATFNYTGRQGAVGRAswlykhIFPFSLIRY-DVMTGEPIrnaqghcmttS 336
Cdd:PRK06164 312 AALARARGVPLTGL--YGSSEvqalvaLQPATDPVSVRIEGGGRP------ASPEARVRArDPQDGALL----------P 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 337 PGEPGLLvaPVSQQSPFLGYAGAPELAKDKLlkdvfwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVA 416
Cdd:PRK06164 374 DGESGEI--EIRAPSLMRGYLDNPDATARAL------TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
330 340
....*....|....*....|.
gi 755503902 417 EVLETLDFLQEVNIYGVTVPG 437
Cdd:PRK06164 446 HALEALPGVAAAQVVGATRDG 466
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
142-284 |
6.76e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 61.54 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHlKVL------QCQG----FYhlcgVHQEDVIYLALPLYHMSgSLLGIVGC-LGIGATVVLKPKF 210
Cdd:PLN02246 186 YSSGTTGLPKGVMLTH-KGLvtsvaqQVDGenpnLY----FHSDDVILCVLPMFHIY-SLNSVLLCgLRVGAAILIMPKF 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 211 SASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLaVGSGLRP--DTWERFLRRFGPLQIL-ETYGMTE 284
Cdd:PLN02246 260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRM-VLSGAAPlgKELEDAFRAKLPNAVLgQGYGMTE 335
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
46-454 |
8.92e-10 |
|
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: 61.14 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 46 PPLYAEdpcctASAAAVRVRSCWPQLGLPT-LVEFleSLEPDLPALRAMGLHLwatgpetnvaGISNLLSEAADQVDEPV 124
Cdd:cd05906 97 PPTYDE-----PNARLRKLRHIWQLLGSPVvLTDA--ELVAEFAGLETLSGLP----------GIRVLSIEELLDTAADH 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 125 PGYLSAPQnimDTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSL-LGI----VGCL 198
Cdd:cd05906 160 DLPQSRPD---DLALLMLTSGSTGFPKAVPLTHRNILaRSAGKIQHNGLTPQDVFLNWVPLDHVGGLVeLHLravyLGCQ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 199 GIGA---TVVLKPkfsaSQFWDDCQKHRVTV-----FQYiGELCRYLVNQPPSKAECDhKVRLAVGSG--LRPDTWERFL 268
Cdd:cd05906 237 QVHVpteEILADP----LRWLDLIDRYRVTItwapnFAF-ALLNDLLEEIEDGTWDLS-SLRYLVNAGeaVVAKTIRRLL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 269 RRFGPLQ-----ILETYGMTE-GNVATFNYTGRQGAVGRASwlykhifPF-SLIRydVMTGEPIRNAQGHCMTTSPGEPG 341
Cdd:cd05906 311 RLLEPYGlppdaIRPAFGMTEtCSGVIYSRSFPTYDHSQAL-------EFvSLGR--PIPGVSMRIVDDEGQLLPEGEVG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLvaPVSQQSPFLGYAGAPELAKDKLLKDvFWsgdvfFNTGDLLVCDEqGFLHFHDRTGDTFRWKGENVATTEVAEVLET 421
Cdd:cd05906 382 RL--QVRGPVVTKGYYNNPEANAEAFTED-GW-----FRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEE 452
|
410 420 430
....*....|....*....|....*....|...
gi 755503902 422 LDflqevniyGVTVpghegrAGMAALALRPPQA 454
Cdd:cd05906 453 VP--------GVEP------SFTAAFAVRDPGA 471
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
136-432 |
1.27e-09 |
|
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: 60.45 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKpkfSASQ 214
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYF-IFACGCSQAYT---SIRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQ---------YIGeLCRYLVNQPPSKAECDH------KVRLAV-GSGLRPDTWERFLRRFGpLQILE 278
Cdd:cd17640 165 LKDDLKRVKPHYIVsvprlweslYSG-IQKQVSKSSPIKQFLFLfflsggIFKFGIsGGGALPPHVDTFFEAIG-IEVLN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 279 TYGMTE-GNVATFNYTGR--QGAVGraswlykHIFPFSLIRY-DVMTGEPirnaqghcmtTSPGEPGLLVApvsqQSP-- 352
Cdd:cd17640 243 GYGLTEtSPVVSARRLKCnvRGSVG-------RPLPGTEIKIvDPEGNVV----------LPPGEKGIVWV----RGPqv 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 353 FLGYAGAPElAKDKLLkdvfwSGDVFFNTGDL--LVCDeqGFLHFHDRTGDTFRWK-GENVATTEVAEVLETLDFLQEVN 429
Cdd:cd17640 302 MKGYYKNPE-ATSKVL-----DSDGWFNTGDLgwLTCG--GELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIM 373
|
...
gi 755503902 430 IYG 432
Cdd:cd17640 374 VVG 376
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
141-476 |
1.45e-09 |
|
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: 60.26 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQGFYHLC-GVHQED--VIYLAlplYHMSGSLLGIVGCLGIGATVVLKP---KFSASQ 214
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPYfGVTPADksLVYAS---FSFDASAWEIFPHLTAGAALHVVPserRLDLDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVFQYIGELCRYLVNQPpskaecDHKVRLAVGSGlrpDTWERFLRRfgPLQILETYGMTEGNV-ATfnyt 293
Cdd:cd17645 187 LNDYFNQEGITISFLPTGAAEQFMQLD------NQSLRVLLTGG---DKLKKIERK--GYKLVNNYGPTENTVvAT---- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 grqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLL 368
Cdd:cd17645 252 ---------------SFEIDKPYANIPIGKPIDNTRvyilDEALQLQPiGVAGELC--IAGEGLARGYLNRPELTAEKFI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 KDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEvniygVTVPGHEGRAGMAALA 448
Cdd:cd17645 315 VHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIEL-----AAVLAKEDADGRKYLV 389
|
330 340 350
....*....|....*....|....*....|
gi 755503902 449 --LRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17645 390 ayVTAPEEIPHEELREWLKNDLPDYMIPTY 419
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
83-477 |
1.88e-09 |
|
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: 59.98 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPALRAMGL-----------HLWATGPETNVAGISNLLSEAADQVDEPVPGyLSAPQnimDTCLYIFTSGTTGLPK 151
Cdd:cd12114 67 VDIDQPAARREAIladagarlvltDGPDAQLDVAVFDVLILDLDALAAPAPPPPV-DVAPD---DLAYVIFTSGSTGTPK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 152 AARISHLKVLQ-CQGFYHLCGVHQEDVIyLALPLYHMSGSLLGIVGCLGIGATVVLKP---KFSASQFWDDCQKHRVTVF 227
Cdd:cd12114 143 GVMISHRAALNtILDINRRFAVGPDDRV-LALSSLSFDLSVYDIFGALSAGATLVLPDearRRDPAHWAELIERHGVTLW 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 228 QYIGELCRYLVNQPPSKAECDHKVRLAVGSG--LRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWL 305
Cdd:cd12114 222 NSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 306 YKhiFPFSLIRYDVMtgepirNAQG-HCMTTSPGE---PGLLVApvsqqspfLGYAGAPELAKDKLLKDVfwSGDVFFNT 381
Cdd:cd12114 302 YG--RPLANQRYRVL------DPRGrDCPDWVPGElwiGGRGVA--------LGYLGDPELTAARFVTHP--DGERLYRT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 382 GDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETldfLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQ-- 459
Cdd:cd12114 364 GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQA---HPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPda 440
|
410
....*....|....*...
gi 755503902 460 LYSHVSENLPPYARPRFL 477
Cdd:cd12114 441 LRAFLAQTLPAYMIPSRV 458
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
142-433 |
5.94e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 58.67 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVL-------QCQGFYHlcgvhqEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLK-PKFSAS 213
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnngyfigEAMKLTE------EDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPgEGFDPL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWDDCQKHRVTVFQ-----YIGELcrylvnQPPSKAECDHkvrlavgSGLR---------P-DTWERFLRRFGPLQILE 278
Cdd:PRK08315 280 ATLAAVEEERCTALYgvptmFIAEL------DHPDFARFDL-------SSLRtgimagspcPiEVMKRVIDKMHMSEVTI 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 279 TYGMTEGN-VATFNYTG-----RQGAVGRAswlykhiFPFSLIR-YDVMTGEpirnaqghcmTTSPGEPGLLVApvSQQS 351
Cdd:PRK08315 347 AYGMTETSpVSTQTRTDdplekRVTTVGRA-------LPHLEVKiVDPETGE----------TVPRGEQGELCT--RGYS 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 352 PFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDEQGFLHFhdrTGdtfRWK------GENVATTEVAEVLETLDFL 425
Cdd:PRK08315 408 VMKGYWNDPEKTAEAIDAD----G--WMHTGDLAVMDEEGYVNI---VG---RIKdmiirgGENIYPREIEEFLYTHPKI 475
|
....*...
gi 755503902 426 QEVNIYGV 433
Cdd:PRK08315 476 QDVQVVGV 483
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
115-421 |
7.66e-09 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 58.16 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 115 EAADQVDEPVPGyLSAPQNIMdtclyiFTSGTTGLPKAARISH----LKVLQCQGFYHLCGvHQEDVIYLA-LPLYHMSG 189
Cdd:cd05929 112 AEGGSPETPIED-EAAGWKML------YSGGTTGRPKGIKRGLpggpPDNDTLMAAALGFG-PGADSVYLSpAPLYHAAP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 190 SLLGIVGcLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPpskAECDHKVRLA-------VGSGLRPD 262
Cdd:cd05929 184 FRWSMTA-LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLP---EAVRNAYDLSslkrvihAAAPCPPW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 263 TWERFLRRFGPLqILETYGMTEGNVATF----NYTGRQGAVGRAswlykhifpfslirydVMTGEPIRNAQGH-CMTTSP 337
Cdd:cd05929 260 VKEQWIDWGGPI-IWEYYGGTEGQGLTIingeEWLTHPGSVGRA----------------VLGKVHILDEDGNeVPPGEI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 GEPGLLVAPvsqqsPFLgYAGAPELAKDKLLKDVFWSgdvffnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAE 417
Cdd:cd05929 323 GEVYFANGP-----GFE-YTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIEN 390
|
....
gi 755503902 418 VLET 421
Cdd:cd05929 391 ALIA 394
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
91-466 |
1.14e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 57.69 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 91 RAMGL-HLWATGPetnvAGISNLLSEAADQVdEPVPgyLSAPQNIMDTCLYIFTSGTTGLPKAARISH-----LKVLQCQ 164
Cdd:PRK06188 130 RVPSLkHVLTLGP----VPDGVDLLAAAAKF-GPAP--LVAAALPPDIAGLAYTGGTTGKPKGVMGTHrsiatMAQIQLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 165 GFYHlcgvhQEDVIYLAL-PLYHMSGSLlgIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPS 243
Cdd:PRK06188 203 EWEW-----PADPRFLMCtPLSHAGGAF--FLPTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 244 KAECDHKVRLAV--GSGLRPDTWERFLRRFGPLqILETYGMTE-GNVATF--------NYTGRQGAVGRASwlykhifPF 312
Cdd:PRK06188 276 RTRDLSSLETVYygASPMSPVRLAEAIERFGPI-FAQYYGQTEaPMVITYlrkrdhdpDDPKRLTSCGRPT-------PG 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 313 SLIRYDVMTGEPIrnaqghcmttSPGEPG-LLVApvsqqSPFL--GYAGAPElAKDKLLKDVfWsgdvfFNTGDLLVCDE 389
Cdd:PRK06188 348 LRVALLDEDGREV----------AQGEVGeICVR-----GPLVmdGYWNRPE-ETAEAFRDG-W-----LHTGDVAREDE 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 390 QGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAGMAALALRPPQALNLVQLYSHVSE 466
Cdd:PRK06188 406 DGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKE 481
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
141-448 |
1.28e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 57.71 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLK------VLQCQGFYHLCGVHQEdVIYLALPLYHMSGsLLGIVGCLGIGATVVLKPKFSAS- 213
Cdd:PRK05857 175 IFTSGTTGEPKAVLLANRTffavpdILQKEGLNWVTWVVGE-TTYSPLPATHIGG-LWWILTCLMHGGLCVTGGENTTSl 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 -QFWDDcqkHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWE-RFLRRFGpLQILETYGMTE------- 284
Cdd:PRK05857 253 lEILTT---NAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADvRFIEATG-VRTAQVYGLSEtgctalc 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 -----GNVATFnytgRQGAVGRaswlykhifPFSLIR-YdvmtgepIRNAQGHCMTTSPGEPGLLVAPVSQQSP--FLGY 356
Cdd:PRK05857 329 lptddGSIVKI----EAGAVGR---------PYPGVDvY-------LAATDGIGPTAPGAGPSASFGTLWIKSPanMLGY 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLkdvfwsgDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVP 436
Cdd:PRK05857 389 WNNPERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
|
330
....*....|..
gi 755503902 437 GHEGRAGMAALA 448
Cdd:PRK05857 462 EFGALVGLAVVA 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
107-474 |
1.93e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 107 AGISNLLSEAADQVDEpVPGYLSAPQNIMDTCLY-IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPl 184
Cdd:PRK12316 2118 AGVARLPLDRDAEWAD-YPDTAPAVQLAGENLAYvIYTSGSTGLPKGVAVSHGALVAhCQAAGERYELSPADCELQFMS- 2195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 185 YHMSGSLLGIVGCLGIGATVVLKPK--FSASQFWDDCQKHRVTV-------FQYIGELCRYLVNQPPSKAECdhkvrlAV 255
Cdd:PRK12316 2196 FSFDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTIldfppvyLQQLAEHAERDGRPPAVRVYC------FG 2269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 256 GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYT-GRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMT 334
Cdd:PRK12316 2270 GEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKcRPQDPCGAAY---------------VPIGRALGNRRAYILD 2334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 335 TS-----PGEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:PRK12316 2335 ADlnllaPGMAGELY--LGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGF 2412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 409 NVATTEVAEVLETLDFLQEVNIygVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVP 2476
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
136-427 |
2.22e-08 |
|
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: 56.68 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQ 214
Cdd:cd05914 90 DVALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FwDDCQKHRVTVFqyIGeLCRYLV-------NQPPSKAECDHKVRLAV-----------------------------GSG 258
Cdd:cd05914 170 I-IALAFAQVTPT--LG-VPVPLViekifkmDIIPKLTLKKFKFKLAKkinnrkirklafkkvheafggnikefvigGAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 259 LRPDTwERFLRRFGpLQILETYGMTE-GNVATFNYTGRqgavgraswlykhifpfslIRYDvMTGEPIRNAQghCMTTSP 337
Cdd:cd05914 246 INPDV-EEFLRTIG-FPYTIGYGMTEtAPIISYSPPNR-------------------IRLG-SAGKVIDGVE--VRIDSP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 ---GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDvFWsgdvfFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATT 413
Cdd:cd05914 302 dpaTGEGEII--VRGPNVMKGYYKNPEATAEAFDKD-GW-----FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPE 373
|
330 340
....*....|....*....|.
gi 755503902 414 EV-------AEVLETLDFLQE 427
Cdd:cd05914 374 EIeakinnmPFVLESLVVVQE 394
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
141-479 |
2.74e-08 |
|
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: 56.17 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQCQGFY-HLCGVHQedviyLALPLYHMSG----SLLGIVGCLGIGATVVLKPkfSASQF 215
Cdd:cd12115 111 IYTSGSTGRPKGVAIEHRNAAAFLQWAaAAFSAEE-----LAGVLASTSIcfdlSVFELFGPLATGGKVVLAD--NVLAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 WDDCQKHRVTVFQYIGELCRYLVNQP--PSKAECdhkVRLAvGSGLRPDTWERFLRRFGPLQILETYGMTEgnvATFNYT 293
Cdd:cd12115 184 PDLPAAAEVTLINTVPSAAAELLRHDalPASVRV---VNLA-GEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYST 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 294 GrqGAVGRASwlykhifpfsliRYDVMTGEPIRNAQGHCMTTS-----PGEPGLLV---APVSQqspflGYAGAPELAKD 365
Cdd:cd12115 257 V--APVPPGA------------SGEVSIGRPLANTQAYVLDRAlqpvpLGVPGELYiggAGVAR-----GYLGRPGLTAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 366 KLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVnIYGVTVPGHEGRAGMA 445
Cdd:cd12115 318 RFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREA-VVVAIGDAAGERRLVA 396
|
330 340 350
....*....|....*....|....*....|....*
gi 755503902 446 ALALRPPQALNLVQLYSHVSENLPPYARP-RFLRL 479
Cdd:cd12115 397 YIVAEPGAAGLVEDLRRHLGTRLPAYMVPsRFVRL 431
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
136-477 |
3.16e-08 |
|
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: 56.33 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLY-IFTSGTTGLPKAARISHLKVLQCQGFY--HLCGVHQEDVIYLALPLYHMSGSllGIVGCLGIGATVVLKP---K 209
Cdd:cd17656 128 DDLLYiIYTSGTTGKPKGVQLEHKNMVNLLHFEreKTNINFSDKVLQFATCSFDVCYQ--EIFSTLLSGGTLYIIReetK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 210 FSASQFWDDCQKHR-------VTVFQYIGELCRYLvnqpPSKAEC-DHKVrlAVGSGLR-PDTWERFLRRFGpLQILETY 280
Cdd:cd17656 206 RDVEQLFDLVKRHNievvflpVAFLKFIFSEREFI----NRFPTCvKHII--TAGEQLViTNEFKEMLHEHN-VHLHNHY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 281 GMTEGNVATfNYTGRQGAvgraswlykHIFPFSLIrydvmtGEPIRNAQ----GHCMTTSP-GEPGLLVapVSQQSPFLG 355
Cdd:cd17656 279 GPSETHVVT-TYTINPEA---------EIPELPPI------GKPISNTWiyilDQEQQLQPqGIVGELY--ISGASVARG 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQE--VNIYGV 433
Cdd:cd17656 341 YLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEavVLDKAD 420
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755503902 434 TVPGHEGRAGMAALalrppQALNLVQLYSHVSENLPPYARPRFL 477
Cdd:cd17656 421 DKGEKYLCAYFVME-----QELNISQLREYLAKQLPEYMIPSFF 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-474 |
4.16e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPALRAM------GLHLWATGPE---TNVAGISNLLSEA-ADQVDEPVPGYLSAPQNImdtCLYIFTSGTTGLPKA 152
Cdd:PRK12316 3137 LDPEYPEERLAymledsGAQLLLSQSHlrlPLAQGVQVLDLDRgDENYAEANPAIRTMPENL---AYVIYTSGSTGKPKG 3213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 153 ARISHLKVLQcqgfyHLCGVHQ-----EDVIYLALPLYHMSGSLLGIVGCLGIGATVVLkpkfSASQFWDD-------CQ 220
Cdd:PRK12316 3214 VGIRHSALSN-----HLCWMQQayglgVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL----AGPEDWRDpallvelIN 3284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 221 KHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFlrrFGPLQILETYGMTEgnvatfnytgrqGAVG 300
Cdd:PRK12316 3285 SEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTE------------ATIT 3349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 301 RASWLYKHIFPFSlirydVMTGEPIRNAQGHCM----TTSP-GEPGLLVapVSQQSPFLGYAGAPELAKDKLLKDVFWSG 375
Cdd:PRK12316 3350 VTHWQCVEEGKDA-----VPIGRPIANRACYILdgslEPVPvGALGELY--LGGEGLARGYHNRPGLTAERFVPDPFVPG 3422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 376 DVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLetldfLQEVNIYGVTVPGHEGRAGMAALALRPPQAL 455
Cdd:PRK12316 3423 ERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL-----LEHPWVREAVVLAVDGRQLVAYVVPEDEAGD 3497
|
410
....*....|....*....
gi 755503902 456 NLVQLYSHVSENLPPYARP 474
Cdd:PRK12316 3498 LREALKAHLKASLPEYMVP 3516
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
74-408 |
8.84e-08 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. 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: 54.94 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 74 PTLVEFLESLEPDLPALRA-----MGLHLWATGPETNVAgISNLLSEAADQVDEPVpgylsAPQNIMDTCLYifTSGTTG 148
Cdd:cd12119 105 RDFLPLLEAIAPRLPTVEHvvvmtDDAAMPEPAGVGVLA-YEELLAAESPEYDWPD-----FDENTAAAICY--TSGTTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 149 LPKAARISH-------LKVLQCQGFyhlcGVHQEDVIYLALPLYHMSGSLLGIVgCLGIGATVVLKPKF----SASQFWD 217
Cdd:cd12119 177 NPKGVVYSHrslvlhaMAALLTDGL----GLSESDVVLPVVPMFHVNAWGLPYA-AAMVGAKLVLPGPYldpaSLAELIE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 dcqKHRVTVFQ-----YIGELCRYLVNqppsKAECDHKVRLAV-GSGLRPDTWERFLRRFgpLQILETYGMTEgnvatfn 291
Cdd:cd12119 252 ---REGVTFAAgvptvWQGLLDHLEAN----GRDLSSLRRVVIgGSAVPRSLIEAFEERG--VRVIHAWGMTE------- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 292 yTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEP-------IRNAQGHCMTTSPGEPGLLVApvsqQSPFL--GYAGAPEl 362
Cdd:cd12119 316 -TSPLGTVARPPSEHSNLSEDEQLALRAKQGRPvpgvelrIVDDDGRELPWDGKAVGELQV----RGPWVtkSYYKNDE- 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 755503902 363 akdkllKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGE 408
Cdd:cd12119 390 ------ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGE 429
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-480 |
1.33e-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: 341278 [Multi-domain] Cd Length: 432 Bit Score: 54.11 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLK--VLQCQGFYHLcGVHQEDViylalplyHMSGSLLG--------IVGCLGIGATVV 205
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDV--------HWNISSPGwakhawscFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 206 L--KPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAecDHKVRLAVGSG--LRPDTWERFLRRFGpLQILETYG 281
Cdd:cd05974 157 LfnYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF--DVKLREVVGAGepLNPEVIEQVRRAWG-LTIRDGYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 282 MTEGNVATFNYTG---RQGAVGRAswlykhifpfsLIRYDVMTGEPIrnaqghcmtTSPGEPGLLVAPVSQQSP---FLG 355
Cdd:cd05974 234 QTETTALVGNSPGqpvKAGSMGRP-----------LPGYRVALLDPD---------GAPATEGEVALDLGDTRPvglMKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 356 YAGAPELAKDKLlkdvfwsGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIygVTV 435
Cdd:cd05974 294 YAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV--VPS 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALAL-----RPPQALNLVqLYSHVSENLPPYARPRflRLQ 480
Cdd:cd05974 365 PDPVRLSVPKAFIVlragyEPSPETALE-IFRFSRERLAPYKRIR--RLE 411
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
136-288 |
1.90e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.85 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQE-DVIYLALPLYH-MsgsllGIVGCLGI----GATVVlkp 208
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAVQITHGNLYANaEAMFVAAEFDVEtDVMVSWLPLFHdM-----GMVGFLTVpmyfGAELV--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 209 KFSASQFWDD-------CQKHRVTV-----FQYiGELCRYLVNQPPSKAECDHKVRLAV--GSGLRPDTWERFLR---RF 271
Cdd:PRK07768 225 KVTPMDFLRDpllwaelISKYRGTMtaapnFAY-ALLARRLRRQAKPGAFDLSSLRFALngAEPIDPADVEDLLDagaRF 303
|
170
....*....|....*....
gi 755503902 272 G--PLQILETYGMTEGNVA 288
Cdd:PRK07768 304 GlrPEAILPAYGMAEATLA 322
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
82-284 |
2.41e-07 |
|
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: 53.40 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 82 SLEPDLPALRAMGLHLWATGPETnVAGISNLLSEAADQVDEPVPGYLsapqnimDTCLYIFTSGTTGLPKAARISHLKVL 161
Cdd:cd05931 104 TTAAALAAVRAFAASRPAAGTPR-LLVVDLLPDTSAADWPPPSPDPD-------DIAYLQYTSGSTGTPKGVVVTHRNLL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 162 -QCQGFYHLCGVHQEDVIYLALPLYH-MsgsllGIVGCLGI----GATVVLkpkFSASQF------W-DDCQKHRVTV-- 226
Cdd:cd05931 176 aNVRQIRRAYGLDPGDVVVSWLPLYHdM-----GLIGGLLTplysGGPSVL---MSPAAFlrrplrWlRLISRYRATIsa 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755503902 227 ---FQYigELC-RYLvnQPPSKAECD-HKVRLAVgSG---LRPDTWERFLRRFGPL-----QILETYGMTE 284
Cdd:cd05931 248 apnFAY--DLCvRRV--RDEDLEGLDlSSWRVAL-NGaepVRPATLRRFAEAFAPFgfrpeAFRPSYGLAE 313
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
136-432 |
4.15e-07 |
|
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: 52.60 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVL-QCQGFYH----LCGVHQEDVIYLALPLYHMSGSLLgIVGCLGIGATV------ 204
Cdd:cd05927 115 DLATICYTSGTTGNPKGVMLTHGNIVsNVAGVFKileiLNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIgfysgd 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 ---------VLKPKFSAS------QFWDDCQKHRV-------TVFQYIGELCRYLVNQPPSKAE------CDHKVRLAVG 256
Cdd:cd05927 194 irlllddikALKPTVFPGvprvlnRIYDKIFNKVQakgplkrKLFNFALNYKLAELRSGVVRASpfwdklVFNKIKQALG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 257 SGLR----------PDTwERFLRR-FGpLQILETYGMTEGNVATFnyTGRQGavgraSWLYKHI---FPFSLIR------ 316
Cdd:cd05927 274 GNVRlmltgsaplsPEV-LEFLRVaLG-CPVLEGYGQTECTAGAT--LTLPG-----DTSVGHVggpLPCAEVKlvdvpe 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 317 --YDVMTGEP-----IRnaqGHCMttspgepgllvapvsqqspFLGYAGAPELAKDKLLKDvfwsGdvFFNTGDLLVCDE 389
Cdd:cd05927 345 mnYDAKDPNPrgevcIR---GPNV-------------------FSGYYKDPEKTAEALDED----G--WLHTGDIGEWLP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 755503902 390 QGFLHFHDRTGDTFRW-KGENVAttevAEVLETL----DFLQEVNIYG 432
Cdd:cd05927 397 NGTLKIIDRKKNIFKLsQGEYVA----PEKIENIyarsPFVAQIFVYG 440
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
136-476 |
4.41e-07 |
|
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: 51.92 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLqCQGFyHLCGVHQ--EDVIYL-ALPLYHMsGSLLGIVGCLGIGATVVLKPKFSA 212
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALL-AQAL-VLAVLQAidEGTVFLnSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 213 SQFWDDCQKHRVT----VFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGplqileTYGMTE-GNV 287
Cdd:cd17636 78 EEVLELIEAERCThaflLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG------GYGQTEvMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 ATFNYTGRQ--GAVGRASwlykhifPFSLIRydvmtgepIRNAQGHcmTTSPGEPGLLVApvsqQSP--FLGYAGAPELA 363
Cdd:cd17636 152 ATFAALGGGaiGGAGRPS-------PLVQVR--------ILDEDGR--EVPDGEVGEIVA----RGPtvMAGYWNRPEVN 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 364 KDKlLKDVFWsgdvffNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHeGRAG 443
Cdd:cd17636 211 ARR-TRGGWH------HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRW-AQSV 282
|
330 340 350
....*....|....*....|....*....|...
gi 755503902 444 MAALALRPPQALNLVQLYSHVSENLPPYARPRF 476
Cdd:cd17636 283 KAIVVLKPGASVTEAELIEHCRARIASYKKPKS 315
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
138-284 |
5.35e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 52.09 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 138 CLYIFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIYLALPLyHMSGSLLGIVGCLGIGATVVLKP---KFSAS 213
Cdd:cd17654 121 AYVIHTSGTTGTPKIVAVPHKCILPnIQHFRSLFNITSEDILFLTSPL-TFDPSVVEIFLSLSSGATLLIVPtsvKVLPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 214 QFWD-DCQKHRVTVFQyigeLCRYLVNQPPSKAECDHKVR-------LAVGSGLRP-DTWERFLRRFGP-LQILETYGMT 283
Cdd:cd17654 200 KLADiLFKRHRITVLQ----ATPTLFRRFGSQSIKSTVLSatsslrvLALGGEPFPsLVILSSWRGKGNrTRIFNIYGIT 275
|
.
gi 755503902 284 E 284
Cdd:cd17654 276 E 276
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
83-474 |
1.28e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 83 LEPDLPALR----------AMGLHLWATGPETNV-AGISNLlseAADQVDEPVPGYLSAPqniMDTCLY-------IFTS 144
Cdd:PRK12316 591 LDPEYPAERlaymledsgvQLLLSQSHLGRKLPLaAGVQVL---DLDRPAAWLEGYSEEN---PGTELNpenlayvIYTS 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 145 GTTGLPKAARISH--LKVLQC--QGFYHLcGVHQEdviYLALPLYHMSGSLLGIVGCLGIGATVVLKPK---FSASQFWD 217
Cdd:PRK12316 665 GSTGKPKGAGNRHraLSNRLCwmQQAYGL-GVGDT---VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 DCQKHRVTVFQYIGELCRYLVnQPPSKAECDHKVRLAV-GSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQ 296
Cdd:PRK12316 741 LINREGVDTLHFVPSMLQAFL-QDEDVASCTSLRRIVCsGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVE 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 297 gAVGRAswlykhifpfslirydVMTGEPIRNAQGHCMttspgEPGLLVAPVSQQSPFL--------GYAGAPELAKDKLL 368
Cdd:PRK12316 820 -EGGDS----------------VPIGRPIANLACYIL-----DANLEPVPVGVLGELYlagrglarGYHGRPGLTAERFV 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 369 KDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVtvpghEGRAGMAALA 448
Cdd:PRK12316 878 PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGKQLVGYVV 952
|
410 420
....*....|....*....|....*.
gi 755503902 449 LRPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK12316 953 LESEGGDWREALKAHLAASLPEYMVP 978
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
414-479 |
1.51e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 46.00 E-value: 1.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755503902 414 EVAEVLETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRL 479
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDE-LKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVF 65
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
141-209 |
5.87e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 49.10 E-value: 5.87e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755503902 141 IFTSGTTGLPKAArishlkVLQCQGfyHLC---GV------HQEDVIYLALPLYHMSGslLGIV-GCLGIGATVVLKPK 209
Cdd:PRK09029 141 TLTSGSTGLPKAA------VHTAQA--HLAsaeGVlslmpfTAQDSWLLSLPLFHVSG--QGIVwRWLYAGATLVVRDK 209
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
60-284 |
1.08e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 48.17 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 60 AAVRVRSCWPQLgLPTLVEFLeslePDLPALR------AMGLHLWATGPETNV--AGISNLLSEAADQVDEPVPgylSAP 131
Cdd:PLN02736 149 AEVAAIFCVPQT-LNTLLSCL----SEIPSVRlivvvgGADEPLPSLPSGTGVeiVTYSKLLAQGRSSPQPFRP---PKP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 132 QNIMDTClyiFTSGTTGLPKAARISHLK-VLQCQGFYHLCGVHQEDVIYLALPLYHMSgSLLGIVGCLGIGATV------ 204
Cdd:PLN02736 221 EDVATIC---YTSGTTGTPKGVVLTHGNlIANVAGSSLSTKFYPSDVHISYLPLAHIY-ERVNQIVMLHYGVAVgfyqgd 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 205 VLKpkfsasqFWDDCQKHRVTVF------------------QYIGELCRYLVN-------------QPPS---------- 243
Cdd:PLN02736 297 NLK-------LMDDLAALRPTIFcsvprlynriydgitnavKESGGLKERLFNaaynakkqalengKNPSpmwdrlvfnk 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755503902 244 -KAECDHKVRLaVGSG---LRPDTWErFLRR-FGPlQILETYGMTE 284
Cdd:PLN02736 370 iKAKLGGRVRF-MSSGaspLSPDVME-FLRIcFGG-RVLEGYGMTE 412
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
139-242 |
1.36e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 48.20 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLalpLYHMS-GSL---LGIVGCLGIGATVVL------K 207
Cdd:PTZ00237 257 LYIlYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVV---FSHSSiGWVsfhGFLYGSLSLGNTFVMfeggiiK 333
|
90 100 110
....*....|....*....|....*....|....*
gi 755503902 208 PKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP 242
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDP 368
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
72-227 |
3.13e-05 |
|
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: 46.88 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 72 GLPTLVEFLEslepdLPALRAMGLHLWATGPetNVAGISNLLSEAADQVDEPVPGYLSAPqnimdtcLYI-FTSGTTGLP 150
Cdd:cd05943 199 GLPSLLAVVV-----VPYTVAAGQPDLSKIA--KALTLEDFLATGAAGELEFEPLPFDHP-------LYIlYSSGTTGLP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 151 KA-------ARISHLKVLQCQgfyhlCGVHQEDVI-YLALPLYHMSGSLlgiVGCLGIGATVVL------KPKFSAsqFW 216
Cdd:cd05943 265 KCivhgaggTLLQHLKEHILH-----CDLRPGDRLfYYTTCGWMMWNWL---VSGLAVGATIVLydgspfYPDTNA--LW 334
|
170
....*....|.
gi 755503902 217 DDCQKHRVTVF 227
Cdd:cd05943 335 DLADEEGITVF 345
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
85-302 |
4.58e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 46.03 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 85 PDLPALRAMGLHLWATGPETNVAGISnLLSEAADQVDEPVPGYLSApqnimDTCLYIFTSGTTGLPKAA--RISHLKVLQ 162
Cdd:PRK07798 119 PRLPKLRTLVVVEDGSGNDLLPGAVD-YEDALAAGSPERDFGERSP-----DDLYLLYTGGTTGMPKGVmwRQEDIFRVL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 163 CQGFYHLCG--VHQED------------VIYLALPLYHMSGsLLGIVGCLGIGATVVL--KPKFSASQFWDDCQKHRVTV 226
Cdd:PRK07798 193 LGGRDFATGepIEDEEelakraaagpgmRRFPAPPLMHGAG-QWAAFAALFSGQTVVLlpDVRFDADEVWRTIEREKVNV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 227 FQYIGE-LCRYLVN--QPPSKAECDHKVrlAVGSG---LRPDTWERFLRRFGPLQILETYGMTEgnvATFNYTGRQ--GA 298
Cdd:PRK07798 272 ITIVGDaMARPLLDalEARGPYDLSSLF--AIASGgalFSPSVKEALLELLPNVVLTDSIGSSE---TGFGGSGTVakGA 346
|
....
gi 755503902 299 VGRA 302
Cdd:PRK07798 347 VHTG 350
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
117-284 |
4.59e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 117 ADQVDEPVPgYLSAPQNimdTCLYIFTSGTTGLPKAARISHLKV-LQCQGFYHLCGVHQEDViylALPLYHM-----SGS 190
Cdd:PRK05691 2319 AAYSDAPLP-FLSLPQH---QAYLIYTSGSTGKPKGVVVSHGEIaMHCQAVIERFGMRADDC---ELHFYSInfdaaSER 2391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 191 LLGIVGClgiGATVVLKpkfsASQFWDD---CQ---KHRVTVF----QYIGELCRYLVNQPPSKAecdhkVRLAV--GSG 258
Cdd:PRK05691 2392 LLVPLLC---GARVVLR----AQGQWGAeeiCQlirEQQVSILgftpSYGSQLAQWLAGQGEQLP-----VRMCItgGEA 2459
|
170 180
....*....|....*....|....*.
gi 755503902 259 LRPDTWERFLRRFGPLQILETYGMTE 284
Cdd:PRK05691 2460 LTGEHLQRIRQAFAPQLFFNAYGPTE 2485
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
108-437 |
5.70e-05 |
|
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: 45.91 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 108 GISNL---LSEAADQvdepvpGYLSAPQnIMDTCLYIFTSGTTGLPKAARISH-LKVLQCQGFYHLCGVHQEDVIYLALP 183
Cdd:cd05910 62 GRKNLkqcLQEAEPD------AFIGIPK-ADEPAAILFTSGSTGTPKGVVYRHgTFAAQIDALRQLYGIRPGEVDLATFP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 184 LYHMSGSLLGIvgclgigATVV-----LKPKFSASQF-WDDCQKHRVT-------VFQYIGELCRYLVNQPPSkaecdhk 250
Cdd:cd05910 135 LFALFGPALGL-------TSVIpdmdpTRPARADPQKlVGAIRQYGVSivfgspaLLERVARYCAQHGITLPS------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 251 VR--LAVGSGLRPDTWERFLRRFGP-LQILETYGMTE-------GNVATFNYTGRQGAVGRASWLyKHIFPFSLIRYDVM 320
Cdd:cd05910 201 LRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvssiGSRELLATTTAATSGGAGTCV-GRPIPGVRVRIIEI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 321 TGEPIRNAQG-HCMttSPGEPGLLVAPVSQQSP-FLGYAGAPELAKDKLLKDVFWSgdvffNTGDLLVCDEQGFLHFHDR 398
Cdd:cd05910 280 DDEPIAEWDDtLEL--PRGEIGEITVTGPTVTPtYVNRPVATALAKIDDNSEGFWH-----RMGDLGYLDDEGRLWFCGR 352
|
330 340 350
....*....|....*....|....*....|....*....
gi 755503902 399 TGDTFRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPG 437
Cdd:cd05910 353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
139-478 |
5.89e-05 |
|
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: 46.02 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAarishlkVLQCQGFYhLCGV----------HQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVL- 206
Cdd:cd05966 234 LFIlYTSGSTGKPKG-------VVHTTGGY-LLYAattfkyvfdyHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMf 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 207 --KPKF-SASQFWDDCQKHRVTVFqY-----IGELCRYlVNQPPSKaeCDHK-VRL--AVGSGLRPDTWERFLRRFGP-- 273
Cdd:cd05966 306 egTPTYpDPGRYWDIVEKHKVTIF-YtaptaIRALMKF-GDEWVKK--HDLSsLRVlgSVGEPINPEAWMWYYEVIGKer 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 274 LQILETYGMTEgnvatfnyTG------RQGAV----GRASwlykhiFPFSLIRYDVM--TGEPIRNAQGhcmttspgepG 341
Cdd:cd05966 382 CPIVDTWWQTE--------TGgimitpLPGATplkpGSAT------RPFFGIEPAILdeEGNEVEGEVE----------G 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 342 LLVAPVSQQSPFLGYAGAPElakdkLLKDVFWS--GDVFFnTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:cd05966 438 YLVIKRPWPGMARTIYGDHE-----RYEDTYFSkfPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESAL 511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755503902 420 ETLDFLQEVNIYGVTvpgHE--GRAGMAALALRP--PQALNLVQ-LYSHVSENLPPYARPRFLR 478
Cdd:cd05966 512 VAHPAVAEAAVVGRP---HDikGEAIYAFVTLKDgeEPSDELRKeLRKHVRKEIGPIATPDKIQ 572
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
142-417 |
6.90e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.54 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISH----LKVLQCQGFYHLCGVHQEDVIyLALPLYH-----------MSGSLLGIVG-------CLG 199
Cdd:PRK05620 188 YSTGTTGAPKGVVYSHrslyLQSLSLRTTDSLAVTHGESFL-CCVPIYHvlswgvplaafMSGTPLVFPGpdlsaptLAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 200 IGATVVLKPKFSASQFWddcqkhrvtvfqyIGELCRYLVNqPPSKAECdhKVRLAVGSGLRP---DTWERflrRFGpLQI 276
Cdd:PRK05620 267 IIATAMPRVAHGVPTLW-------------IQLMVHYLKN-PPERMSL--QEIYVGGSAVPPiliKAWEE---RYG-VDV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 277 LETYGMTE----GNVATfnytGRQGAVGRASWLYKHI---FPFSLiRYDVMTgepirnaQGHCMTTS---PGE---PGLL 343
Cdd:PRK05620 327 VHVWGMTEtspvGTVAR----PPSGVSGEARWAYRVSqgrFPASL-EYRIVN-------DGQVMESTdrnEGEiqvRGNW 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 344 VAPVSQQSPFLGYAGAPELAKDKLLKDV--FWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKG--------EN--VA 411
Cdd:PRK05620 395 VTASYYHSPTEEGGGAASTFRGEDVEDAndRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGewiysaqlENyiMA 474
|
....*.
gi 755503902 412 TTEVAE 417
Cdd:PRK05620 475 APEVVE 480
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
139-475 |
9.46e-05 |
|
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: 45.14 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYIFTSGTTGLPKAARISHLKVLQC-QGFYHLCGVHQEDVIYLA-LPLYHMSGSLLgIVGCLGIGATVVLKPKFSASQFW 216
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNfMPMSHIAGRIS-LYGTLARGGTAYFAAASDMSTLF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 217 DDCQKHRVT-----------VFQ-YIGELCRYLVN-------QPPSKAECDHKV---RLA---VGSGLRPDTWERFLRRF 271
Cdd:cd17632 306 DDLALVRPTelflvprvcdmLFQrYQAELDRRSVAgadaetlAERVKAELRERVlggRLLaavCGSAPLSAEMKAFMESL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 272 GPLQILETYGMTEGNVATFNytgrqGAVGRASWL-YKHIfpfsliryDVmtgePirnAQGHCMTTSPGEPGLLVapVSQQ 350
Cdd:cd17632 386 LDLDLHDGYGSTEAGAVILD-----GVIVRPPVLdYKLV--------DV----P---ELGYFRTDRPHPRGELL--VKTD 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 351 SPFLGYAGAPELAkdkllKDVFwSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRW-KGENVATTEVAEVLETLDFLQEVN 429
Cdd:cd17632 444 TLFPGYYKRPEVT-----AEVF-DEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIF 517
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755503902 430 IYG---------VTVPGHEGRAGMAALALRPPQALNLVQLYShvSENLPPYARPR 475
Cdd:cd17632 518 VYGnserayllaVVVPTQDALAGEDTARLRAALAESLQRIAR--EAGLQSYEIPR 570
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
263-475 |
1.10e-04 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 44.99 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 263 TWERFLR--RFGPLQILETYGMTE--GNVATfnytgrqgavgraswlykhIFPFSLIRYDVMTGEPIRNAQghcMTTSPG 338
Cdd:PRK07445 242 AWPSLLEqaRQLQLRLAPTYGMTEtaSQIAT-------------------LKPDDFLAGNNSSGQVLPHAQ---ITIPAN 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 339 EPGLLVapVSQQSPFLGYAgaPElakdkllkdvFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEV 418
Cdd:PRK07445 300 QTGNIT--IQAQSLALGYY--PQ----------ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAA 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755503902 419 LETLDFLQEVNIYGVTVPgHEGRAGMAALALRPPQaLNLVQLYSHVSENLPPYARPR 475
Cdd:PRK07445 366 ILATGLVQDVCVLGLPDP-HWGEVVTAIYVPKDPS-ISLEELKTAIKDQLSPFKQPK 420
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
139-227 |
1.63e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 44.40 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKA-------ARISHLKVLQcqgfYHlCGVHQEDVI-YLALPLYHMSGSLlgiVGCLGIGATVVL--- 206
Cdd:PRK03584 266 LWIlYSSGTTGLPKCivhghggILLEHLKELG----LH-CDLGPGDRFfWYTTCGWMMWNWL---VSGLLVGATLVLydg 337
|
90 100
....*....|....*....|....
gi 755503902 207 ---KPKFSAsqFWDDCQKHRVTVF 227
Cdd:PRK03584 338 spfYPDPNV--LWDLAAEEGVTVF 359
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
136-284 |
1.95e-04 |
|
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: 44.13 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 136 DTCLYIFTSGTTGLPKAARISHLKVLQ-CQGFYH-LCGVHQEDVIYLA-LPLYH-----------MSGSLLG-------- 193
Cdd:cd17639 89 DLACIMYTSGSTGNPKGVMLTHGNLVAgIAGLGDrVPELLGPDDRYLAyLPLAHifelaaenvclYRGGTIGygsprtlt 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 194 ---IVGCLgiGATVVLKPKFSAS--QFWDDCQK-----------HRVTVFQYIGELCRYLVNQPPSKAECD----HKVRL 253
Cdd:cd17639 169 dksKRGCK--GDLTEFKPTLMVGvpAIWDTIRKgvlaklnpmggLKRTLFWTAYQSKLKALKEGPGTPLLDelvfKKVRA 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 755503902 254 AVGSGLR----------PDTwERFLRRF-GPlqILETYGMTE 284
Cdd:cd17639 247 ALGGRLRymlsggaplsADT-QEFLNIVlCP--VIQGYGLTE 285
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
142-419 |
2.05e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 44.17 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHL-KVLQCQGFYHLCGVHQEDViYL-ALPLYHMSGSLLGIVGCLGIGATVVLKpKFSASQFWDDC 219
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRgAYLNALSNILAWGMPKHPV-YLwTLPMFHCNGWCFPWTVAARAGTNVCLR-KVDPKLIFDLI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 220 QKHRVTvfqyigELC------RYLVNQPPS-KAECDHKVRLAVGSGLRPDTWERFLRRFGpLQILETYGMTE--GNV--- 287
Cdd:PRK08162 267 REHGVT------HYCgapivlSALINAPAEwRAGIDHPVHAMVAGAAPPAAVIAKMEEIG-FDLTHVYGLTEtyGPAtvc 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 288 --------------ATFNytGRQGavgraswlykhifpfslIRY---------DVMTGEPIrNAQGHCMttspGE---PG 341
Cdd:PRK08162 340 awqpewdalplderAQLK--ARQG-----------------VRYplqegvtvlDPDTMQPV-PADGETI----GEimfRG 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 342 LLVAPvsqqspflGYagapeLAKDKLLKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK08162 396 NIVMK--------GY-----LKNPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
76-455 |
2.50e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.39 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 76 LVEFLESLEPDL--------PALRAMGLHLWATGPEtnVAGISNLLSEAADQVDEP-VPGylsapqniMDTCLYIFTSGT 146
Cdd:PRK05691 108 LLSIIADAEPRLlltvadlrDSLLQMEELAAANAPE--LLCVDTLDPALAEAWQEPaLQP--------DDIAFLQYTSGS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 147 TGLPKAARISHL-----KVLQCQGFYhlCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLkpkFSASQFWDDCQK 221
Cdd:PRK05691 178 TALPKGVQVSHGnlvanEQLIRHGFG--IDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVL---MSPAYFLERPLR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 222 HRVTVFQYIG----------ELCRYLVNQPPSKAECDHKVRLAVgSG---LRPDTWERFLRRFG-----PLQILETYGMT 283
Cdd:PRK05691 253 WLEAISEYGGtisggpdfayRLCSERVSESALERLDLSRWRVAY-SGsepIRQDSLERFAEKFAacgfdPDSFFASYGLA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 284 EgnvATFNYTGRQGAVGRASwLYKHIFPFSLIRYDVMTGEPIRNaqghCMTTSPGEPGLLVAPVSQQ------------- 350
Cdd:PRK05691 332 E---ATLFVSGGRRGQGIPA-LELDAEALARNRAEPGTGSVLMS----CGRSQPGHAVLIVDPQSLEvlgdnrvgeiwas 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 351 --SPFLGYAGAPElAKDKLLkdVFWSGDVFFNTGDLLVCDEqGFLHFHDRTGDTFRWKGENVATTEVAEVLET-LDFLQE 427
Cdd:PRK05691 404 gpSIAHGYWRNPE-ASAKTF--VEHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTVEReVEVVRK 479
|
410 420 430
....*....|....*....|....*....|....*.
gi 755503902 428 --VNIYGVTVPGHEGrAGMAALALR------PPQAL 455
Cdd:PRK05691 480 grVAAFAVNHQGEEG-IGIAAEISRsvqkilPPQAL 514
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
139-475 |
2.81e-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: 43.84 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 139 LYI-FTSGTTGLPKAarishlkVLQCQGFY---------HLCGVHQEDVIYlalplyhmSGSLLGIV--------GCLGI 200
Cdd:cd05967 233 LYIlYTSGTTGKPKG-------VVRDNGGHavalnwsmrNIYGIKPGDVWW--------AASDVGWVvghsyivyGPLLH 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 201 GATVVL---KPKFS--ASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAE---CD---HKVRLAVGSGLRPDTWErFLR 269
Cdd:cd05967 298 GATTVLyegKPVGTpdPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYikkYDlssLRTLFLAGERLDPPTLE-WAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 270 RFGPLQILETYGMTE-GNVATFNYTG------RQGAVGRaswlykhifpfSLIRYDVM----TGEPIR-NAQGHCMTTSP 337
Cdd:cd05967 377 NTLGVPVIDHWWQTEtGWPITANPVGleplpiKAGSPGK-----------PVPGYQVQvldeDGEPVGpNELGNIVIKLP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 338 GEPGLLvapvsqqspflgyagaPELAK-DKLLKDVFWSGDV-FFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEV 415
Cdd:cd05967 446 LPPGCL----------------LTLWKnDERFKKLYLSKFPgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755503902 416 AEVLETLDFLQEVNIYGVtvpgHEGRAGMAALAL--------RPPQALnLVQLYSHVSENLPPYARPR 475
Cdd:cd05967 510 EESVLSHPAVAECAVVGV----RDELKGQVPLGLvvlkegvkITAEEL-EKELVALVREQIGPVAAFR 572
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
141-480 |
3.70e-04 |
|
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: 43.01 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ-CQGFYHLCGVHQEDVIylaLPLYHMS--GSLLGIVGCLGIGATVVLKPK---FSASQ 214
Cdd:cd17652 99 IYTSGSTGRPKGVVVTHRGLANlAAAQIAAFDVGPGSRV---LQFASPSfdASVWELLMALLAGATLVLAPAeelLPGEP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 215 FWDDCQKHRVTVfqyigelcrylVNQPPS-----KAECDHKVRLAVGSGLRP-----DTWERFlRRFgplqiLETYGMTE 284
Cdd:cd17652 176 LADLLREHRITH-----------VTLPPAalaalPPDDLPDLRTLVVAGEACpaelvDRWAPG-RRM-----INAYGPTE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 285 gnvATFNYTGRQGAVGRASwlykhifpfslirydVMTGEPIRNAQGHCMTTS-----PGEPG-LLVApvsqqSPFL--GY 356
Cdd:cd17652 239 ---TTVCATMAGPLPGGGV---------------PPIGRPVPGTRVYVLDARlrpvpPGVPGeLYIA-----GAGLarGY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 357 AGAPELAKDKLLKDVF-WSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEvniygVTV 435
Cdd:cd17652 296 LNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-----AVV 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 755503902 436 PGHEGRAGMAALAL----RPPQALNLVQLYSHVSENLPPYARPR-FLRLQ 480
Cdd:cd17652 371 VVRDDRPGDKRLVAyvvpAPGAAPTAAELRAHLAERLPGYMVPAaFVVLD 420
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
371-474 |
3.91e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 43.10 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 371 VFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYgvtvPGHEGRAG-MAALAL 449
Cdd:PRK08308 285 VVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY----RGKDPVAGeRVKAKV 360
|
90 100
....*....|....*....|....*
gi 755503902 450 RPPQALNLVQLYSHVSENLPPYARP 474
Cdd:PRK08308 361 ISHEEIDPVQLREWCIQHLAPYQVP 385
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|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
133-204 |
5.37e-04 |
|
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: 42.73 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 133 NIMDT------CLYIFTSGTTGLPKAARISHLKVL-----QCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIG 201
Cdd:cd05933 142 AIISSqkpnqcCTLIYTSGTTGMPKGVMLSHDNITwtakaASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVG 221
|
...
gi 755503902 202 ATV 204
Cdd:cd05933 222 GQV 224
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|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
142-419 |
1.04e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 41.80 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 142 FTSGTTGLPKAARISHLKVLQ--CQGFYHLcGVHQEDVIY-LALPLYhMSGSLLGIVGCLGIGAT-VVLKPKFSASQFWD 217
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHNAMLQhyQTGKYVL-DLHEDDVYWcTADPGW-VTGTSYGIFAPWLNGATnVIDGGRFSPERWYR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 218 DCQKHRVTVFQYIGELCRYLVNQPPSKAEC-DHK-VR--LAVGSGLRPD--TWERflRRFGpLQILETYGMTE-GNVATF 290
Cdd:PRK04319 290 ILEDYKVTVWYTAPTAIRMLMGAGDDLVKKyDLSsLRhiLSVGEPLNPEvvRWGM--KVFG-LPIHDNWWMTEtGGIMIA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 291 NYTG---RQGAVGRaswlykhifPFSLIRYDVMTgepiRNAQGhcmtTSPGEPGLLVAPVSQQSPFLGYAGAPElakdkL 367
Cdd:PRK04319 367 NYPAmdiKPGSMGK---------PLPGIEAAIVD----DQGNE----LPPNRMGNLAIKKGWPSMMRGIWNNPE-----K 424
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 755503902 368 LKDVFWSGdvFFNTGDLLVCDEQGFLHFHDRTGDTFRWKGENVATTEVAEVL 419
Cdd:PRK04319 425 YESYFAGD--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKL 474
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|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
141-288 |
1.86e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 141 IFTSGTTGLPKAARISHLKVLQ-----CQGFyhlcGVhQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKfsasqf 215
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSftnwmLEDF----AL-PEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK------ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 216 wddcqkhrvTVFQYIGELCRYLVNQP-------PSKAE-C--------DHKVRLAV----GSGLRPDTWERFLRRFGPLQ 275
Cdd:PRK04813 218 ---------DMTANFKQLFETLPQLPinvwvstPSFADmClldpsfneEHLPNLTHflfcGEELPHKTAKKLLERFPSAT 288
|
170
....*....|...
gi 755503902 276 ILETYGMTEGNVA 288
Cdd:PRK04813 289 IYNTYGPTEATVA 301
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
103-432 |
1.86e-03 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 40.88 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 103 ETNVAGISNLLSEAADQVD-EPVPGYLSA------PQNIMDTCLYI---FTSGTTGLPKAARISHlkvlqcQGFY---HL 169
Cdd:cd05915 111 EAIRGELKTVQHFVVMDEKaPEGYLAYEEalgeeaDPVRVPERAACgmaYTTGTTGLPKGVVYSH------RALVlhsLA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 170 CGVHQEDV-----IYL-ALPLYHMSG-SLLGIVGCLGiGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPP 242
Cdd:cd05915 185 ASLVDGTAlsekdVVLpVVPMFHVNAwCLPYAATLVG-AKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 243 S-KAECDHKVRLAVGSGLRPDTWERfLRRFGPLQILETYGMTEGNvatfnytgrqgAVGRAS-WL--YKHIFPFSLIRYD 318
Cdd:cd05915 264 StGHRLKTLRRLVVGGSAAPRSLIA-RFERMGVEVRQGYGLTETS-----------PVVVQNfVKshLESLSEEEKLTLK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503902 319 VMTG-----EPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYagapelAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFL 393
Cdd:cd05915 332 AKTGlpiplVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGY------YGNEEATRSALTPDGFFRTGDIAVWDEEGYV 405
|
330 340 350
....*....|....*....|....*....|....*....
gi 755503902 394 HFHDRTGDTFRWKGENVATTEVAEVLETLDFLQEVNIYG 432
Cdd:cd05915 406 EIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA 444
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|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
129-170 |
7.18e-03 |
|
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: 39.06 E-value: 7.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755503902 129 SAPQNIMdtclY-IFTSGTTGLPKAARISHLKVlqCQGFYHLC 170
Cdd:cd05918 103 SSPSDAA----YvIFTSGSTGKPKGVVIEHRAL--STSALAHG 139
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