|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2-540 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 938.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 2 MADFETGLGKNEANYTPLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPA 81
Cdd:PRK08162 1 MNIYEQGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 82 MVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDELGP-KDVEPFSDI 160
Cdd:PRK08162 81 MVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEyPGGRFIGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 161 EYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCF 240
Cdd:PRK08162 161 DYEAFLASGDPDFAWTLPADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNGWCF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 241 AWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMG 320
Cdd:PRK08162 241 PWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVHVYGLTEVYGPSAVCAEKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKTIGELMFRGNIVMK 400
Cdd:PRK08162 321 FDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRGNIVMK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEV 480
Cdd:PRK08162 401 GYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 481 PVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGELAKTATGKIQKFELRKQAEAL 540
Cdd:PRK08162 481 PCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVFGELPKTSTGKIQKFVLREQAKSL 540
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
16-535 |
0e+00 |
|
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: 799.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 16 YTPLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV 95
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 96 LLALNVRLETEGLIYCLQHGEAEFLLVDSEFaphipeikkalpalkiiqvndelgpkdvepfsdiEYEGFLQSAEDLDNW 175
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREF----------------------------------EYEDLLAEGDPDFEW 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 176 VLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLR 255
Cdd:cd12118 127 IPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNVCLR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGP 335
Cdd:cd12118 207 KVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 SAVCAEKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKTIGELMFRGNIVMKGYLKNPAETGKSFAG 415
Cdd:cd12118 287 ATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAFRG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE 495
Cdd:cd12118 367 GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092482886 496 EELDQYCRERLAGFKRPKYYVFGELAKTATGKIQKFELRK 535
Cdd:cd12118 447 EEIIAFCREHLAGFMVPKTVVFGELPKTSTGKIQKFVLRD 486
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
9-540 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 647.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 9 LGKNEANYTPLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFG 88
Cdd:PLN02479 10 LPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 89 VPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKAL---------PALKIIQVNDELGPKDVEPF-- 157
Cdd:PLN02479 90 VPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILaekkkssfkPPLLIVIGDPTCDPKSLQYAlg 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 158 -SDIEYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCN 236
Cdd:PLN02479 170 kGAIEYEKFLETGDPEFAWKPPADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 237 GWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKA-GIDHPVSAMVAGAAPPEAVLAR 315
Cdd:PLN02479 250 GWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETIlPLPRVVHVMTAGAAPPPSVLFA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 316 MEQMGFHMVHVYGLTEVYGPSAVCAEKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKTIGELMFRG 395
Cdd:PLN02479 330 MSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPADGKTMGEIVMRG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 396 NIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADE 475
Cdd:PLN02479 410 NMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 476 KWGEVPVAFVELKDDAQVSEE-----ELDQYCRERLAGFKRPKYYVFGELAKTATGKIQKFELRKQAEAL 540
Cdd:PLN02479 490 RWGESPCAFVTLKPGVDKSDEaalaeDIMKFCRERLPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEM 559
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
13-540 |
1.42e-169 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 492.61 E-value: 1.42e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 13 EANYTPLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMS 92
Cdd:PLN03102 8 EANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 93 GGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPA------LKIIQVNDELGPKdvEPFS-DIEYEGF 165
Cdd:PLN03102 88 GAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSedsnlnLPVIFIHEIDFPK--RPSSeELDYECL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 166 LQSAED----LDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFA 241
Cdd:PLN03102 166 IQRGEPtpslVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 242 WTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGF 321
Cdd:PLN03102 246 WGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 322 HMVHVYGLTEVYGPSAVCAEKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKTIGELMFRGNIVMKG 401
Cdd:PLN03102 326 QVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 402 YLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVP 481
Cdd:PLN03102 406 YLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 482 VAFVELK----------DDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEAL 540
Cdd:PLN03102 486 CAFVVLEkgettkedrvDKLVTRERDLIEYCRENLPHFMCPRKVVFlQELPKNGNGKILKPKLRDIAKGL 555
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
14-536 |
2.25e-143 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 423.44 E-value: 2.25e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 14 ANYTPLTpIDFLVRAH-EVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMS 92
Cdd:PRK06187 1 MQDYPLT-IGRILRHGaRKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 93 GGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDElGPKDVEPFSDIEYEGFLQSAEDL 172
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGD-GPAAPLAPEVGEYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 173 DNWVLPkDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWcfAWTIAA--RGGV 250
Cdd:PRK06187 159 FDFPDI-DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAW--GLPYLAlmAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 251 NVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEmkAGID-HPVSAMVAGAAP-PEAVLAR-MEQMGFHMVHVY 327
Cdd:PRK06187 236 QVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRA--YFVDfSSLRLVIYGGAAlPPALLREfKEKFGIDLVQGY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 328 GLTEVyGPSAVCAeKPEWDELSVED--RAAQKARQGVRntlqgaLTVLDPEtMEPVPADGKTIGELMFRGNIVMKGYLKN 405
Cdd:PRK06187 314 GMTET-SPVVSVL-PPEDQLPGQWTkrRSAGRPLPGVE------ARIVDDD-GDELPPDGGEVGEIIVRGPWLMQGYWNR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 406 PAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFV 485
Cdd:PRK06187 385 PEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVV 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 486 ELKDDAQVSEEELDQYCRERLAGFKRPK-YYVFGELAKTATGKIQKFELRKQ 536
Cdd:PRK06187 465 VLKPGATLDAKELRAFLRGRLAKFKLPKrIAFVDELPRTSVGKILKRVLREQ 516
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
22-540 |
1.61e-142 |
|
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: 418.44 E-value: 1.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 22 IDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNV 101
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 102 RLETEGLIYCLQHGEAEFLLVdsefaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkde 181
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 wdaIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPK 260
Cdd:COG0318 103 ---ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLVLLPRFDPE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 261 TCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQ-MGFHMVHVYGLTEVygpSAVC 339
Cdd:COG0318 180 RVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTET---SPVV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AEKPEwdelsvEDRAAQKARQGVRntLQGA-LTVLDPETmEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF 418
Cdd:COG0318 257 TVNPE------DPGERRPGSVGRP--LPGVeVRIVDEDG-RELPPG--EVGEIVVRGPNVMKGYWNDPEATAEAFRDGWL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEEL 498
Cdd:COG0318 326 RTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEEL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1092482886 499 DQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEAL 540
Cdd:COG0318 406 RAFLRERLARYKVPRRVEFvDELPRTASGKIDRRALRERYAAG 448
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
24-535 |
1.79e-129 |
|
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: 387.76 E-value: 1.79e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 24 FLVRAHEVFGDDLaIVHGSI-----RQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLA 98
Cdd:cd12119 1 LLEHAARLHGDRE-IVSRTHegevhRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 99 LNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALK-IIQVNDELGPKDVEPFSDIEYEGFLQSAEDLDNWVL 177
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEhVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 178 pKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNA--IAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTiAARGGVNVCL- 254
Cdd:cd12119 160 -FDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAmaALLTDGLGLSESDVVLPVVPMFHVNAWGLPYA-AAMVGAKLVLp 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 255 -RKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVY 333
Cdd:cd12119 238 gPYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 GPSAVCAEKPEWDELSVEDRAAQKARQG-----VRntlqgaLTVLDPETmEPVPADGKTIGELMFRGNIVMKGYLKNPAE 408
Cdd:cd12119 318 PLGTVARPPSEHSNLSEDEQLALRAKQGrpvpgVE------LRIVDDDG-RELPWDGKAVGELQVRGPWVTKSYYKNDEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 409 TGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK 488
Cdd:cd12119 391 SEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLK 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1092482886 489 DDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRK 535
Cdd:cd12119 471 EGATVTAEELLEFLADKVAKWWLPDDVVFvDEIPKTSTGKIDKKALRE 518
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
18-535 |
9.06e-127 |
|
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: 380.62 E-value: 9.06e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPIDFLVRAHEVFGDDlaiVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLL 97
Cdd:cd05915 1 LERAAALFGRKEVVSRLH---TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 98 ALNVRLETEGLIYCLQHGEAEFLLVDSEFaphIPEIKKALPALKIIQVNdelgPKDVEPFSdiEYEGFLQSAEDLDNWVL 177
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNL---LPLVEAIRGELKTVQHF----VVMDEKAP--EGYLAYEEALGEEADPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 178 PKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRP--VYLWTLPLFHCNGWCFAWTIAARGGVNVCLR 255
Cdd:cd05915 149 RVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEkdVVLPVVPMFHVNAWCLPYAATLVGAKQVLPG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 K-FDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLaRMEQMG-FHMVHVYGLTEVY 333
Cdd:cd05915 229 PrLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLI-ARFERMgVEVRQGYGLTETS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 GPSAVCAEKPEWDELSVEDRAAQKARQGVrNTLQGALTVLDPETMEpVPADGKTIGELMFRGNIVMKGYLKNPAET-GKS 412
Cdd:cd05915 308 PVVVQNFVKSHLESLSEEEKLTLKAKTGL-PIPLVRLRVADEEGRP-VPKDGKALGEVQLKGPWITGGYYGNEEATrSAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 413 FAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKdDAQ 492
Cdd:cd05915 386 TPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR-GEK 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1092482886 493 VSEEELDQYCRERLAGFKR-PKYYVF-GELAKTATGKIQKFELRK 535
Cdd:cd05915 465 PTPEELNEHLLKAGFAKWQlPDAYVFaEEIPRTSAGKFLKRALRE 509
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
27-530 |
1.38e-117 |
|
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: 354.22 E-value: 1.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 27 RAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETE 106
Cdd:cd17631 3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 107 GLIYCLQHGEAEfLLVDsefaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIA 186
Cdd:cd17631 83 EVAYILADSGAK-VLFD-----------------------------------------------------------DLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 187 LNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGW-CFAWTIAARGGVNVCLRKFDPKTCFDL 265
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAALANAPA-------EMKAGIdhpvsamVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGpsAV 338
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALLQHPRfattdlsSLRAVI-------YGGAPMPERLLRALQARGVKFVQGYGMTETSP--GV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CAEKPEwDELSVEdRAAQKARQGVRntlqgaLTVLDPEtMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF 418
Cdd:cd17631 254 TFLSPE-DHRRKL-GSAGRPVFFVE------VRIVDPD-GREVPPG--EVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEEL 498
Cdd:cd17631 323 HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDEL 402
|
490 500 510
....*....|....*....|....*....|...
gi 1092482886 499 DQYCRERLAGFKRPKYYVF-GELAKTATGKIQK 530
Cdd:cd17631 403 IAHCRERLARYKIPKSVEFvDALPRNATGKILK 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
23-542 |
5.73e-99 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 309.17 E-value: 5.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVR 102
Cdd:PRK08316 15 DILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 103 LETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIqVNDELGPKDVePFSDIEYEGFLQSAEDLDNWVLPKDEw 182
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLI-LSLVLGGREA-PGGWLDFADWAEAGSVAEPDVELADD- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRgaALnaIAQSL----EFDMPKRPVYLWTLPLFHCNGW-CFAWTIAARGGVNVCLRKF 257
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHR--AL--IAEYVscivAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVILDAP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 258 DPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKagidHPVSAMVA---GAAP-PEAVLARME----QMGFHmvHVYGL 329
Cdd:PRK08316 248 DPELILRTIEAERITSFFAPPTVWISLLRHPDFDT----RDLSSLRKgyyGASImPVEVLKELRerlpGLRFY--NCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 330 TEVyGPSAVCaekpewdeLSVEDRAAQKARQGvRNTLQGALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAET 409
Cdd:PRK08316 322 TEI-APLATV--------LGPEEHLRRPGSAG-RPVLNVETRVVD-DDGNDVAPG--EVGEIVHRSPQLMLGYWDDPEKT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKD 489
Cdd:PRK08316 389 AEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1092482886 490 DAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEALFS 542
Cdd:PRK08316 469 GATVTEDELIAHCRARLAGFKVPKRVIFvDELPRNPSGKILKRELRERYAGAFT 522
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-445 |
2.38e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 293.83 E-value: 2.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 30 EVFGDDLAIVHGS-IRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGL 108
Cdd:pfam00501 6 ARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 109 IYCLQHGEAEFLLVDSEF-APHIPEIKKALPALKIIQVNDELGPKDVEPFSDIEyegflQSAEDLDNWVLPKDEWDAIAL 187
Cdd:pfam00501 86 AYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEA-----KPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 NYTSGTTGNPKGVVYHHRGAALNAIAQSLE----FDMPKRPVYLWTLPLFHCNGWCFA-WTIAARGGVNVCLRKF---DP 259
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFpalDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 KTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQ-MGFHMVHVYGLTEVygpSAV 338
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRElFGGALVNGYGLTET---TGV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CAEKPEWDelsveDRAAQKARQG--VRNTlqgALTVLDPETMEPVPaDGKTiGELMFRGNIVMKGYLKNPAETGKSF-AG 415
Cdd:pfam00501 318 VTTPLPLD-----EDLRSLGSVGrpLPGT---EVKIVDDETGEPVP-PGEP-GELCVRGPGVMKGYLNDPELTAEAFdED 387
|
410 420 430
....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISG 445
Cdd:pfam00501 388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
183-529 |
6.23e-93 |
|
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: 287.26 E-value: 6.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTC 262
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 263 FDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMVHVYGLTEVYGPSAVCAE 341
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 kpewDELSVEDRAAQKARQGVRntlqgaLTVLDPETmEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTG 421
Cdd:cd04433 161 ----DDDARKPGSVGRPVPGVE------VRIVDPDG-GELPPGE--IGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQY 501
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 1092482886 502 CRERLAGFKRPKYYVF-GELAKTATGKIQ 529
Cdd:cd04433 308 VRERLAPYKVPRRVVFvDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-534 |
1.81e-92 |
|
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: 290.62 E-value: 1.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVR 102
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 103 LETEGLIYCLQHGEAEFLLVDSEFaphipeikkalpalkiiqvndelgpkdvepfsdieyEGFLQSAEDLDNWVLPKDEw 182
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVAVSF------------------------------------TDLLAAGAPLGERVALTPE- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHR--GAALNAIAQSLEFDMPKRPVYLWTLPLFHCngwcFAWTIA-----ARGGVNVCLR 255
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRnlVANALQIKAWLEDLLEGDDVVLAALPLFHV----FGLTVAlllplALGATIVLIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHpVSAMVAGAAP-PEAVLARMEQM-GFHMVHVYGLTEVy 333
Cdd:cd05936 202 RFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSS-LRLCISGGAPlPVEVAERFEELtGVPIVEGYGLTET- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 GPsAVCAEKPEWdelsvedraaqKARQG-----VRNTLqgaLTVLDPETmEPVPaDGKTiGELMFRGNIVMKGYLKNPAE 408
Cdd:cd05936 280 SP-VVAVNPLDG-----------PRKPGsigipLPGTE---VKIVDDDG-EELP-PGEV-GELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 409 TGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK 488
Cdd:cd05936 342 TAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1092482886 489 DDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05936 422 EGASLTEEEIIAFCREQLAGYKVPRQVEFrDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
18-536 |
1.56e-87 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 279.10 E-value: 1.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLL 97
Cdd:PRK07656 4 WMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 98 ALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIqVNDELGPKDVEPFSDIEYEGFLQSAEDLDNWVL 177
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHV-VICETEEDDPHTEKMKTFTDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 178 PKDEWDAIALnYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWtIAA--RGGVNVCLR 255
Cdd:PRK07656 163 VDPDDVADIL-FTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGV-NAPlmRGATILPLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMV-HVYGLTEVY 333
Cdd:PRK07656 241 VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESElGVDIVlTGYGLSEAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 GpsAVCAEKPEWDelsVEDRAAQKAR--QGVRNTLQGALTvldpetmEPVPADgkTIGELMFRGNIVMKGYLKNPAETGK 411
Cdd:PRK07656 321 G--VTTFNRLDDD---RKTVAGTIGTaiAGVENKIVNELG-------EEVPVG--EVGELLVRGPNVMKGYYDDPEATAA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 412 SF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDD 490
Cdd:PRK07656 387 AIdADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1092482886 491 AQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK07656 467 AELTEEELIAYCREHLAKYKVPRSIEFlDELPKNATGKVLKRALREK 513
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
39-536 |
1.11e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 272.74 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 39 VHGSI-RQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEA 117
Cdd:PRK07008 33 VEGDIhRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 118 EFLLVDSEFAPHIPEIKKALPALK--IIQVNDELGPKDVEPFsdIEYEGFLqSAEDlDNWVLPK-DEWDAIALNYTSGTT 194
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNVKgwVAMTDAAHLPAGSTPL--LCYETLV-GAQD-GDYDWPRfDENQASSLCYTSGTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 195 GNPKGVVYHHRGAALNAIAQSLE--FDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQERV 271
Cdd:PRK07008 189 GNPKGALYSHRSTVLHAYGAALPdaMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEAERV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 272 GFYCAAPVVHAALAN--APAEMKAGidhPVSAMVAG--AAPPEAVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPEWDE 347
Cdd:PRK07008 269 TFSAGVPTVWLGLLNhmREAGLRFS---TLRRTVIGgsACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 LSVEDRAAQKARQGvRNTLQGALTVLDPETMEpVPADGKTIGELMFRGNIVMKGYLKNpaeTGKSFAGGWFHTGDLGVLH 427
Cdd:PRK07008 346 LPLDEQRKLLEKQG-RVIYGVDMKIVGDDGRE-LPWDGKAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATID 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 428 PDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLA 507
Cdd:PRK07008 421 ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVA 500
|
490 500 510
....*....|....*....|....*....|
gi 1092482886 508 GFKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK07008 501 KWWIPDDVVFvDAIPHTATGKLQKLKLREQ 530
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
39-536 |
1.55e-81 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 264.31 E-value: 1.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 39 VHGSI-RQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEA 117
Cdd:PRK06018 33 VEGPIvRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 118 EFLLVDSEFAPHIPEIKKALPALKIIQVndeLGPKDVEPFSDIE----YEGFLQSAEDLDNWVLpKDEWDAIALNYTSGT 193
Cdd:PRK06018 113 RVVITDLTFVPILEKIADKLPSVERYVV---LTDAAHMPQTTLKnavaYEEWIAEADGDFAWKT-FDENTAAGMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIA--QSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQER 270
Cdd:PRK06018 189 TGDPKGVLYSHRSNVLHALManNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPgAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 271 VGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPEWDELSV 350
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLPG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 351 EDRAAQKARQGvRNTLQGALTVLDPETMEpVPADGKTIGELMFRGNIVMKGYLKnpAETGKSFAGGWFHTGDLGVLHPDG 430
Cdd:PRK06018 349 DARLDVLQKQG-YPPFGVEMKITDDAGKE-LPWDGKTFGRLKVRGPAVAAAYYR--VDGEILDDDGFFDTGDVATIDAYG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 431 YAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFK 510
Cdd:PRK06018 425 YMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWW 504
|
490 500
....*....|....*....|....*..
gi 1092482886 511 RPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK06018 505 MPDDVAFvDAIPHTATGKILKTALREQ 531
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
34-540 |
2.42e-77 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 251.81 E-value: 2.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGsiRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYC 111
Cdd:PRK03640 17 DRTAIEFE--EKKVTfmELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 112 LQHGEAEFLLVDSEFAPhipeikkalpALKIIQvndelgPKDVEPFSDIEYE-GFLQSAEDLDnwvlpkdewDAIALNYT 190
Cdd:PRK03640 95 LDDAEVKCLITDDDFEA----------KLIPGI------SVKFAELMNGPKEeAEIQEEFDLD---------EVATIMYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWcfawTIAARG---GVNVCL-RKFDPKTCFDLI 266
Cdd:PRK03640 150 SGTTGKPKGVIQTYGNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGL----SILMRSviyGMRVVLvEKFDAEKINKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVgfyCAAPVVHAALANAPAEMKAGIDHP-VSAMVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVygPSAVCAEKPE 344
Cdd:PRK03640 226 QTGGV---TIISVVSTMLQRLLERLGEGTYPSsFRCMLLGGGPaPKPLLEQCKEKGIPVYQSYGMTET--ASQIVTLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 345 WDELSVEdrAAQKARQGVRntlqgaLTVLDpetmEPVPADGKTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLG 424
Cdd:PRK03640 301 DALTKLG--SAGKPLFPCE------LKIEK----DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWFKTGDIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 425 VLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELkdDAQVSEEELDQYCRE 504
Cdd:PRK03640 369 YLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEE 446
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092482886 505 RLAGFKRPK-YYVFGELAKTATGKIQKFELRKQAEAL 540
Cdd:PRK03640 447 KLAKYKVPKrFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
23-541 |
2.60e-77 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 253.58 E-value: 2.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIV--HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALN 100
Cdd:PRK08315 20 QLLDRTAARYPDREALVyrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 101 VRLETEGLIYCLQHGEAEFLLVDSEFAPH---------IPEIK---------KALPALK-IIQVNDELGPkDVEPFSDIE 161
Cdd:PRK08315 100 PAYRLSELEYALNQSGCKALIAADGFKDSdyvamlyelAPELAtcepgqlqsARLPELRrVIFLGDEKHP-GMLNFDELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 162 YEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNA--IAQSLEFDMPKR---PVylwtlPLFHCN 236
Cdd:PRK08315 179 ALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGyfIGEAMKLTEEDRlciPV-----PLYHCF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 237 GwCFAWTIAA--RGGVNVC-LRKFDPKTCFDLIRQERvgfyCAApvvhaaLANAPAEMKAGIDHPVSAM----------V 303
Cdd:PRK08315 254 G-MVLGNLACvtHGATMVYpGEGFDPLATLAAVEEER----CTA------LYGVPTMFIAELDHPDFARfdlsslrtgiM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 304 AGAAPPEAVLAR-MEQMgfHMVHV---YGLTE---VYGPSAVcaekpewDElSVEDRAAQKARQG----VRntlqgaltV 372
Cdd:PRK08315 323 AGSPCPIEVMKRvIDKM--HMSEVtiaYGMTEtspVSTQTRT-------DD-PLEKRVTTVGRALphleVK--------I 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 373 LDPETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISS 451
Cdd:PRK08315 385 VDPETGETVPRG--EQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 452 IEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQK 530
Cdd:PRK08315 463 REIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFvDEFPMTVTGKIQK 542
|
570
....*....|.
gi 1092482886 531 FELRKQAEALF 541
Cdd:PRK08315 543 FKMREMMIEEL 553
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
34-536 |
3.59e-77 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 251.70 E-value: 3.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVhgSIRQNWT--ETYHRCRQMAAALRQN-GADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIY 110
Cdd:PRK06839 17 DRIAII--TEEEEMTykQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 111 CLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDELGPKDVEPfsdieyegflqsaEDLDnwvlPKDEWDAIALNYT 190
Cdd:PRK06839 95 QLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRKI-------------DNFV----EKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGW-CFAWTIAARGGVNVCLRKFDPKTCFDLIRQE 269
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIgLFAFPTLFAGGVIIVPRKFEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAPVVHAALANAPAEMKAGIDHpVSAMVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVyGPSAVcaekpewdeL 348
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFETTNLQS-VRWFYNGGAPcPEELMREFIDRGFLFGQGFGMTET-SPTVF---------M 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 349 SVEDRAAQKARQGVRNTLQGALTVLDPETMEpVPADGktIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHP 428
Cdd:PRK06839 307 LSEEDARRKVGSIGKPVLFCDYELIDENKNK-VEVGE--VGELLIRGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 429 DGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAG 508
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAK 463
|
490 500
....*....|....*....|....*....
gi 1092482886 509 FKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK06839 464 YKIPKEIVFlKELPKNATGKIQKAQLVNQ 492
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-534 |
5.41e-77 |
|
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: 248.75 E-value: 5.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDsef 126
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 aphipeikkalpalkiiqvndelgpkdvePFSDIeyegflqsaedldnwvlpkdewdaialnYTSGTTGNPKGVVYHHRG 206
Cdd:cd05934 83 -----------------------------PASIL----------------------------YTSGTTGPPKGVVITHAN 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 207 AALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALA 285
Cdd:cd05934 106 LTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAAlSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 286 NAPAEMKAGiDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGPSAvcAEKPEwdelSVEDRAAQKARQGVrnt 365
Cdd:cd05934 186 AQPPSPDDR-AHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVI--GPRDE----PRRPGSIGRPAPGY--- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 366 lqgALTVLDPETmEPVPADgkTIGELMFR---GNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII 442
Cdd:cd05934 256 ---EVRIVDDDG-QELPAG--EPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 443 ISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELA 521
Cdd:cd05934 330 RRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFvDDLP 409
|
490
....*....|...
gi 1092482886 522 KTATGKIQKFELR 534
Cdd:cd05934 410 KTPTEKVAKAQLR 422
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-534 |
1.28e-73 |
|
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: 237.95 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNA--IAQSLEFDMPKR---PVylwtlPLFHCNGWCFAWTIAARGGVNVCL--R 255
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGyfIGERLGLTEQDRlciPV-----PLFHCFGSVLGVLACLTHGATMVFpsP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARM-EQMGFHMVHV-YGLTEVy 333
Cdd:cd05917 78 SFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRViEVMNMKDVTIaYGMTET- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 gpSAVCAEKpewdelSVEDRAAQKARQGVRNTLQGALTVLDPETmEPVPADGkTIGELMFRGNIVMKGYLKNPAETGKSF 413
Cdd:cd05917 157 --SPVSTQT------RTDDSIEKRVNTVGRIMPHTEAKIVDPEG-GIVPPVG-VPGELCIRGYSVMKGYWNDPEKTAEAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 AG-GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQ 492
Cdd:cd05917 227 DGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1092482886 493 VSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05917 307 LTEEDIKAYCKGKIAHYKVPRYVFFvDEFPLTVSGKIQKFKLR 349
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
49-535 |
1.86e-69 |
|
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: 228.77 E-value: 1.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 49 ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFllvdsefap 128
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 129 hipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIA-LNYTSGTTGNPKGVVYHHRGA 207
Cdd:cd05912 77 ------------------------------------------------------DDIAtIMYTSGTTGKPKGVQQTFGNH 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 208 ALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWcfawTIAARGGVNVC----LRKFDPKTCFDLIRQERVGFYCAAPVVHAA 283
Cdd:cd05912 103 WWSAIGSALNLGLTEDDNWLCALPLFHISGL----SILMRSVIYGMtvylVDKFDAEQVLHLINSGKVTIISVVPTMLQR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 284 LAnapAEMKAGIDHPVSAMVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVYgpSAVCAEKPEWDELSVEdrAAQKARQGV 362
Cdd:cd05912 179 LL---EILGEGYPNNLRCILLGGGPaPKPLLEQCKEKGIPVYQSYGMTETC--SQIVTLSPEDALNKIG--SAGKPLFPV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 363 RntlqgaLTVLDPETMEpvpadgKTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII 442
Cdd:cd05912 252 E------LKIEDDGQPP------YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 443 ISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDaqVSEEELDQYCRERLAGFKRPK-YYVFGELA 521
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPKkIYFVDELP 397
|
490
....*....|....
gi 1092482886 522 KTATGKIQKFELRK 535
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
34-538 |
4.60e-69 |
|
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: 230.28 E-value: 4.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYC 111
Cdd:cd05926 2 DAPALVVPGSTPALTyaDLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 112 LQHGEAEFLLVDS-EFAPHIPEIKKALPALKIIQVNDELGPKDVEPfSDIEYEGFLQSAEDLDNWVLPKDewDAIALnYT 190
Cdd:cd05926 82 LADLGSKLVLTPKgELGPASRAASKLGLAILELALDVGVLIRAPSA-ESLSNLLADKKNAKSEGVPLPDD--LALIL-HT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAALNA--IAQSLEFDmPKRPVYLwTLPLFHCNGW-CFAWTIAARGGVNVCLRKFDPKTCFDLIR 267
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASAtnITNTYKLT-PDDRTLV-VMPLFHVHGLvASLLSTLAAGGSVVLPPRFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAP-PEAVLARMEQMgFH--MVHVYGLTEVygpSAVCAEKPe 344
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASlPPAVLEALEAT-FGapVLEAYGMTEA---AHQMTSNP- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 345 wdeLSVEDRAAQKARQGVRNTLQgaltVLDpETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKS-FAGGWFHTGDL 423
Cdd:cd05926 311 ---LPPGPRKPGSVGKPVGVEVR----ILD-EDGEILPPGVV--GEICLRGPNVTRGYLNNPEANAEAaFKDGWFRTGDL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 424 GVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCR 503
Cdd:cd05926 381 GYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 1092482886 504 ERLAGFKRPKYYVF-GELAKTATGKIQKfelRKQAE 538
Cdd:cd05926 461 KHLAAFKVPKKVYFvDELPKTATGKIQR---RKVAE 493
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
16-536 |
1.53e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 229.87 E-value: 1.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 16 YTPLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV 95
Cdd:PRK06188 9 HSGATYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 96 LLALNVRLETEGLIYCLQHGEAEFLLVDS-EFAPHIPEIKKALPALKiiqvndelgpkDVEPFSDIEY-EGFLQSAEDLD 173
Cdd:PRK06188 89 RTALHPLGSLDDHAYVLEDAGISTLIVDPaPFVERALALLARVPSLK-----------HVLTLGPVPDgVDLLAAAAKFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 174 NWVL--PKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAaRGGVN 251
Cdd:PRK06188 158 PAPLvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPTLL-RGGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 252 VCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALanapaemkagIDHPVSA---------MVAGAAP--PEAVLARMEQMG 320
Cdd:PRK06188 237 IVLAKFDPAEVLRAIEEQRITATFLVPTMIYAL----------LDHPDLRtrdlssletVYYGASPmsPVRLAEAIERFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVHVYGLTEVygPSAVCAEKPEWDELSVEDRAAQKARQGVRNTLQgaltVLDPEtMEPVPADgkTIGELMFRGNIVMK 400
Cdd:PRK06188 307 PIFAQYYGQTEA--PMVITYLRKRDHDPDDPKRLTSCGRPTPGLRVA----LLDED-GREVAQG--EVGEICVRGPLVMD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEV 480
Cdd:PRK06188 378 GYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEA 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092482886 481 PVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQ 536
Cdd:PRK06188 458 VTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDsLPLTALGKPDKKALRAR 514
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
32-537 |
3.01e-67 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 227.35 E-value: 3.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 32 FGDDLAIV--HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLI 109
Cdd:PRK12583 31 FPDREALVvrHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 110 YCLQHGEAEFLLVDSEFAPH---------IPEIKKA---------LPALKIIQVNDELGPKDVEPFSDIEYEGFLQSAED 171
Cdd:PRK12583 111 YALGQSGVRWVICADAFKTSdyhamlqelLPGLAEGqpgalacerLPELRGVVSLAPAPPPGFLAWHELQARGETVSREA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 172 LDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNA--IAQSLEFDMPKR---PVylwtlPLFHCNGWCFAWTIAA 246
Cdd:PRK12583 191 LAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGyfVAESLGLTEHDRlcvPV-----PLYHCFGMVLANLGCM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 247 RGGVNVCL--RKFDPKTCFDLIRQERVgfycaapvvhAALANAPAEMKAGIDHP------VSAM----VAGAAPPEAVLA 314
Cdd:PRK12583 266 TVGACLVYpnEAFDPLATLQAVEEERC----------TALYGVPTMFIAELDHPqrgnfdLSSLrtgiMAGAPCPIEVMR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 315 R-MEQMgfHMVHV---YGLTEVygpSAVCAEKPEWD--ELSVEDRAAQKARQGVRntlqgaltVLDPETmEPVPADgkTI 388
Cdd:PRK12583 336 RvMDEM--HMAEVqiaYGMTET---SPVSLQTTAADdlERRVETVGRTQPHLEVK--------VVDPDG-ATVPRG--EI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 389 GELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANV 467
Cdd:PRK12583 400 GELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 468 AVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQA 537
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFvDEFPMTVTGKVQKFRMREIS 550
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
37-529 |
1.17e-66 |
|
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: 223.63 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 37 AIVHGSIRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQH 114
Cdd:cd05911 1 AQIDADTGKELTyaQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 115 GEAEFLLVDSEFAPHIPEIKKALPAL-KIIQVNDEL-----GPKDVEPFSDIEYEGFLQSAEDLDNwvlpkdewDAIALN 188
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPKdKIIVLDDKPdgvlsIEDLLSPTLGEEDEDLPPPLKDGKD--------DTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNA-IAQSLEFD-MPKRPVYLWTLPLFHcnGWCFAWTIAA--RGGVNVCLRKFDPKTCFD 264
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLIANLsQVQTFLYGnDGSNDVILGFLPLYH--IYGLFTTLASllNGATVIIMPKFDSELFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGF--HMVHVYGLTEVygpSAVCAEK 342
Cdd:cd05911 231 LIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPnaTIKQGYGMTET---GGILTVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 343 PEWDEL--SVedraaqkarqG--VRNTLqgaLTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKSF-AGGW 417
Cdd:cd05911 308 PDGDDKpgSV----------GrlLPNVE---AKIVDDDGKDSLGPNEP--GEICVRGPQVMKGYYNNPEATKETFdEDGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 418 FHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEE 497
Cdd:cd05911 373 LHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKE 452
|
490 500 510
....*....|....*....|....*....|....
gi 1092482886 498 LDQYCRERLAGFK--RPKYYVFGELAKTATGKIQ 529
Cdd:cd05911 453 VKDYVAKKVASYKqlRGGVVFVDEIPKSASGKIL 486
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
47-536 |
1.74e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 224.66 E-value: 1.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEF 126
Cdd:PRK07786 45 WRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 APHIPEIKKALPALKIIQVNDELGPKDVepfsdIEYEGFLQSAEDLDNWV-LPKDEWDAIAlnYTSGTTGNPKGVVYHHr 205
Cdd:PRK07786 125 APVATAVRDIVPLLSTVVVAGGSSDDSV-----LGYEDLLAEAGPAHAPVdIPNDSPALIM--YTSGTTGRPKGAVLTH- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 gaaLNAIAQSL------EFDMPKRpVYLWTLPLFHCNGWCFAWTIAARGGVNVC--LRKFDPKTCFDLIRQERV-GFYCA 276
Cdd:PRK07786 197 ---ANLTGQAMtclrtnGADINSD-VGFVGVPLFHIAGIGSMLPGLLLGAPTVIypLGAFDPGQLLDVLEAEKVtGIFLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 277 APVVHAALANAPAEmkaGIDHPVSAMVAGAAP-PEAVLARMEQM--GFHMVHVYGLTEVYGPSAVcaekpewdeLSVEDR 353
Cdd:PRK07786 273 PAQWQAVCAEQQAR---PRDLALRVLSWGAAPaSDTLLRQMAATfpEAQILAAFGQTEMSPVTCM---------LLGEDA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 354 AAQKARQG-VRNTLqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYA 432
Cdd:PRK07786 341 IRKLGSVGkVIPTV--AARVVD-ENMNDVPVG--EVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 433 QIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK-DDAQVSEEELDQYCRERLAGFKR 511
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRnDDAALTLEDLAEFLTDRLARYKH 495
|
490 500
....*....|....*....|....*.
gi 1092482886 512 PKYY-VFGELAKTATGKIQKFELRKQ 536
Cdd:PRK07786 496 PKALeIVDALPRNPAGKVLKTELRER 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-538 |
4.52e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 222.45 E-value: 4.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 37 AIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGE 116
Cdd:PRK06145 20 ALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 117 AEFLLVDSEFAphipeikkALPALKIIQ-VNDELGPKDVEPFSdieyEGFLQSAEdldnwVLPKDEWDAIALNYTSGTTG 195
Cdd:PRK06145 100 AKLLLVDEEFD--------AIVALETPKiVIDAAAQADSRRLA----QGGLEIPP-----QAAVAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 196 NPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCnGWCFAWTIA--ARGGVNVCLRKFDPKTCFDLIRQERVGF 273
Cdd:PRK06145 163 RPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHV-GAFDLPGIAvlWVGGTLRIHREFDPEAVLAAIERHRLTC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 274 YCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM--GFHMVHVYGLTEVYGPSAVCAEKPEWDELSVE 351
Cdd:PRK06145 242 AWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDTLMEAGREIEKIGST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 352 DRAAQKARQGVRNTLQGALtvldpetmepvPADGKtiGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGY 431
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWL-----------PPNMK--GEICMRGPKVTKGYWKDPEKTAEAFYGDWFRSGDVGYLDEEGF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 432 AQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKR 511
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKV 468
|
490 500
....*....|....*....|....*...
gi 1092482886 512 PKYYVF-GELAKTATGKIQKFELRKQAE 538
Cdd:PRK06145 469 PRQLKVrDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
14-541 |
5.30e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 213.32 E-value: 5.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 14 ANYTPLTP----------IDFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMV 83
Cdd:PRK05605 17 QSYAPWTPhdldygdttlVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 84 EAGFGVPMSGGVLLALN---VRLETEGLiyCLQHGeAEFLLVDSEFAPHIPEIKKALPALKIIQVN-------------- 146
Cdd:PRK05605 97 VAFYAVLRLGAVVVEHNplyTAHELEHP--FEDHG-ARVAIVWDKVAPTVERLRRTTPLETIVSVNmiaampllqrlalr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 147 ----------DEL-GPKDvepfSDIEYEGFLQSAEDLDNWVL--PKDEWDAIAL-NYTSGTTGNPKGVVYHHRGAALNAi 212
Cdd:PRK05605 174 lpipalrkarAALtGPAP----GTVPWETLVDAAIGGDGSDVshPRPTPDDVALiLYTSGTTGKPKGAQLTHRNLFANA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 213 AQSLEF--DMPKRP-VYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAP 288
Cdd:PRK05605 249 AQGKAWvpGLGDGPeRVLAALPMFHAYGLTLCLTLAvSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 289 AEmkAGID-HPVSAMVAGAAP-PEAVLARMEQM-GFHMVHVYGLTEVygpSAVCAEKPewdeLSvEDRaaqkaRQG---- 361
Cdd:PRK05605 329 EE--RGVDlSGVRNAFSGAMAlPVSTVELWEKLtGGLLVEGYGLTET---SPIIVGNP----MS-DDR-----RPGyvgv 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 362 ------VRntlqgaltVLDPETMEPVPADGKTiGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIK 435
Cdd:PRK05605 394 pfpdteVR--------IVDPEDPDETMPDGEE-GELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 436 DRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPK-Y 514
Cdd:PRK05605 465 DRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRrF 544
|
570 580
....*....|....*....|....*..
gi 1092482886 515 YVFGELAKTATGKIQKFELRKQAEALF 541
Cdd:PRK05605 545 YHVDELPRDQLGKVRRREVREELLEKL 571
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
44-535 |
3.50e-60 |
|
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: 205.31 E-value: 3.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 44 RQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVD 123
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 SEFAPHIPEikkALPalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIA-LNYTSGTTGNPKGVVY 202
Cdd:cd05903 81 ERFRQFDPA---AMP--------------------------------------------DAVAlLLFTSGTTGEPKGVMH 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 203 HHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQERVGFYCAAPVVH 281
Cdd:cd05903 114 SHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqDIWDPDKALALMREHGVTFMMGATPFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 282 AALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMV-HVYGLTEVYGPSAVCAEKPEWDELSVEDRAaqkaRQ 360
Cdd:cd05903 194 TDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVcSAYGSTECPGAVTSITPAPEDRRLYTDGRP----LP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 361 GVRNTLqgaltvldpetmepVPADGKT-----IGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIK 435
Cdd:cd05903 270 GVEIKV--------------VDDTGATlapgvEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRIT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 436 DRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYC-RERLAGFKRP-K 513
Cdd:cd05903 336 GRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPeR 415
|
490 500
....*....|....*....|..
gi 1092482886 514 YYVFGELAKTATGKIQKFELRK 535
Cdd:cd05903 416 LVHVDDLPRTPSGKVQKFRLRE 437
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
36-536 |
4.95e-60 |
|
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: 206.21 E-value: 4.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 36 LAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHG 115
Cdd:cd05923 20 IADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 116 E--AEFLLVDSEFAPHIpeikkALPALKIIQVNDELGpkdvepfsdieyEGFLQSAEDLDNWVLPKDEWDAIALnYTSGT 193
Cdd:cd05923 100 EmtAAVIAVDAQVMDAI-----FQSGVRVLALSDLVG------------LGEPESAGPLIEDPPREPEQPAFVF-YTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQS----LEFDMPKRPVYLwtLPLFHCNGWcFAWTIA--ARGGVNVCLRKFDPKTCFDLIR 267
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMStqagLRHGRHNVVLGL--MPLYHVIGF-FAVLVAalALDGTYVVVEEFDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQ-MGFHMVHVYGLTEVYgpSAVCAEKPewd 346
Cdd:cd05923 239 QERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhLPGEKVNIYGTTEAM--NSLYMRDA--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 347 elsvedRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKTIGELmfRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVL 426
Cdd:cd05923 314 ------RTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAA--AADAAFTGYLNQPEATAKKLQDGWYRTGDVGYV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 427 HPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKdDAQVSEEELDQYCRE-R 505
Cdd:cd05923 386 DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPR-EGTLSADELDQFCRAsE 464
|
490 500 510
....*....|....*....|....*....|..
gi 1092482886 506 LAGFKRPKYYVF-GELAKTATGKIqkfeLRKQ 536
Cdd:cd05923 465 LADFKRPRRYFFlDELPKNAMNKV----LRRQ 492
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
24-539 |
5.75e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 206.82 E-value: 5.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 24 FLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRL 103
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 104 ETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDElgpkdvePFSDIEYEGFLqsAEDLDNWVLPK--DE 181
Cdd:PRK07470 92 TPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGG-------ARAGLDYEALV--ARHLGARVANAavDH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 WDAIALNYTSGTTGNPKGVVYHHRGAAL---NAIAqSLEFDMPKRPVYLWTLPLFHCNGwCFAWTIAARGGVNVCL--RK 256
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTHGQMAFvitNHLA-DLMPGTTEQDASLVVAPLSHGAG-IHQLCQVARGAATVLLpsER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 257 FDPKTCFDLIRQERVGFYCAAPVVHAALANAPAemKAGIDHPVSAMV--AGA----APPEAVLARMeqmGFHMVHVYGLT 330
Cdd:PRK07470 241 FDPAEVWALVERHRVTNLFTVPTILKMLVEHPA--VDRYDHSSLRYViyAGApmyrADQKRALAKL---GKVLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 EVYGPSAV---CAEKPEwDELSVEDRAAQKARQGVRntlqgaLTVLDPEtMEPVPAdGKTiGELMFRGNIVMKGYLKNPA 407
Cdd:PRK07470 316 EVTGNITVlppALHDAE-DGPDARIGTCGFERTGME------VQIQDDE-GRELPP-GET-GEICVIGPAVFAGYYNNPE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 408 ETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVEL 487
Cdd:PRK07470 386 ANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 488 KDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEA 539
Cdd:PRK07470 466 RDGAPVDEAELLAWLDGKVARYKLPKRFFFwDALPKSGYGKITKKMVREELEE 518
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-536 |
2.27e-59 |
|
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: 204.78 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPIDFLVRahEVFGDDLAIVHGSIRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV 95
Cdd:cd05904 6 PLDSVSFLFA--SAHPSRPALIDAATGRALTyaELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 96 LLALNvRLETEGLIyclQH----GEAEFLLVDSEFAPHIPEIkkalpALKIIqvndeLGPKDVEPFSDIEYEGFLQSAED 171
Cdd:cd05904 84 VTTAN-PLSTPAEI---AKqvkdSGAKLAFTTAELAEKLASL-----ALPVV-----LLDSAEFDSLSFSDLLFEADEAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 172 LDNWVLPKDewDAIALNYTSGTTGNPKGVVYHHRG--AALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWC-FAWTIAARG 248
Cdd:cd05904 150 PPVVVIKQD--DVAALLYSSGTTGRSKGVMLTHRNliAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSsFALGLLRLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 249 GVNVCLRKFDPKTCFDLIRQERV-GFYCAAPVVhAALANAPAemkaGIDHPVSAM---VAGAAP-----PEAVLARMEQM 319
Cdd:cd05904 228 ATVVVMPRFDLEELLAAIERYKVtHLPVVPPIV-LALVKSPI----VDKYDLSSLrqiMSGAAPlgkelIEAFRAKFPNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 320 GFhmVHVYGLTEVYGPSAVCAekpewdelsveDRAAQKARQG-----VRNTlqgALTVLDPETMEPVPAdGKTiGELMFR 394
Cdd:cd05904 303 DL--GQGYGMTESTGVVAMCF-----------APEKDRAKYGsvgrlVPNV---EAKIVDPETGESLPP-NQT-GELWIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 395 GNIVMKGYLKNPAETGKSFAG-GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALA 473
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYP 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092482886 474 DEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIqkfeLRKQ 536
Cdd:cd05904 445 DEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDaIPKSPSGKI----LRKE 504
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
47-528 |
3.09e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 206.04 E-value: 3.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEF 126
Cdd:PRK06710 52 FSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 APHIPEIKKALPALKII--QVNDELG-PKD-VEPFSDIEYEGFL---QSAEDLDNW------------VLPKDEWDAIAL 187
Cdd:PRK06710 132 FPRVTNVQSATKIEHVIvtRIADFLPfPKNlLYPFVQKKQSNLVvkvSESETIHLWnsvekevntgveVPCDPENDLALL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 NYTSGTTGNPKGVVYHHRGAALNAI--AQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVN-VCLRKFDPKTCFD 264
Cdd:PRK06710 212 QYTGGTTGFPKGVMLTHKNLVSNTLmgVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKmVLIPKFDMKMVFE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVVHAALANAPAEMKAGIDhPVSAMVAGAAP-PEAVLARMEQM-GFHMVHVYGLTEvygPSAVCAEK 342
Cdd:PRK06710 292 AIKKHKVTLFPGAPTIYIALLNSPLLKEYDIS-SIRACISGSAPlPVEVQEKFETVtGGKLVEGYGLTE---SSPVTHSN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 343 PEWdelsvEDRAAQKArqGVRNTLQGALtVLDPETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGD 422
Cdd:PRK06710 368 FLW-----EKRVPGSI--GVPWPDTEAM-IMSLETGEALPPG--EIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 423 LGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYC 502
Cdd:PRK06710 438 VGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFA 517
|
490 500
....*....|....*....|....*..
gi 1092482886 503 RERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:PRK06710 518 RKYLAAYKVPKVYEFrDELPKTTVGKI 544
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
47-533 |
1.86e-58 |
|
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: 200.75 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEF 126
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 AphipeiKKALPALKIiqvnDELGPKDVEpfsDIEYEGFLQSaedldnwvlpkdewDAIA-LNYTSGTTGNPKGVVYHHR 205
Cdd:TIGR01923 82 E------EKDFQADSL----DRIEAAGRY---ETSLSASFNM--------------DQIAtLMFTSGTTGKPKAVPHTFR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAI--AQSLEFDMPKRpvYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDpkTCFDLIRQERVGFYCAAPVVHAA 283
Cdd:TIGR01923 135 NHYASAVgsKENLGFTEDDN--WLLSLPLYHISGLSILFRWLIEGATLRIVDKFN--QLLEMIANERVTHISLVPTQLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 284 LANapaemKAGIDHPVSAMVAGAAPPEAVLARM-EQMGFHMVHVYGLTEVYgpSAVCAEKPEWDelsvedraaqKARQGV 362
Cdd:TIGR01923 211 LLD-----EGGHNENLRKILLGGSAIPAPLIEEaQQYGLPIYLSYGMTETC--SQVTTATPEML----------HARPDV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 363 RNTLQGALTVLDPETMEPVpadgktiGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII 442
Cdd:TIGR01923 274 GRPLAGREIKIKVDNKEGH-------GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 443 ISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDaqVSEEELDQYCRERLAGFKRPK-YYVFGELA 521
Cdd:TIGR01923 347 ISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD--ISQAKLIAYLTEKLAKYKVPIaFEKLDELP 424
|
490
....*....|..
gi 1092482886 522 KTATGKIQKFEL 533
Cdd:TIGR01923 425 YNASGKILRNQL 436
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
34-535 |
8.87e-58 |
|
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: 199.05 E-value: 8.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGAD-RGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNvrletegliycL 112
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLN-----------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAE--FLLVDSEfaphipeikkalPALKIiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIALNYT 190
Cdd:cd05941 70 SYPLAEleYVITDSE------------PSLVL----------------------------------------DPALILYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHR--GAALNAIAQSLEFDmpKRPVYLWTLPLFHCNGWCFAWTIAARGGVNV-CLRKFDPKTCFDLIR 267
Cdd:cd05941 98 SGTTGRPKGVVLTHAnlAANVRALVDAWRWT--EDDVLLHVLPLHHVHGLVNALLCPLFAGASVeFLPKFDPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFYCAAPVVHAALANAPAEMKAGIDHPVSA-------MVAGAAP-PEAVLARMEQ-MGFHMVHVYGLTEVygpsav 338
Cdd:cd05941 176 MPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAaaerlrlMVSGSAAlPVPTLEEWEAiTGHTLLERYGMTEI------ 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 caekpewdELSVEDRAAQKARQG-VRNTLQGA-LTVLDPETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF-AG 415
Cdd:cd05941 250 --------GMALSNPLDGERRPGtVGMPLPGVqARIVDEETGEPLPRG--EVGEIQVRGPSVFKEYWNKPEATKEEFtDD 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSK-DIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDA-QV 493
Cdd:cd05941 320 GWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaAL 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRK 535
Cdd:cd05941 400 SLEELKEWAKQRLAPYKRPRRLILvDELPRNAMGKVNKKELRK 442
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
35-539 |
6.30e-57 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 199.12 E-value: 6.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 35 DLAIVHGSIRQ-NWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK13295 45 AVRLGTGAPRRfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEF-----APHIPEIKKALPALKIIQVNDELGPKDVEP-FSDIEYEGFLQSAEDLDNWVLPKDewDAIAL 187
Cdd:PRK13295 125 HAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEAlLITPAWEQEPDAPAILARLRPGPD--DVTQL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 NYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRK-FDPKTCFDLI 266
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDiWDPARAAELI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAPVVHAALANAPAEMkagiDHPVSAM----VAGAAPPEAVLARMEQ-MGFHMVHVYGLTEvygPSAVCAE 341
Cdd:PRK13295 283 RTEGVTFTMASTPFLTDLTRAVKES----GRPVSSLrtflCAGAPIPGALVERARAaLGAKIVSAWGMTE---NGAVTLT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEwDELSVEDRAAQKARQGVRntlqgaLTVLDPETmEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSfAGGWFHTG 421
Cdd:PRK13295 356 KLD-DPDERASTTDGCPLPGVE------VRVVDADG-APLPAG--QIGRLQVRGCSNFGGYLKRPQLNGTD-ADGWFDTG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEE---- 497
Cdd:PRK13295 425 DLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEmvef 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1092482886 498 LD------QYCRERLAgfkrpkyyVFGELAKTATGKIQKFELRKQAEA 539
Cdd:PRK13295 505 LKaqkvakQYIPERLV--------VRDALPRTPSGKIQKFRLREMLRG 544
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
53-536 |
1.63e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 194.35 E-value: 1.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPE 132
Cdd:PRK08276 20 RSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 133 IKKALPA-LKIIQVNDElgpkDVEPFSDIEYEGFLQSAEDLDnwvlpkDEWDAIALNYTSGTTGNPKGVVYHHRG----A 207
Cdd:PRK08276 100 LAAELPAgVPLLLVVAG----PVPGFRSYEEALAAQPDTPIA------DETAGADMLYSSGTTGRPKGIKRPLPGldpdE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 208 ALNAIAQSLEFDMPKRP--VYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALA 285
Cdd:PRK08276 170 APGMMLALLGFGMYGGPdsVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 286 NAPAEMKAGIDhpVSAM---VAGAAP-PEAVLARM-EQMGFHMVHVYGLTEVYGPSAVCAEkpEWdelsvedraaqKARQ 360
Cdd:PRK08276 250 KLPEEVRARYD--VSSLrvaIHAAAPcPVEVKRAMiDWWGPIIHEYYASSEGGGVTVITSE--DW-----------LAHP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 361 G-VRNTLQGALTVLDpETMEPVPAdgKTIGELMFRGNIVMKGYLKNPAETGKSFAG-GWFHTGDLGVLHPDGYAQIKDRS 438
Cdd:PRK08276 315 GsVGKAVLGEVRILD-EDGNELPP--GEIGTVYFEMDGYPFEYHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDRK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 439 KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYY 515
Cdd:PRK08276 392 SDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWLRGRLAHYKCPRSI 471
|
490 500
....*....|....*....|..
gi 1092482886 516 VF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK08276 472 DFeDELPRTPTGKLYKRRLRDR 493
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
23-538 |
2.99e-55 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 194.95 E-value: 2.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGS---IRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLL 97
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGedgEERTLTyaELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 98 ALNVRLETEGLIYCLQHGEAEFLLVDSEFA------PHIPEIKKALPAL----KIIQVNDELGPKDVEpfSDIEYEGFLQ 167
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKVLITADGGLrggkviDLKEKVDEALEELpsleHVIVVGRTGADVPME--GDLDWDELLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 168 SA-EDLDNWVLPKDewDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQS-LEFDMpkRP--VYLWTLPLfhcnGW----- 238
Cdd:COG0365 171 AAsAEFEPEPTDAD--DPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAkYVLDL--KPgdVFWCTADI----GWatghs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 239 ---CFAW----TIAARGGVNVclrkF-DPKTCFDLIRQERVGFYCAAPVVHAALanapaeMKAGIDHPVS--------AM 302
Cdd:COG0365 243 yivYGPLlngaTVVLYEGRPD----FpDPGRLWELIEKYGVTVFFTAPTAIRAL------MKAGDEPLKKydlsslrlLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 303 VAG-AAPPEAVLARMEQMGFHMVHVYGLTEVYGPsaVCAEKPEWDelsVEDRAAQKARQGVRntlqgaLTVLDpETMEPV 381
Cdd:COG0365 313 SAGePLNPEVWEWWYEAVGVPIVDGWGQTETGGI--FISNLPGLP---VKPGSMGKPVPGYD------VAVVD-EDGNPV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 382 PADgkTIGELMFRGNI--VMKGYLKNPAETGKSFAG---GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVED 456
Cdd:COG0365 381 PPG--EEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIES 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 457 VLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFE 532
Cdd:COG0365 459 ALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFvDELPKTRSGKIMRRL 538
|
....*.
gi 1092482886 533 LRKQAE 538
Cdd:COG0365 539 LRKIAE 544
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
16-534 |
7.86e-54 |
|
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: 189.89 E-value: 7.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 16 YTPLTPIDFLVRahEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV 95
Cdd:cd05959 3 YNAATLVDLNLN--EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 96 LLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHI-PEIKKALPALKIIQVNDELGPKDVEPfsdiEYEGFLQSAEDLDN 174
Cdd:cd05959 81 PVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLVVLIVSGGAGPEAGAL----LLAELVAAEAEQLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 175 wvlPKDEW-DAIAL-NYTSGTTGNPKGVVYHHRG--AALNAIAQSL----EFDmpkrpVYLWTLPLFHC----NGWCFAW 242
Cdd:cd05959 157 ---PAATHaDDPAFwLYSSGSTGRPKGVVHLHADiyWTAELYARNVlgirEDD-----VCFSAAKLFFAyglgNSLTFPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 243 TIaarGGVNVCLRKF-DPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARME-QMG 320
Cdd:cd05959 229 SV---GATTVLMPERpTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKaRFG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVHVYGLTEVYgpSAVCAEKPEwdelSVEDRAAQKARQGVRNTLQGaltvldpETMEPVPADGktIGELMFRGNIVMK 400
Cdd:cd05959 306 LDILDGIGSTEML--HIFLSNRPG----RVRYGTTGKPVPGYEVELRD-------EDGGDVADGE--PGELYVRGPSSAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEV 480
Cdd:cd05959 371 MYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTK 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 481 PVAFVELK---DDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05959 451 PKAFVVLRpgyEDSEALEEELKEFVKDRLAPYKYPRWIVFvDELPKTATGKIQRFKLR 508
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
46-528 |
4.22e-53 |
|
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: 186.15 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 46 NWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSE 125
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 FaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaEDLdnwvlpkdewdAIaLNYTSGTTGNPKGVVYHHR 205
Cdd:cd05935 83 L-------------------------------------------DDL-----------AL-IPYTSGTTGLPKGCMHTHF 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAAL 284
Cdd:cd05935 108 SAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAvYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 285 ANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMVHVYGLTEVYGPSavcaekpewdelSVEDRAAQKAR-QGV 362
Cdd:cd05935 188 LATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQT------------HTNPPLRPKLQcLGI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 363 RNTLQGALtVLDPETMEPVPaDGKtIGELMFRGNIVMKGYLKNPAETGKSFA--GG--WFHTGDLGVLHPDGYAQIKDRS 438
Cdd:cd05935 256 P*FGVDAR-VIDIETGRELP-PNE-VGEIVVRGPQIFKGYWNRPEETEESFIeiKGrrFFRTGDLGYMDEEGYFFFVDRV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 439 KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDD--AQVSEEELDQYCRERLAGFKRPKYYV 516
Cdd:cd05935 333 KRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVE 412
|
490
....*....|...
gi 1092482886 517 F-GELAKTATGKI 528
Cdd:cd05935 413 FvDELPRSASGKI 425
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
18-537 |
7.46e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 189.78 E-value: 7.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPIDFLVRAHEVFGDDLAIV--------HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGv 89
Cdd:PRK07529 24 PASTYELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 90 PMSGGVLLALNVRLETEGLIYCLQHGEAEFLLV-----DSEFAPHIPEIKKALPALK-IIQVN--DELGP------KDVE 155
Cdd:PRK07529 103 GEAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIWQKVAEVLAALPELRtVVEVDlaRYLPGpkrlavPLIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 156 PFSDIEYEGFL-----QSAEDLDNWVLPKDEwDAIALNYTSGTTGNPKGVVYHHRGAALNA-IAQSLEFDMPKRpVYLWT 229
Cdd:PRK07529 183 RKAHARILDFDaelarQPGDRLFSGRPIGPD-DVAAYFHTGGTTGMPKLAQHTHGNEVANAwLGALLLGLGPGD-TVFCG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 230 LPLFHCNGwCFAWTIA--ARGGVNV-----------CLRKFdpktcFDLIRQERVGFYCAAPVVHAALANAPAEmkagiD 296
Cdd:PRK07529 261 LPLFHVNA-LLVTGLAplARGAHVVlatpqgyrgpgVIANF-----WKIVERYRINFLSGVPTVYAALLQVPVD-----G 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 297 HPVS----AMVAGAAPPEAVLAR-MEQMGFHMVHVYGLTEvyGPSAVCAEKPEWDEL--SVEDRAA-QKARqgvrntlqg 368
Cdd:PRK07529 330 HDISslryALCGAAPLPVEVFRRfEAATGVRIVEGYGLTE--ATCVSSVNPPDGERRigSVGLRLPyQRVR--------- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 369 aLTVLDPETMEPVPADGKTIGELMFRGNIVMKGYLkNPAETGKSFA-GGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGE 447
Cdd:PRK07529 399 -VVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLeDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 448 NISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAgfKR---PKY-YVFGELAKT 523
Cdd:PRK07529 477 NIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIA--ERaavPKHvRILDALPKT 554
|
570
....*....|....
gi 1092482886 524 ATGKIQKFELRKQA 537
Cdd:PRK07529 555 AVGKIFKPALRRDA 568
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
183-528 |
1.39e-52 |
|
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: 182.08 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRgaalNAIAQSLEFDMP----KRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFD 258
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHG----NLIAANLQLIHAmgltEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 259 PKTCFDLIRQERVGFYCAAPVVHAALANAPAemKAGIDHPVSAMVAGAAPPEaVLARMEQMG---FHMVhvYGLTEVYGP 335
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAE--KSGVDLSSLRHVLGLDAPE-TIQRFEETTgatFWSL--YGQTETSGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 SAVCaekpewdelSVEDRAAQKARQGVRNTLQgaltVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAG 415
Cdd:cd17637 152 VTLS---------PYRERPGSAGRPGPLVRVR----IVD-DNDRPVPAG--ETGEIVVRGPLVFQGYWNLPELTAYTFRN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRS--KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQV 493
Cdd:cd17637 216 GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATL 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKI 528
Cdd:cd17637 296 TADELIEFVGSRIARYKKPRYVVFVEaLPKTADGSI 331
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
18-539 |
1.77e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 187.09 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPI-DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQ-NGADRGTTVATLLHNTPAMVEAGFGVPMSGGV 95
Cdd:PRK08314 8 PETSLfHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 96 LLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPhipEIKKALPALKIIQV-----NDELGPKDVEPFSDieyegFLQSAE 170
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAP---KVAPAVGNLRLRHVivaqySDYLPAEPEIAVPA-----WLRAEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 171 DLDNWVLPKD-EW-DAIA-----------------LNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLP 231
Cdd:PRK08314 160 PLQALAPGGVvAWkEALAaglappphtagpddlavLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 232 LFHCNGW--CFAWTIAARGGVnVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPP 309
Cdd:PRK08314 240 LFHVTGMvhSMNAPIYAGATV-VLMPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 310 EAVLARM-EQMGFHMVHVYGLTEVYGPSAV---------CAEKPEWDelsVEDRaaqkarqgvrntlqgaltVLDPETME 379
Cdd:PRK08314 319 EAVAERLkELTGLDYVEGYGLTETMAQTHSnppdrpklqCLGIPTFG---VDAR------------------VIDPETLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 380 PVPaDGKtIGELMFRGNIVMKGYLKNPAETGKSFA--GG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVE 455
Cdd:PRK08314 378 ELP-PGE-VGEIVVHGPQVFKGYWNRPEATAEAFIeiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 456 DVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQ--VSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFE 532
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFvDSLPKSGSGKILWRQ 535
|
....*..
gi 1092482886 533 LRKQAEA 539
Cdd:PRK08314 536 LQEQEKA 542
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
25-536 |
6.04e-52 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 185.73 E-value: 6.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 25 LVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLE 104
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 105 TEGLIYCLQHGEAEFLLVDSEFAPHI---PEIKKALPALKIIqvnDELGPKDVEPfsDIEYEGFLQSAEDLDnwVLPKDE 181
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALeaaDPGDLPLPAVWLL---DAPASVSVPA--GWSTAPLPPLDAPAP--AAAVQP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 WDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKT 261
Cdd:PRK06155 180 GDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 CFDLIRQER--VGFYCAApVVHAALANAPAEMKAGidHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGPSAVc 339
Cdd:PRK06155 260 FWPAVRRHGatVTYLLGA-MVSILLSQPARESDRA--HRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAV- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 aekpewdelsvedrAAQKARQGVRNTLQGALT--VLDpETMEPVPADgkTIGELMFRGN---IVMKGYLKNPAETGKSFA 414
Cdd:PRK06155 336 --------------THGSQRPGSMGRLAPGFEarVVD-EHDQELPDG--EPGELLLRADepfAFATGYFGMPEKTVEAWR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 415 GGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWG-EVPVAFVeLKDDAQV 493
Cdd:PRK06155 399 NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVV-LRDGTAL 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK06155 478 EPVALVRHCEPRLAYFAVPRYVEFvAALPKTENGKVQKFVLREQ 521
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
189-530 |
8.84e-52 |
|
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: 179.62 E-value: 8.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPKTCFDLIR 267
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVAClLTGATVVPVAVFDVDAILEAIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARM-EQMGFHMV-HVYGLTEvygpsAVCAE--KP 343
Cdd:cd17638 87 RERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFETVlTAYGLTE-----AGVATmcRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 344 EWDELSVEDRAAqKARQGVRNTLQGAltvldpetmepvpadgktiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGD 422
Cdd:cd17638 162 GDDAETVATTCG-RACPGFEVRIADD-------------------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 423 LGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYC 502
Cdd:cd17638 222 VGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWC 301
|
330 340
....*....|....*....|....*....
gi 1092482886 503 RERLAGFKRPKYYVF-GELAKTATGKIQK 530
Cdd:cd17638 302 RERLANYKVPRFVRFlDELPRNASGKVMK 330
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
53-536 |
3.54e-51 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 182.97 E-value: 3.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPE 132
Cdd:PRK13391 33 RSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 133 IKKALPALKIIQVNDelGPKDVEPFsdieyEGFLQSAEDLDNWVLPkDEWDAIALNYTSGTTGNPKGVVyhhRGAALNAI 212
Cdd:PRK13391 113 LLKQCPGVRHRLVLD--GDGELEGF-----VGYAEAVAGLPATPIA-DESLGTDMLYSSGTTGRPKGIK---RPLPEQPP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 213 AQSLEFDMPKRP--------VYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAAL 284
Cdd:PRK13391 182 DTPLPLTAFLQRlwgfrsdmVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 285 ANAPAEMKAGIDHP-VSAMVAGAAP-PEAVLARMEQMGFHMVH-VYGLTEVYGPSAVCAEkpEWdelsvedraaqKARQG 361
Cdd:PRK13391 262 LKLPEEVRDKYDLSsLEVAIHAAAPcPPQVKEQMIDWWGPIIHeYYAATEGLGFTACDSE--EW-----------LAHPG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 362 -VRNTLQGALTVLDpETMEPVPAdgKTIGELMFRGNIVMKgYLKNPAET--GKSFAGGWFHTGDLGVLHPDGYAQIKDRS 438
Cdd:PRK13391 329 tVGRAMFGDLHILD-DDGAELPP--GEPGTIWFEGGRPFE-YLNDPAKTaeARHPDGTWSTVGDIGYVDEDGYLYLTDRA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 439 KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE---EELDQYCRERLAGFKRPKYY 515
Cdd:PRK13391 405 AFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPRSI 484
|
490 500
....*....|....*....|..
gi 1092482886 516 VF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK13391 485 DFeDELPRLPTGKLYKRLLRDR 506
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
18-535 |
3.71e-49 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 178.82 E-value: 3.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTPIDFLVRAHEVFGDDLAIVHGSIRQNWTETYH---RCRQMAAALRQN-GADRGTTVATLLHNTPAMVEAGFGVPMSG 93
Cdd:PRK05620 9 PLSLTRILEYGSTVHGDTTVTTWGGAEQEQTTFAAigaRAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 94 GVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVndeLGPKDV--------EPFSDIEYEGF 165
Cdd:PRK05620 89 AVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECPCVRAVVF---IGPSDAdsaaahmpEGIKVYSYEAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 166 LQSAEDLDNWvlPK-DEWDAIALNYTSGTTGNPKGVVYHHRgaALNAIAQSL----EFDMPKRPVYLWTLPLFHCNGWCF 240
Cdd:PRK05620 166 LDGRSTVYDW--PElDETTAAAICYSTGTTGAPKGVVYSHR--SLYLQSLSLrttdSLAVTHGESFLCCVPIYHVLSWGV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 241 AwtIAA-RGGVNVCL--RKFDPKTCFDLIRQervgfycAAP-VVHAALANAPAEMKAGIDHPVSAM------VAGAA-PP 309
Cdd:PRK05620 242 P--LAAfMSGTPLVFpgPDLSAPTLAKIIAT-------AMPrVAHGVPTLWIQLMVHYLKNPPERMslqeiyVGGSAvPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 310 EAVLARMEQMGFHMVHVYGLTEVyGPSAVCAEKPEwdELSVEDRAAQKARQGVRNTLQGALTVLDPETMEpvpADGKTIG 389
Cdd:PRK05620 313 ILIKAWEERYGVDVVHVWGMTET-SPVGTVARPPS--GVSGEARWAYRVSQGRFPASLEYRIVNDGQVME---STDRNEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 390 ELMFRGNIVMKGYLKNPAETGKSFAG-----------------GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSI 452
Cdd:PRK05620 387 EIQVRGNWVTASYYHSPTEEGGGAAStfrgedvedandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 453 EVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFvDEIDKTSVGKF 546
|
....*..
gi 1092482886 529 QKFELRK 535
Cdd:PRK05620 547 DKKDLRQ 553
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
93-535 |
5.99e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 171.85 E-value: 5.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 93 GGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFA-----PHIPEIKKALPALKIIQVNDELGPKDvepfSDIEYEGFLQ 167
Cdd:PRK06087 98 GAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKqtrpvDLILPLQNQLPQLQQIVGVDKLAPAT----SSLSLSQIIA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 168 SAEDLDNWVlPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWcFAWTIAAR 247
Cdd:PRK06087 174 DYEPLTTAI-TTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGF-LHGVTAPF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 248 --GGVNVCLRKFDPKTCFDLIRQERVGFYCAA-PVVHAALAN---APAEMKAgidhpVSAMVAGAAP-PEAVLARMEQMG 320
Cdd:PRK06087 252 liGARSVLLDIFTPDACLALLEQQRCTCMLGAtPFIYDLLNLlekQPADLSA-----LRFFLCGGTTiPKKVARECQQRG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVHVYGLTEVYGPSAVCAEKPewdeLSVEDRAAQKARQGVRntlqgaLTVLDpETMEPVPADGKtiGELMFRGNIVMK 400
Cdd:PRK06087 327 IKLLSVYGSTESSPHAVVNLDDP----LSRFMHTDGYAAAGVE------IKVVD-EARKTLPPGCE--GEEASRGPNVFM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGE 479
Cdd:PRK06087 394 GYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGE 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 480 VPVAFVELKDDAQVS--EEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRK 535
Cdd:PRK06087 474 RSCAYVVLKAPHHSLtlEEVVAFFSRKRVAKYKYPEHIVViDKLPRTASGKIQKFLLRK 532
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
47-534 |
1.04e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 171.09 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEF 126
Cdd:PRK13382 71 WRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 APHIPEIKKALP-ALKIIQVNDELGPKDVEPFSDIEYEGFLQSAEDldnwvlpkdEWDAIALnyTSGTTGNPKGVvyHHR 205
Cdd:PRK13382 151 SATVDRALADCPqATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGR---------KGRVILL--TSGTTGTPKGA--RRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAIAQSLEFDMP---KRPVYLwTLPLFHcnGWCFAWTI--AARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVV 280
Cdd:PRK13382 218 GPGGIGTLKAILDRTPwraEEPTVI-VAPMFH--AWGFSQLVlaASLACTIVTRRRFDPEATLDLIDRHRATGLAVVPVM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 281 HAALANAPAEMK---AGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVygpSAVCAEKPEwdELSVEDRAAQK 357
Cdd:PRK13382 295 FDRIMDLPAEVRnrySGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA---GMIATATPA--DLRAAPDTAGR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 358 ARQGVRntlqgaLTVLDPETMEpVPaDGKtIGELMFRGNIVMKGYlkNPAETgKSFAGGWFHTGDLGVLHPDGYAQIKDR 437
Cdd:PRK13382 370 PAEGTE------IRILDQDFRE-VP-TGE-VGTIFVRNDTQFDGY--TSGST-KDFHDGFMASGDVGYLDENGRLFVVGR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 438 SKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF 517
Cdd:PRK13382 438 DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVV 517
|
490
....*....|....*...
gi 1092482886 518 -GELAKTATGKIQKFELR 534
Cdd:PRK13382 518 lDELPRGATGKILRRELQ 535
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
30-527 |
1.09e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 170.84 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 30 EVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLI 109
Cdd:PRK07798 14 DAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 110 YCLQHGEAEFLLVDSEFAPHIPEIKKALPALK-IIQVNDELGPkDVEPFSdIEYEGFL--QSAEDLDnwvlPKDEWDAIA 186
Cdd:PRK07798 94 YLLDDSDAVALVYEREFAPRVAEVLPRLPKLRtLVVVEDGSGN-DLLPGA-VDYEDALaaGSPERDF----GERSPDDLY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 187 LNYTSGTTGNPKGVVYHH---RGAALNAIAQ------SLEFDMPKR------PVYLWTLPLFHCNGWCFAWTIAARGGVN 251
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQediFRVLLGGRDFatgepiEDEEELAKRaaagpgMRRFPAPPLMHGAGQWAAFAALFSGQTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 252 VCLR--KFDPKTCFDLIRQERV------GFYCAAPVVHAALANAPAEMKAgidhpVSAMVAGAAP--PEAVLARMEqmgf 321
Cdd:PRK07798 248 VLLPdvRFDADEVWRTIEREKVnvitivGDAMARPLLDALEARGPYDLSS-----LFAIASGGALfsPSVKEALLE---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 322 HMVHV-----YGLTEV-YGPSAVCAEKPEwdelsvedraaqkARQGVRNTLQGALTVLDPETmEPVPADGKTIGELMFRG 395
Cdd:PRK07798 319 LLPNVvltdsIGSSETgFGGSGTVAKGAV-------------HTGGPRFTIGPRTVVLDEDG-NPVEPGSGEIGWIARRG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 396 NIVMkGYLKNPAETGKSF--AGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVA 471
Cdd:PRK07798 385 HIPL-GYYKDPEKTAETFptIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092482886 472 LADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFG-ELAKTATGK 527
Cdd:PRK07798 464 VPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVdEVQRSPAGK 520
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
23-462 |
1.11e-46 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 172.21 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVH----GSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLA 98
Cdd:COG1022 15 DLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 99 LNVRLETEGLIYCLQHGEAEFLLV-DSEFAPHIPEIKKALPALK-IIQVNDELGPKDVEPFSdieYEGFLQSAEDLDNWV 176
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRhIVVLDPRGLRDDPRLLS---LDELLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 177 LPKDEWDAIALN------YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGV 250
Cdd:COG1022 172 ELEARRAAVKPDdlatiiYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYALAAGAT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 251 NVCLRkfDPKTCFDLIRQERVGFYCAAP--------VVHAALANAPAE--------MKAGIDH--------PVSA----- 301
Cdd:COG1022 252 VAFAE--SPDTLAEDLREVKPTFMLAVPrvwekvyaGIQAKAEEAGGLkrklfrwaLAVGRRYararlagkSPSLllrlk 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 302 ----------------------MVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVYGPSAVcaekpewdelsvedRAAQKA 358
Cdd:COG1022 330 haladklvfsklrealggrlrfAVSGGAAlGPELARFFRALGIPVLEGYGLTETSPVITV--------------NRPGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 359 RQGvrntlqgalTVldpetmePVPADGKTI-----GELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYA 432
Cdd:COG1022 396 RIG---------TV-------GPPLPGVEVkiaedGEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDIGELDEDGFL 459
|
490 500 510
....*....|....*....|....*....|.
gi 1092482886 433 QIKDRSKDIII-SGGENISSIEVEDVLYKHP 462
Cdd:COG1022 460 RITGRKKDLIVtSGGKNVAPQPIENALKASP 490
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
53-540 |
1.52e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 171.38 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCrqmAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPE 132
Cdd:PRK06178 70 RF---AALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 133 IKKA--------------LPALKIIQVNDELGPKDVEPFSDIEyegFLQSAEDLD-NWVLPKDEWDAIA-LNYTSGTTGN 196
Cdd:PRK06178 147 VRAEtslrhvivtsladvLPAEPTLPLPDSLRAPRLAAAGAID---LLPALRACTaPVPLPPPALDALAaLNYTGGTTGM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 197 PKGVVYHHR-----GAALNAIAQSLEFDmpkrPVYLWTLPLFhcngwcfaWtIAAR----------GGVNVCLRKFDPKT 261
Cdd:PRK06178 224 PKGCEHTQRdmvytAAAAYAVAVVGGED----SVFLSFLPEF--------W-IAGEnfgllfplfsGATLVLLARWDAVA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 CFDLIRQERVGfYCAAPVVHAAlanapaEMkagIDHPVSA-------MVAGAAP------PEAVLARMEQMGFHMVHV-Y 327
Cdd:PRK06178 291 FMAAVERYRVT-RTVMLVDNAV------EL---MDHPRFAeydlsslRQVRVVSfvkklnPDYRQRWRALTGSVLAEAaW 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 328 GLTEVYGPSAVCAEKPEWDElsveDRAAQKARQG--VRNTlqgALTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKN 405
Cdd:PRK06178 361 GMTETHTCDTFTAGFQDDDF----DLLSQPVFVGlpVPGT---EFKICDFETGELLPLGAE--GEIVVRTPSLLKGYWNK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 406 PAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFV 485
Cdd:PRK06178 432 PEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFV 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1092482886 486 ELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGELAKTATGKIQKFELRKQAEAL 540
Cdd:PRK06178 512 QLKPGADLTAAALQAWCRENMAVYKVPEIRIVDALPMTATGKVRKQDLQALAEEL 566
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-537 |
1.64e-46 |
|
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: 166.50 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL---RKFDP 259
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLagpAGYRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 KTCFD----LIRQERVGFYCAAPVVHAALANAPAEmkAGIDHPVSAMVAGAAPPEAVLARME-QMGFHMVHVYGLTEvyg 334
Cdd:cd05944 83 PGLFDnfwkLVERYRITSLSTVPTVYAALLQVPVN--ADISSLRFAMSGAAPLPVELRARFEdATGLPVVEGYGLTE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 335 psAVCAEKpewdeLSVEDRAAQKARQGVR-NTLQGALTVLDPETMEPVPADGKTIGELMFRGNIVMKGYLKNPAETGKSF 413
Cdd:cd05944 158 --ATCLVA-----VNPPDGPKRPGSVGLRlPYARVRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQV 493
Cdd:cd05944 231 ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1092482886 494 SEEELDQYCRERLAgfKR---PKY-YVFGELAKTATGKIQKFELRKQA 537
Cdd:cd05944 311 EEEELLAWARDHVP--ERaavPKHiEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-536 |
2.10e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 169.22 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYC 111
Cdd:PRK09088 10 QRLAAVDLALGRRWTyaELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 112 LQHGEAEFLLVDSEFAPHIPEIKkALPALkiIQVNDELGPKDVEPfsdieyegflqsaedldnwvLPKDEWDAIAlnYTS 191
Cdd:PRK09088 90 LQDAEPRLLLGDDAVAAGRTDVE-DLAAF--IASADALEPADTPS--------------------IPPERVSLIL--FTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 192 GTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAW-TIAARGGVNVCLRKFDPKTCFDLIRQER 270
Cdd:PRK09088 145 GTSGQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVrPVLAVGGSILVSNGFEPKRTLGRLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 271 VGF--YCAAPVVHAALANAPAEMKAGIDHpVSAMVAGAAP--PEAVLARMEQmGFHMVHVYGLTE---VYGPSAVCAEkp 343
Cdd:PRK09088 225 LGIthYFCVPQMAQAFRAQPGFDAAALRH-LTALFTGGAPhaAEDILGWLDD-GIPMVDGFGMSEagtVFGMSVDCDV-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 344 ewdelsvedraaqkarqgVRNTLQGALTVLDPETMEPVPADGKTI-----GELMFRGNIVMKGYLKNPAETGKSFAG-GW 417
Cdd:PRK09088 301 ------------------IRAKAGAAGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGdGW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 418 FHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEE 497
Cdd:PRK09088 363 FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLER 442
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092482886 498 LDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQ 536
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDaLPRTASGKLQKARLRDA 482
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
54-539 |
6.36e-46 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 169.01 E-value: 6.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 54 CRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNvRLETEGLIY-CLQHGEAEFLLVDSEFAPHIPE 132
Cdd:PLN02246 60 SRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN-PFYTPAEIAkQAKASGAKLIITQSCYVDKLKG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 133 IKkALPALKIIQVNDElgPKDVEPFSDIeyegfLQSAEDldnwVLPKDEW---DAIALNYTSGTTGNPKGVVYHHRGAaL 209
Cdd:PLN02246 139 LA-EDDGVTVVTIDDP--PEGCLHFSEL-----TQADEN----ELPEVEIspdDVVALPYSSGTTGLPKGVMLTHKGL-V 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 210 NAIAQSLEFDMP-----KRPVYLWTLPLFHcngwcfawtIAARGGVNVC----------LRKFDPKTCFDLIRQERVGFY 274
Cdd:PLN02246 206 TSVAQQVDGENPnlyfhSDDVILCVLPMFH---------IYSLNSVLLCglrvgaailiMPKFEIGALLELIQRHKVTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 275 CAAPVVHAALANAPAEMKagidHPVSA--MV-AGAAP-------------PEAVLARmeqmGfhmvhvYGLTEVyGPS-A 337
Cdd:PLN02246 277 PFVPPIVLAIAKSPVVEK----YDLSSirMVlSGAAPlgkeledafraklPNAVLGQ----G------YGMTEA-GPVlA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 338 VC---AEKPewdelsvedraaQKARQG-----VRNTlqgALTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAET 409
Cdd:PLN02246 342 MClafAKEP------------FPVKSGscgtvVRNA---ELKIVDPETGASLPRNQP--GEICIRGPQIMKGYLNDPEAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK 488
Cdd:PLN02246 405 ANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRS 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 489 DDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQAEA 539
Cdd:PLN02246 485 NGSEITEDEIKQFVAKQVVFYKRIHKVFFVDsIPKAPSGKILRKDLRAKLAA 536
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
25-541 |
4.88e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 166.90 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 25 LVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLE 104
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 105 TEGLIYCLQHGEAEFLLVDSEFAPHIPEIKK-ALPALKIIQVNDELGPKDVEPFSDIEyegflqSAEDLDNWVLPKDE-- 181
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLVTDETCSSWYEELQNdRLPSLMWQVFLESPSSSVFIFLNSFL------TTEMLKQRALGTTEld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 --W---DAIALNYTSGTTGNPKGVVYHHRgaALnaIAQSL---------EFDmpkrpVYLWTLPLFHCNGWCFAWTIAAR 247
Cdd:PLN02860 167 yaWapdDAVLICFTSGTTGRPKGVTISHS--AL--IVQSLakiaivgygEDD-----VYLHTAPLCHIGGLSSALAMLMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 248 GGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALAnAPAEMKAGID--HPVSAMVAGAAPPEAVLARMEQMGF---H 322
Cdd:PLN02860 238 GACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLI-SLTRKSMTWKvfPSVRKILNGGGSLSSRLLPDAKKLFpnaK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 323 MVHVYGLTEVygpsavCA-------EKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETME-PVPADGK-TIGELMF 393
Cdd:PLN02860 317 LFSAYGMTEA------CSsltfmtlHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPAPHVElKIGLDESsRVGRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 394 RGNIVMKGYL-KNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVAL 472
Cdd:PLN02860 391 RGPHVMLGYWgQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 473 ADEKWGEVPVAFVELKD--------------DAQVSEEELDQYCRER-LAGFKRPKYYVFGE--LAKTATGKIQKFELRK 535
Cdd:PLN02860 471 PDSRLTEMVVACVRLRDgwiwsdnekenakkNLTLSSETLRHHCREKnLSRFKIPKLFVQWRkpFPLTTTGKIRRDEVRR 550
|
....*.
gi 1092482886 536 QAEALF 541
Cdd:PLN02860 551 EVLSHL 556
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
56-535 |
5.16e-44 |
|
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: 161.35 E-value: 5.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 56 QMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEfaphipeikk 135
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 136 alpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQS 215
Cdd:cd05972 82 -----------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 216 LEFDMPKRPVYlWTL--PlfhcnGWC-FAW-TIAARGGVNVC-----LRKFDPKTCFDLIRQERVGFYCAAPVVHAALan 286
Cdd:cd05972 115 YWLGLRPDDIH-WNIadP-----GWAkGAWsSFFGPWLLGATvfvyeGPRFDAERILELLERYGVTSFCGPPTAYRML-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 287 apaeMKAGIDH----PVSAMVAGAAP--PEAVLARMEQMGFHMVHVYGLTEVygpSAVCAEKPEwdeLSVEDRAAQKARQ 360
Cdd:cd05972 187 ----IKQDLSSykfsHLRLVVSAGEPlnPEVIEWWRAATGLPIRDGYGQTET---GLTVGNFPD---MPVKPGSMGRPTP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 361 GVRntlqgaLTVLDPETMEPVPAdgkTIGELMFRGNIV--MKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRS 438
Cdd:cd05972 257 GYD------VAIIDDDGRELPPG---EEGDIAIKLPPPglFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 439 KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYY 515
Cdd:cd05972 328 DDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPREI 407
|
490 500
....*....|....*....|.
gi 1092482886 516 VF-GELAKTATGKIQKFELRK 535
Cdd:cd05972 408 EFvEELPKTISGKIRRVELRD 428
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
58-535 |
6.08e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 163.56 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 58 AAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKAL 137
Cdd:PRK07788 88 ARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 138 PALKIIQVNdelgpKDVEPFSDIEYEGFLQSAEDLDNWVLPK-DEWDAIALnYTSGTTGNPKGVVyHHRGAALNAIAQSL 216
Cdd:PRK07788 168 GRLRAWGGN-----PDDDEPSGSTDETLDDLIAGSSTAPLPKpPKPGGIVI-LTSGTTGTPKGAP-RPEPSPLAPLAGLL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 217 -EFDMPKRPVYLWTLPLFHCNGWCfAWTIAARGGVNVCL-RKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAG 294
Cdd:PRK07788 241 sRVPFRAGETTLLPAPMFHATGWA-HLTLAMALGSTVVLrRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 295 IDhpVSAM----VAGAA-PPEAVLARMEQMGFHMVHVYGLTEVygpsAVCA-EKPEwdELSVEDRAAQKARQGVRntlqg 368
Cdd:PRK07788 320 YD--TSSLkiifVSGSAlSPELATRALEAFGPVLYNLYGSTEV----AFATiATPE--DLAEAPGTVGRPPKGVT----- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 369 aLTVLDPETmEPVPadGKTIGELMFRGNIVMKGYlknpaeTG---KSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISG 445
Cdd:PRK07788 387 -VKILDENG-NEVP--RGVVGRIFVGNGFPFEGY------TDgrdKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 446 GENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTA 524
Cdd:PRK07788 457 GENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFlDELPRNP 536
|
490
....*....|.
gi 1092482886 525 TGKIQKFELRK 535
Cdd:PRK07788 537 TGKVLKRELRE 547
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
46-462 |
4.18e-43 |
|
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: 159.30 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 46 NWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVdse 125
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 faphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaEDLDnwvlpkdewDAIALNYTSGTTGNPKGVVYHHR 205
Cdd:cd05907 84 --------------------------------------------EDPD---------DLATIIYTSGTTGRPKGVMLSHR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAIAQSLEFDMPKRPVYLWTLPLFHC---NGWCFAWtIAARGGVNVCLrkfDPKTCFDLIRQERVGFYCAAP---- 278
Cdd:cd05907 111 NILSNALALAERLPATEGDRHLSFLPLAHVferRAGLYVP-LLAGARIYFAS---SAETLLDDLSEVRPTVFLAVPrvwe 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 279 -VVHAALANAPAEMKAGIDH-----PVSAMVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVygpSAVCAEKPEWDElsve 351
Cdd:cd05907 187 kVYAAIKVKAVPGLKRKLFDlavggRLRFAASGGAPlPAELLHFFRALGIPVYEGYGLTET---SAVVTLNPPGDN---- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 352 dRAAQKARQGVRNTLQgaltvLDPEtmepvpadgktiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDG 430
Cdd:cd05907 260 -RIGTVGKPLPGVEVR-----IADD------------GEILVRGPNVMLGYYKNPEATAEALdADGWLHTGDLGEIDEDG 321
|
410 420 430
....*....|....*....|....*....|...
gi 1092482886 431 YAQIKDRSKDIII-SGGENISSIEVEDVLYKHP 462
Cdd:cd05907 322 FLHITGRKKDLIItSGGKNISPEPIENALKASP 354
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
190-537 |
1.79e-42 |
|
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: 154.41 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 190 TSGTTGNPKGVVyhHRGAALNAIAQSLEFDMPKRP--VYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPktcfdlIR 267
Cdd:cd17630 8 TSGSTGTPKAVV--HTAANLLASAAGLHSRLGFGGgdSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA------LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFycaaPVVHAALAnaPAEMK------AGIDHPVS---AMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVygPSAV 338
Cdd:cd17630 80 EDLAPP----GVTHVSLV--PTQLQrlldsgQGPAALKSlraVLLGGAPIPPELLERAADRGIPLYTTYGMTET--ASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CAEKPewdelsvedraAQKARQGVRNTLQGA-LTVLDPetmepvpadgktiGELMFRGNIVMKGYLKNPaETGKSFAGGW 417
Cdd:cd17630 152 ATKRP-----------DGFGRGGVGVLLPGReLRIVED-------------GEIWVGGASLAMGYLRGQ-LVPEFNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 418 FHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELkdDAQVSEEE 497
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG--RGPADPAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1092482886 498 LDQYCRERLAGFKRPK-YYVFGELAKTATGKIQKFELRKQA 537
Cdd:cd17630 285 LRAWLKDKLARFKLPKrIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
37-536 |
1.82e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 158.71 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 37 AIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGE 116
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 117 AEFLLVDSEF----APHIPEikkALPALKI-----IQVNDELGPKDVE-PFSDIEYEGFLQSAEDLDNWVLPKdewdAIA 186
Cdd:PRK12406 84 ARVLIAHADLlhglASALPA---GVTVLSVptppeIAAAYRISPALLTpPAGAIDWEGWLAQQEPYDGPPVPQ----PQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 187 LNYTSGTTGNPKGVvyhHRGAALNAIAQSLE------FDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPK 260
Cdd:PRK12406 157 MIYTSGTTGHPKGV---RRAAPTPEQAAAAEqmraliYGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 261 TCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGID-HPVSAMVAGAA--PPEAVLARMEQMGFHMVHVYGLTEVygpSA 337
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDvSSLRHVIHAAApcPADVKRAMIEWWGPVIYEYYGSTES---GA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 338 VCAEKPEwDELSvEDRAAQKARQGVRntlqgaLTVLDpETMEPVPADgkTIGELMFR--GNIVMKgYLKNPAETGKSFAG 415
Cdd:PRK12406 311 VTFATSE-DALS-HPGTVGKAAPGAE------LRFVD-EDGRPLPQG--EIGEIYSRiaGNPDFT-YHNKPEKRAEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE 495
Cdd:PRK12406 379 GFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1092482886 496 EELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEImAELPREDSGKIFKRRLRDP 500
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
23-539 |
2.12e-41 |
|
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: 156.46 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV-LLAL-- 99
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpVFALpa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 100 NVRLETEGLIyclQHGEAEFLLVDSEFA-----PHIPEIKKALPALKIIQVNDElgPKDVEPFSDIEyegflqsAEDLDN 174
Cdd:COG1021 109 HRRAEISHFA---EQSEAVAYIIPDRHRgfdyrALARELQAEVPSLRHVLVVGD--AGEFTSLDALL-------AAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 175 WVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALN--AIAQSLEFDMpkRPVYLWTLPLFHcNgwcFAW-------TIA 245
Cdd:COG1021 177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSvrASAEICGLDA--DTVYLAALPAAH-N---FPLsspgvlgVLY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 246 ARGGVnVCLRKFDPKTCFDLIRQERVGFYCAAP-VVHAALANAPAEmkagiDHPVSAM----VAGAAPPEAVLAR-MEQM 319
Cdd:COG1021 251 AGGTV-VLAPDPSPDTAFPLIERERVTVTALVPpLALLWLDAAERS-----RYDLSSLrvlqVGGAKLSPELARRvRPAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 320 GFHMVHVYGLTEvyGPsaVCAEKPEwDELSVedraaqkarqgVRNTlQG-------ALTVLDPETmEPVPaDGkTIGELM 392
Cdd:COG1021 325 GCTLQQVFGMAE--GL--VNYTRLD-DPEEV-----------ILTT-QGrpispddEVRIVDEDG-NPVP-PG-EVGELL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 393 FRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVA 471
Cdd:COG1021 385 TRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 472 LADEKWGEVPVAFVELkDDAQVSEEELDQYCRER-LAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEA 539
Cdd:COG1021 465 MPDEYLGERSCAFVVP-RGEPLTLAELRRFLRERgLAAFKLPDRLEFvDALPLTAVGKIDKKALRAALAA 533
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
34-537 |
2.57e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 155.99 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALR-QNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCL 112
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAEFLLVDSefaPHIPEIKKALPALKIIQVN-----DELGPKDVEPFSDIEYegflqSAEDLdnwvlpkdewdaIAL 187
Cdd:PRK07867 98 AHADCQLVLTES---AHAELLDGLDPGVRVINVDspawaDELAAHRDAEPPFRVA-----DPDDL------------FML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 NYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLR-KFDPKTCFDLI 266
Cdd:PRK07867 158 IFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRrKFSASGFLPDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGF--YCAAPVvHAALANAPAEMKAgiDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEvyGPSAVcAEKPE 344
Cdd:PRK07867 238 RRYGATYanYVGKPL-SYVLATPERPDDA--DNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTE--GGVAI-TRTPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 345 wdelsvedraaqkARQGVRNTLQGALTVLDPETMEPVP-----ADGKT-----IGELM-FRGNIVMKGYLKNPAETGKSF 413
Cdd:PRK07867 312 -------------TPPGALGPLPPGVAIVDPDTGTECPpaedaDGRLLnadeaIGELVnTAGPGGFEGYYNDPEADAERM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQV 493
Cdd:PRK07867 379 RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKF 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1092482886 494 SEEELDQYCRER--LAGFKRPKYY-VFGELAKTATGKIQKFELRKQA 537
Cdd:PRK07867 459 DPDAFAEFLAAQpdLGPKQWPSYVrVCAELPRTATFKVLKRQLSAEG 505
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
183-534 |
3.19e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 154.76 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIAL-NYTSGTTGNPKGVVYHHRGAA--LNAIAQSLEfdmpkrpvylWT--------LPLFHCNGWCFAWTIAAR-GGV 250
Cdd:PRK07787 128 DAPALiVYTSGTTGPPKGVVLSRRAIAadLDALAEAWQ----------WTaddvlvhgLPLFHVHGLVLGVLGPLRiGNR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 251 NVCLRKFDPktcfDLIRQERVG---FYCAAPVVHAALANAPAEMKAGidHPVSAMVAGAAP-PEAVLARMEQM-GFHMVH 325
Cdd:PRK07787 198 FVHTGRPTP----EAYAQALSEggtLYFGVPTVWSRIAADPEAARAL--RGARLLVSGSAAlPVPVFDRLAALtGHRPVE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 326 VYGLTEVYgpsavcaekpewdeLSVEDRAAQKARQG-VRNTLQGALTVLDPETMEPVPADGKTIGELMFRGNIVMKGYLK 404
Cdd:PRK07787 272 RYGMTETL--------------ITLSTRADGERRPGwVGLPLAGVETRLVDEDGGPVPHDGETVGELQVRGPTLFDGYLN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 405 NPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDR-SKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPV 482
Cdd:PRK07787 338 RPDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIV 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 483 AFVELKDDaqVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:PRK07787 418 AYVVGADD--VAADELIDFVAQQLSVHKRPREVRFvDALPRNAMGKVLKKQLL 468
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-534 |
3.43e-41 |
|
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: 153.74 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 43 IRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFL 120
Cdd:cd05971 3 TPEKVTfkELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 121 LVD--SEfaphipeikkalPALKIiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewdaialnYTSGTTGNPK 198
Cdd:cd05971 83 VTDgsDD------------PALII----------------------------------------------YTSGTTGPPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 199 GVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLfhcnGWcfAWtIAARGGVNVC------------LRKFDPKTCFDLI 266
Cdd:cd05971 105 GALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPA----DW--AW-IGGLLDVLLPslyfgvpvlahrMTKFDPKAALDLM 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAPVVHAALANAPAEMKagiDHPVS--AMVAGAAPPEAVL---ARmEQMGFHMVHVYGLTEVygpSAVCAE 341
Cdd:cd05971 178 SRYGVTTAFLPPTALKMMRQQGEQLK---HAQVKlrAIATGGESLGEELlgwAR-EQFGVEVNEFYGQTEC---NLVIGN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEWdeLSVEDRAAQKARQGVRntlqgaLTVLDPETmEPVPADGKTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTG 421
Cdd:cd05971 251 CSAL--FPIKPGSMGKPIPGHR------VAIVDDNG-TPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDWLLTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---EL 498
Cdd:cd05971 322 DLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEI 401
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092482886 499 DQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05971 402 QELVKTRLAAHEYPREIEFvNELPRTATGKIRRRELR 438
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
65-534 |
6.88e-41 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 154.46 E-value: 6.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 65 GADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPA-LKII 143
Cdd:PRK08008 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATpLRHI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 144 QVNDELGPKDvEPFSDIEYEGFLQSAEDLDNWVLPKDewDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKR 223
Cdd:PRK08008 138 CLTRVALPAD-DGVSSFTQLKAQQPATLCYAPPLSTD--DTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 224 PVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPKTCFDLIRQERvgfycaAPVVHAAlanaPAEMKAGIDHPVSA- 301
Cdd:PRK08008 215 DVYLTVMPAFHIDCQCTAAMAAfSAGATFVLLEKYSARAFWGQVCKYR------ATITECI----PMMIRTLMVQPPSAn 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 302 ---------MVAGAAPPEAVLARMEQMGFHMVHVYGLTE----VYGPSAvcAEKPEWDELSvedRAAQKARQGVRNtlqg 368
Cdd:PRK08008 285 drqhclrevMFYLNLSDQEKDAFEERFGVRLLTSYGMTEtivgIIGDRP--GDKRRWPSIG---RPGFCYEAEIRD---- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 369 altvldpETMEPVPADgkTIGELMFRG---NIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIIS 444
Cdd:PRK08008 356 -------DHNRPLPAG--EIGEICIKGvpgKTIFKEYYLDPKATAKVLeADGWLHTGDTGYVDEEGFFYFVDRRCNMIKR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 445 GGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKT 523
Cdd:PRK08008 427 GGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKdLPRN 506
|
490
....*....|.
gi 1092482886 524 ATGKIQKFELR 534
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
57-530 |
1.38e-40 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 153.89 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 57 MAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEfAPHipeiKKA 136
Cdd:PRK05852 56 LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD-GPH----DRA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 137 LPALKIIQVNDELGPKD------VEPFSDIEYEGFLQSAEDLDnwvLPKDewDAIALnYTSGTTGNPKGVVYHHRGAALN 210
Cdd:PRK05852 131 EPTTRWWPLTVNVGGDSgpsggtLSVHLDAATEPTPATSTPEG---LRPD--DAMIM-FTGGTTGLPKMVPWTHANIASS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 211 AIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAW--TIAARGGVNVCLR-KFDPKTCFDLIRQERVGFYCAAPVVHAALANA 287
Cdd:PRK05852 205 VRAIITGYRLSPRDATVAVMPLYHGHGLIAALlaTLASGGAVLLPARgRFSAHTFWDDIKAVGATWYTAVPTIHQILLER 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 288 PAEMKAGIDHPVSAMV-AGAAP--PEAVLARMEQMGFHMVHVYGLTEVygPSAVCAEKPEWdelsvedrAAQKARQGVRN 364
Cdd:PRK05852 285 AATEPSGRKPAALRFIrSCSAPltAETAQALQTEFAAPVVCAFGMTEA--THQVTTTQIEG--------IGQTENPVVST 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 365 TLQGALTVLDPETM----EPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKD 440
Cdd:PRK05852 355 GLVGRSTGAQIRIVgsdgLPLPAG--AVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 441 IIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRP-KYYVFGE 519
Cdd:PRK05852 433 LINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPaSFQEASG 512
|
490
....*....|.
gi 1092482886 520 LAKTATGKIQK 530
Cdd:PRK05852 513 LPHTAKGSLDR 523
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
189-526 |
1.80e-40 |
|
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: 149.37 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQ 268
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEVLELIEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 269 ERV-GFYCAAPVVHAAlanapAEMKAGIDHPVSAMVAGAAPPE--AVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPew 345
Cdd:cd17636 87 ERCtHAFLLPPTIDQI-----VELNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPGGYGQTEVMGLATFAALGG-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 346 DELSVEDRAAQKARqgVRntlqgaltVLDPETMEpVPaDGKTiGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGV 425
Cdd:cd17636 160 GAIGGAGRPSPLVQ--VR--------ILDEDGRE-VP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 426 LHPDG---YAQIKDRskdIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYC 502
Cdd:cd17636 227 REPDGslsFVGPKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHC 303
|
330 340
....*....|....*....|....*
gi 1092482886 503 RERLAGFKRPKYYVFGE-LAKTATG 526
Cdd:cd17636 304 RARIASYKKPKSVEFADaLPRTAGG 328
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
31-534 |
1.99e-40 |
|
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: 151.85 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 31 VFGDDLAIVHGSIRQnwtetyhRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIY 110
Cdd:cd05919 4 FYAADRSVTYGQLHD-------GANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 111 CLQHGEAEFLLVDSEfaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIALNYT 190
Cdd:cd05919 77 IARDCEARLVVTSAD---------------------------------------------------------DIAYLLYS 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLP-LFHC----NGWCFAWTIAARGGVNVCLRkfDPKTCFDL 265
Cdd:cd05919 100 SGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAkMFFGyglgNSLWFPLAVGASAVLNPGWP--TAERVLAT 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAAL---ANAPAEMKAGIDHPVSAmvaGAAPPEAVLAR-MEQMGFHMVHVYGLTEVyGPSAVCAE 341
Cdd:cd05919 178 LARFRPTVLYGVPTFYANLldsCAGSPDALRSLRLCVSA---GEALPRGLGERwMEHFGGPILDGIGATEV-GHIFLSNR 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEWdelsvedRAAQKARQgvrntLQGA-LTVLDPETMEpVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHT 420
Cdd:cd05919 254 PGAW-------RLGSTGRP-----VPGYeIRLVDEEGHT-IPPG--EEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 421 GDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE---EE 497
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQEslaRD 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092482886 498 LDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05919 399 IHRHLLERLSAHKVPRRIAFvDELPRTATGKLQRFKLR 436
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
55-534 |
2.63e-40 |
|
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: 152.15 E-value: 2.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 55 RQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIY-CLQHGEAEFLLVDSEFAPHIPEI 133
Cdd:cd05929 8 RAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWkCGACPAYKSSRAPRAEACAIIEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 134 KKALPALKIIQVNDELGPkdvepfsdieYEGFLQSAEDLDNwVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNA-- 211
Cdd:cd05929 88 KAAALVCGLFTGGGALDG----------LEDYEAAEGGSPE-TPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNdt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 212 -IAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAE 290
Cdd:cd05929 157 lMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 291 MKAGIDhpVSAM---VAGAAP-PEAVLARMEQMGFHMVH-VYGLTEVYGPSAVCAEkpEWdelsvedraaQKARQGVRNT 365
Cdd:cd05929 237 VRNAYD--LSSLkrvIHAAAPcPPWVKEQWIDWGGPIIWeYYGGTEGQGLTIINGE--EW----------LTHPGSVGRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 366 LQGALTVLDpETMEPVPAdgKTIGELMFRGNiVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIIS 444
Cdd:cd05929 303 VLGKVHILD-EDGNEVPP--GEIGEVYFANG-PGFEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIIS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 445 GGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVE---LKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GEL 520
Cdd:cd05929 379 GGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQpapGADAGTALAEELIAFLRDRLSRYKCPRSIEFvAEL 458
|
490
....*....|....
gi 1092482886 521 AKTATGKIQKFELR 534
Cdd:cd05929 459 PRDDTGKLYRRLLR 472
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
183-534 |
5.53e-40 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 152.87 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIA-LNYTSGTTGNPKGVVYHHRgaalNAIAQSLE--------FDMPKRPVYLWT---LPLFHCngwcFAWTIAA---- 246
Cdd:PRK07059 204 DDVAfLQYTGGTTGVSKGATLLHR----NIVANVLQmeawlqpaFEKKPRPDQLNFvcaLPLYHI----FALTVCGllgm 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 247 -RGGVNVCLRkfDPKTCFDLIR---QERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GF 321
Cdd:PRK07059 276 rTGGRNILIP--NPRDIPGFIKelkKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMtGC 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 322 HMVHVYGLTEVyGPSAVCaEKPEWDELSvedraaqkarqgvrntlqGALTVldpetmePVPA--------DGK-----TI 388
Cdd:PRK07059 354 PITEGYGLSET-SPVATC-NPVDATEFS------------------GTIGL-------PLPStevsirddDGNdlplgEP 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 389 GELMFRGNIVMKGYLKNPAETGKS-FAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANV 467
Cdd:PRK07059 407 GEICIRGPQVMAGYWNRPDETAKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEV 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 468 AVVALADEKWGEVPVAFVELKDDAqVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:PRK07059 487 AAVGVPDEHSGEAVKLFVVKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFrTELPKTNVGKILRRELR 553
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
33-535 |
8.67e-39 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 148.45 E-value: 8.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCL 112
Cdd:TIGR02262 19 GGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYML 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAEFLLVDSEFAPHIPEIKKALPALK--IIQVNDELGPKDVEPFSDIEYEGFLQSAEDLDN---WVlpkdewdaial 187
Cdd:TIGR02262 99 EDSRARVVFVSGALLPVIKAALGKSPHLEhrVVVGRPEAGEVQLAELLATESEQFKPAATQADDpafWL----------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 nYTSGTTGNPKGVVYHHrgAALNAIAqslefDMPKRP--------VYLWTLPLFHCNGWCFAWTIAARGGVNVCL--RKF 257
Cdd:TIGR02262 168 -YSSGSTGMPKGVVHTH--SNPYWTA-----ELYARNtlgireddVCFSAAKLFFAYGLGNALTFPMSVGATTVLmgERP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 258 DPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARME-QMGFHMVHVYGLTEVYgpS 336
Cdd:TIGR02262 240 TPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQaRFGVDIVDGIGSTEML--H 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 337 AVCAEKPEwdelSVEDRAAQKARQGVRNTLQGaltvldpETMEPVpADGKtIGELMFRGNIVMKGYLKNPAETGKSFAGG 416
Cdd:TIGR02262 318 IFLSNLPG----DVRYGTSGKPVPGYRLRLVG-------DGGQDV-ADGE-PGELLISGPSSATMYWNNRAKSRDTFQGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 417 WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE 496
Cdd:TIGR02262 385 WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALET 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092482886 497 ELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRK 535
Cdd:TIGR02262 465 ELKEHVKDRLAPYKYPRWIVFvDDLPKTATGKIQRFKLRE 504
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-527 |
2.26e-38 |
|
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: 144.45 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHR--------GAALNAIAQSLEFDMPKR------PVYLWTLPLFHCNGWcFAWTIAARG 248
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQEdifrmlmgGADFGTGEFTPSEDAHKAaaaaagTVMFPAPPLMHGTGS-WTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 249 GVNVCL--RKFDPKTCFDLIRQERVGfycAAPVVHAALAnAP--AEMKAGIDHPVSAMVA----GAAPPEAVLARMEQMG 320
Cdd:cd05924 83 GQTVVLpdDRFDPEEVWRTIEKHKVT---SMTIVGDAMA-RPliDALRDAGPYDLSSLFAissgGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVhvygLTEVYGPSavcaekpEWDELSVEDRAAQKARQGVRNTLQGALTVLDPETmEPVPADGKTIGELMFRGNIVMk 400
Cdd:cd05924 159 PNIT----LVDAFGSS-------ETGFTGSGHSAGSGPETGPFTRANPDTVVLDDDG-RVVPPGSGGVGWIARRGHIPL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSF--AGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEK 476
Cdd:cd05924 226 GYYGDEAKTAETFpeVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDER 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 477 WGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGK 527
Cdd:cd05924 306 WGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFvDEIERSPAGK 357
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
19-536 |
2.88e-38 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 147.82 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 19 LTPIDFLVRAHEVFGDDLAIVHGSIRQNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVL 96
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTGKAVTygEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 97 LALN-VRLETEgLIYCLQHGEAEFLLVDsefAPHIPEIKK-ALPALKIIQVNDE--LGPKDVEPFSD-----IEYEGFLQ 167
Cdd:PLN02330 108 SGANpTALESE-IKKQAEAAGAKLIVTN---DTNYGKVKGlGLPVIVLGEEKIEgaVNWKELLEAADragdtSDNEEILQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 168 SaedldnwvlpkdewDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQ--SLEFDMPKRPVYLWTLPLFHC---NGWCFAw 242
Cdd:PLN02330 184 T--------------DLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfSVGPEMIGQVVTLGLIPFFHIygiTGICCA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 243 TIAARGGVnVCLRKFDPKTCFD-LIRQErVGFYCAAPVVHAALANAPAEMKAGIDH-PVSAMVAGAAP--PEAVLARMEQ 318
Cdd:PLN02330 249 TLRNKGKV-VVMSRFELRTFLNaLITQE-VSFAPIVPPIILNLVKNPIVEEFDLSKlKLQAIMTAAAPlaPELLTAFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 319 M-GFHMVHVYGLTEvygpsAVCAEKPEWDElsveDRAAQKARQGVRNTLQGALTV--LDPETMEPVPADgkTIGELMFRG 395
Cdd:PLN02330 327 FpGVQVQEAYGLTE-----HSCITLTHGDP----EKGHGIAKKNSVGFILPNLEVkfIDPDTGRSLPKN--TPGELCVRS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 396 NIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALAD 474
Cdd:PLN02330 396 QCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPD 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 475 EKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQ 536
Cdd:PLN02330 476 EEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDsIPKSLSGKIMRRLLKEK 538
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-530 |
1.97e-37 |
|
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: 144.39 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGV-LLAL-- 99
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpVLALps 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 100 NVRLETEGLIyclQHGEAEFLLVDSEFAPHIPEikkalpalkiiqvndELGPKDVEPFSDIEYegFLQSaedldnwvlpk 179
Cdd:cd05920 99 HRRSELSAFC---AHAEAVAYIVPDRHAGFDHR---------------ALARELAESIPEVAL--FLLS----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 180 dewdaialnytSGTTGNPKGVVYHHRGAALN--AIAQSLEFDmpKRPVYLWTLPLFH-----CNGwcfAWTIAARGGVNV 252
Cdd:cd05920 148 -----------GGTTGTPKLIPRTHNDYAYNvrASAEVCGLD--QDTVYLAVLPAAHnfplaCPG---VLGTLLAGGRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 253 CLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDhPVSAMVAGAAPPEAVLARM--EQMGFHMVHVYGLT 330
Cdd:cd05920 212 LAPDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLS-SLRLLQVGGARLSPALARRvpPVLGCTLQQVFGMA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 EvygpSAVCAEKPEwdelsveDRAAQKAR-QGVRNTLQGALTVLDPETmEPVPaDGkTIGELMFRGNIVMKGYLKNPAET 409
Cdd:cd05920 291 E----GLLNYTRLD-------DPDEVIIHtQGRPMSPDDEIRVVDEEG-NPVP-PG-EEGELLTRGPYTIRGYYRAPEHN 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK 488
Cdd:cd05920 357 ARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092482886 489 dDAQVSEEELDQYCRER-LAGFKRPKYYVF-GELAKTATGKIQK 530
Cdd:cd05920 437 -DPPPSAAQLRRFLRERgLAAYKLPDRIEFvDSLPLTAVGKIDK 479
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
25-542 |
2.08e-37 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 144.63 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 25 LVRAHEVFGDDLAI-VHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRL 103
Cdd:PRK07514 8 ALRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 104 ETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALpalkiiqvndelGPKDVEPFSDIEYEGFLQSAEDL--DNWVLPKDE 181
Cdd:PRK07514 88 TLAELDYFIGDAEPALVVCDPANFAWLSKIAAAA------------GAPHVETLDADGTGSLLEAAAAApdDFETVPRGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 WDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIA-ARGGVNVCLRKFDPK 260
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVAlLAGASMIFLPKFDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 261 TCFDLIRQERV-----GFYC---AAPVVHAALAnapAEMKAgidhpvsaMVAGAAP--PEAVLARMEQMGFHMVHVYGLT 330
Cdd:PRK07514 236 AVLALMPRATVmmgvpTFYTrllQEPRLTREAA---AHMRL--------FISGSAPllAETHREFQERTGHAILERYGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 EvygpSAVCAEKPewdeLSVEDRAAQkarqgVRNTLQG-ALTVLDPETMEPVPADGktIGELMFRGNIVMKGYLKNPAET 409
Cdd:PRK07514 305 E----TNMNTSNP----YDGERRAGT-----VGFPLPGvSLRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVL-------------YKHPavanvavvalade 475
Cdd:PRK07514 370 AEEFrADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIdelpgvvesavigVPHP------------- 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 476 KWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEALFS 542
Cdd:PRK07514 437 DFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFvDELPRNTMGKVQKNLLREQYADLFA 504
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
33-537 |
1.27e-36 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 142.86 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDD-LAIVHGSIRQNWTETYHRCRQMAAALRQNGA-DRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIY 110
Cdd:PRK13388 14 GDDtIAVRYGDRTWTWREVLAEAAARAAALIALADpDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 111 CLQHGEAEFLLVDSEFAPHIPEIKkaLPALKIIQVndelgpkdvepfSDIEYEGFLQSAEDLdNWVLPKDEWDAIALNYT 190
Cdd:PRK13388 94 DIRRADCQLLVTDAEHRPLLDGLD--LPGVRVLDV------------DTPAYAELVAAAGAL-TPHREVDAMDPFMLIFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLR-KFDPKTCFDLIRQE 269
Cdd:PRK13388 159 SGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPaKFSASGFLDDVRRY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYcaaPVVHAALAN--APAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEvyGPSAVCAEkpewde 347
Cdd:PRK13388 239 GATYF---NYVGKPLAYilATPERPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSE--GAVIVVRE------ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 lsvedraaqkarqgvRNTLQGAL-------TVLDPETMEPVP-----ADGK------TIGELMFR-GNIVMKGYLKNPAE 408
Cdd:PRK13388 308 ---------------PGTPPGSIgrgapgvAIYNPETLTECAvarfdAHGAllnadeAIGELVNTaGAGFFEGYYNNPEA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 409 TGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELK 488
Cdd:PRK13388 373 TAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLR 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 489 DDAQVSEEELDQYCRER--LAGFKRPKY-YVFGELAKTATGKIQKFELRKQA 537
Cdd:PRK13388 453 DGATFDPDAFAAFLAAQpdLGTKAWPRYvRIAADLPSTATNKVLKRELIAQG 504
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
130-537 |
6.19e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 141.11 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 130 IPEIKKALPALKIIQVndelgpkdvepfsdIEYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAAL 209
Cdd:PRK12492 169 VDKVKKMVPAYHLPQA--------------VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 210 N---AIAQSLEFDMPKRP-------VYLWTLPLFHCngwcFAWT-----IAARGGVNVCLRkfDPKTCFDLIRQE---RV 271
Cdd:PRK12492 235 NmlqVRACLSQLGPDGQPlmkegqeVMIAPLPLYHI----YAFTancmcMMVSGNHNVLIT--NPRDIPGFIKELgkwRF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 272 GFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMVHVYGLTEVygpSAVCAEKPEwdelsv 350
Cdd:PRK12492 309 SALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLtGCTIVEGYGLTET---SPVASTNPY------ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 351 edraAQKARQG-----VRNTlqgALTVLDPETMEpVPADGKtiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLG 424
Cdd:PRK12492 380 ----GELARLGtvgipVPGT---ALKVIDDDGNE-LPLGER--GELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 425 VLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVeLKDDAQVSEEELDQYCRE 504
Cdd:PRK12492 450 VIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFV-VARDPGLSVEELKAYCKE 528
|
410 420 430
....*....|....*....|....*....|....
gi 1092482886 505 RLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQA 537
Cdd:PRK12492 529 NFTGYKVPKHIVLRDsLPMTPVGKILRRELRDIA 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
46-456 |
9.74e-36 |
|
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: 140.96 E-value: 9.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 46 NWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSE 125
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVENQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 F-APHIPEIKKALPALK-IIQVNDELGPKDVEPFSdieYEGFLQSAEDLdnwvlPKDEWDAI----------ALNYTSGT 193
Cdd:cd05933 90 KqLQKILQIQDKLPHLKaIIQYKEPLKEKEPNLYS---WDEFMELGRSI-----PDEQLDAIissqkpnqccTLIYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPV-------YL------------WTlPLFHCNGWCFAWTIAARGGVNVCL 254
Cdd:cd05933 162 TGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLplshiaaqildiWL-PIKVGGQVYFAQPDALKGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 255 RKFDPKTCFDLIR-----QERV--GFYCAAPVVHAALANApaeMKAGIDHPVSAMVAGAAPP-------EAVLARMEQM- 319
Cdd:cd05933 241 REVRPTAFMGVPRvwekiQEKMkaVGAKSGTLKRKIASWA---KGVGLETNLKLMGGESPSPlfyrlakKLVFKKVRKAl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 320 GFHMVH--------------------------VYGLTEVYGPSAVCAEKpewdelSVEDRAAQKARQGVRNTLQgaltvl 373
Cdd:cd05933 318 GLDRCQkfftgaapisretlefflslnipimeLYGMSETSGPHTISNPQ------AYRLLSCGKALPGCKTKIH------ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 374 DPEtmepvpADGktIGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIII-SGGENISS 451
Cdd:cd05933 386 NPD------ADG--IGEICFWGRHVFMGYLNMEDKTEEAIdEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPP 457
|
....*
gi 1092482886 452 IEVED 456
Cdd:cd05933 458 VPIED 462
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
22-540 |
2.85e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 139.11 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 22 IDFLVRAHEvfgDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNV 101
Cdd:PRK06164 16 LDAHARARP---DAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 102 RLETEGLIYCLQHGEAEFLLVDS-----EFAPHIPEIKK-ALPALKIIQVNDELGPK--DVEPFSDIEYEGFLQSAEDLD 173
Cdd:PRK06164 93 RYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVPPdALPPLRAIAVVDDAADAtpAPAPGARVQLFALPDPAPPAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 174 NWVLPKDEwDAIALNYT-SGTTGNPKGVVyhHRGAAL----NAIAQSLEFDmpKRPVYLWTLPLfhCNGWCFAWTIA--A 246
Cdd:PRK06164 173 AGERAADP-DAGALLFTtSGTTSGPKLVL--HRQATLlrhaRAIARAYGYD--PGAVLLAALPF--CGVFGFSTLLGalA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 247 RGGVNVCLRKFDPKTCFDLIRQERVgfycaapvVHAALANapaEM------KAGIDHPVSAM----VAGAAPPEA-VLAR 315
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRV--------THTFGND---EMlrrildTAGERADFPSArlfgFASFAPALGeLAAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 316 MEQMGFHMVHVYGLTEVYgpsAVCAEKPEWDELSVEDRAAqkarqGVRNTLQGALTVLDPETMEPVPaDGKtIGELMFRG 395
Cdd:PRK06164 315 ARARGVPLTGLYGSSEVQ---ALVALQPATDPVSVRIEGG-----GRPASPEARVRARDPQDGALLP-DGE-SGEIEIRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 396 NIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALAD 474
Cdd:PRK06164 385 PSLMRGYLDNPDATARALtDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALP-GVAAAQVVGAT 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 475 EKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRP-KYYVFGELAKTATG---KIQKFELRKQAEAL 540
Cdd:PRK06164 464 RDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPaRVQVVEAFPVTESAngaKIQKHRLREMAQAR 533
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
57-534 |
4.19e-35 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 138.82 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 57 MAAALRQNGADR-GTTVATLLHNTPAMVEAGFGVPMSGGVLLALN-------VRLETEGLIYCLQHGEaefllvdsefap 128
Cdd:PLN02574 79 MAAGLYHVMGVRqGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpssslgeIKKRVVDCSVGLAFTS------------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 129 hiPEIKKALPALKI--IQVNDELGPKDVEPFSDIEYEGFLQSAEDLDNWVLPKDewDAIALNYTSGTTGNPKGVVYHHRg 206
Cdd:PLN02574 147 --PENVEKLSPLGVpvIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPVIKQD--DVAAIMYSSGTTGASKGVVLTHR- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 207 aalNAIA--------QSLEFDMPKRP-VYLWTLPLFHCNGWC-FAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCA 276
Cdd:PLN02574 222 ---NLIAmvelfvrfEASQYEYPGSDnVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 277 APVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLarMEQMGFHMVHV-----YGLTEvygpsavcaekpewdELSVE 351
Cdd:PLN02574 299 VPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKF--IQDFVQTLPHVdfiqgYGMTE---------------STAVG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 352 DRAAQkARQGVRNTLQGALT------VLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLG 424
Cdd:PLN02574 362 TRGFN-TEKLSKYSSVGLLApnmqakVVDWSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATQSTIdKDGWLRTGDIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 425 VLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRE 504
Cdd:PLN02574 439 YFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAK 518
|
490 500 510
....*....|....*....|....*....|.
gi 1092482886 505 RLAGFKRPKYYVFGE-LAKTATGKIQKFELR 534
Cdd:PLN02574 519 QVAPYKKVRKVVFVQsIPKSPAGKILRRELK 549
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
130-537 |
1.59e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 137.20 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 130 IPEIKKALPALKIiqvndelgPKDVePFSDIEYEGFLQSAEDLDnwvlPKDEwDAIALNYTSGTTGNPKGVVYHHRGAAL 209
Cdd:PRK05677 169 VKHVKKMVPAYHL--------PQAV-KFNDALAKGAGQPVTEAN----PQAD-DVAVLQYTGGTTGVAKGAMLTHRNLVA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 210 NA------IAQSLEfdmPKRPVYLWTLPLFHCNGW---CFAWTIAarGGVNVCL---RKFdPKTCFDLIRQERVGFyCAA 277
Cdd:PRK05677 235 NMlqcralMGSNLN---EGCEILIAPLPLYHIYAFtfhCMAMMLI--GNHNILIsnpRDL-PAMVKELGKWKFSGF-VGL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 278 PVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMVHVYGLTEVygpSAVCAEKPEwdelsvedRAAQ 356
Cdd:PRK05677 308 NTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTET---SPVVSVNPS--------QAIQ 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 357 KARQG--VRNTLqgaLTVLDPETMEpVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQ 433
Cdd:PRK05677 377 VGTIGipVPSTL---CKVIDDDGNE-LPLG--EVGELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 434 IKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPK 513
Cdd:PRK05677 451 IVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPK 530
|
410 420
....*....|....*....|....*
gi 1092482886 514 YYVF-GELAKTATGKIQKFELRKQA 537
Cdd:PRK05677 531 AVEFrDELPTTNVGKILRRELRDEE 555
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
183-534 |
3.33e-34 |
|
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: 134.53 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRgaALNAIAQSLEFDMPK-RP--VYLWTLPLFHCNGW----CFAWTIAARGgvnVCLR 255
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHR--DPLASADRYAVNVLRlREddRFVGSPPLAFTFGLggvlLFPFGVGASG---VLLE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARM-EQMGFHMVHVYGLTEVYG 334
Cdd:cd05958 173 EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWkEATGIPIIDGIGSTEMFH 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 335 PSavcaekpewdeLSVEDRAAQKARQGvrNTLQG-ALTVLDPETmEPVPADgkTIGELMFRGNIVMKgYLKNPAETgKSF 413
Cdd:cd05958 253 IF-----------ISARPGDARPGATG--KPVPGyEAKVVDDEG-NPVPDG--TIGRLAVRGPTGCR-YLADKRQR-TYV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQV 493
Cdd:cd05958 315 QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP 394
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1092482886 494 SE---EELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05958 395 GPvlaRELQDHAKAHIAPYKYPRAIEFvTELPRTATGKLQRFALR 439
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
58-534 |
1.55e-33 |
|
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: 132.63 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 58 AAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAphipeikkal 137
Cdd:cd05969 14 ANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELY---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 138 palkiiqvnDELGPKDvepfsdieyeGFLqsaedldnwvlpkdewdaiaLNYTSGTTGNPKGVVYHHRGAALNAIAQSLE 217
Cdd:cd05969 84 ---------ERTDPED----------PTL--------------------LHYTSGTTGTPKGVLHVHDAMIFYYFTGKYV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 218 FDMPKRPVYlwtlplfhcngWCFA------------WTIAARGGVNVCLR-KFDPKTCFDLIRQERVGFYCAAPVVHAAL 284
Cdd:cd05969 125 LDLHPDDIY-----------WCTAdpgwvtgtvygiWAPWLNGVTNVVYEgRFDAESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 285 ANAPAEMKAGID-HPVSAMVAGAAP--PEAVLARMEQMGFHMVHVYGLTEVyGPSAVCaekpewdelsveDRAAQKARQG 361
Cdd:cd05969 194 MKEGDELARKYDlSSLRFIHSVGEPlnPEAIRWGMEVFGVPIHDTWWQTET-GSIMIA------------NYPCMPIKPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 362 -VRNTLQGALTVLDPETMEPVPADgkTIGELMFRGNI--VMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRS 438
Cdd:cd05969 261 sMGKPLPGVKAAVVDENGNELPPG--TKGILALKPGWpsMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 439 KDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYY 515
Cdd:cd05969 339 DDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREI 418
|
490 500
....*....|....*....|
gi 1092482886 516 VFGE-LAKTATGKIQKFELR 534
Cdd:cd05969 419 EFVDnLPKTRSGKIMRRVLK 438
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
34-533 |
2.94e-33 |
|
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: 131.88 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEfaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIALNYTSGT 193
Cdd:cd05930 82 DSGAKLVLTDPD---------------------------------------------------------DLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYL-WTLPLFHCNGWCFAWTIAArGGVNVCLRK---FDPKTCFDLIRQE 269
Cdd:cd05930 105 TGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLqFTSFSFDVSVWEIFGALLA-GATLVVLPEevrKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAPVVHAALANAPAEmkAGIDHPVSAMVAGAAPPEAVLARMEQMGF--HMVHVYGLTEVYGPSAVCaekpewde 347
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELEL--AALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEATVDATYY-------- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 lSVEDRAAQKAR----QGVRNTlqgALTVLDPEtMEPVPaDGKTiGELMFRGNIVMKGYLKNPAETGKSF------AGGW 417
Cdd:cd05930 254 -RVPPDDEEDGRvpigRPIPNT---RVYVLDEN-LRPVP-PGVP-GELYIGGAGLARGYLNRPELTAERFvpnpfgPGER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 418 FH-TGDLGVLHPDG---YA-----QIKdrskdiiISG-----GEnissieVEDVLYKHPAVANVAVVALADEKWGEVPVA 483
Cdd:cd05930 327 MYrTGDLVRWLPDGnleFLgriddQVK-------IRGyrielGE------IEAALLAHPGVREAAVVAREDGDGEKRLVA 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 484 FVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFEL 533
Cdd:cd05930 394 YVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVlDALPLTPNGKVDRKAL 444
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
48-534 |
8.90e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 131.28 E-value: 8.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 48 TETYHRCRQMAAALRQ----NGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVD 123
Cdd:PRK13390 24 QVSYRQLDDDSAALARvlydAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 SEFAPHIPEIKKALPalkiiqVNDELGPKdVEPFSDieYEGFLQSAEDldnwVLPKDEWDAIALnYTSGTTGNPKGV--- 200
Cdd:PRK13390 104 AALDGLAAKVGADLP------LRLSFGGE-IDGFGS--FEAALAGAGP----RLTEQPCGAVML-YSSGTTGFPKGIqpd 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 201 ----VYHHRGAALNAIAQSLeFDMPKRPVYLWTLPLFHCNG--WCfaWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFY 274
Cdd:PRK13390 170 lpgrDVDAPGDPIVAIARAF-YDISESDIYYSSAPIYHAAPlrWC--SMVHALGGTVVLAKRFDAQATLGHVERYRITVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 275 CAAPVVHAALANAPAEMKAGIDHP-VSAMVAGAAP-PEAVL-ARMEQMGFHMVHVYGLTEVYGPSAVcaEKPEWdelsve 351
Cdd:PRK13390 247 QMVPTMFVRLLKLDADVRTRYDVSsLRAVIHAAAPcPVDVKhAMIDWLGPIVYEYYSSTEAHGMTFI--DSPDW------ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 352 draaqKARQG-VRNTLQGALTVLDPETMEpVPAdGKtIGELMFRGNIVMKGYLKNPAETGKSFAGG---WFHTGDLGVLH 427
Cdd:PRK13390 319 -----LAHPGsVGRSVLGDLHICDDDGNE-LPA-GR-IGTVYFERDRLPFRYLNDPEKTAAAQHPAhpfWTTVGDLGSVD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 428 PDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRE 504
Cdd:PRK13390 391 EDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDElarELIDYTRS 470
|
490 500 510
....*....|....*....|....*....|.
gi 1092482886 505 RLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:PRK13390 471 RIAHYKAPRSVEFvDELPRTPTGKLVKGLLR 501
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
181-539 |
1.05e-32 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 131.92 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 181 EWDAIA-LNYTSGTTGNPKGVVYHHRGAALN--------AIAQSLEfdmPKRPVYLWTLPLFH-----CNGWCFawtiAA 246
Cdd:PRK08751 206 EPDDIAfLQYTGGTTGVAKGAMLTHRNLVANmqqahqwlAGTGKLE---EGCEVVITALPLYHifaltANGLVF----MK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 247 RGGVNVCLRK-FDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GFHMV 324
Cdd:PRK08751 279 IGGCNHLISNpRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVtGLTLV 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 325 HVYGLTEVyGPSAvCAEKPEWDELSvedraaqkarqgvrntlqGALTVLDPETMEPVPADGKT------IGELMFRGNIV 398
Cdd:PRK08751 359 EAYGLTET-SPAA-CINPLTLKEYN------------------GSIGLPIPSTDACIKDDAGTvlaigeIGELCIKGPQV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 399 MKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKW 477
Cdd:PRK08751 419 MKGYWKRPEETAKVMdADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKS 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 478 GEVpVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEA 539
Cdd:PRK08751 499 GEI-VKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFrKELPKTNVGKILRRELRDAAKA 560
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
34-538 |
2.32e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 129.90 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNgADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPEIKkaLPALKIIQVNdelgpKDVEPFSDIEYEGflqsaEDLDNwvlpkdewDAIALNYTSGT 193
Cdd:PRK07638 95 ISNADMIVTERYKLNDLPDEE--GRVIEIDEWK-----RMIEKYLPTYAPI-----ENVQN--------APFYMGFTSGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNgWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQERVG 272
Cdd:PRK07638 155 TGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL-FLYGAISTLYVGQTVHLmRKFIPNQVLDKLETENIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 273 FYCAAPvvhaALANAPAEMKAGIDHPVSAMVAGAA-PPEAVlarmEQMGFHMVHVyGLTEVYGPSavcaekpewdELS-- 349
Cdd:PRK07638 234 VMYTVP----TMLESLYKENRVIENKMKIISSGAKwEAEAK----EKIKNIFPYA-KLYEFYGAS----------ELSfv 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 350 ---VEDRAAQKARQGVRNtlqgaltvLDPETMEPVPADGKT-----IGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTG 421
Cdd:PRK07638 295 talVDEESERRPNSVGRP--------FHNVQVRICNEAGEEvqkgeIGTVYVKSPQFFMGYIIGGVLARELNADGWMTVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQvseeELDQY 501
Cdd:PRK07638 367 DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQ----QLKSF 442
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092482886 502 CRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAE 538
Cdd:PRK07638 443 CLQRLSSFKIPKEWHFvDEIPYTNSGKIARMEAKSWIE 480
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
56-534 |
6.51e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 127.94 E-value: 6.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 56 QMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGG----VLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIp 131
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 132 eiKKALPALKIiqvndelgpkdvePFSDIEYEGFLQSAEDLDNWVLPKDewDAIALNYTSGTTGNPKGVVYHHRG--AAL 209
Cdd:cd05922 84 --RDALPASPD-------------PGTVLDADGIRAARASAPAHEVSHE--DLALLLYTSGSTGSPKLVRLSHQNllANA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 210 NAIAQSLEFDmpKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFD-PKTCFDLIRQERVGFYCAAPVVHAALAN-- 286
Cdd:cd05922 147 RSIAEYLGIT--ADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVlDDAFWEDLREHGATGLAGVPSTYAMLTRlg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 287 -APAEMkagidhPVSAMV--AGAAPPEAVLARMEQM--GFHMVHVYGLTEV-----YGPSAVCAEKPEwdelsvedrAAQ 356
Cdd:cd05922 225 fDPAKL------PSLRYLtqAGGRLPQETIARLRELlpGAQVYVMYGQTEAtrrmtYLPPERILEKPG---------SIG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 357 KARQGvrntlqGALTVLDPETMEPVPadgKTIGELMFRGNIVMKGYLKNPAETGK-SFAGGWFHTGDLGVLHPDGYAQIK 435
Cdd:cd05922 290 LAIPG------GEFEILDDDGTPTPP---GEPGEIVHRGPNVMKGYWNDPPYRRKeGRGGGVLHTGDLARRDEDGFLFIV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 436 DRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKwGEVPVAFVELKDdaQVSEEELDQYCRERLAGFKRPKYY 515
Cdd:cd05922 361 GRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPD--KIDPKDVLRSLAERLPPYKVPATV 437
|
490 500
....*....|....*....|
gi 1092482886 516 VF-GELAKTATGKIQKFELR 534
Cdd:cd05922 438 RVvDELPLTASGKVDYAALR 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
175-539 |
6.53e-31 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 126.71 E-value: 6.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 175 WVLPKDEWDAIA-LNYTSGTTGNPKGVVYHHRGAALN---AIAQSLEFDMPKRPVYLWTLPLFHCngwcFAWTIAA---- 246
Cdd:PRK08974 198 YVKPELVPEDLAfLQYTGGTTGVAKGAMLTHRNMLANleqAKAAYGPLLHPGKELVVTALPLYHI----FALTVNCllfi 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 247 -RGGVNVCLRkfDPKTCFDLIRQERVGFYCAAPVVHA---ALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM-GF 321
Cdd:PRK08974 274 eLGGQNLLIT--NPRDIPGFVKELKKYPFTAITGVNTlfnALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLtGQ 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 322 HMVHVYGLTEVygpSAVCAEKP-EWDELSvedraaqkarqgvrntlqGALTVLDPET-MEPVPADGKTI-----GELMFR 394
Cdd:PRK08974 352 YLLEGYGLTEC---SPLVSVNPyDLDYYS------------------GSIGLPVPSTeIKLVDDDGNEVppgepGELWVK 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 395 GNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALAD 474
Cdd:PRK08974 411 GPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPS 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 475 EKWGEVPVAFVeLKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAEA 539
Cdd:PRK08974 491 EVSGEAVKIFV-VKKDPSLTEEELITHCRRHLTGYKVPKLVEFrDELPKSNVGKILRRELRDEARA 555
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
40-531 |
8.19e-31 |
|
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: 124.86 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 40 HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEF 119
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 120 LLVdsefaphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpKDEWDAIALNYTSGTTGNPKG 199
Cdd:cd05914 83 IFV--------------------------------------------------------SDEDDVALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 200 VVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPV 279
Cdd:cd05914 107 VMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 280 VHAAL---------ANAPAEMKAGIDHPVSA---------------------MVAGAAP-PEAVLARMEQMGFHMVHVYG 328
Cdd:cd05914 187 PLVIEkifkmdiipKLTLKKFKFKLAKKINNrkirklafkkvheafggnikeFVIGGAKiNPDVEEFLRTIGFPYTIGYG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 329 LTEVyGPsAVCAEKPEWDELSvedrAAQKARQGVrntlQGALTVLDPETMEpvpadgktiGELMFRGNIVMKGYLKNPAE 408
Cdd:cd05914 267 MTET-AP-IISYSPPNRIRLG----SAGKVIDGV----EVRIDSPDPATGE---------GEIIVRGPNVMKGYYKNPEA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 409 TGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISG-GENISSIEVEDVLYKHPAVANVAVVALADEkwgEVPVAFVE 486
Cdd:cd05914 328 TAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVVQEKK---LVALAYID 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 487 lKDDAQVS------------EEELDQYCRE-----RLAGFKrpkyYVFGELAKTATGKIQKF 531
Cdd:cd05914 405 -PDFLDVKalkqrniidaikWEVRDKVNQKvpnykKISKVK----IVKEEFEKTPKGKIKRF 461
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
47-537 |
1.78e-29 |
|
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: 120.92 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDsef 126
Cdd:cd05940 6 YAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 aphipeikkalPALKIiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewdaialnYTSGTTGNPK-GVVYHHR 205
Cdd:cd05940 83 -----------AALYI----------------------------------------------YTSGTTGLPKaAIISHRR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAIAQSLEFDMPKRPVYLwTLPLFHCNGWCFAWTIAARGGVNVCLR-KFDPKTCFDLIRQER------VGFYCAAp 278
Cdd:cd05940 106 AWRGGAFFAGSGGALPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRkKFSASNFWDDIRKYQatifqyIGELCRY- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 279 vvhaaLANAPAEMKAGiDHPVSAMVAGAAPPEaVLARMeQMGFHMVHVYgltEVYGPS-AVCAekpeWDELSVEDRAAQK 357
Cdd:cd05940 184 -----LLNQPPKPTER-KHKVRMIFGNGLRPD-IWEEF-KERFGVPRIA---EFYAATeGNSG----FINFFGKPGAIGR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 358 ARQGVRNTLQGALTVLDPETMEPV-PADGKTI-------GELMFRGNIV--MKGYLKNPAETGK----SFAGG--WFHTG 421
Cdd:cd05940 249 NPSLLRKVAPLALVKYDLESGEPIrDAEGRCIkvprgepGLLISRINPLepFDGYTDPAATEKKilrdVFKKGdaWFNTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVvaladekWG-EVP-------VAFVELKDDAQV 493
Cdd:cd05940 329 DLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV-------YGvQVPgtdgragMAAIVLQPNEEF 401
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYY-VFGELAKTATGKIQKFELRKQA 537
Cdd:cd05940 402 DLSALAAHLEKNLPGYARPLFLrLQPEMEITGTFKQQKVDLRNEG 446
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
44-462 |
8.83e-29 |
|
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: 119.00 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 44 RQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVD 123
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 SefaphipeikkalpalkiiqvndelGPKDVEpfsdieyegflqsaedldnwvlpkdewdaiALNYTSGTTGNPKGVVYH 203
Cdd:cd17640 85 N-------------------------DSDDLA------------------------------TIIYTSGTTGNPKGVMLT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 204 HRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVC---------LRKFDPKTcfdLIRQERV--G 272
Cdd:cd17640 110 HANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYtsirtlkddLKRVKPHY---IVSVPRLweS 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 273 FYCAapvVHAALANAPA-------------EMKAGIDHpvsamvAGAAPPEAVLArMEQMGFHMVHVYGLTEVYGPSAvc 339
Cdd:cd17640 187 LYSG---IQKQVSKSSPikqflflfflsggIFKFGISG------GGALPPHVDTF-FEAIGIEVLNGYGLTETSPVVS-- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 aekpewdelsvedraAQKARQGVRNTL-----QGALTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKSF- 413
Cdd:cd17640 255 ---------------ARRLKCNVRGSVgrplpGTEIKIVDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVLd 317
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 AGGWFHTGDLGVLHPDGYAQIKDRSKD-IIISGGENISSIEVEDVLYKHP 462
Cdd:cd17640 318 SDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSP 367
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
183-530 |
9.63e-29 |
|
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: 116.98 E-value: 9.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNAI-AQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKF-DPK 260
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENtTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 261 TCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGF-HMVHVYGLTEVygpSAVC 339
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLtNTAQVYGLSET---GTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AEKPEWDELSVedraaqkarQGVRNTLQGALTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKSFAGGWFH 419
Cdd:cd17635 159 CLPTDDDSIEI---------NAVGRPYPGVDVYLAATDGIAGPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 420 TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFV---ELKDDAQVSEE 496
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVvasAELDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|....*
gi 1092482886 497 ELDqyCRERLAGFKRPKYYVFGE-LAKTATGKIQK 530
Cdd:cd17635 308 KHT--IRRELEPYARPSTIVIVTdIPRTQSGKVKR 340
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
179-535 |
9.80e-29 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 119.94 E-value: 9.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 179 KDEWDAIALNyTSGTTGNPKGVVYHHRgaalNAIAQsleFDMPKRPVY----------LWTLPLFHCNGWCFAWTIAARG 248
Cdd:cd17642 182 RDEQVALIMN-SSGSTGLPKGVQLTHK----NIVAR---FSHARDPIFgnqiipdtaiLTVIPFHHGFGMFTTLGYLICG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 249 GVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHpVSAMVAGAAPPEAVLARMEQMGFHMVHV-- 326
Cdd:cd17642 254 FRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSN-LHEIASGGAPLSKEVGEAVAKRFKLPGIrq 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 327 -YGLTEVygPSAVCAEkPEWDelsVEDRAAQKARQGVrntlqgALTVLDPETmepvpadGKTIG-----ELMFRGNIVMK 400
Cdd:cd17642 333 gYGLTET--TSAILIT-PEGD---DKPGAVGKVVPFF------YAKVVDLDT-------GKTLGpnergELCVKGPMIMK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGE 479
Cdd:cd17642 394 GYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGE 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 480 VPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYV--FGELAKTATGKIQKFELRK 535
Cdd:cd17642 474 LPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRGGVkfVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-535 |
1.46e-28 |
|
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: 118.00 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 50 TYHRCRQM----AAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALnvrletegliyclqhgeaeFllvdSE 125
Cdd:cd05973 2 TFGELRALsarfANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPL-------------------F----TA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 FAPHIPEIKKALPALKIIQVndelgpkdvepfsdieyegflqsaeDLDNwvLPKDEWDAIALNYTSGTTGNPKGVVYHHR 205
Cdd:cd05973 59 FGPKAIEHRLRTSGARLVVT-------------------------DAAN--RHKLDSDPFVMMFTSGTTGLPKGVPVPLR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 gaALNAIAQSLEFDMPKRP--VYlWTL--PlfhcnGWCFAWTIAARG----GVNVCLRK--FDPKTCFDLIRQERVGFYC 275
Cdd:cd05973 112 --ALAAFGAYLRDAVDLRPedSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSVESTWRVIERLGVTNLA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 276 AAPVVHAALANAPAEMKAGIDHPVSAMVAGAAP--PEAVLARMEQMGFHMVHVYGLTEVYGPSAvcaeKPEWDELSVEDR 353
Cdd:cd05973 184 GSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPltPEVIRWFDAALGVPIHDHYGQTELGMVLA----NHHALEHPVHAG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 354 AAQKARQGVRntlqgaLTVLDPETMEPVPadgktiGELmfrGNIVM----------KGYLKNPAetgKSFAGGWFHTGDL 423
Cdd:cd05973 260 SAGRAMPGWR------VAVLDDDGDELGP------GEP---GRLAIdiansplmwfRGYQLPDT---PAIDGGYYLTGDT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 424 GVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQ 500
Cdd:cd05973 322 VEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQL 401
|
490 500 510
....*....|....*....|....*....|....*.
gi 1092482886 501 YCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRK 535
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFvDELPKTPSGKIQRFLLRR 437
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
47-536 |
1.67e-28 |
|
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: 119.27 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGAdRGTTVATLLHNTPAMVEAGFG--------VPMSGGVLLALNVRLETegliyCLQHGEAE 118
Cdd:cd05931 27 YAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGclyagaiaVPLPPPTPGRHAERLAA-----ILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 119 FLLVDSEFAPHIPEIKKALPALKIIQVndelgpkdvePFSDieyegfLQSAEDLDNWVLPKDEWDAIA-LNYTSGTTGNP 197
Cdd:cd05931 101 VVLTTAAALAAVRAFAASRPAAGTPRL----------LVVD------LLPDTSAADWPPPSPDPDDIAyLQYTSGSTGTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 198 KGVVYHHRG--AALNAIAQSLEFDmPKRPVYLWtLPLFHCNGWCFAWTIAARGGVNVCLrkFDPktcFDLIRQ------- 268
Cdd:cd05931 165 KGVVVTHRNllANVRQIRRAYGLD-PGDVVVSW-LPLYHDMGLIGGLLTPLYSGGPSVL--MSP---AAFLRRplrwlrl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 269 --ERVGFYCAAP------VVHAAlanaPAEMKAGID-HPVSAMVAGAAP--PEAV---LARMEQMGF-HMVHV--YGLTE 331
Cdd:cd05931 238 isRYRATISAAPnfaydlCVRRV----RDEDLEGLDlSSWRVALNGAEPvrPATLrrfAEAFAPFGFrPEAFRpsYGLAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 332 --VYGPSAVCAEKP---EWDELSVEDRAAQKARQGVRNT-------LQGALTVL--DPETMEPVPADgkTIGELMFRGNI 397
Cdd:cd05931 314 atLFVSGGPPGTGPvvlRVDRDALAGRAVAVAADDPAARelvscgrPLPDQEVRivDPETGRELPDG--EVGEIWVRGPS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 398 VMKGYLKNPAETGKSF-------AGGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVV 470
Cdd:cd05931 392 VASGYWGRPEATAETFgalaatdEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 471 A--LADEKWGEVPVAFVELKDDAQVSEE-ELDQYCRERLA---G-------FKRPkyyvfGELAKTATGKIQKFELRKQ 536
Cdd:cd05931 471 AafSVPDDGEERLVVVAEVERGADPADLaAIAAAIRAAVArehGvapadvvLVRP-----GSIPRTSSGKIQRRACRAA 544
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
19-536 |
1.98e-28 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 118.73 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 19 LTPIDFLVRAHEvfGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLA 98
Cdd:TIGR03098 2 LHHLLEDAAARL--PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 99 LNVRLETEGLIYCLQHGEAEFLLVDSEfapHIPEIKKALPAL----KIIQVNDELGPKDVEPFSDIEYEGFLQSAEDLDN 174
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLLVTSSE---RLDLLHPALPGChdlrTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 175 WVLPKDEwDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL 254
Cdd:TIGR03098 157 PHPVIDS-DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 255 RKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGiDHPVSAMVAGAAPPEAVLARMEQMG-----FHMvhvYGL 329
Cdd:TIGR03098 236 DYLLPRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAA-PSLRYLTNSGGAMPRATLSRLRSFLpnarlFLM---YGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 330 TEVYGPSAVcaeKPEwdELsveDRAAQKARQGVRNTlqgALTVLDPETMEPVPADgktIGELMFRGNIVMKGYLKNPAET 409
Cdd:TIGR03098 312 TEAFRSTYL---PPE--EV---DRRPDSIGKAIPNA---EVLVLREDGSECAPGE---EGELVHRGALVAMGYWNDPEKT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSF------------AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKW 477
Cdd:TIGR03098 378 AERFrplppfpgelhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTL 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 478 GEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQ 536
Cdd:TIGR03098 458 GQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQaLPRNANGKIDRKALAKE 517
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
23-537 |
2.62e-28 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 119.21 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 23 DFLVRAHEVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVR 102
Cdd:PRK08279 41 DVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 103 LETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDELGPKDVEPFSDIEYEGFLQSAEDLD--NWVLPKD 180
Cdd:PRK08279 121 QRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPAsrSGVTAKD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 181 ewdaIALN-YTSGTTGNPKGVVY-HHRG-AALNAIAQSLEFDmPKRPVYLwTLPLFHCNGWCFAWTIAARGGVNVCL-RK 256
Cdd:PRK08279 201 ----TAFYiYTSGTTGLPKAAVMsHMRWlKAMGGFGGLLRLT-PDDVLYC-CLPLYHNTGGTVAWSSVLAAGATLALrRK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 257 FDPKTCFDLIRQER------VGFYCaapvvhAALANAPAEMKAGiDHPVSAMVAGAAPPEaVLARMEQMgFHMVHV---Y 327
Cdd:PRK08279 275 FSASRFWDDVRRYRatafqyIGELC------RYLLNQPPKPTDR-DHRLRLMIGNGLRPD-IWDEFQQR-FGIPRIlefY 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 328 GLTE-------VYGPSAVCAEKPEWDElsvedraaqkarqgvrntLQGALTVLDPETMEPV-PADGKTI-------GELM 392
Cdd:PRK08279 346 AASEgnvgfinVFNFDGTVGRVPLWLA------------------HPYAIVKYDVDTGEPVrDADGRCIkvkpgevGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 393 frGNIVMK----GYLkNPAETGKS-----FAGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKH 461
Cdd:PRK08279 408 --GRITDRgpfdGYT-DPEASEKKilrdvFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGF 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 462 PAVANVAVvaladekWG-EVP-------VAFVELKDDAQVSEEELDQYCRERLAGFKRPkyyVF----GELAKTATGKIQ 529
Cdd:PRK08279 485 PGVEEAVV-------YGvEVPgtdgragMAAIVLADGAEFDLAALAAHLYERLPAYAVP---LFvrlvPELETTGTFKYR 554
|
....*...
gi 1092482886 530 KFELRKQA 537
Cdd:PRK08279 555 KVDLRKEG 562
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
30-515 |
1.86e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 114.97 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 30 EVFGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLI 109
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 110 YCLQHGEAEFLLVDSEFaphipeikKALPALKIIQVNDELGPkdvepfsdieyegflqsaedldnwvlPKDEWDAIAL-- 187
Cdd:PRK09029 94 ELLPSLTLDFALVLEGE--------NTFSALTSLHLQLVEGA--------------------------HAVAWQPQRLat 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 -NYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVnvclrkfdpktcfdLI 266
Cdd:PRK09029 140 mTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQGIVWRWLYAGAT--------------LV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFY-CAAPVVHAALAnaPAEMKAGIDHPVSAMV------AGAAPPEAVLARMEQMGFHMVHVYGLTEVygPSAVC 339
Cdd:PRK09029 206 VRDKQPLEqALAGCTHASLV--PTQLWRLLDNRSEPLSlkavllGGAAIPVELTEQAEQQGIRCWCGYGLTEM--ASTVC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AEKPEwdelsvedraaqkARQGVRNTLQG-ALTVLDpetmepvpadgktiGELMFRGNIVMKGYLKNpaetGKSF----A 414
Cdd:PRK09029 282 AKRAD-------------GLAGVGSPLPGrEVKLVD--------------GEIWLRGASLALGYWRQ----GQLVplvnD 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 415 GGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVs 494
Cdd:PRK09029 331 EGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAV- 408
|
490 500
....*....|....*....|..
gi 1092482886 495 eEELDQYCRERLAGFKRP-KYY 515
Cdd:PRK09029 409 -VNLAEWLQDKLARFQQPvAYY 429
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
43-536 |
2.77e-27 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 115.64 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 43 IRQNWTETYHRCRQMAAALRQN-GADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLL 121
Cdd:cd05928 40 VKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 122 VDSEFAPHIPEIKKALPALKIIQVndeLGPKDVEPFSDieYEGFLQSAEDLDNWVLPKDEwDAIALNYTSGTTGNPKGVV 201
Cdd:cd05928 120 TSDELAPEVDSVASECPSLKTKLL---VSEKSRDGWLN--FKELLNEASTEHHCVETGSQ-EPMAIYFTSGTTGSPKMAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 202 YHHRGAALNAIAQSLEFDMPKRPVYLWTLPlfhCNGWCFA--WTIAARGGVNVC-----LRKFDPKTCFDLIRQERVGFY 274
Cdd:cd05928 194 HSHSSLGLGLKVNGRYWLDLTASDIMWNTS---DTGWIKSawSSLFEPWIQGACvfvhhLPRFDPLVILKTLSSYPITTF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 275 CAAPVVHAALAN---APAEMKAgIDHPVSAmvAGAAPPEAVLARMEQMGFHMVHVYGLTEVygpSAVCAekpewdelsve 351
Cdd:cd05928 271 CGAPTVYRMLVQqdlSSYKFPS-LQHCVTG--GEPLNPEVLEKWKAQTGLDIYEGYGQTET---GLICA----------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 352 draaqkARQGVRntlqgaltvLDPETM-EPVPA-DGKTIGElmfRGNIVMKG--------------------YLKNPAET 409
Cdd:cd05928 334 ------NFKGMK---------IKPGSMgKASPPyDVQIIDD---NGNVLPPGtegdigirvkpirpfglfsgYVDNPEKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 410 GKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKD 489
Cdd:cd05928 396 AATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAP 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 490 DAQVSE-----EELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQ 536
Cdd:cd05928 476 QFLSHDpeqltKELQQHVKSVTAPYKYPRKVEFvQELPKTVTGKIQRNELRDK 528
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
58-528 |
3.17e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 115.76 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 58 AAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPeiKKAL 137
Cdd:PRK04319 87 ANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKP--ADDL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 138 PALKIIQVNDELGPKDvEPFSDIEYEgFLQSAEDLDnwVLPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLE 217
Cdd:PRK04319 165 PSLKHVLLVGEDVEEG-PGTLDFNAL-MEQASDEFD--IEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 218 FDMPKRPVYlwtlplfhcngWCFA---W-TIAARG-------GVNVCLR--KFDPKTCFDLIRQERVGFYCAAPVVHAAL 284
Cdd:PRK04319 241 LDLHEDDVY-----------WCTAdpgWvTGTSYGifapwlnGATNVIDggRFSPERWYRILEDYKVTVWYTAPTAIRML 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 285 anapaeMKAGID----HPVSAM-----VAGAAPPEAVLARMEqmgfhmvhVYGL--------TEVyGPSAVCaekpewde 347
Cdd:PRK04319 310 ------MGAGDDlvkkYDLSSLrhilsVGEPLNPEVVRWGMK--------VFGLpihdnwwmTET-GGIMIA-------- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 lsveDRAAQKARQG-------------VRNTLQGaltvLDPETMepvpadgktiGEL--------MFRGnivmkgYLKNP 406
Cdd:PRK04319 367 ----NYPAMDIKPGsmgkplpgieaaiVDDQGNE----LPPNRM----------GNLaikkgwpsMMRG------IWNNP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 407 AETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVE 486
Cdd:PRK04319 423 EKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1092482886 487 LKDDAQVSEE---ELDQYCRERLAGFKRPKYYVFGE-LAKTATGKI 528
Cdd:PRK04319 503 LRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDkLPKTRSGKI 548
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
58-534 |
7.38e-27 |
|
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: 114.13 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 58 AAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEfaPHIPE-IKKA 136
Cdd:cd05970 61 ANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--DNIPEeIEKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 137 LPALKIIQVNDELGPKDVEPFSDIEyEGFLQSAEDL----DNwVLPKDEwDAIALNYTSGTTGNPKGVVYHHrgaalnai 212
Cdd:cd05970 139 APECPSKPKLVWVGDPVPEGWIDFR-KLIKNASPDFerptAN-SYPCGE-DILLVYFSSGTTGMPKMVEHDF-------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 213 aqslefdmpkrpvylwTLPLFHCNGWCFaW----------TIAARG---------------GVNVCL---RKFDPKTCFD 264
Cdd:cd05970 208 ----------------TYPLGHIVTAKY-WqnvregglhlTVADTGwgkavwgkiygqwiaGAAVFVydyDKFDPKALLE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVVHAALANAPAEMK--AGIDHpvsAMVAGAAPPEAVLARM-EQMGFHMVHVYGLTEvygpSAVCAE 341
Cdd:cd05970 271 KLSKYGVTTFCAPPTIYRFLIREDLSRYdlSSLRY---CTTAGEALNPEVFNTFkEKTGIKLMEGFGQTE----TTLTIA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEWDElsvedraAQKARQGvRNTLQGALTVLDPETmEPVPA-----------DGKTIGelMFRgnivmkGYLKNPAETG 410
Cdd:cd05970 344 TFPWME-------PKPGSMG-KPAPGYEIDLIDREG-RSCEAgeegeivirtsKGKPVG--LFG------GYYKDAEKTA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 411 KSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDD 490
Cdd:cd05970 407 EVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1092482886 491 AQVSEE---ELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05970 487 YEPSEElkkELQDHVKKVTAPYKYPRIVEFvDELPKTISGKIRRVEIR 534
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
50-537 |
2.18e-26 |
|
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: 112.42 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 50 TYHRCRQMAAALR---QNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQhgeaefllvdsef 126
Cdd:cd05909 9 TYRKLLTGAIALArklAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIK------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 127 aphIPEIKKALPALKIIQVNDELGPKDVEPFSDIEY--------------EGFLQS---AEDLDNW--VLPKDEWDAIAL 187
Cdd:cd05909 76 ---LAGIKTVLTSKQFIEKLKLHHLFDVEYDARIVYledlrakiskadkcKAFLAGkfpPKWLLRIfgVAPVQPDDPAVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 188 NYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFA-WTIAARGGVNVCL-RKFDPKTCFDL 265
Cdd:cd05909 153 LFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGClWLPLLSGIKVVFHpNPLDYKKIPEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAALANA--PAEMKAgidhpVSAMVAGAappEAVLARMEQM-----GFHMVHVYGLTEVygpSAV 338
Cdd:cd05909 233 IYDKKATILLGTPTFLRGYARAahPEDFSS-----LRLVVAGA---EKLKDTLRQEfqekfGIRILEGYGTTEC---SPV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CA-EKPEWDelsvedraaqkARQG-VRNTLQG-ALTVLDPETMEPVPAdGKTiGELMFRGNIVMKGYLKNPAETGKSFAG 415
Cdd:cd05909 302 ISvNTPQSP-----------NKEGtVGRPLPGmEVKIVSVETHEEVPI-GEG-GLLLVRGPNVMLGYLNEPELTSFAFGD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKH-PAVANVAVVALADEKWGEVPVAFVELKDdaqVS 494
Cdd:cd05909 369 GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTD---TD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1092482886 495 EEELDQYCRE-RLAGFKRPKYY-VFGELAKTATGKIQKFELRKQA 537
Cdd:cd05909 446 PSSLNDILKNaGISNLAKPSYIhQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
31-536 |
3.64e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.01 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 31 VFGDDLAIVHGSIrQNWTETyhrcrqMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIY 110
Cdd:PRK13383 54 IIDDDGALSYREL-QRATES------LARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 111 CLQHGEAEFLLVDSEFAPHIPEIKKALPAL--KIIQVNDELGPKDVEPFSDIeyegflqsaedldnwVLpkdewdaialn 188
Cdd:PRK13383 127 ALRAHHISTVVADNEFAERIAGADDAVAVIdpATAGAEESGGRPAVAAPGRI---------------VL----------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTL--PLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLI 266
Cdd:PRK13383 181 LTSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVamPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAPVVHAALANAPAEMKAGIDHP-VSAMVAGAAPPEAVLAR--MEQMGFHMVHVYGLTEV-YGPSAVCAEK 342
Cdd:PRK13383 261 SLHRADAFTAVPVVLARILELPPRVRARNPLPqLRVVMSSGDRLDPTLGQrfMDTYGDILYNGYGSTEVgIGALATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 343 PEWDELSVEDRAAQKARQGVRNTLqgaltvldpetmepvPADGKTIGELMFRGNIVMKGYLKNpaeTGKSFAGGWFHTGD 422
Cdd:PRK13383 341 RDAPETVGKPVAGCPVRILDRNNR---------------PVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDGMTSTGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 423 LGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYC 502
Cdd:PRK13383 403 MGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYL 482
|
490 500 510
....*....|....*....|....*....|....*
gi 1092482886 503 RERLAGFKRPK-YYVFGELAKTATGKIqkfeLRKQ 536
Cdd:PRK13383 483 KDRVSRFEQPRdINIVSSIPRNPTGKV----LRKE 513
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
33-528 |
5.09e-26 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 111.21 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCL 112
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAEFLLVDSEFAPHIPeikkALPALKIIQVNDELGPKDVEPfsdieyegflqsaedldnWVLPKDEwDAIALNYTSG 192
Cdd:cd17646 92 ADAGPAVVLTTADLAARLP----AGGDVALLGDEALAAPPATPP------------------LVPPRPD-NLAYVIYTSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPL-FHCNGWCFAWTIAARGGVNVC--LRKFDPKTCFDLIRQE 269
Cdd:cd17646 149 STGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLsFDVSVWELFWPLVAGARLVVArpGGHRDPAYLAALIREH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAP-VVHAALANAPAEMKAGIDHpvsAMVAGAAPPEAVLAR-MEQMGFHMVHVYGLTEVYGPSAVCAEKPEWDE 347
Cdd:cd17646 229 GVTTCHFVPsMLRVFLAEPAAGSCASLRR---VFCSGEALPPELAARfLALPGAELHNLYGPTEAAIDVTHWPVRGPAET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 LSVE-DRAaqkarqgVRNTlqgALTVLDPEtMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF-------H 419
Cdd:cd17646 306 PSVPiGRP-------VPNT---RLYVLDDA-LRPVPVG--VPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmyR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 420 TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQ-VSEEEL 498
Cdd:cd17646 373 TGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAAL 452
|
490 500 510
....*....|....*....|....*....|.
gi 1092482886 499 DQYCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd17646 453 RAHLAERLPEYMVPAAFVvLDALPLTANGKL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-462 |
6.22e-26 |
|
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: 110.05 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 50 TYH----RCRQMAAALRQN-GADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDS 124
Cdd:TIGR01733 1 TYReldeRANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 125 EFAPHIPEIkkalpALKIIqvndELGPKDVEPFSDIEYEGFLQSAEDLDN--WVLpkdewdaialnYTSGTTGNPKGVVY 202
Cdd:TIGR01733 81 ALASRLAGL-----VLPVI----LLDPLELAALDDAPAPPPPDAPSGPDDlaYVI-----------YTSGSTGRPKGVVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 203 HHRGAALNAIAQSLEFDMPKRPVYLWTLPLfHCNGWCFAWTIAARGGVNVCL-----RKFDPKTCFDLIRQERVGFYCAA 277
Cdd:TIGR01733 141 THRSLVNLLAWLARRYGLDPDDRVLQFASL-SFDASVEEIFGALLAGATLVVppedeERDDAALLAALIAEHPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 278 PVVHAALANAPAEMKAGIDHpvsAMVAGAAPPEAVLARMEQMgFHMVHVYGLtevYGPS--AVCAekpewdelSVEDRAA 355
Cdd:TIGR01733 220 PSLLALLAAALPPALASLRL---VILGGEALTPALVDRWRAR-GPGARLINL---YGPTetTVWS--------TATLVDP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 356 QKARQGVRNTLQGALT-----VLDPEtMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSFA---------GGWFHTG 421
Cdd:TIGR01733 285 DDAPRESPVPIGRPLAntrlyVLDDD-LRPVPVGV--VGELYIGGPGVARGYLNRPELTAERFVpdpfaggdgARLYRTG 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1092482886 422 DLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHP 462
Cdd:TIGR01733 362 DLVRYLPDGnleFLgriddQVKIR--------GYRIELGEIEAALLRHP 402
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
45-462 |
6.46e-26 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 112.22 E-value: 6.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 45 QNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDS 124
Cdd:PLN02430 77 KTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 125 EFAPHI--PEIKKAlPALKII----QVNDELGPK----DVEPFSdieYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTT 194
Cdd:PLN02430 157 KKIKELlePDCKSA-KRLKAIvsftSVTEEESDKasqiGVKTYS---WIDFLHMGKENPSETNPPKPLDICTIMYTSGTS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 195 GNPKGVVYHHRGAALNAIAQSL---EFD--MPKRPVYLWTLPLFHC-----NGWCFawtiaaRGGVNVCLRKFDPKTCFD 264
Cdd:PLN02430 233 GDPKGVVLTHEAVATFVRGVDLfmeQFEdkMTHDDVYLSFLPLAHIldrmiEEYFF------RKGASVGYYHGDLNALRD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVV----HAALANAPAE-------------------MKAGIDH----PVSAMVA------------- 304
Cdd:PLN02430 307 DLMELKPTLLAGVPRVferiHEGIQKALQElnprrrlifnalykyklawMNRGYSHkkasPMADFLAfrkvkaklggrlr 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 305 ----GAAP----PEAVLaRMEQMGFhMVHVYGLTEVYGPSAVCAEkpewDELSVEDRAaqkarqgvrntlqGALTVLDPE 376
Cdd:PLN02430 387 llisGGAPlsteIEEFL-RVTSCAF-VVQGYGLTETLGPTTLGFP----DEMCMLGTV-------------GAPAVYNEL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 377 TMEPVPADG------KTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENI 449
Cdd:PLN02430 448 RLEEVPEMGydplgePPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYV 527
|
490
....*....|...
gi 1092482886 450 SSIEVEDVLYKHP 462
Cdd:PLN02430 528 ALEYLENVYGQNP 540
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
189-528 |
1.03e-25 |
|
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: 107.49 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHC---NGWCFA-WTiaarGGVNVCLRKFDPKTCFD 264
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSlflYGAISAlYL----GGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVVHAALANapaemkagIDHPVSAMV---AGAAPPEAVLARMEQMGFHMVHVYgltEVYGPSavcae 341
Cdd:cd17633 83 KINQYNATVIYLVPTMLQALAR--------TLEPESKIKsifSSGQKLFESTKKKLKNIFPKANLI---EFYGTS----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 kpewdELS-VEDRAAQKARQgvRNTLQGALTVLDPETMEpvpADGKTIGELMFRGNIVMKGYLKnpaeTGKSFAGGWFHT 420
Cdd:cd17633 147 -----ELSfITYNFNQESRP--PNSVGRPFPNVEIEIRN---ADGGEIGKIFVKSEMVFSGYVR----GGFSNPDGWMSV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 421 GDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKddaQVSEEELDQ 500
Cdd:cd17633 213 GDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYKQLKR 289
|
330 340
....*....|....*....|....*....
gi 1092482886 501 YCRERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFvDSLPYTSSGKI 318
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
47-462 |
1.08e-25 |
|
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: 110.64 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVD--- 123
Cdd:cd05932 9 WGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGkld 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 --SEFAPHIPE--IKKALPalkiiqvndelgPKDVEPFSDiEYEGFLQSAEDLDNWVLPKDEwDAIALNYTSGTTGNPKG 199
Cdd:cd05932 89 dwKAMAPGVPEglISISLP------------PPSAANCQY-QWDDLIAQHPPLEERPTRFPE-QLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 200 VVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVC-----------LRKFDPKTCF----- 263
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAfaesldtfvedVQRARPTLFFsvprl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 264 ---------DLIRQERVGFYCAAPVVhAALANAPAEMKAGIDHpVSAMVAGAAP-PEAVLARMEQMGFHMVHVYGLTEVY 333
Cdd:cd05932 235 wtkfqqgvqDKIPQQKLNLLLKIPVV-NSLVKRKVLKGLGLDQ-CRLAGCGSAPvPPALLEWYRSLGLNILEAYGMTENF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 334 GPSAVCaeKPEWDELSVedraaqkarqgVRNTLQGALTVLDPEtmepvpadgktiGELMFRGNIVMKGYLKNPAETGKSF 413
Cdd:cd05932 313 AYSHLN--YPGRDKIGT-----------VGNAGPGVEVRISED------------GEILVRSPALMMGYYKDPEATAEAF 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 414 -AGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENISSIEVEDVLYKHP 462
Cdd:cd05932 368 tADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHD 418
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
183-537 |
2.25e-25 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 108.81 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYL-WTLPLFHCNGW-CF--AWTIAArGGVNVCLRKFD 258
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWnISSPGWAKHAWsCFfaPWNAGA-TVFLFNYARFD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 259 PKTCFDLIRQERVGFYCAAPVVHAALANAPAemkAGIDHPVSAMVAGAAP--PEAVLARMEQMGFHMVHVYGLTEVygpS 336
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQQDL---ASFDVKLREVVGAGEPlnPEVIEQVRRAWGLTIRDGYGQTET---T 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 337 AVCAEKPEWdelSVEDRAAQKARQGVRntlqgaLTVLDPETMepvPADGktiGELMF-----RGNIVMKGYLKNPAETGK 411
Cdd:cd05974 239 ALVGNSPGQ---PVKAGSMGRPLPGYR------VALLDPDGA---PATE---GEVALdlgdtRPVGLMKGYAGDPDKTAH 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 412 SFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDA 491
Cdd:cd05974 304 AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGY 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1092482886 492 QVSEE---ELDQYCRERLAGFKRPKYYVFGELAKTATGKIQKFELRKQA 537
Cdd:cd05974 384 EPSPEtalEIFRFSRERLAPYKRIRRLEFAELPKTISGKIRRVELRRRE 432
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
46-458 |
3.19e-25 |
|
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: 109.23 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 46 NWTETYHRCRQMAAALRQNGADRGTT--VATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVD 123
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 sefaphipeikkalPALKIIQVND--ELGPKDVEPFsdieyegflqsaedldnwVLPKDEwdAIALN-YTSGTTGNPKGV 200
Cdd:cd05927 87 --------------AGVKVYSLEEfeKLGKKNKVPP------------------PPPKPE--DLATIcYTSGTTGNPKGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 201 VYHHRG--AALNAIAQSLEFDMPKRP--VYLWTLPLFHCNGWCFAWTIAARGGvnvCLRKF--DPKTCFDLIRQERVGFY 274
Cdd:cd05927 133 MLTHGNivSNVAGVFKILEILNKINPtdVYISYLPLAHIFERVVEALFLYHGA---KIGFYsgDIRLLLDDIKALKPTVF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 275 CAAPVV-----------------------HAALANAPAEMKAGID--HP-----------------VSAMVAGAAPPEA- 311
Cdd:cd05927 210 PGVPRVlnriydkifnkvqakgplkrklfNFALNYKLAELRSGVVraSPfwdklvfnkikqalggnVRLMLTGSAPLSPe 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 312 VLARMEQ-MGFHMVHVYGLTEVYGPSAVcaekpewdelsvedraaqkARQGVRNT------LQGALTVLD--PEtMEPVP 382
Cdd:cd05927 290 VLEFLRVaLGCPVLEGYGQTECTAGATL-------------------TLPGDTSVghvggpLPCAEVKLVdvPE-MNYDA 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 383 ADGKTIGELMFRGNIVMKGYLKNPAETGKSFA-GGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENISSIEVEDVL 458
Cdd:cd05927 350 KDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDeDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIY 427
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
34-528 |
6.27e-25 |
|
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: 107.55 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEfaphipeikkalpalkiiqvndelgpkdvepfsDIEYegflqsaedldnwvlpkdewdaiaLNYTSGT 193
Cdd:cd17650 82 DSGAKLLLTQPE---------------------------------DLAY------------------------VIYTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWC--FAWTIAARGGVNVCLR--KFDPKTCFDLIRQE 269
Cdd:cd17650 105 TGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAgdFARSLLNGGTLVICPDevKLDPAALYDLILKS 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAPVVHAALAN-------APAEMKAGIdhpVSAMVAGAAPPEAVLARMEQmGFHMVHVYGLTEVYGPSAVCaek 342
Cdd:cd17650 185 RITLMESTPALIRPVMAyvyrnglDLSAMRLLI---VGSDGCKAQDFKTLAARFGQ-GMRIINSYGVTEATIDSTYY--- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 343 pEWDELSVEDRAAQKARQGVRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF------AGG 416
Cdd:cd17650 258 -EEGRDPLGDSANVPIGRPLPNT---AMYVLD-ERLQPQPVG--VAGELYIGGAGVARGYLNRPELTAERFvenpfaPGE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 417 -WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVelKDDAQVSE 495
Cdd:cd17650 331 rMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYV--VAAATLNT 408
|
490 500 510
....*....|....*....|....*....|....
gi 1092482886 496 EELDQYCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd17650 409 AELRAFLAKELPSYMIPSYYVqLDALPLTPNGKV 442
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
34-533 |
7.37e-25 |
|
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: 107.74 E-value: 7.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPEIKKALPALKIIQVNDELGPK-DVEPfSDIEYegflqsaedldnwVLpkdewdaialnYTSG 192
Cdd:cd12114 82 DAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPvDVAP-DDLAY-------------VI-----------FTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHRgAALNAIAQ-----------------SLEFDMpkrPVYlwtlPLFhcngwcfawTIAARGGVNV--- 252
Cdd:cd12114 137 STGTPKGVMISHR-AALNTILDinrrfavgpddrvlalsSLSFDL---SVY----DIF---------GALSAGATLVlpd 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 253 CLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQM--GFHMVHVYGLT 330
Cdd:cd12114 200 EARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGAT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 E-----VYGPsaVCAEKPEWDelSV---EDRAAQKARqgvrntlqgaltVLDPEtMEPVPaDGkTIGELMFRGNIVMKGY 402
Cdd:cd12114 280 EasiwsIYHP--IDEVPPDWR--SIpygRPLANQRYR------------VLDPR-GRDCP-DW-VPGELWIGGRGVALGY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 403 LKNPAETGKSF-----AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALADEKW 477
Cdd:cd12114 341 LGDPELTAARFvthpdGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHP-GVARAVVVVLGDPG 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 478 GEVPVAFVELKDDA-QVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFEL 533
Cdd:cd12114 420 GKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEaLPLTANGKVDRAAL 477
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
47-441 |
9.77e-25 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 107.89 E-value: 9.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLV-DSE 125
Cdd:cd17641 14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAeDEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 FAPHIPEIKKALPALKIIQVNDELG------PKdVEPFSDIEYEGFLQSAED---LDNWVLPKDEWDAIALNYTSGTTGN 196
Cdd:cd17641 94 QVDKLLEIADRIPSVRYVIYCDPRGmrkyddPR-LISFEDVVALGRALDRRDpglYEREVAAGKGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 197 PKGVVYHHRgAALNAIAQSLEFDmPKRPV--YLWTLPLfhcnGWC--FAWTIA----ARGGVNvclrkF--DPKTCFDLI 266
Cdd:cd17641 173 PKLAMLSHG-NFLGHCAAYLAAD-PLGPGdeYVSVLPL----PWIgeQMYSVGqalvCGFIVN-----FpeEPETMMEDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAP-VVHAALANAPAEM-------KAGIDHpvsAMVAGAAPPEAVLaRMEQMGFHMVHVYGLTE--VYGP- 335
Cdd:cd17641 242 REIGPTFVLLPPrVWEGIAADVRARMmdatpfkRFMFEL---GMKLGLRALDRGK-RGRPVSLWLRLASWLADalLFRPl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 ----------SAVCAEKPEWDELSVEDRA-AQKARQGVRNT-LQGALTV-----LDPETMEpVPADGKTI-----GELMF 393
Cdd:cd17641 318 rdrlgfsrlrSAATGGAALGPDTFRFFHAiGVPLKQLYGQTeLAGAYTVhrdgdVDPDTVG-VPFPGTEVridevGEILV 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1092482886 394 RGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDI 441
Cdd:cd17641 397 RSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
189-530 |
2.72e-24 |
|
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: 105.47 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVylWTLplFHCNGWCFA----WTIAARGGVNVCLRKF---DPKT 261
Cdd:cd17643 100 YTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDV--WTL--FHSYAFDFSvweiWGALLHGGRLVVVPYEvarSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 CFDLIRQERVGFYCAAPvvHAALANAPAEMKAGIDHPVSAMV--AGAAPPEAVLA----RMEQMGFHMVHVYGLTEVygp 335
Cdd:cd17643 176 FARLLRDEGVTVLNQTP--SAFYQLVEAADRDGRDPLALRYVifGGEALEAAMLRpwagRFGLDRPQLVNMYGITET--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 sAVCAEkpeWDELSVEDrAAQKARQGVRNTLQG-ALTVLDpETMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSF- 413
Cdd:cd17643 251 -TVHVT---FRPLDAAD-LPAAAASPIGRPLPGlRVYVLD-ADGRPVPPGV--VGELYVSGAGVARGYLGRPELTAERFv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 ---AGG----WFHTGDLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHPAVANVAVVALADEKWG 478
Cdd:cd17643 323 anpFGGpgsrMYRTGDLARRLPDGeleYLgradeQVKIR--------GFRIELGEIEAALATHPSVRDAAVIVREDEPGD 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 479 EVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYV-FGELAKTATGKIQK 530
Cdd:cd17643 395 TRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVpLDALPLTVNGKLDR 447
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
128-538 |
1.24e-22 |
|
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: 101.62 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 128 PHIPEIKKAL-----PALKIIQVNDELGPKD-VEPFSDIEYEGFLQSAEDLDnwVLPKDEWDAIALNYTSGTTGNPKGVV 201
Cdd:cd05967 172 PYKPLLDKALelsghKPHHVLVLNRPQVPADlTKPGRDLDWSELLAKAEPVD--CVPVAATDPLYILYTSGTTGKPKGVV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 202 YHHRG--AALNAIAQSLeFDMPKRPVYL------WTL--------PLFHcnGwcfAWTIAARGGVnvcLRKFDPKTCFDL 265
Cdd:cd05967 250 RDNGGhaVALNWSMRNI-YGIKPGDVWWaasdvgWVVghsyivygPLLH--G---ATTVLYEGKP---VGTPDPGAFWRV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAM----VAG--AAPPEAVLARmEQMGFHMVHVYGLTEVygPSAVC 339
Cdd:cd05967 321 IEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLrtlfLAGerLDPPTLEWAE-NTLGVPVIDHWWQTET--GWPIT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AEKPEWDELSVEDRAAQKARQGVRntlqgaLTVLDpETMEPVPADGKtigelmfrGNIVMKGYL---------KNPAETG 410
Cdd:cd05967 398 ANPVGLEPLPIKAGSPGKPVPGYQ------VQVLD-EDGEPVGPNEL--------GNIVIKLPLppgclltlwKNDERFK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 411 KSFAG---GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVEL 487
Cdd:cd05967 463 KLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL 542
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 488 KDDAQVSEEELDQYC----RERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAE 538
Cdd:cd05967 543 KEGVKITAEELEKELvalvREQIGPVAAFRLVIFvKRLPKTRSGKILRRTLRKIAD 598
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
34-430 |
1.75e-22 |
|
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: 102.24 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSirQNWTetY----HRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLI 109
Cdd:COG1020 491 DAVAVVFGD--QSLT--YaelnARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 110 YCLQHGEAEFLLVDSEFAPHIPEikkalPALKIIQVndelgpkDVEPFSDieyegflQSAEDLDNWVLPkdewDAIA-LN 188
Cdd:COG1020 567 YMLEDAGARLVLTQSALAARLPE-----LGVPVLAL-------DALALAA-------EPATNPPVPVTP----DDLAyVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAA--LNAIAQslEFDMPKRPVYLWTLPL-FHCNGWCFAWTIAArGGVNVCLRK---FDPKTC 262
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVnlLAWMQR--RYGLGPGDRVLQFASLsFDASVWEIFGALLS-GATLVLAPPearRDPAAL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 263 FDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHpvsAMVAGAAPPEAVLARMEQM--GFHMVHVYGLTEvygpSAVCA 340
Cdd:COG1020 701 AELLARHRVTVLNLTPSLLRALLDAAPEALPSLRL---VLVGGEALPPELVRRWRARlpGARLVNLYGPTE----TTVDS 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 341 ekpEWDELSVEDRAAQKARQG--VRNTlqgALTVLDpETMEPVPaDGkTIGELMFRGNIVMKGYLKNPAETGKSF----- 413
Cdd:COG1020 774 ---TYYEVTPPDADGGSVPIGrpIANT---RVYVLD-AHLQPVP-VG-VPGELYIGGAGLARGYLNRPELTAERFvadpf 844
|
410 420
....*....|....*....|
gi 1092482886 414 --AGG-WFHTGDLGVLHPDG 430
Cdd:COG1020 845 gfPGArLYRTGDLARWLPDG 864
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
40-539 |
1.97e-22 |
|
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: 100.82 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 40 HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNV-------RLETEGLIYCL 112
Cdd:cd05906 35 GSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptydepNARLRKLRHIW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAEFLLVDSEFAPHIPEIKKALPalkiiqvndelgpkdVEPFSDIEYEGFLQSAEDLDnwVLPKDEWDAIALNYTSG 192
Cdd:cd05906 115 QLLGSPVVLTDAELVAEFAGLETLSG---------------LPGIRVLSIEELLDTAADHD--LPQSRPDDLALLMLTSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHRG--AALNAIAQSLEFDmPKRPVYLWtLPLFHCNGWCFAWTIAARGG---VNV----CLRkfDPKTCF 263
Cdd:cd05906 178 STGFPKAVPLTHRNilARSAGKIQHNGLT-PQDVFLNW-VPLDHVGGLVELHLRAVYLGcqqVHVpteeILA--DPLRWL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 264 DLIRQERVGfYCAAPVVHAALANAPAEMKAGIDHPVSAM----VAGaappEAVLARM--------EQMG---FHMVHVYG 328
Cdd:cd05906 254 DLIDRYRVT-ITWAPNFAFALLNDLLEEIEDGTWDLSSLrylvNAG----EAVVAKTirrllrllEPYGlppDAIRPAFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 329 LTEVygpSAVCAekpeWDELSVEDRAAQKAR--------QGVRntlqgaLTVLDPETmEPVPADgkTIGELMFRGNIVMK 400
Cdd:cd05906 329 MTET---CSGVI----YSRSFPTYDHSQALEfvslgrpiPGVS------MRIVDDEG-QLLPEG--EVGRLQVRGPVVTK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSF-AGGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVLykhpavanvavvaladEKWGE 479
Cdd:cd05906 393 GYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAV----------------EEVPG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 480 VPVAFV---ELKDDAQVSEE-------------ELDQYCRE------RLAGFkRPKYYV---FGELAKTATGKIQKFELR 534
Cdd:cd05906 456 VEPSFTaafAVRDPGAETEElaiffvpeydlqdALSETLRAirsvvsREVGV-SPAYLIplpKEEIPKTSLGKIQRSKLK 534
|
....*
gi 1092482886 535 KQAEA 539
Cdd:cd05906 535 AAFEA 539
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
57-533 |
3.06e-22 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 100.08 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 57 MAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEF---APHIPEI 133
Cdd:PRK05857 54 LAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSkmaSSAVPEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 134 KKALPAlkiIQVNDELGPKDVEPFSDIEY-EGFLQSAEDldnwvlpkdewDAIALNYTSGTTGNPKGVVYHHRgaALNAI 212
Cdd:PRK05857 134 LHSIPV---IAVDIAAVTRESEHSLDAASlAGNADQGSE-----------DPLAMIFTSGTTGEPKAVLLANR--TFFAV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 213 AQSLE------FDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVnvCLRKFDPKTCF-DLIRQERVGFYCAAPVVHAALA 285
Cdd:PRK05857 198 PDILQkeglnwVTWVVGETTYSPLPATHIGGLWWILTCLMHGGL--CVTGGENTTSLlEILTTNAVATTCLVPTLLSKLV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 286 napAEMK-AGIDHPVSAMVA--GAAPPEAVLARMEQMGFHMVHVYGLTEVyGPSAVCaekpewdeLSVEDRAAQKARQG- 361
Cdd:PRK05857 276 ---SELKsANATVPSLRLVGygGSRAIAADVRFIEATGVRTAQVYGLSET-GCTALC--------LPTDDGSIVKIEAGa 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 362 VRNTLQGALTVL-DPETMEPVPADG---KTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDR 437
Cdd:PRK05857 344 VGRPYPGVDVYLaATDGIGPTAPGAgpsASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 438 SKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGE-VPVAFVELKDDAQVSEEELDQ-----YCRERLAGFKR 511
Cdd:PRK05857 424 SSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAlVGLAVVASAELDESAARALKHtiaarFRRESEPMARP 503
|
490 500
....*....|....*....|..
gi 1092482886 512 PKYYVFGELAKTATGKIQKFEL 533
Cdd:PRK05857 504 STIVIVTDIPRTQSGKVMRASL 525
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
34-528 |
3.46e-22 |
|
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: 99.73 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd17651 10 DAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPeikkalpalkiiqvndelgpkdVEPFSDIEYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGT 193
Cdd:cd17651 90 DAGPVLVLTHPALAGELA----------------------VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDM-PKRPVYLWTLPLFHCngwcFAWTI--AARGGVNVCLR----KFDPKTCFDLI 266
Cdd:cd17651 148 TGRPKGVVMPHRSLANLVAWQARASSLgPGARTLQFAGLGFDV----SVQEIfsTLCAGATLVLPpeevRTDPPALAAWL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAG-AAPPEAVLARM--EQMGFHMVHVYGLTEVYGPSA--VCAE 341
Cdd:cd17651 224 DEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGeQLVLTEDLREFcaGLPGLRLHNHYGPTETHVVTAlsLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEWDELSVEDRAAQKARqgvrntlqgaLTVLDpETMEPVPaDGKTiGELMFRGNIVMKGYLKNPAETGKSFAGGWF--- 418
Cdd:cd17651 304 PAAWPAPPPIGRPIDNTR----------VYVLD-AALRPVP-PGVP-GELYIGGAGLARGYLNRPELTAERFVPDPFvpg 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 ----HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVS 494
Cdd:cd17651 371 armyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVD 450
|
490 500 510
....*....|....*....|....*....|....*
gi 1092482886 495 EEELDQYCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd17651 451 AAELRAALATHLPEYMVPSAFVlLDALPLTPNGKL 485
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
33-528 |
3.79e-22 |
|
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: 99.29 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCL 112
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 113 QHGEAEFLLVDSEFAPHIPEIkkaLPALKIIQVNDELGPKDVEPfsdieyegflQSAEDLDNWVLpkdewdaialnYTSG 192
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAG---LPVLLLALAAAAAAPAAPRT----------PVSPDDLAYVI-----------YTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHRGAA--LNAIAQSLEFDMPKRPVYLWT-----------LPLfhcngWCFAWTIAARGGVNVclrkfDP 259
Cdd:cd12116 137 STGRPKGVVVSHRNLVnfLHSMRERLGLGPGDRLLAVTTyafdisllellLPL-----LAGARVVIAPRETQR-----DP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 KTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGidhpVSAMVAGAAPPEAVLARMeqmgfhMVHVYGLTEVYGPSavc 339
Cdd:cd12116 207 EALARLIEAHSITVMQATPATWRMLLDAGWQGRAG----LTALCGGEALPPDLAARL------LSRVGSLWNLYGPT--- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 aEKPEWD---ELSVEDRAAQKARQgVRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF--- 413
Cdd:cd12116 274 -ETTIWStaaRVTAAAGPIPIGRP-LANT---QVYVLD-AALRPVPPG--VPGELYIGGDGVAQGYLGRPALTAERFvpd 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 ----AGG-WFHTGDLGVLHPDGY--------AQIKDRskdiiisgGENISSIEVEDVLYKHPAVANVAVVALADEKWGEV 480
Cdd:cd12116 346 pfagPGSrLYRTGDLVRRRADGRleylgradGQVKIR--------GHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1092482886 481 pVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd12116 418 -VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVrLDALPLTANGKL 465
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
18-540 |
4.36e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 99.68 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 18 PLTpiDFLVRAHEvfGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTP-------AMVEAGFgVP 90
Cdd:PRK10946 26 PLT--DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAefyitffALLKLGV-AP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 91 MSG------GVLLALNVRLETEGLIYCLQHGeaefLLVDSEFaphIPEIKKALPALKIIQVNDELGPKDVEPFSDIEYEG 164
Cdd:PRK10946 101 VNAlfshqrSELNAYASQIEPALLIADRQHA----LFSDDDF---LNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAED 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 165 FLQSAEdldnwvlPKDEwdaIALNYTSG-TTGNPKGVVYHHRGA--ALNAIAQSLEFDMPKRpvYLWTLPLFHcN----- 236
Cdd:PRK10946 174 FTATPS-------PADE---VAFFQLSGgSTGTPKLIPRTHNDYyySVRRSVEICGFTPQTR--YLCALPAAH-Nypmss 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 237 ----GWCFAwtiaarGGVNVCLRKFDPKTCFDLIRQERVGFycAAPVVHAALANAPAEMKAGIDHPVSAM----VAGAAP 308
Cdd:PRK10946 241 pgalGVFLA------GGTVVLAPDPSATLCFPLIEKHQVNV--TALVPPAVSLWLQAIAEGGSRAQLASLkllqVGGARL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 309 PEAVLARM-EQMGFHMVHVYGLTEvygpSAVCAEKPEWDElsvedraaqkarQGVRNTlQG-------ALTVLDpETMEP 380
Cdd:PRK10946 313 SETLARRIpAELGCQLQQVFGMAE----GLVNYTRLDDSD------------ERIFTT-QGrpmspddEVWVAD-ADGNP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 381 VPaDGkTIGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLY 459
Cdd:PRK10946 375 LP-QG-EVGRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 460 KHPAVANVAVVALADEKWGEVPVAFVELKDDaqVSEEELDQYCRER-LAGFKRP-KYYVFGELAKTATGKIQKFELRKQA 537
Cdd:PRK10946 453 RHPAVIHAALVSMEDELMGEKSCAFLVVKEP--LKAVQLRRFLREQgIAEFKLPdRVECVDSLPLTAVGKVDKKQLRQWL 530
|
...
gi 1092482886 538 EAL 540
Cdd:PRK10946 531 ASR 533
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
26-530 |
2.32e-21 |
|
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: 97.27 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 26 VRAHevfGDDLAIVHGSirQNWTetYH----RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNV 101
Cdd:cd12117 7 AART---PDAVAVVYGD--RSLT--YAelneRANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 102 RLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIkkaLPALKIIQVNDelgpkdvepfsdieyegflqsAEDLDNWVLPKDE 181
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGL---EVAVVIDEALD---------------------AGPAGNPAVPVSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 182 wDAIA-LNYTSGTTGNPKGVVYHHRG----------AALNA---IAQ--SLEFDMPkrpvylwTLPLFHC--NGWCFAwt 243
Cdd:cd12117 136 -DDLAyVMYTSGSTGRPKGVAVTHRGvvrlvkntnyVTLGPddrVLQtsPLAFDAS-------TFEIWGAllNGARLV-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 244 IAARGGVnvclrkFDPKTCFDLIRQERVG-FYCAAPVVHAaLANAPAEMKAGIDHpvsAMVAG-AAPPEAVLARMEQM-G 320
Cdd:cd12117 206 LAPKGTL------LDPDALGALIAEEGVTvLWLTAALFNQ-LADEDPECFAGLRE---LLTGGeVVSPPHVRRVLAACpG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 321 FHMVHVYGLTEvygpSAVCAEKPEWDELSVEDRAAQKARQgVRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMK 400
Cdd:cd12117 276 LRLVNGYGPTE----NTTFTTSHVVTELDEVAGSIPIGRP-IANT---RVYVLD-EDGRPVPPG--VPGELYVGGDGLAL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 401 GYLKNPAETGKSFA-------GGWFHTGDLGVLHPDGY--------AQIKDRskdiiisgGENISSIEVEDVLYKHPAVA 465
Cdd:cd12117 345 GYLNRPALTAERFVadpfgpgERLYRTGDLARWLPDGRleflgridDQVKIR--------GFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 466 NVAVVALADEKWGEVPVAFVELkdDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQK 530
Cdd:cd12117 417 EAVVVVREDAGGDKRLVAYVVA--EGALDAAELRAFLRERLPAYMVPAAFVVlDELPLTANGKVDR 480
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-528 |
3.18e-21 |
|
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: 97.26 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDDLAIV----------HGSIRQNWTETyhrCRqMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVR 102
Cdd:cd17634 67 GDRTAIIyegddtsqsrTISYRELHREV---CR-FAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 103 LETEGLIYCLQHGEAEFLLVDSEF------APHIPEIKKAL-----PALKIIQVNDELGPKDVEPFSDIEYEGFLQSAED 171
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGGvragrsVPLKKNVDDALnpnvtSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 172 LDNWVlPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAiAQSLE--FDMPKRPVYLWTLPLfhcnGWCFAWTIAARGG 249
Cdd:cd17634 223 EHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYA-ATTMKyvFDYGPGDIYWCTADV----GWVTGHSYLLYGP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 250 VNVCLRKF---------DPKTCFDLIRQERVGFYCAAPVVHAALAnaPAEMKAGIDHPVSAM-VAGAA----PPEAVLAR 315
Cdd:cd17634 297 LACGATTLlyegvpnwpTPARMWQVVDKHGVNILYTAPTAIRALM--AAGDDAIEGTDRSSLrILGSVgepiNPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 316 MEQMGFH---MVHVYGLTEVYGpsAVCAEKPEWDELSVEdrAAQKARQGVRntlqgaLTVLDPETMepvPADGKTIGELM 392
Cdd:cd17634 375 WKKIGKEkcpVVDTWWQTETGG--FMITPLPGAIELKAG--SATRPVFGVQ------PAVVDNEGH---PQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 393 FRGNI--VMKGYLKNPAETGKS----FAGGWFHtGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVAN 466
Cdd:cd17634 442 ITDPWpgQTRTLFGDHERFEQTyfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 467 VAVVALADEKWGEVPVAFVELKDDAQVSEE---ELDQYCRERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHGVEPSPElyaELRNWVRKEIGPLATPDVVHWvDSLPKTRSGKI 586
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
189-533 |
4.09e-21 |
|
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: 96.52 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRG--AALNAIAQSLEFDMPKRPVYLWTLPLFH-----CNGWCFAW------------TIAARGG 249
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLAYLPLAHifelaAENVCLYRggtigygsprtlTDKSKRG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 250 VNVCLRKFDP----------------------------KTCFDL---IRQERVGFYCAAPVVHAALANAPAEMKAGidhP 298
Cdd:cd17639 175 CKGDLTEFKPtlmvgvpaiwdtirkgvlaklnpmgglkRTLFWTayqSKLKALKEGPGTPLLDELVFKKVRAALGG---R 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 299 VSAMVAGAAPPEAVLAR-MEQMGFHMVHVYGLTEVYGpsavCAEKPEWDELSVeDRAAQkarqgvrntLQGALTV--LD- 374
Cdd:cd17639 252 LRYMLSGGAPLSADTQEfLNIVLCPVIQGYGLTETCA----GGTVQDPGDLET-GRVGP---------PLPCCEIklVDw 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 375 PE----TMEPVPAdgktiGELMFRGNIVMKGYLKNPAETGKSFAG-GWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGEN 448
Cdd:cd17639 318 EEggysTDKPPPR-----GEILIRGPNVFKGYYKNPEKTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEY 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 449 ISSIEVEDVLYKHPAVANVAVVALADEKWgevPVAFV-----ELKDDAQ---VSEEELDQYCRErlagfKRPKYYVFGEL 520
Cdd:cd17639 393 IALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVvpnekHLTKLAEkhgVINSEWEELCED-----KKLQKAVLKSL 464
|
410
....*....|....
gi 1092482886 521 AKTA-TGKIQKFEL 533
Cdd:cd17639 465 AETArAAGLEKFEI 478
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
31-530 |
1.18e-20 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 95.09 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 31 VFGDDlaivhgsirqnwTETYH----RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETE 106
Cdd:cd17655 17 VFEDQ------------TLTYRelneRANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 107 GLIYCLQHGEAEFLLVDSEFAPHIPEIKKalpalkIIQVNDElgpkdvepfsDIEYEgflqSAEDLDNWVLPKDEWDAIa 186
Cdd:cd17655 85 RIQYILEDSGADILLTQSHLQPPIAFIGL------IDLLDED----------TIYHE----ESENLEPVSKSDDLAYVI- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 187 lnYTSGTTGNPKGVVYHHRG------AALNAIAQSLEFDMPKRPVYLWTLPLFHcngwcfAWTIAARGGVNVCLRK---F 257
Cdd:cd17655 144 --YTSGSTGKPKGVMIEHRGvvnlveWANKVIYQGEHLRVALFASISFDASVTE------IFASLLSGNTLYIVRKetvL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 258 DPKTCFDLIRQERVGFYCAAPvvhaALANAPAEMKAGIDHPVSAMVAG--AAPPEAVlarmEQMGFHMVHVYGLTEVYGP 335
Cdd:cd17655 216 DGQALTQYIRQNRITIIDLTP----AHLKLLDAADDSEGLSLKHLIVGgeALSTELA----KKIIELFGTNPTITNAYGP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 S--AVCAekpewdelSVEDRAAQKARQG-------VRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNP 406
Cdd:cd17655 288 TetTVDA--------SIYQYEPETDQQVsvpigkpLGNT---RIYILD-QYGRPQPVG--VAGELYIGGEGVARGYLNRP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 407 AETGKSF------AGG-WFHTGDLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHPAVANVAVVA 471
Cdd:cd17655 354 ELTAEKFvddpfvPGErMYRTGDLARWLPDGnieFLgridhQVKIR--------GYRIELGEIEARLLQHPDIKEAVVIA 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 472 LADEKWGEVPVAFVELKDDAQVseEELDQYCRERLAGFKRPKYYV-FGELAKTATGKIQK 530
Cdd:cd17655 426 RKDEQGQNYLCAYIVSEKELPV--AQLREFLARELPDYMIPSYFIkLDEIPLTPNGKVDR 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-530 |
3.27e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 36 LAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHG 115
Cdd:PRK12316 528 PALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDS 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 116 EAEFLLVDSEFAPHIPeikkaLPA-LKIIQVNDelgpkdvepfSDIEYEGflQSAEDLDNWVLPKDEWDAIalnYTSGTT 194
Cdd:PRK12316 608 GVQLLLSQSHLGRKLP-----LAAgVQVLDLDR----------PAAWLEG--YSEENPGTELNPENLAYVI---YTSGST 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 195 GNPKGVVYHHRGAA--LNAIAQSLEFDMPKRpVYLWTLPLFHCNGWCFAWTIA--ARGGVNVCLRKFDPKTCFDLIRQER 270
Cdd:PRK12316 668 GKPKGAGNRHRALSnrLCWMQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMsgARLVVAAPGDHRDPAKLVELINREG 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 271 VGFYCAAPVVHAALANAPAEMKAGidhPVSAMVAGAappEAVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPEWdelSV 350
Cdd:PRK12316 747 VDTLHFVPSMLQAFLQDEDVASCT---SLRRIVCSG---EALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHW---TC 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 351 EDRAAQKARQGvRNTLQGALTVLDPEtMEPVPAdgKTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF-------HTGDL 423
Cdd:PRK12316 818 VEEGGDSVPIG-RPIANLACYILDAN-LEPVPV--GVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermyRTGDL 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 424 GVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALAdekwGEVPVAFVELKDDAQVSEEELDQYCR 503
Cdd:PRK12316 894 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLA 969
|
490 500
....*....|....*....|....*...
gi 1092482886 504 ERLAGFKRPKYYVFGE-LAKTATGKIQK 530
Cdd:PRK12316 970 ASLPEYMVPAQWLALErLPLTPNGKLDR 997
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
31-455 |
4.74e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 93.52 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 31 VFGDdlaiVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLAL-------NVRL 103
Cdd:PRK07768 20 VTGE----PDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLhqptprtDLAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 104 ETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKAlpALKIIQVNDELGPKDVEPfsdieyegflqsaedldnwvLPKDEwD 183
Cdd:PRK07768 96 WAEDTLRVIGMIGAKAVVVGEPFLAAAPVLEEK--GIRVLTVADLLAADPIDP--------------------VETGE-D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 184 AIAL-NYTSGTTGNPKGVVYHHRGAALN--AIAQSLEFDMPKRPVYLWtLPLFHCNGWCFAWTIA-ARGGVNVCLRKFD- 258
Cdd:PRK07768 153 DLALmQLTSGSTGSPKAVQITHGNLYANaeAMFVAAEFDVETDVMVSW-LPLFHDMGMVGFLTVPmYFGAELVKVTPMDf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 259 ---PKTCFDLIRQERvGFYCAAP-----VVHAALANAPAEmkAGIDhpVSA---MVAGAAP--PEAVLARMEQ---MGFH 322
Cdd:PRK07768 232 lrdPLLWAELISKYR-GTMTAAPnfayaLLARRLRRQAKP--GAFD--LSSlrfALNGAEPidPADVEDLLDAgarFGLR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 323 ---MVHVYGLTE---------VYGPSAVCaeKPEWDELSVEDRAAQKARQGVRntlqgALTVLDPetmePVP-------- 382
Cdd:PRK07768 307 peaILPAYGMAEatlavsfspCGAGLVVD--EVDADLLAALRRAVPATKGNTR-----RLATLGP----PLPglevrvvd 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 383 ADGKT-----IGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVE 455
Cdd:PRK07768 376 EDGQVlpprgVGVIELRGESVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
34-528 |
8.92e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 92.00 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd12115 14 DAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEfaphipeikkalpalkiiqvndelgpkdvepfsDIEYegflqsaedldnwVLpkdewdaialnYTSGT 193
Cdd:cd12115 94 DAQARLVLTDPD---------------------------------DLAY-------------VI-----------YTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAAlnAIAQslefdmpkrpvylWTLPLFHCNGWcfAWTIAArggvnvclrkfdPKTCFDLIRQERVGF 273
Cdd:cd12115 117 TGRPKGVAIEHRNAA--AFLQ-------------WAAAAFSAEEL--AGVLAS------------TSICFDLSVFELFGP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 274 YCA-----------APVVHAALANA------PAEMKAGIDH---PVSAMV---AGAAPPEAVLARMEQMGfHMVHVYGLt 330
Cdd:cd12115 168 LATggkvvladnvlALPDLPAAAEVtlintvPSAAAELLRHdalPASVRVvnlAGEPLPRDLVQRLYARL-QVERVVNL- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 evYGPSavcaEKPEWDELSVEDRAAQKARQGVRNTLQGALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETG 410
Cdd:cd12115 246 --YGPS----EDTTYSTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLG--VPGELYIGGAGVARGYLGRPGLTA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 411 KSFAGGWFH-------TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVA 483
Cdd:cd12115 317 ERFLPDPFGpgarlyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1092482886 484 FVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:cd12115 397 YIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRlDALPLTPNGKI 442
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
189-541 |
9.15e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 93.45 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHR--GAALNAIAQSLEFDmpKRPVYLWTLPLFHCNGWCFA-WTIAARGGVNVClrKFDP---KTC 262
Cdd:PRK08633 789 FSSGSEGEPKGVMLSHHniLSNIEQISDVFNLR--NDDVILSSLPFFHSFGLTVTlWLPLLEGIKVVY--HPDPtdaLGI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 263 FDLIRQERVGFYCAAPVVHAALANAP---AEMKAGIDhpvsAMVAGAA--PPEAVLARMEQMGFHMVHVYGLTEVYGPSA 337
Cdd:PRK08633 865 AKLVAKHRATILLGTPTFLRLYLRNKklhPLMFASLR----LVVAGAEklKPEVADAFEEKFGIRILEGYGATETSPVAS 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 338 VCAekPewDELSVEDRAAQKARQG-VRNTLQG-ALTVLDPETMEPVPAdgKTIGELMFRGNIVMKGYLKNPAETGK---- 411
Cdd:PRK08633 941 VNL--P--DVLAADFKRQTGSKEGsVGMPLPGvAVRIVDPETFEELPP--GEDGLILIGGPQVMKGYLGDPEKTAEvikd 1014
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 412 SFAGGWFHTGDLGVLHPDGYAQIKDR----SKdIiisGGENISSIEVEDVLYK--HPAVANVAVVALADEKWGEvpvAFV 485
Cdd:PRK08633 1015 IDGIGWYVTGDKGHLDEDGFLTITDRysrfAK-I---GGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE---KLV 1087
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092482886 486 ELKDDAQVSEEELdqycRERLAG------FKRPKYYVFGELAKTATGKIQKFELRKQAEALF 541
Cdd:PRK08633 1088 VLHTCGAEDVEEL----KRAIKEsglpnlWKPSRYFKVEALPLLGSGKLDLKGLKELALALL 1145
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
34-528 |
8.44e-19 |
|
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: 88.85 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFaphipeikkalPALKIiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewdaialnYTSGT 193
Cdd:cd17652 82 DARPALLLTTPDN-----------LAYVI----------------------------------------------YTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYL-WTLPLFHCNGW--CFAWTIAARGGVNVCLRKFDPKTCFDLIRQER 270
Cdd:cd17652 105 TGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLqFASPSFDASVWelLMALLAGATLVLAPAEELLPGEPLADLLREHR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 271 VGFYCAAPvvhAALANAPAEMKAGIDHpvsAMVAGAAPPEAVLARMEQmGFHMVHVYGLTEvygpSAVCAEkpewdeLSV 350
Cdd:cd17652 185 ITHVTLPP---AALAALPPDDLPDLRT---LVVAGEACPAELVDRWAP-GRRMINAYGPTE----TTVCAT------MAG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 351 EDRAAQKARQG--VRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF--------HT 420
Cdd:cd17652 248 PLPGGGVPPIGrpVPGT---RVYVLD-ARLRPVPPG--VPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmyRT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 421 GDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQ 500
Cdd:cd17652 322 GDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRA 401
|
490 500
....*....|....*....|....*....
gi 1092482886 501 YCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd17652 402 HLAERLPGYMVPAAFVvLDALPLTPNGKL 430
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
34-528 |
1.06e-18 |
|
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: 88.84 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGgvllalnvrletegliyclq 113
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG-------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 hgeaefllvdsefAPHIPeIKKALPALKIIQVNDELGPKdvepfsdieyegflqsaedldnwVLPKDEWDAIALNYTSGT 193
Cdd:cd05945 66 -------------HAYVP-LDASSPAERIREILDAAKPA-----------------------LLIADGDDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAA--LNAIAQslEFDMPKRPVYLWTLPL-FHCN--GWCFAWtiaARGGVNVCLRK---FDPKTCFDL 265
Cdd:cd05945 109 TGRPKGVQISHDNLVsfTNWMLS--DFPLGPGDVFLNQAPFsFDLSvmDLYPAL---ASGATLVPVPRdatADPKQLFRF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAP-VVHAALANAP--AEMKAGIDHpvsAMVAGAAPPEAvLARMEQMGFHMVHVYGLtevYGPS----AV 338
Cdd:cd05945 184 LAEHGITVWVSTPsFAAMCLLSPTftPESLPSLRH---FLFCGEVLPHK-TARALQQRFPDARIYNT---YGPTeatvAV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CAEkpEWDElSVEDRAAQ----KARQGVRntlqgaLTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF- 413
Cdd:cd05945 257 TYI--EVTP-EVLDGYDRlpigYAKPGAK------LVILD-EDGRPVPPG--EKGELVISGPSVSKGYLNNPEKTAAAFf 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 ---AGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKD- 489
Cdd:cd05945 325 pdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPg 404
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092482886 490 DAQVSEEELDQYCRERLAGFKRP-KYYVFGELAKTATGKI 528
Cdd:cd05945 405 AEAGLTKAIKAELAERLPPYMIPrRFVYLDELPLNANGKI 444
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
47-536 |
1.08e-18 |
|
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: 88.64 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 47 WTETYHRCRQMAAALRQN-GADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSE 125
Cdd:cd05937 8 YSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 faphipeikkalpalkiiqvndelgpkdvepfsdieyegflqsaedldnwvlpkdewDAIALNYTSGTTGNPKGVVYHHR 205
Cdd:cd05937 88 ---------------------------------------------------------DPAILIYTSGTTGLPKAAAISWR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 GAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQERVGFYCAAPVVHAAL 284
Cdd:cd05937 111 RTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALsRKFSASQFWKDVRDSGATIIQYVGELCRYL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 285 ANAPAEMKAGiDHPVSAMVAGAAPPEAVLARMEQMGFHMVH-VYGLTEvyGPSAVcaekpewDELSVEDRAAQK-ARQG- 361
Cdd:cd05937 191 LSTPPSPYDR-DHKVRVAWGNGLRPDIWERFRERFNVPEIGeFYAATE--GVFAL-------TNHNVGDFGAGAiGHHGl 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 362 -VRNTLQGALTV--LDPETMEPV--PADGKTI-------GELMFRGNIVMK----GYLKNPAETGKS-----FAGG--WF 418
Cdd:cd05937 261 iRRWKFENQVVLvkMDPETDDPIrdPKTGFCVrapvgepGEMLGRVPFKNReafqGYLHNEDATESKlvrdvFRKGdiYF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKW-GEVPVAFVELKDDAQVSEE- 496
Cdd:cd05937 341 RTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGRAGCAAITLEESSAVPTEf 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092482886 497 ---ELDQYCRERLAGFKRPKYY-VFGELAKTATGKIQKFELRKQ 536
Cdd:cd05937 421 tksLLASLARKNLPSYAVPLFLrLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-530 |
1.51e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 89.84 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPeIKKALPALKIIQVNDELgpkdvepfsdieyEGFlqSAEDLDNWVLPKDEWDAIalnYTSGT 193
Cdd:PRK12467 607 DSGVRLLLTQSHLLAQLP-VPAGLRSLCLDEPADLL-------------CGY--SGHNPEVALDPDNLAYVI---YTSGS 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAA--LNAIAQSLEFdMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRK--FDPKTCFDLIRQE 269
Cdd:PRK12467 668 TGQPKGVAISHGALAnyVCVIAERLQL-AADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDcaRDAEAFAALMADQ 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAPVVHAALANAPAemkAGIDHPVSAMV-AGAAPPEAVLARMEQMGFHMvhvyGLTEVYGPSAVCAEKPEWdEL 348
Cdd:PRK12467 747 GVTVLKIVPSHLQALLQASR---VALPRPQRALVcGGEALQVDLLARVRALGPGA----RLINHYGPTETTVGVSTY-EL 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 349 SVEDRAAQKARQGV--RNTlqgALTVLDPEtMEPVPadGKTIGELMFRGNIVMKGYLKNPAETGKSF-------AGG-WF 418
Cdd:PRK12467 819 SDEERDFGNVPIGQplANL---GLYILDHY-LNPVP--VGVVGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGrLY 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVPVAFV---ELKDDA--QV 493
Cdd:PRK12467 893 RTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQP-GVREAVVLAQPGDAGLQLVAYLvpaAVADGAehQA 971
|
490 500 510
....*....|....*....|....*....|....*...
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQK 530
Cdd:PRK12467 972 TRDELKAQLRQVLPDYMVPAHLLLLDsLPLTPNGKLDR 1009
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
103-458 |
4.62e-18 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 87.86 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 103 LETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPALK-IIQVNDE----------LGPKDVEPFSDIEYEGfLQSAED 171
Cdd:PLN02387 165 LGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLETVKrVIYMDDEgvdsdsslsgSSNWTVSSFSEVEKLG-KENPVD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 172 LDnwvLPKDEwDAIALNYTSGTTGNPKGVVYHHRG-----AALNAIAQSLEfdmpKRPVYLWTLPLFH------------ 234
Cdd:PLN02387 244 PD---LPSPN-DIAVIMYTSGSTGLPKGVMMTHGNivatvAGVMTVVPKLG----KNDVYLAYLPLAHilelaaesvmaa 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 235 ---CNGWCFAWTIA-------------------------------ARGGVnvcLRKFDP-----KTCFDLIRQERV---- 271
Cdd:PLN02387 316 vgaAIGYGSPLTLTdtsnkikkgtkgdasalkptlmtavpaildrVRDGV---RKKVDAkgglaKKLFDIAYKRRLaaie 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 272 GFYCAAPVVHAALANAPA--EMKAGIDHPVSAMVAGAAPPEAVLARMEQ--MGFHMVHVYGLTEVygpsavCAEK--PEW 345
Cdd:PLN02387 393 GSWFGAWGLEKLLWDALVfkKIRAVLGGRIRFMLSGGAPLSGDTQRFINicLGAPIGQGYGLTET------CAGAtfSEW 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 346 DELSVedraaqkARQG---------VRNTLQGALTVLDpetmEPVPAdgktiGELMFRGNIVMKGYLKNPAETGKSF--- 413
Cdd:PLN02387 467 DDTSV-------GRVGpplpccyvkLVSWEEGGYLISD----KPMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYkvd 530
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1092482886 414 --AGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENISSIEVEDVL 458
Cdd:PLN02387 531 erGMRWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAAL 578
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-516 |
7.31e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.71 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 32 FGDDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYC 111
Cdd:PRK12316 4564 TPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYM 4643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 112 LQHGEAEFLLVDSEFAPHIPeIKKALPALKIIQVNDELGPKDVEPfsdieyegflQSAEDLDN--WVLpkdewdaialnY 189
Cdd:PRK12316 4644 MEDSGAALLLTQSHLLQRLP-IPDGLASLALDRDEDWEGFPAHDP----------AVRLHPDNlaYVI-----------Y 4701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 190 TSGTTGNPKGVVYHHrGAALNAIAQSLEF--DMPKRPVYLWTLPLFHCNGWCFAWTIAArgGVNVCLRK---FDPKTCFD 264
Cdd:PRK12316 4702 TSGSTGRPKGVAVSH-GSLVNHLHATGERyeLTPDDRVLQFMSFSFDGSHEGLYHPLIN--GASVVIRDdslWDPERLYA 4778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 265 LIRQERVGFYCAAPVVHAALANAPAEmkAGIDHPVSAMVAGAappEAVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPE 344
Cdd:PRK12316 4779 EIHEHRVTVLVFPPVYLQQLAEHAER--DGEPPSLRVYCFGG---EAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLL 4853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 345 WDEL--SVEDRAAQKARQGVRNTlqgALTVLDPEtMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSF--------A 414
Cdd:PRK12316 4854 WKARdgDACGAAYMPIGTPLGNR---SGYVLDGQ-LNPLPVGV--AGELYLGGEGVARGYLERPALTAERFvpdpfgapG 4927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 415 GGWFHTGDLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVPVAFVE 486
Cdd:PRK12316 4928 GRLYRTGDLARYRADGvidYLgrvdhQVKIR--------GFRIELGEIEARLREHP-AVREAVVIAQEGAVGKQLVGYVV 4998
|
490 500 510
....*....|....*....|....*....|...
gi 1092482886 487 LKDDAQVSEEELDQYCRERL-AGFKR--PKYYV 516
Cdd:PRK12316 4999 PQDPALADADEAQAELRDELkAALRErlPEYMV 5031
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-530 |
7.57e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK12467 1589 EAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIE 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPEIKKaLPALKIIQVNDEL-GPKDVEPfsdieyegflQSAEDLDN--WVLpkdewdaialnYT 190
Cdd:PRK12467 1669 DSGIELLLTQSHLQARLPLPDG-LRSLVLDQEDDWLeGYSDSNP----------AVNLAPQNlaYVI-----------YT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHrGAALN---AIAQSLEFDmPKRPVYLWTLPLFHCNGWCFAWTIAArgGVNVCLRKF----DPKTCF 263
Cdd:PRK12467 1727 SGSTGRPKGAGNRH-GALVNrlcATQEAYQLS-AADVVLQFTSFAFDVSVWELFWPLIN--GARLVIAPPgahrDPEQLI 1802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 264 DLIRQERVGFYCAAPVVHAALanapAEMKAGIDHPVS--AMVAG--AAPPEAVLARMEQMGFHmvhvyGLTEVYGPSAVC 339
Cdd:PRK12467 1803 QLIERQQVTTLHFVPSMLQQL----LQMDEQVEHPLSlrRVVCGgeALEVEALRPWLERLPDT-----GLFNLYGPTETA 1873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AEKPEW--DELSVEDRAAQKARQGVRNTlqgALTVLDpETMEPVPAdgKTIGELMFRGNIVMKGYLKNPAETGKSF---- 413
Cdd:PRK12467 1874 VDVTHWtcRRKDLEGRDSVPIGQPIANL---STYILD-ASLNPVPI--GVAGELYLGGVGLARGYLNRPALTAERFvadp 1947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 ----AGGWFHTGDLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVP 481
Cdd:PRK12467 1948 fgtvGSRLYRTGDLARYRADGvieYLgridhQVKIR--------GFRIELGEIEARLREQG-GVREAVVIAQDGANGKQL 2018
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 482 VAFV--------ELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQK 530
Cdd:PRK12467 2019 VAYVvptdpglvDDDEAQVALRAILKNHLKASLPEYMVPAHLVFLArMPLTPNGKLDR 2076
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
305-539 |
1.11e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 85.43 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 305 GAAPP-EAVLARMEQMGFHMVHVYGLTEVygPSAVCAEKPEwDELSVEDRAAQkarqgvrnTLQGA-LTVLDPetmepvp 382
Cdd:PRK07445 238 GGAPAwPSLLEQARQLQLRLAPTYGMTET--ASQIATLKPD-DFLAGNNSSGQ--------VLPHAqITIPAN------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 383 adgkTIGELMFRGNIVMKGY---LKNPAetgksfagGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLY 459
Cdd:PRK07445 300 ----QTGNITIQAQSLALGYypqILDSQ--------GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAIL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 460 KHPAVANVAVVALADEKWGEVPVAFVELKDDaQVSEEELDQYCRERLAGFKRPKYYV-FGELAKTATGKIQKFELRKQAE 538
Cdd:PRK07445 368 ATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIpVPQLPRNPQGKINRQQLQQIAV 446
|
.
gi 1092482886 539 A 539
Cdd:PRK07445 447 Q 447
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
49-534 |
1.61e-16 |
|
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: 82.54 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 49 ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFA- 127
Cdd:cd05968 96 ELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTr 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 128 --------PHIPEIKKALPALKIIQVNDELG-PKDVEPFSDIEYEGFLQSAEDLDNWVLPKDEWDAIalnYTSGTTGNPK 198
Cdd:cd05968 176 rgrevnlkEEADKACAQCPTVEKVVVVRHLGnDFTPAKGRDLSYDEEKETAGDGAERTESEDPLMII---YTSGTTGKPK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 199 GVVYHHRGAALNAiAQSLEFDMPKRP--VYLWTLPLfhcnGWCFA-WTIAarGGVNVCLRKF---------DPKTCFDLI 266
Cdd:cd05968 253 GTVHVHAGFPLKA-AQDMYFQFDLKPgdLLTWFTDL----GWMMGpWLIF--GGLILGATMVlydgapdhpKADRLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAPVVHAALANAPAEMKAGIDHpVSAMVAGAA--P--PEAVLARMEQMGFH---MVHVYGLTEVYG----- 334
Cdd:cd05968 326 EDHEITHLGLSPTLIRALKPRGDAPVNAHDL-SSLRVLGSTgePwnPEPWNWLFETVGKGrnpIINYSGGTEISGgilgn 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 335 -------PSAVCAEKPewdelsvedraAQKArqgvrntlqgalTVLDpETMEPVPadgKTIGELMFRGNIV--MKGYLKN 405
Cdd:cd05968 405 vlikpikPSSFNGPVP-----------GMKA------------DVLD-ESGKPAR---PEVGELVLLAPWPgmTRGFWRD 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 406 PA---ETGKS-FAGGWFHtGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVP 481
Cdd:cd05968 458 EDrylETYWSrFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAI 536
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1092482886 482 VAFVELKDDAQVSE---EELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd05968 537 VCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFvKDLPKTRNAKVMRRVIR 593
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
134-439 |
9.01e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 80.41 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 134 KKALPALKIIQVnDELgPKDVE-------PFSDIEYEGflQSAEDLDNWVLPKDEwDAIAL-NYTSGTTGNPKGVVYHHR 205
Cdd:PTZ00216 213 SGGMPNTTIIYL-DSL-PASVDtegcrlvAWTDVVAKG--HSAGSHHPLNIPENN-DDLALiMYTSGTTGDPKGVMHTHG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 206 G--AALNAIAQSL-EFDMPKRP--VYLWTLPLFHCngwcFAWTIA----ARGgVNVC-----------------LRKFDP 259
Cdd:PTZ00216 288 SltAGILALEDRLnDLIGPPEEdeTYCSYLPLAHI----MEFGVTniflARG-ALIGfgsprtltdtfarphgdLTEFRP 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 K------TCFDLIRQ------------ERVGFYCAAPVVHAALanapaemKAGIDHP-----------------VSAMVA 304
Cdd:PTZ00216 363 VfligvpRIFDTIKKaveaklppvgslKRRVFDHAYQSRLRAL-------KEGKDTPywnekvfsapravlggrVRAMLS 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 305 GAAPPEA--------VLARMEQmGfhmvhvYGLTEvygpSAVCAEKPEWDELSVEDrAAQkarqgVRNTLQGALtvLDPE 376
Cdd:PTZ00216 436 GGGPLSAatqefvnvVFGMVIQ-G------WGLTE----TVCCGGIQRTGDLEPNA-VGQ-----LLKGVEMKL--LDTE 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 377 ----TMEPVPAdgktiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSK 439
Cdd:PTZ00216 497 eykhTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
34-535 |
9.86e-16 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 79.28 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd17653 12 DAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLvdsefaphipeikkalpalkiiqvndelgpkdvepfsdieyegFLQSAEDLdnwvlpkdewdAIALnYTSGT 193
Cdd:cd17653 92 TSGATLLL-------------------------------------------TTDSPDDL-----------AYII-FTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGaALNAIAQSlEFDMPKRP---VYLWTLPLFhcngWCFAWTIAA---RGGVnVCLRKfDPKTCFDLIR 267
Cdd:cd17653 117 TGIPKGVMVPHRG-VLNYVSQP-PARLDVGPgsrVAQVLSIAF----DACIGEIFStlcNGGT-LVLAD-PSDPFAHVAR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QerVGFYCAAPVVhaaLANAPAEMKAGIDhpvSAMVAGAAPPEAVLARMEQmGFHMVHVYGLTEVygpSAVCAEKpewdE 347
Cdd:cd17653 189 T--VDALMSTPSI---LSTLSPQDFPNLK---TIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTEC---TISSTMT----E 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 348 LSVEDRAAqkarqgVRNTLQGA-LTVLDPETmEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWFH------- 419
Cdd:cd17653 253 LLPGQPVT------IGKPIPNStCYILDADL-QPVPEG--VVGEICISGVQVARGYLGNPALTASKFVPDPFWpgsrmyr 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 420 TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADekwgEVPVAFVELKDdaqVSEEELD 499
Cdd:cd17653 324 TGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVN----GRLVAFVTPET---VDVDGLR 396
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092482886 500 QYCRERLAGFKRP-KYYVFGELAKTATGKIQKFELRK 535
Cdd:cd17653 397 SELAKHLPSYAVPdRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-535 |
2.84e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.62 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPeIKKALPALkiiqvndelgpkDVEPfsDIEYEGFLQSAedldnwvlPKDEWDAIALN---YT 190
Cdd:PRK12316 2098 DSGAALLLTQRHLLERLP-LPAGVARL------------PLDR--DAEWADYPDTA--------PAVQLAGENLAyviYT 2154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 191 SGTTGNPKGVVYHHRGAA--LNAIAQSLEFDMPKRPVYLWTlplFHCNGWCFAWTIAARGGVNVCLRK---FDPKTCFDL 265
Cdd:PRK12316 2155 SGSTGLPKGVAVSHGALVahCQAAGERYELSPADCELQFMS---FSFDGAHEQWFHPLLNGARVLIRDdelWDPEQLYDE 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAALANapAEMKAGIDHPVSAMVAGAappEAVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPEW 345
Cdd:PRK12316 2232 MERHGVTILDFPPVYLQQLAE--HAERDGRPPAVRVYCFGG---EAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLW 2306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 346 DELSVEDRAAQKARQGvrnTLQGALT--VLDpETMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSF--------AG 415
Cdd:PRK12316 2307 KCRPQDPCGAAYVPIG---RALGNRRayILD-ADLNLLAPGM--AGELYLGGEGLARGYLNRPGLTAERFvpdpfsasGE 2380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVPVAFVELKDDAQVSE 495
Cdd:PRK12316 2381 RLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP-AVREAVVVAQDGASGKQLVAYVVPDDAAEDLL 2459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1092482886 496 EELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRK 535
Cdd:PRK12316 2460 AELRAWLAARLPAYMVPAHWVVLErLPLNPNGKLDRKALPK 2500
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
187-539 |
3.49e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 77.77 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 187 LNYTSGTTGNPKGV--VYHHRGAALNAIAQSLEFDMPKRPVYLwtLPLFHCNGW-CfaWTIAA--RGGVNVCLRKFDPKT 261
Cdd:PRK08308 106 LQYSSGTTGEPKLIrrSWTEIDREIEAYNEALNCEQDETPIVA--CPVTHSYGLiC--GVLAAltRGSKPVIITNKNPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 CFDLIRQERVGFYCAAPVVHAALANAPAEmKAGIDhpvSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVyGPSAVCAE 341
Cdd:PRK08308 182 ALNILRNTPQHILYAVPLMLHILGRLLPG-TFQFH---AVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEA-GCVSICPD 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 342 KPEWDELSVedraaqkarqgvrntlqgaltvldpetmePVPADGKTIGELMfrgnivmkgylKNPAETGKSFAGGWFHTG 421
Cdd:PRK08308 257 MKSHLDLGN-----------------------------PLPHVSVSAGSDE-----------NAPEEIVVKMGDKEIFTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGE-VPVAFVElkdDAQVSEEELDQ 500
Cdd:PRK08308 297 DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVIS---HEEIDPVQLRE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1092482886 501 YCRERLAGFKRPKYYVF-GELAKTATGKIQKfELRKQAEA 539
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESvTEIPKNANGKVSR-KLLELGEV 412
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
45-535 |
3.70e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 78.52 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 45 QNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDS 124
Cdd:PLN02614 80 QTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 125 EfapHIPEIKKALP-ALKIIQVNDELGPKDVEPFSDIE--------YEGFLQSAEDlDNWVLP-KDEWDAIALNYTSGTT 194
Cdd:PLN02614 160 K---KISELFKTCPnSTEYMKTVVSFGGVSREQKEEAEtfglviyaWDEFLKLGEG-KQYDLPiKKKSDICTIMYTSGTT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 195 GNPKGVVYHHRG-----AALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGvNVCLRKFDPKTCFDLIRQE 269
Cdd:PLN02614 236 GDPKGVMISNESivtliAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQHGA-AIGFWRGDVKLLIEDLGEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 270 RVGFYCAAPVV-------------------------------------HAALANAP-------AEMKAGIDHPVSAMVAG 305
Cdd:PLN02614 315 KPTIFCAVPRVldrvysglqkklsdggflkkfvfdsafsykfgnmkkgQSHVEASPlcdklvfNKVKQGLGGNVRIILSG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 306 AAPPEAVLARMEQM--GFHMVHVYGLTEvyGPSAVCAEKPewDELsvedraaqkarqGVRNTLQGALTVLDPEtMEPVP- 382
Cdd:PLN02614 395 AAPLASHVESFLRVvaCCHVLQGYGLTE--SCAGTFVSLP--DEL------------DMLGTVGPPVPNVDIR-LESVPe 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 383 ----ADGKTI-GELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENISSIEVED 456
Cdd:PLN02614 458 meydALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIEN 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 457 VLYKhpavanvavVALADEKW--GEVPVAF-VELKDDAQVSEE----------ELDQYCRErlagfKRPKYYVFGELAKT 523
Cdd:PLN02614 538 IYGE---------VQAVDSVWvyGNSFESFlVAIANPNQQILErwaaengvsgDYNALCQN-----EKAKEFILGELVKM 603
|
570
....*....|...
gi 1092482886 524 AT-GKIQKFELRK 535
Cdd:PLN02614 604 AKeKKMKGFEIIK 616
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
34-540 |
3.71e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 79.23 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK12316 3072 DAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLE 3151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAphipeikkaLPALKIIQVndelgpKDVEPFSDIEYEgflqsaEDLDNWVLPKDEWDAIalnYTSGT 193
Cdd:PRK12316 3152 DSGAQLLLSQSHLR---------LPLAQGVQV------LDLDRGDENYAE------ANPAIRTMPENLAYVI---YTSGS 3207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPL-FHCNGWCFAWTIAArgGVNVCLRK----FDPKTCFDLIRQ 268
Cdd:PRK12316 3208 TGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFsFDVFVEELFWPLMS--GARVVLAGpedwRDPALLVELINS 3285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 269 ERVGFYCAAPvvhAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMVHVYGLTEVYGPSAVcaekpeWDeL 348
Cdd:PRK12316 3286 EGVDVLHAYP---SMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITVTH------WQ-C 3355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 349 SVEDRAAQKARQGVRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF-------HTG 421
Cdd:PRK12316 3356 VEEGKDAVPIGRPIANR---ACYILD-GSLEPVPVG--ALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlyRTG 3429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALAdekwGEVPVAFVELKDDAQVSEEELDQY 501
Cdd:PRK12316 3430 DLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAH 3505
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1092482886 502 CRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQAEAL 540
Cdd:PRK12316 3506 LKASLPEYMVPAHLLFLErMPLTPNGKLDRKALPRPDAAL 3545
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-462 |
6.13e-15 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 77.12 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 43 IRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQhgeaefllv 122
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 123 dsefaphipeikkalpalkiiqvndelgpkDVEPfsdieyEGFLQsaedldnwvLPKDEWDAiALNYTSGTTGNPKGVVY 202
Cdd:cd05910 72 ------------------------------EAEP------DAFIG---------IPKADEPA-AILFTSGSTGTPKGVVY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 203 HHR--GAALNAIAQSleFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVV 280
Cdd:cd05910 106 RHGtfAAQIDALRQL--YGIRPGEVDLATFPLFALFGPALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPAL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 281 HAALANAPAEmkagIDHPVSAM----VAGAAPPEAVLARMEQM---GFHMVHVYGLTEVYGPSAVcaekpEWDELSVEDR 353
Cdd:cd05910 184 LERVARYCAQ----HGITLPSLrrvlSAGAPVPIALAARLRKMlsdEAEILTPYGATEALPVSSI-----GSRELLATTT 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 354 AAQKARQG--VRNTLQGALTVLDPETMEPVPADGKT-------IGELMFRGNIVMKGYLKNPAETG--KSFAGG---WFH 419
Cdd:cd05910 255 AATSGGAGtcVGRPIPGVRVRIIEIDDEPIAEWDDTlelprgeIGEITVTGPTVTPTYVNRPVATAlaKIDDNSegfWHR 334
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1092482886 420 TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHP 462
Cdd:cd05910 335 MGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHP 377
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
34-534 |
1.03e-14 |
|
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: 76.25 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVdsefapHIPEikkalpalkiiqvndelgpkdvepfsdieyegflQSAedldnWVLpkdewdaialnYTSGT 193
Cdd:cd17649 82 DSGAGLLLT------HHPR----------------------------------QLA-----YVI-----------YTSGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPL----FHcNGWCFAWTIAARggvnVCLRK----FDPKTCFDL 265
Cdd:cd17649 106 TGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFnfdgAH-EQLLPPLICGAC----VVLRPdelwASADELAEM 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 266 IRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAG--AAPPEaVLARMEQMGFHMVHVYGLTEVYGPSAVCaekp 343
Cdd:cd17649 181 VRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYIFGgeALSPE-LLRRWLKAPVRLFNAYGPTEATVTPLVW---- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 344 ewdelsveDRAAQKARQGVRNTLQGALT-----VLDPEtMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSF----- 413
Cdd:cd17649 256 --------KCEAGAARAGASMPIGRPLGgrsayILDAD-LNPVPVGV--TGELYIGGEGLARGYLGRPELTAERFvpdpf 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 414 --AGG-WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVPVAFVELKDD 490
Cdd:cd17649 325 gaPGSrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHP-GVREAAVVALDGAGGKQLVAYVVLRAA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1092482886 491 AQVSE--EELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELR 534
Cdd:cd17649 404 AAQPElrAQLRTALRASLPDYMVPAHLVFlARLPLTPNGKLDRKALP 450
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
453-527 |
1.31e-14 |
|
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: 68.73 E-value: 1.31e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 453 EVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGK 527
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFvDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
34-517 |
1.55e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.12 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 34 DDLAIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQ 113
Cdd:PRK12467 3110 EAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIE 3189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 114 HGEAEFLLVDSEFAPHIPeIKKALPALKIIQVndelgpkDVEPFSDieyegflqsaEDLDNWVLPKDEWDAIalnYTSGT 193
Cdd:PRK12467 3190 DSGVKLLLTQAHLLEQLP-APAGDTALTLDRL-------DLNGYSE----------NNPSTRVMGENLAYVI---YTSGS 3248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAA--LNAIAQSLEFDMPKRpVYLWTLPLFHCNGWCFAWTIAARGGVNVCL-RKFDPKTCFDLIRQER 270
Cdd:PRK12467 3249 TGKPKGVGVRHGALAnhLCWIAEAYELDANDR-VLLFMSFSFDGAQERFLWTLICGGCLVVRDnDLWDPEELWQAIHAHR 3327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 271 VGFYCAAPvvhAALANAPAEMKAGIDHPVSAMV-AGAAPPEAVLARMEQmgfHMVHVYgLTEVYGPSAVCAEKPEWDELS 349
Cdd:PRK12467 3328 ISIACFPP---AYLQQFAEDAGGADCASLDIYVfGGEAVPPAAFEQVKR---KLKPRG-LTNGYGPTEAVVTVTLWKCGG 3400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 350 VEDRAAQKARQGvRNTLQGALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF-------AGG-WFHTG 421
Cdd:PRK12467 3401 DAVCEAPYAPIG-RPVAGRSIYVLD-GQLNPVPVG--VAGELYIGGVGLARGYHQRPSLTAERFvadpfsgSGGrLYRTG 3476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 422 DLGVLHPDG---YA-----QIKDRskdiiisgGENISSIEVEDVLYKHPaVANVAVVALADEKWGEVPVAFVELKDDAQV 493
Cdd:PRK12467 3477 DLARYRADGvieYLgridhQVKIR--------GFRIELGEIEARLLQHP-SVREAVVLARDGAGGKQLVAYVVPADPQGD 3547
|
490 500
....*....|....*....|....
gi 1092482886 494 SEEELDQYCRERLAGFKRPKYYVF 517
Cdd:PRK12467 3548 WRETLRDHLAASLPDYMVPAQLLV 3571
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
53-536 |
1.99e-14 |
|
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: 75.79 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALRQNGADR-GTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIP 131
Cdd:cd05938 14 RSNQAARALLAHAGLRpGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPELQEAVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 132 EIkkaLPALKIIQVNDELGPKDVEPfSDIEyeGFLQSAEDLDNWVLPKDEWDAIALN------YTSGTTGNPK-GVVYHH 204
Cdd:cd05938 94 EV---LPALRADGVSVWYLSHTSNT-EGVI--SLLDKVDAASDEPVPASLRAHVTIKspalyiYTSGTTGLPKaARISHL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 205 RGAALNAIAQSleFDMPKRPVYLWTLPLFHCNGW------CFAwtiaaRGGVNVCLRKFDPKTCFDLIRQERVGFYCAAP 278
Cdd:cd05938 168 RVLQCSGFLSL--CGVTADDVIYITLPLYHSSGFllgiggCIE-----LGATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 279 VVHAALANAPaEMKAGIDHPVS-AMVAGAAPP--EAVLARMEQMgfHMVHVYGLTEvygpsavcaekpewDELSVEDRAA 355
Cdd:cd05938 241 ELLRYLCNQP-QSPNDRDHKVRlAIGNGLRADvwREFLRRFGPI--RIREFYGSTE--------------GNIGFFNYTG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 356 QKARQGVRNTLQG-----ALTVLDPETMEPV-PADGKTI----GELmfrGNIVMK--------GYLKNPAETGKS----- 412
Cdd:cd05938 304 KIGAVGRVSYLYKllfpfELIKFDVEKEEPVrDAQGFCIpvakGEP---GLLVAKitqqspflGYAGDKEQTEKKllrdv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 413 FAGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVL-----------YKHPAVANVavvaladekwGE 479
Cdd:cd05938 381 FKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLglldflqevnvYGVTVPGHE----------GR 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 480 VPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFELRKQ 536
Cdd:cd05938 451 IGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDsLEITGTFKQQKVRLVEE 508
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
189-528 |
2.53e-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: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGA---ALNAIAQ-------------SLEFDMPKRPVYlwtlPLfhcngWCFAWTIAARGGvnv 252
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQSLvnlSHGLIKEygitssdrvlqfaSIAFDVAAEEIY----VT-----LLSGATLVLRPE--- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 253 cLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAappEAVLARMEQMGFHMV-------H 325
Cdd:cd17644 181 -EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGG---EAVQPELVRQWQKNVgnfiqliN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 326 VYGLTEVYGPSAVCaekpewDELSVEDRAAQKARQG--VRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYL 403
Cdd:cd17644 257 VYGPTEATIAATVC------RLTQLTERNITSVPIGrpIANT---QVYILD-ENLQPVPVG--VPGELHIGGVGLARGYL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 404 KNPAETGKSFAGGWFH---------TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALAD 474
Cdd:cd17644 325 NRPELTAEKFISHPFNsseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRED 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1092482886 475 EKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPKYYVF-GELAKTATGKI 528
Cdd:cd17644 405 QPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVlEELPLTPNGKI 459
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
183-538 |
5.09e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 74.45 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIA-LNYTSGTTGNPKGVVYHHRGAALN--AIAQSLEFDMPKRpvYLWTLPLFHCNGWCFAWTIAARGGVNvclRKFDP 259
Cdd:cd05908 106 DELAfIQFSSGSTGDPKGVMLTHENLVHNmfAILNSTEWKTKDR--ILSWMPLTHDMGLIAFHLAPLIAGMN---QYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 KTCFdlIRQERVGFYCAAPvvHAA-------------LANAPAEMKAGID-HPVSAMVAGAAP--PEAVLARMEQMGFH- 322
Cdd:cd05908 181 TRLF--IRRPILWLKKASE--HKAtivsspnfgykyfLKTLKPEKANDWDlSSIRMILNGAEPidYELCHEFLDHMSKYg 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 323 -----MVHVYGLTEvygpSAVCAEKPEWDE----LSVEDRAAQ--KARQGVRNTLQGALTVLD-------------PETM 378
Cdd:cd05908 257 lkrnaILPVYGLAE----ASVGASLPKAQSpfktITLGRRHVThgEPEPEVDKKDSECLTFVEvgkpidetdiricDEDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 379 EPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENI-------S 450
Cdd:cd05908 333 KILPDG--YIGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVyphdierI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 451 SIEVEDVLYKHPAVANVAVVALADEkwgEVpVAFVELKDdaqvSEEELDQYCRE------RLAGFKRPKYYVFGELAKTA 524
Cdd:cd05908 410 AEELEGVELGRVVACGVNNSNTRNE---EI-FCFIEHRK----SEDDFYPLGKKikkhlnKRGGWQINEVLPIRRIPKTT 481
|
410
....*....|....
gi 1092482886 525 TGKIQKFELRKQAE 538
Cdd:cd05908 482 SGKVKRYELAQRYQ 495
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
183-536 |
8.11e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 72.77 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNY-TSGTTGNPKGVVYhhRGAALNAIAQSLEFDMPKRPVYLWTLPLFHcngwcfawtIAargGVNVCLRKF---- 257
Cdd:PRK07824 35 DDVALVVaTSGTTGTPKGAML--TAAALTASADATHDRLGGPGQWLLALPAHH---------IA---GLQVLVRSViags 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 258 DPkTCFDLIRqervGFYCAApvvhaaLANAPAEMKAG--------------IDHPVSA---------MVAGAAPPEAVLA 314
Cdd:PRK07824 101 EP-VELDVSA----GFDPTA------LPRAVAELGGGrrytslvpmqlakaLDDPAATaalaeldavLVGGGPAPAPVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 315 RMEQMGFHMVHVYGLTEVYGPsavCaekpewdelsvedraaqkarqgvrntlqgaltVLDPetmepVPADGKTI----GE 390
Cdd:PRK07824 170 AAAAAGINVVRTYGMSETSGG---C--------------------------------VYDG-----VPLDGVRVrvedGR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 391 LMFRGNIVMKGYlKNPAETGKSFAGGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVV 470
Cdd:PRK07824 210 IALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1092482886 471 ALADEKWGEVPVAFVELKDDAQVSEEELDQYCRERLAGFKRPK-YYVFGELAKTATGKIQKFELRKQ 536
Cdd:PRK07824 288 GLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPReLHVVDELPRRGIGKVDRRALVRR 354
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
189-540 |
8.49e-14 |
|
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: 73.73 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWtlplfhcngwcFA-----------WTIAARGGVnVCL--- 254
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ-----------FAsytfdvsileiFTTLAAGGC-LCIpse 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 255 --RKFDPktcFDLIRQERVGFYCAAPVVhAALANaPAEmkagIDHPVSAMVAGAAPPEAVLARMEQmGFHMVHVYGLTEv 332
Cdd:cd05918 181 edRLNDL---AGFINRLRVTWAFLTPSV-ARLLD-PED----VPSLRTLVLGGEALTQSDVDTWAD-RVRLINAYGPAE- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 333 ygpSAVCAekpewdeLSVEDRAAQKARqgvrN---TLQGALTVLDPETME-PVPADGktIGELMFRGNIVMKGYLKNPAE 408
Cdd:cd05918 250 ---CTIAA-------TVSPVVPSTDPR----NigrPLGATCWVVDPDNHDrLVPIGA--VGELLIEGPILARGYLNDPEK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 409 TGKSF--AGGW------------FHTGDLGVLHPDG---Y-----AQIKDRSKDIIISggenissiEVEDVLYKHPAVAN 466
Cdd:cd05918 314 TAAAFieDPAWlkqegsgrgrrlYRTGDLVRYNPDGsleYvgrkdTQVKIRGQRVELG--------EIEHHLRQSLPGAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 467 VAV---VALADEKWGEVPVAFVELK-----------------DDAQVSEEELDQYCRERLAGFKRPKYYV-FGELAKTAT 525
Cdd:cd05918 386 EVVvevVKPKDGSSSPQLVAFVVLDgsssgsgdgdslflepsDEFRALVAELRSKLRQRLPSYMVPSVFLpLSHLPLTAS 465
|
410
....*....|....*
gi 1092482886 526 GKIQKFELRKQAEAL 540
Cdd:cd05918 466 GKIDRRALRELAESL 480
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
20-448 |
1.55e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 73.22 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 20 TPIDFLVRAHEVFGDDLAIVH--------GSIRQ-NWTETYHRCRQMAAALRQNGAdRGTTVATLLHNTPAMVEAGFGVP 90
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRFldfsterdGVARDlTWSQFGARNRAVGARLQQVTK-PGDRVAILAPQNLDYLIAFFGAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 91 MSGGV---LLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPEIKKALPAL---KIIQVN---DELGpkdvepfsdie 161
Cdd:PRK07769 101 YAGRIavpLFDPAEPGHVGRLHAVLDDCTPSAILTTTDSAEGVRKFFRARPAKerpRVIAVDavpDEVG----------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 162 yegflqsaedlDNWVLPKDEWDAIA-LNYTSGTTGNPKGVVYHHRGAALNAIA--QSLEFDMPKRPVYlWtLPLFHCNGW 238
Cdd:PRK07769 170 -----------ATWVPPEANEDTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQviDALEGQEGDRGVS-W-LPFFHDMGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 239 CFAwTIAARGGVNVCL---RKFDPKTcFDLIRQ------ERVGFYCAAP---VVHAALANAPAEMKAGID-HPVSAMVAG 305
Cdd:PRK07769 237 ITV-LLPALLGHYITFmspAAFVRRP-GRWIRElarkpgGTGGTFSAAPnfaFEHAAARGLPKDGEPPLDlSNVKGLLNG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 306 AAPPEAvlARMEQMgFHMVHVYGLT-EVYGPSAVCAEK-------PEWDELSV--EDRAAQKARQGVR--NTLQGALT-- 371
Cdd:PRK07769 315 SEPVSP--ASMRKF-NEAFAPYGLPpTAIKPSYGMAEAtlfvsttPMDEEPTViyVDRDELNAGRFVEvpADAPNAVAqv 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 372 ------------VLDPETMEPVPaDGKtIGELMFRGNIVMKGYLKNPAETGKSF------------AGG------WFHTG 421
Cdd:PRK07769 392 sagkvgvsewavIVDPETASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshAEGapddalWVRTG 469
|
490 500
....*....|....*....|....*..
gi 1092482886 422 DLGVLHpDGYAQIKDRSKDIIISGGEN 448
Cdd:PRK07769 470 DYGVYF-DGELYITGRVKDLVIIDGRN 495
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
137-460 |
2.48e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 72.82 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 137 LPALKIIQV---NDELGPK-------DVEPFSDIEYEGflqsAEDLDNWVLPKDEwDAIALNYTSGTTGNPKGVVYHHRG 206
Cdd:PLN02736 171 IPSVRLIVVvggADEPLPSlpsgtgvEIVTYSKLLAQG----RSSPQPFRPPKPE-DVATICYTSGTTGTPKGVVLTHGN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 207 AALNAIAQSLEFDMPKRPVYLWTLPLFHcngwcfawtIAAR--------GGVNVCLRKFDPKTCFDLIRQERVGFYCAAP 278
Cdd:PLN02736 246 LIANVAGSSLSTKFYPSDVHISYLPLAH---------IYERvnqivmlhYGVAVGFYQGDNLKLMDDLAALRPTIFCSVP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 279 ----VVHAALANA----------------------------PAEM---------KAGIDHPVSAMVAGAAP--PEAvlar 315
Cdd:PLN02736 317 rlynRIYDGITNAvkesgglkerlfnaaynakkqalengknPSPMwdrlvfnkiKAKLGGRVRFMSSGASPlsPDV---- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 316 MEQM----GFHMVHVYGLTE-----------------VYGPSAVCAEK----PEWDELSvEDRaaqkarqgvrntlqgal 370
Cdd:PLN02736 393 MEFLricfGGRVLEGYGMTEtscvisgmdegdnlsghVGSPNPACEVKlvdvPEMNYTS-EDQ----------------- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 371 tvldpetmePVPAdgktiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGEN 448
Cdd:PLN02736 455 ---------PYPR-----GEICVRGPIIFKGYYKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEY 520
|
410
....*....|..
gi 1092482886 449 ISSIEVEDVLYK 460
Cdd:PLN02736 521 IAPEKIENVYAK 532
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
416-538 |
4.01e-13 |
|
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: 71.82 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE 495
Cdd:cd05966 469 GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD 548
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1092482886 496 E---ELDQYCRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQAE 538
Cdd:cd05966 549 ElrkELRKHVRKEIGPIATPDKIQFvPGLPKTRSGKIMRRILRKIAA 595
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
178-457 |
4.01e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 71.72 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 178 PKDEWDAIALNYTSGTTGNPKGVVYHhRGAALN---AIAQSLEFDMPKRPVYLWtLPLFHCNGWCFAWTiAARGGVNVCL 254
Cdd:PRK05851 148 PPDSGGPAVLQGTAGSTGTPRTAILS-PGAVLSnlrGLNARVGLDAATDVGCSW-LPLYHDMGLAFLLT-AALAGAPLWL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 255 RkfdPKTCF--------DLIRQERVGfYCAAPVVHAALANAPAEMKAGIDhpVSAM---VAGAAPP-----EAVLARMEQ 318
Cdd:PRK05851 225 A---PTTAFsaspfrwlSWLSDSRAT-LTAAPNFAYNLIGKYARRVSDVD--LGALrvaLNGGEPVdcdgfERFATAMAP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 319 MGFH---MVHVYGLTEvyGPSAVCAEKP----EWDELSVED-RAAQK-ARQGvrNTLQGALTVLDPeTMEPVPADGKTIG 389
Cdd:PRK05851 299 FGFDagaAAPSYGLAE--STCAVTVPVPgiglRVDEVTTDDgSGARRhAVLG--NPIPGMEVRISP-GDGAAGVAGREIG 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 390 ELMFRGNIVMKGYL-KNPAEtgksfAGGWFHTGDLGVLHPDGYAqIKDRSKDIIISGGENISSIEVEDV 457
Cdd:PRK05851 374 EIEIRGASMMSGYLgQAPID-----PDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERV 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
53-535 |
4.87e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 71.57 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEG-------LIYCLQHGEAEFLLVDSE 125
Cdd:PRK09192 58 RAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGresyiaqLRGMLASAQPAAIITPDE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 126 FAPHIPEIKKALPALKIIQvNDELgpkDVEPFSDIEyegflqsaedldnwvLPKDEWDAIA-LNYTSGTTGNPKGVVYHH 204
Cdd:PRK09192 138 LLPWVNEATHGNPLLHVLS-HAWF---KALPEADVA---------------LPRPTPDDIAyLQYSSGSTRFPRGVIITH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 205 RG--AALNAIAQS-LEFDMPKRPVYlWtLPLFHCNGW--CFAWTIAARGGVNVcLRKFD----PKTCFDLIRQERvGFYC 275
Cdd:PRK09192 199 RAlmANLRAISHDgLKVRPGDRCVS-W-LPFYHDMGLvgFLLTPVATQLSVDY-LPTRDfarrPLQWLDLISRNR-GTIS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 276 AAPVVHAALANAPAEMKAGIDHPVSA-MVAG-------AAPPEAVLARMEQMGFH---MVHVYGLTEV-----YGP--SA 337
Cdd:PRK09192 275 YSPPFGYELCARRVNSKDLAELDLSCwRVAGigadmirPDVLHQFAEAFAPAGFDdkaFMPSYGLAEAtlavsFSPlgSG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 338 VCAEKPEWDELSVEDRAAQKARQGVR-NTLQGALTVLDPETMEPVPADGKTIGELMF-----RGNIVMKGYLKNPAETGK 411
Cdd:PRK09192 355 IVVEEVDRDRLEYQGKAVAPGAETRRvRTFVNCGKALPGHEIEIRNEAGMPLPERVVghicvRGPSLMSGYFRDEESQDV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 412 SFAGGWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVA-LADEKWGEVPVAFVElkdd 490
Cdd:PRK09192 435 LAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAfSIAQENGEKIVLLVQ---- 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 491 AQVSEEELDQYCRERLAGFKRPkyyVFG-----------ELAKTATGKIQKFELRK 535
Cdd:PRK09192 510 CRISDEERRGQLIHALAALVRS---EFGveaavelvpphSLPRTSSGKLSRAKAKK 562
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
45-462 |
6.36e-13 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 71.41 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 45 QNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLV-D 123
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVqE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 124 SEFAPHIPEIKKALPALKII-----------QVNDELGpkdVEPFSdieYEGFLQSAEdLDNWVLPKDEWDAIALNYTSG 192
Cdd:PLN02861 158 SKISSILSCLPKCSSNLKTIvsfgdvsseqkEEAEELG---VSCFS---WEEFSLMGS-LDCELPPKQKTDICTIMYTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHRG--AALNAIAQSLEFD---MPKRPVYLWTLPLFHCNGWCFAwTIAARGGVNVCLRKFDPKTCFDLIR 267
Cdd:PLN02861 231 TTGEPKGVILTNRAiiAEVLSTDHLLKVTdrvATEEDSYFSYLPLAHVYDQVIE-TYCISKGASIGFWQGDIRYLMEDVQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 268 QERVGFYCAAPVVHA---------------------------ALAN----------AP-------AEMKAGIDHPVSAMV 303
Cdd:PLN02861 310 ALKPTIFCGVPRVYDriytgimqkissggmlrkklfdfaynyKLGNlrkglkqeeaSPrldrlvfDKIKEGLGGRVRLLL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 304 AGAAP-PEAVLARMEQMGFH-MVHVYGLTEVYGPSAVcaekpewdelSVEDRAAQKARQGVRNTLQGALTVLDPE----T 377
Cdd:PLN02861 390 SGAAPlPRHVEEFLRVTSCSvLSQGYGLTESCGGCFT----------SIANVFSMVGTVGVPMTTIEARLESVPEmgydA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 378 MEPVPAdgktiGELMFRGNIVMKGYLKNPAETGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENISSIEVED 456
Cdd:PLN02861 460 LSDVPR-----GEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLEN 534
|
....*.
gi 1092482886 457 VLYKHP 462
Cdd:PLN02861 535 TYSRCP 540
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
189-528 |
1.01e-12 |
|
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: 70.12 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAaLNAIAQ-SLEFDMPKRPVYLwtlPLFHCNgWCFAW-----TIAARGGVNVCL----RKFD 258
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSV-VNLRTSlSERYFGRDNGDEA---VLFFSN-YVFDFfveqmTLALLNGQKLVVppdeMRFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 259 PKTCFDLIRQERVGFYCAAPVV--HAALANAPaemkagidHPVSAMVAGAAPPEAVLARM-EQMGFHMVHVYGLTEvygp 335
Cdd:cd17648 176 PDRFYAYINREKVTYLSGTPSVlqQYDLARLP--------HLKRVDAAGEEFTAPVFEKLrSRFAGLIINAYGPTE---- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 336 SAVCAEKPEWdelSVEDRAAQKARQGVRNTlqgALTVLDPEtMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSFAG 415
Cdd:cd17648 244 TTVTNHKRFF---PGDQRFDKSLGRPVRNT---KCYVLNDA-MKRVPVGA--VGELYLGGDGVARGYLNRPELTAERFLP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFH---------------TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEV 480
Cdd:cd17648 315 NPFQteqerargrnarlykTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQS 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1092482886 481 P-----VAFVeLKDDAQVSEEELDQYCRERLAGFKRPKYYV-FGELAKTATGKI 528
Cdd:cd17648 395 RiqkylVGYY-LPEPGHVPESDLLSFLRAKLPRYMVPARLVrLEGIPVTINGKL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
177-507 |
1.16e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 70.31 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 177 LPKDEWDAIAlnYTSGTTGNPKGVVYHHRG--AALNAIAQSL-----EFDMPkrpvylwTLPLFHCNGWCFAWT------ 243
Cdd:PRK09274 171 LAPDDMAAIL--FTSGSTGTPKGVVYTHGMfeAQIEALREDYgiepgEIDLP-------TFPLFALFGPALGMTsvipdm 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 244 IAARGGvnvclrKFDPKTCFDLIRQERVGFYCAAPvvhaALANAPAemKAGIDHPVS------AMVAGAAPPEAVLARME 317
Cdd:PRK09274 242 DPTRPA------TVDPAKLFAAIERYGVTNLFGSP----ALLERLG--RYGEANGIKlpslrrVISAGAPVPIAVIERFR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 318 QMGFHMVHV---YGLTEVYGPSAVcaekpEWDELSVEDRAAqkARQG----VRNTLQGALTVLDPETMEPVP-------- 382
Cdd:PRK09274 310 AMLPPDAEIltpYGATEALPISSI-----ESREILFATRAA--TDNGagicVGRPVDGVEVRIIAISDAPIPewddalrl 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 383 ADGKtIGELMFRGNIVMKGYLKNPAETGKS----FAGGWFH-TGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDV 457
Cdd:PRK09274 383 ATGE-IGEIVVAGPMVTRSYYNRPEATRLAkipdGQGDVWHrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERI 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1092482886 458 LYKHPAVANVAVVALAdEKWGEVPVAFVELKDDAQVSEEELDQYCRERLA 507
Cdd:PRK09274 462 FNTHPGVKRSALVGVG-VPGAQRPVLCVELEPGVACSKSALYQELRALAA 510
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
45-533 |
2.04e-11 |
|
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: 66.04 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 45 QNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLV 122
Cdd:cd17645 22 QSLTykQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 123 DSEfaphipeikkalpalkiiqvndelgpkdvepfsDIEYegflqsaedldnwvlpkdewdaiaLNYTSGTTGNPKGVVY 202
Cdd:cd17645 102 NPD---------------------------------DLAY------------------------VIYTSGSTGLPKGVMI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 203 HHR---------------GAALNA-IAQSLEFDmpkrpvylwtlplfhcngwCFAWTIAARGGVNVCLRKFDPKTCFDLI 266
Cdd:cd17645 125 EHHnlvnlcewhrpyfgvTPADKSlVYASFSFD-------------------ASAWEIFPHLTAGAALHVVPSERRLDLD 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERvgfYCAAP-VVHAALANAPAEMKAGID-HPVSAMVAGAAppeaVLARMEQMGFHMVHVYGLTEVYGPSAVCAEKPE 344
Cdd:cd17645 186 ALND---YFNQEgITISFLPTGAAEQFMQLDnQSLRVLLTGGD----KLKKIERKGYKLVNNYGPTENTVVATSFEIDKP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 345 WDELSVedraaQKARQGVRNTLQGALTVLDPETMEpvpadgktiGELMFRGNIVMKGYLKNPAETGKSFAGGWF------ 418
Cdd:cd17645 259 YANIPI-----GKPIDNTRVYILDEALQLQPIGVA---------GELCIAGEGLARGYLNRPELTAEKFIVHPFvpgerm 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 -HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVseEE 497
Cdd:cd17645 325 yRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH--EE 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 1092482886 498 LDQYCRERLAGFKRPKYYV-FGELAKTATGKIQKFEL 533
Cdd:cd17645 403 LREWLKNDLPDYMIPTYFVhLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
40-533 |
4.11e-11 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 65.19 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 40 HGSIRQNWTETYH----RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYclqhg 115
Cdd:cd17656 5 VAVVFENQKLTYRelneRSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 116 eaefLLVDSefaphipeikkalpALKIIQVNDELGPKDVEPFSDIEYEGFLQSAEDLDNWVLPKDEWDAIALNYTSGTTG 195
Cdd:cd17656 80 ----IMLDS--------------GVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 196 NPKGVVYHHRgAALNAIAQSLEFDMPKR--PVYLWTLPLFHCngwCFAWTIAA--RGGVNVCLR---KFDPKTCFDLIRQ 268
Cdd:cd17656 142 KPKGVQLEHK-NMVNLLHFEREKTNINFsdKVLQFATCSFDV---CYQEIFSTllSGGTLYIIReetKRDVEQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 269 ER---VGFYCAAPVVHAALANAPAEMKAGIDHpvsAMVAGAAPPEAVLARmEQMGFHMVHVYGLtevYGPSAV------- 338
Cdd:cd17656 218 HNievVFLPVAFLKFIFSEREFINRFPTCVKH---IITAGEQLVITNEFK-EMLHEHNVHLHNH---YGPSEThvvttyt 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 339 CAEKPEWDELSVEDRAAQkarqgvrNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSFAGGWF 418
Cdd:cd17656 291 INPEAEIPELPPIGKPIS-------NT---WIYILD-QEQQLQPQG--IVGELYISGASVARGYLNRQELTAEKFFPDPF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 419 -------HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVA-FVELKdd 490
Cdd:cd17656 358 dpnermyRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyFVMEQ-- 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1092482886 491 aQVSEEELDQYCRERLAGFKRPKYYVFGE-LAKTATGKIQKFEL 533
Cdd:cd17656 436 -ELNISQLREYLAKQLPEYMIPSFFVPLDqLPLTPNGKVDRKAL 478
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
174-461 |
7.05e-11 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 64.84 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 174 NWVL------PKDEWDAIALNYTSGTTGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGW--CFAWTIA 245
Cdd:PRK06334 169 EWLMrwfgvsDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFnsCTLFPLL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 246 ARGGVNVCLRKFDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMKAGIDHPVSAMVAGAAPPEAVLARMEQMGFHMV- 324
Cdd:PRK06334 249 SGVPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 325 -HVYGLTEVygpSAVcaekpewdeLSVEDRAAQKARQGVRNTLQGA-LTVLDPETMEPVPAdGKTiGELMFRGNIVMKGY 402
Cdd:PRK06334 329 rQGYGTTEC---SPV---------ITINTVNSPKHESCVGMPIRGMdVLIVSEETKVPVSS-GET-GLVLTRGTSLFSGY 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 403 LKNPAETGKSFAGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKH 461
Cdd:PRK06334 395 LGEDFGQGFVELGGetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
122-437 |
2.42e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.99 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 122 VDSefapHIPE------IKKALPALkIIQVND---ELGPKDVEPFSDIEYEGFLQSAEDLDNWVLPKDEWDAIalnYTSG 192
Cdd:PRK04813 82 VDV----SSPAeriemiIEVAKPSL-IIATEElplEILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYII---FTSG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 193 TTGNPKGVVYHHrgAALNAIAQSL--EFDMPKRPVYLwTLPLFHCNGWCFAWTIA-ARGGVNVCLRK---FDPKTCFDLI 266
Cdd:PRK04813 154 TTGKPKGVQISH--DNLVSFTNWMleDFALPEGPQFL-NQAPYSFDLSVMDLYPTlASGGTLVALPKdmtANFKQLFETL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 267 RQERVGFYCAAP-VVHAAL--ANAPAEMKAGIDHpvsAMVAGAAPPEAVlARMEQMGFHMVHVYgltEVYGPS----AVC 339
Cdd:PRK04813 231 PQLPINVWVSTPsFADMCLldPSFNEEHLPNLTH---FLFCGEELPHKT-AKKLLERFPSATIY---NTYGPTeatvAVT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 340 AekpewdeLSV-EDRAAQKARQGVRNTLQGALTVLDPETMEPVPADGKtiGELMFRGNIVMKGYLKNPAETGKSF---AG 415
Cdd:PRK04813 304 S-------IEItDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQ--GEIVISGPSVSKGYLNNPEKTAEAFftfDG 374
|
330 340
....*....|....*....|...
gi 1092482886 416 GW-FHTGDLGVLhPDGYAQIKDR 437
Cdd:PRK04813 375 QPaYHTGDAGYL-EDGLLFYQGR 396
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
53-458 |
2.70e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALrQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLAL-----NVRLETEGLIYCLQHGEAEFLLVDSEFA 127
Cdd:PRK05691 49 RARTIAAAL-QARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAyppesARRHHQERLLSIIADAEPRLLLTVADLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 128 PHIPEIkkalpalkiiqvnDELGPKDVEPFSDIEYegfLQSAEdLDNWVLPKDEWDAIA-LNYTSGTTGNPKGVVYHHRG 206
Cdd:PRK05691 128 DSLLQM-------------EELAAANAPELLCVDT---LDPAL-AEAWQEPALQPDDIAfLQYTSGSTALPKGVQVSHGN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 207 AALNA--IAQSLEFDMPKRPVYLWTLPLFHCNG-----------------------------WCFAwtIAARGGVNVCLR 255
Cdd:PRK05691 191 LVANEqlIRHGFGIDLNPDDVIVSWLPLYHDMGliggllqpifsgvpcvlmspayflerplrWLEA--ISEYGGTISGGP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 KFDPKTC-----------FDLIRQeRVGFYCAAPVVHAALAnAPAEMKAGIDHPVSAMVAGAAPPEAVLarmeqmgfhmv 324
Cdd:PRK05691 269 DFAYRLCservsesalerLDLSRW-RVAYSGSEPIRQDSLE-RFAEKFAACGFDPDSFFASYGLAEATL----------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 325 HVYGLTEVYGPSAVcaekpewdELSVEDRAAQKARQGVRNTLQG--------ALTVLDPETMEpVPADGKtIGELMFRGN 396
Cdd:PRK05691 336 FVSGGRRGQGIPAL--------ELDAEALARNRAEPGTGSVLMScgrsqpghAVLIVDPQSLE-VLGDNR-VGEIWASGP 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 397 IVMKGYLKNPAETGKSF---AG-GWFHTGDLGVLHpDGYAQIKDRSKDIIISGGENISSIEVEDVL 458
Cdd:PRK05691 406 SIAHGYWRNPEASAKTFvehDGrTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
171-448 |
3.27e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 62.65 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 171 DLD---NWVLPKDEWDAIA-LNYTSGTTGNPKGVVYHHRgaalNAIA---QSLE--F-DMPKRP-----VYLWtLPLFHC 235
Cdd:PRK05850 145 DLDsprGSDARPRDLPSTAyLQYTSGSTRTPAGVMVSHR----NVIAnfeQLMSdyFgDTGGVPppdttVVSW-LPFYHD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 236 NGW---CFAWTIAARGGVNVC----LRKfdPKTCFDLIRQERVGFyCAAPVVHAALA---NAPAEMkAGID--HpVSAMV 303
Cdd:PRK05850 220 MGLvlgVCAPILGGCPAVLTSpvafLQR--PARWMQLLASNPHAF-SAAPNFAFELAvrkTSDDDM-AGLDlgG-VLGII 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 304 AGAappEAV--------LARMEQMGFH---MVHVYGLTE--VYGPSAVCAEKPE-----WDELS---VEDRAAQKARQGV 362
Cdd:PRK05850 295 SGS---ERVhpatlkrfADRFAPFNLRetaIRPSYGLAEatVYVATREPGQPPEsvrfdYEKLSaghAKRCETGGGTPLV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 363 RNTLQGALTV--LDPETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGKSF------------AGGWFHTGDLGVLHp 428
Cdd:PRK05850 372 SYGSPRSPTVriVDPDTCIECPAG--TVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtpEGPWLRTGDLGFIS- 448
|
330 340
....*....|....*....|
gi 1092482886 429 DGYAQIKDRSKDIIISGGEN 448
Cdd:PRK05850 449 EGELFIVGRIKDLLIVDGRN 468
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
45-537 |
4.12e-10 |
|
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: 62.06 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 45 QNWT--ETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAefllv 122
Cdd:cd05939 2 RHWTfrELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 123 dsefaphipeikKALpalkIIQVNDELgpkdvepfsdieyegfLQSAEDLDNWVLPKDEWDAIALNYTSGTTGNPKGVVY 202
Cdd:cd05939 77 ------------KAL----IFNLLDPL----------------LTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 203 HH----RGAALNAIAqsleFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRK-FDPKTCF-DLIRQ-----ERV 271
Cdd:cd05939 125 VHsryyRIAAGAYYA----FGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKkFSASNFWdDCVKYnctivQYI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 272 GFYC----AAPVVhaalanaPAEMKagidHPVSAMVAGAAPP---EAVLARmeqmgFHMVHV---YGLTE-------VYG 334
Cdd:cd05939 201 GEICryllAQPPS-------EEEQK----HNVRLAVGNGLRPqiwEQFVRR-----FGIPQIgefYGATEgnsslvnIDN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 335 PSAVCAEKPewdelsvedRAAQKARQgVRntlqgaLTVLDPETMEPV-PADGKTI-------GELMFR---GNIVMK--G 401
Cdd:cd05939 265 HVGACGFNS---------RILPSVYP-IR------LIKVDEDTGELIrDSDGLCIpcqpgepGLLVGKiiqNDPLRRfdG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 402 YLkNPAETGKSFAGGWFHTGDLG-----VLHPD--GYAQIKDRSKDIIISGGENISSIEVEDVLykHPAVANVAVVALAD 474
Cdd:cd05939 329 YV-NEGATNKKIARDVFKKGDSAflsgdVLVMDelGYLYFKDRTGDTFRWKGENVSTTEVEGIL--SNVLGLEDVVVYGV 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 475 E------KWGEVPVAFVELKDDAQVSEEELdqycRERLAGFKRPKYYVF-GELAKTATGKIQKFELRKQA 537
Cdd:cd05939 406 EvpgvegRAGMAAIVDPERKVDLDRFSAVL----AKSLPPYARPQFIRLlPEVDKTGTFKLQKTDLQKEG 471
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
177-504 |
7.13e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 61.65 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 177 LPKDEWDAIALNYTSGTTGNPKGVVYHHRGAALN-----AIAqslefDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVN 251
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANveqikTIA-----DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 252 VCLR------KFDPKTCFDliRQERVGFYCAAPVVHAALANAPAEMkagidHPVSAMVAGAAPPEAVLAR--MEQMGFHM 323
Cdd:PRK08043 435 VFLYpsplhyRIVPELVYD--RNCTVLFGTSTFLGNYARFANPYDF-----ARLRYVVAGAEKLQESTKQlwQDKFGLRI 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 324 VHVYGLTEvygpsavCAEKpewdeLSVEDRAAQKArqgvrNTLQGALTVLDPETMePVP--ADGktiGELMFRGNIVMKG 401
Cdd:PRK08043 508 LEGYGVTE-------CAPV-----VSINVPMAAKP-----GTVGRILPGMDARLL-SVPgiEQG---GRLQLKGPNIMNG 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 402 YLK--NPAE----TGKSFAG----GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVA 471
Cdd:PRK08043 567 YLRveKPGVlevpTAENARGemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAI 646
|
330 340 350
....*....|....*....|....*....|...
gi 1092482886 472 LADEKWGEVPVAFVElkdDAQVSEEELDQYCRE 504
Cdd:PRK08043 647 KSDASKGEALVLFTT---DSELTREKLQQYARE 676
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
17-422 |
8.13e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.43 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 17 TPLTPI-----DFLVRAHEVFGDDLAIV-----HGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPA---MV 83
Cdd:PRK08180 32 EPLGDYprrltDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEhalLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 84 EAGF--GVP----------MSGGVL-LALNVRLETEGLIYcLQHGEAefllvdseFAPHIPEIkkALPALKIIQVNDELG 150
Cdd:PRK08180 112 LAAMyaGVPyapvspayslVSQDFGkLRHVLELLTPGLVF-ADDGAA--------FARALAAV--VPADVEVVAVRGAVP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 151 PKDVEPFSDIEYEGFLQSAEDLDNWVLPkdewDAIA-LNYTSGTTGNPKGVVYHHRGAALN--AIAQSLEFDMPKRPVYL 227
Cdd:PRK08180 181 GRAATPFAALLATPPTAAVDAAHAAVGP----DTIAkFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPPVLV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 228 WTLPLFHcngwcfawTIAARGGVNVCLR---------------KFDpKTcFDLIRQERVGFYCAAPVVHAALANAPAEMK 292
Cdd:PRK08180 257 DWLPWNH--------TFGGNHNLGIVLYnggtlyiddgkptpgGFD-ET-LRNLREISPTVYFNVPKGWEMLVPALERDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 293 AGIDHPVSAMV----AGAAPPEAVLARMEQMGFH-------MVHVYGLTEVyGPSAVCAEKPEwdelsveDRAaqkarqg 361
Cdd:PRK08180 327 ALRRRFFSRLKllfyAGAALSQDVWDRLDRVAEAtcgerirMMTGLGMTET-APSATFTTGPL-------SRA------- 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 362 vrntlqGALTVLDPET-MEPVPADGKTigELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGD 422
Cdd:PRK08180 392 ------GNIGLPAPGCeVKLVPVGGKL--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
183-542 |
5.03e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.21 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIALNYTSGTTGNPKGVVYHHRGAALNAiAQSL-EFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVnvclrkfdpkt 261
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANR-AQVAaRIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGV----------- 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 cfdlirqeRVGFYcAAP----VVHAALANAPAEMKAGID----------HP-----VSAMVAGAappEAVLAR-----ME 317
Cdd:PRK06814 862 --------KVFLY-PSPlhyrIIPELIYDTNATILFGTDtflngyaryaHPydfrsLRYVFAGA---EKVKEEtrqtwME 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 318 QMGFHMVHVYGLTEVygpSAVcaekpewdeLSVEDRAAQKArqgvrNTLQGALTVLDPEtMEPVPA--DGktiGELMFRG 395
Cdd:PRK06814 930 KFGIRILEGYGVTET---APV---------IALNTPMHNKA-----GTVGRLLPGIEYR-LEPVPGidEG---GRLFVRG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 396 NIVMKGYLK--NPAeTGKSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALA 473
Cdd:PRK06814 989 PNVMLGYLRaeNPG-VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIP 1067
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 474 DEKWGEvpvAFVELKDDAQVSEEELDQYCRERLAG-FKRPK-YYVFGELAKTATGKIQKFELRKQAEALFS 542
Cdd:PRK06814 1068 DARKGE---RIILLTTASDATRAAFLAHAKAAGASeLMVPAeIITIDEIPLLGTGKIDYVAVTKLAEEAAA 1135
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
46-448 |
6.15e-09 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 58.60 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 46 NWTETYHRCRQMAAALRQNgADRGTTVATLlhnTPAMVE--AGFGVPMSGGV----LLALNVRLETEGLIYCLQHGEAEF 119
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAIL---APQGIDyvAGFFAAIKAGTiavpLFAPELPGHAERLDTALRDAEPTV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 120 LLVDSEFAPHIPEIKKALPALK------IIQVNDELGpkdvepfsdieyEGFLQSAEDLDnwvlpkdewDAIALNYTSGT 193
Cdd:PRK12476 146 VLTTTAAAEAVEGFLRNLPRLRrprviaIDAIPDSAG------------ESFVPVELDTD---------DVSHLQYTSGS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 194 TGNPKGVVYHHRGAALNAIAQSLEFDMPKRPVY--LWtLPLFH------------CNG----------------WC---- 239
Cdd:PRK12476 205 TRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgvSW-LPLYHdmglsmigfpavYGGhstlmsptafvrrpqrWIkals 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 240 --------------FAWTIAARGGVnvclrkfdPKTCFDLIRQERVGFYCAAPVVHAALAN-----APAEMKAGIDHPVS 300
Cdd:PRK12476 284 egsrtgrvvtaapnFAYEWAAQRGL--------PAEGDDIDLSNVVLIIGSEPVSIDAVTTfnkafAPYGLPRTAFKPSY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 301 AM---------VAGAAPPEAVLARMEQMGF-HMVHVYGLTevygPSAVcaekpewdelsVEDRAAQKARQgvrntlQGAL 370
Cdd:PRK12476 356 GIaeatlfvatIAPDAEPSVVYLDREQLGAgRAVRVAADA----PNAV-----------AHVSCGQVARS------QWAV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 371 TVlDPETMEPVPaDGkTIGELMFRGNIVMKGYLKNPAETGKSF-------------AGG------WFHTGDLGVlHPDGY 431
Cdd:PRK12476 415 IV-DPDTGAELP-DG-EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshADGaaddgtWLRTGDLGV-YLDGE 490
|
490
....*....|....*..
gi 1092482886 432 AQIKDRSKDIIISGGEN 448
Cdd:PRK12476 491 LYITGRIADLIVIDGRN 507
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
183-447 |
8.29e-09 |
|
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: 58.24 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIA-LNYTSGTTGNPKGVVY-HHRGAALNAIAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDPK 260
Cdd:cd17632 223 DPLAlLIYTSGSTGTPKGAMYtERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 261 TCFD---LIRQERVGF------------------YCAAPVVHAALAnapAEMKAGIDHPV------SAMVAGAAPPEAVL 313
Cdd:cd17632 303 TLFDdlaLVRPTELFLvprvcdmlfqryqaeldrRSVAGADAETLA---ERVKAELRERVlggrllAAVCGSAPLSAEMK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 314 ARMEQ-MGFHMVHVYGLTEVYGpsavcaekpewdeLSVEDRAAQKArqgvrntlqgaltVLD------PE-----TMEPV 381
Cdd:cd17632 380 AFMESlLDLDLHDGYGSTEAGA-------------VILDGVIVRPP-------------VLDyklvdvPElgyfrTDRPH 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 382 PAdgktiGELMFRGNIVMKGYLKNPAETGKSF-AGGWFHTGD-LGVLHPDGYAQIKDRSKDIIISGGE 447
Cdd:cd17632 434 PR-----GELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDvMAELGPDRLVYVDRRNNVLKLSQGE 496
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
413-538 |
2.64e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 56.69 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 413 FAGGWFhTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQ 492
Cdd:PRK00174 481 FKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEE 559
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1092482886 493 VSEE---ELDQYCRERLAGFKRPKYYVFG-ELAKTATGKIQKFELRKQAE 538
Cdd:PRK00174 560 PSDElrkELRNWVRKEIGPIAKPDVIQFApGLPKTRSGKIMRRILRKIAE 609
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
33-296 |
4.70e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 55.74 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 33 GDDLAIVHGSIRQN-----WTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEG 107
Cdd:cd05943 82 ADDPAAIYAAEDGErtevtWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 108 LIYCLQHGEAEFLLVDSEF---------APHIPEIKKALPAL-KIIQVNDELGP--KDVEPFSD-IEYEGFLQSAEDldn 174
Cdd:cd05943 162 VLDRFGQIEPKVLFAVDAYtyngkrhdvREKVAELVKGLPSLlAVVVVPYTVAAgqPDLSKIAKaLTLEDFLATGAA--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 175 wvlPKDEWDAIALN------YTSGTTGNPKGVVYHHRGAALNAI-AQSLEFDMPKRPVYLWtlplFHCNGW-CFAWTIAA 246
Cdd:cd05943 239 ---GELEFEPLPFDhplyilYSSGTTGLPKCIVHGAGGTLLQHLkEHILHCDLRPGDRLFY----YTTCGWmMWNWLVSG 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 247 RG-GVNVCLrkFD-------PKTCFDLIRQERVGFYCAAPVVHAALanapaeMKAGID 296
Cdd:cd05943 312 LAvGATIVL--YDgspfypdTNALWDLADEEGITVFGTSAKYLDAL------EKAGLK 361
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
37-462 |
5.39e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.82 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 37 AIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGE 116
Cdd:PRK10252 476 ALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDAR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 117 AEFLLVDSEFAPHIPEIkkalPALKIIQVNDELGPKDVEPFsdieyegflqsaedldnwVLPKDEwDAIALNYTSGTTGN 196
Cdd:PRK10252 556 PSLLITTADQLPRFADV----PDLTSLCYNAPLAPQGAAPL------------------QLSQPH-HTAYIIFTSGSTGR 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 197 PKGVVYHHRgaalnAIAQSLEFdM----PKRP--VYLWTLPL-FHCNGWCFAWTIAArggvNVCL--------RkfDPKT 261
Cdd:PRK10252 613 PKGVMVGQT-----AIVNRLLW-MqnhyPLTAddVVLQKTPCsFDVSVWEFFWPFIA----GAKLvmaepeahR--DPLA 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 262 CFDLIRQERVGFYCAAPVVHAALANAPAEmkAGIDHPVSAM----VAGAAPPEAVLARMEQMGFHMVH-VYGLTEvygpS 336
Cdd:PRK10252 681 MQQFFAEYGVTTTHFVPSMLAAFVASLTP--EGARQSCASLrqvfCSGEALPADLCREWQQLTGAPLHnLYGPTE----A 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 337 AVcaeKPEWDELSVEDRAAQKARQ-----GVRNTlqgALTVLDpETMEPVPADgkTIGELMFRGNIVMKGYLKNPAETGK 411
Cdd:PRK10252 755 AV---DVSWYPAFGEELAAVRGSSvpigyPVWNT---GLRILD-ARMRPVPPG--VAGDLYLTGIQLAQGYLGRPDLTAS 825
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 412 SFAGGWF-------HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHP 462
Cdd:PRK10252 826 RFIADPFapgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALP 883
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
183-422 |
6.70e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 55.13 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 183 DAIA-LNYTSGTTGNPKGVVYHHRGAALNA--IAQSLEFDMPKRPVYLWTLPLFHCNGWCFAWTIAARGGVNVCLRKFDP 259
Cdd:cd05921 165 DTVAkFLFTSGSTGLPKAVINTQRMLCANQamLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDDGKP 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 260 -----KTCFDLIRQERVGFYCAAPVVHAALANAP-----------AEMKAgidhpvsAMVAGAAPPEAVLARMEQMGFH- 322
Cdd:cd05921 245 mpggfEETLRNLREISPTVYFNVPAGWEMLVAALekdealrrrffKRLKL-------MFYAGAGLSQDVWDRLQALAVAt 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 323 ------MVHVYGLTEVYGPSAVCaekpEWDelsvedraaqKARQG-VRNTLQGAltvldpeTMEPVPADGKTigELMFRG 395
Cdd:cd05921 318 vgeripMMAGLGATETAPTATFT----HWP----------TERSGlIGLPAPGT-------ELKLVPSGGKY--EVRVKG 374
|
250 260
....*....|....*....|....*...
gi 1092482886 396 NIVMKGYLKNPAETGKSF-AGGWFHTGD 422
Cdd:cd05921 375 PNVTPGYWRQPELTAQAFdEEGFYCLGD 402
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
38-539 |
9.46e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.04 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 38 IVHGSIRQNwtetyhrCRQMAAALRQNGADRGTTVATLLHNTPAMVEagfgvpmsggVLLAlnvrletegliyCLQHGEA 117
Cdd:PRK06060 31 VTHGQIHDG-------AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQ----------LLLA------------CLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 118 EFLLvdsefAPHIPEIKKALP------ALKIIQ--VNDELGPKDVEPFSDIEYEGflQSAEDLDNWVLPKDEWdAIAlNY 189
Cdd:PRK06060 82 AFLA-----NPELHRDDHALAarntepALVVTSdaLRDRFQPSRVAEAAELMSEA--ARVAPGGYEPMGGDAL-AYA-TY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 190 TSGTTGNPKGVVyhHRGAALNAIAQSL---EFDMPKRPVYLWTLPLFHCNGWCFA-WTIAARGGVNVC------------ 253
Cdd:PRK06060 153 TSGTTGPPKAAI--HRHADPLTFVDAMcrkALRLTPEDTGLCSARMYFAYGLGNSvWFPLATGGSAVInsapvtpeaaai 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 254 -LRKFDPKTCFDLirqerVGFYcaAPVVHAALANAPAEMKAgidhpvsAMVAGAAPPEAVLARMEQM--GFHMVHVYGLT 330
Cdd:PRK06060 231 lSARFGPSVLYGV-----PNFF--ARVIDSCSPDSFRSLRC-------VVSAGEALELGLAERLMEFfgGIPILDGIGST 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 EVyGPSAVCAEKPEWdelsvedraaqkaRQGvrnTLQgalTVLDPETMEPVPADGKTIG-----ELMFRGNIVMKGYLKN 405
Cdd:PRK06060 297 EV-GQTFVSNRVDEW-------------RLG---TLG---RVLPPYEIRVVAPDGTTAGpgvegDLWVRGPAIAKGYWNR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 406 PAETGKSfaGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFV 485
Cdd:PRK06060 357 PDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1092482886 486 ELKDDAQVSEEELDQYCRE---RLAGFKRP-KYYVFGELAKTATGKIQKFELRKQAEA 539
Cdd:PRK06060 435 VATSGATIDGSVMRDLHRGllnRLSAFKVPhRFAVVDRLPRTPNGKLVRGALRKQSPT 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-430 |
2.14e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.02 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 37 AIVHGSIRQNWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGE 116
Cdd:PRK05691 1149 ALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 117 AEFLLVDSefapHIPEIKKALPALKIIQVnDELgpkdvepfsdieyegflqsaeDLDNWvlpKDEWDAIALN-------- 188
Cdd:PRK05691 1229 VELLLTQS----HLLERLPQAEGVSAIAL-DSL---------------------HLDSW---PSQAPGLHLHgdnlayvi 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRgaalnAIAQSL-----EFDMPKRPVYLWTLPL-FHCNGW-CFaWTIAArgGVNVCL----RKF 257
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHA-----ALAERLqwmqaTYALDDSDVLMQKAPIsFDVSVWeCF-WPLIT--GCRLVLagpgEHR 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 258 DPKTCFDLIRQERVgfycaapvvhAALANAPAEMKAGIDHPVSA-------MVAG--AAPPE---AVLARMEQMGFHmvh 325
Cdd:PRK05691 1352 DPQRIAELVQQYGV----------TTLHFVPPLLQLFIDEPLAAactslrrLFSGgeALPAElrnRVLQRLPQVQLH--- 1418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 326 vygltEVYGPSAVCAEKPEWdelsvEDRAAQKARQGVRNTLQGALT-VLDPEtMEPVPADgkTIGELMFRGNIVMKGYLK 404
Cdd:PRK05691 1419 -----NRYGPTETAINVTHW-----QCQAEDGERSPIGRPLGNVLCrVLDAE-LNLLPPG--VAGELCIGGAGLARGYLG 1485
|
410 420 430
....*....|....*....|....*....|....
gi 1092482886 405 NPAETGKSF-------AGG-WFHTGDLGVLHPDG 430
Cdd:PRK05691 1486 RPALTAERFvpdplgeDGArLYRTGDRARWNADG 1519
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
411-537 |
2.15e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 53.75 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 411 KSFAGGWFhTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDD 490
Cdd:PLN02654 509 KPFAGYYF-SGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEG 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1092482886 491 AQVSEE---ELDQYCRERLAGFKRP-KYYVFGELAKTATGKIQKFELRKQA 537
Cdd:PLN02654 588 VPYSEElrkSLILTVRNQIGAFAAPdKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
190-462 |
2.30e-07 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 53.40 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 190 TSGTTGNPKGVVYHHRGAA--LNAIAQSLEFDMPKRPV--------YLWTlplfhcNGWCF--------AWTIAARGGvn 251
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDvwAELVARCLDAAGVTPGDrvqnaygyGLFT------GGLGFhygaerlgALVIPAGGG-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 252 vclrkfDPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMkaGID---HPVSAMVAGAAP-PEAVLARMEQ-MGFHMVHV 326
Cdd:cd05913 158 ------NTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEE--GIDpreLSLKVGIFGAEPwTEEMRKRIERrLGIKAYDI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 327 YGLTEVYGPSAV--CAEKPE---W-DELSVEdraaqkarqgvrntlqgaltVLDPETMEPVPaDGKtIGELMF-----RG 395
Cdd:cd05913 230 YGLTEIIGPGVAfeCEEKDGlhiWeDHFIPE--------------------IIDPETGEPVP-PGE-VGELVFttltkEA 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092482886 396 NIVMKgylknpaetgksfaggwFHTGDLGVLHPDGYA---------QIKDRSKDIIISGGENISSIEVEDVLYKHP 462
Cdd:cd05913 288 MPLIR-----------------YRTRDITRLLPGPCPcgrthrridRITGRSDDMLIIRGVNVFPSQIEDVLLKIP 346
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
190-462 |
3.01e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 52.84 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 190 TSGTTGNPKGVVYHHRGAALNA--IAQSLE-FDMPKRPVYLWTLPlFHCN--GWCFawTIAAR---------GGVNvclr 255
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAelFARSLRaAGVRPGDRVQNAFG-YGLFtgGLGL--HYGAErlgatvipaGGGN---- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 256 kfdPKTCFDLIRQERVGFYCAAPVVHAALANAPAEMkaGID---HPVSAMVAGAAP-PEAVLARMEQ-MGFHMVHVYGLT 330
Cdd:COG1541 164 ---TERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEE--GIDprdLSLKKGIFGGEPwSEEMRKEIEErWGIKAYDIYGLT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 331 EVyGPsAVCAEKPE------W-DELSVEdraaqkarqgvrntlqgaltVLDPETMEPVPaDGKTiGEL-----------M 392
Cdd:COG1541 239 EV-GP-GVAYECEAqdglhiWeDHFLVE--------------------IIDPETGEPVP-EGEE-GELvvttltkeampL 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 393 FRgnivmkgylknpaetgksfaggwFHTGDLGVLHPDGYA---------QIKDRSKDIIISGGENISSIEVEDVLYKHP 462
Cdd:COG1541 295 IR-----------------------YRTGDLTRLLPEPCPcgrthprigRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
411-540 |
4.32e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 52.64 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 411 KSFAGGWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDD 490
Cdd:PRK10524 468 SLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDS 547
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 491 AQVS--------EEELDQYCRERLAGFKRP-KYYVFGELAKTATGKIqkfeLRKQAEAL 540
Cdd:PRK10524 548 DSLAdrearlalEKEIMALVDSQLGAVARPaRVWFVSALPKTRSGKL----LRRAIQAI 602
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
53-462 |
2.41e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 53 RCRQMAAALRQNGADRGTTVATLLHNTPAMVEAGFGVPMSGGVLLALNVRLETEGLIYCLQHGEAEFLLVDSEFAPHIPE 132
Cdd:PRK05691 2222 RANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGE 2301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 133 ikkaLPAlkiiQVNDELGPKDVEPFSDieyegflQSAEDLDNWVLPKDEWDAIalnYTSGTTGNPKGVVYHHRGAALNAI 212
Cdd:PRK05691 2302 ----LPA----GVARWCLEDDAAALAA-------YSDAPLPFLSLPQHQAYLI---YTSGSTGKPKGVVVSHGEIAMHCQ 2363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 213 AQSLEFDMpkRP------VY----------LWTlPLFhcngwcfawtiaarGGVNVCLR---KFDPKTCFDLIRQERVGF 273
Cdd:PRK05691 2364 AVIERFGM--RAddcelhFYsinfdaaserLLV-PLL--------------CGARVVLRaqgQWGAEEICQLIREQQVSI 2426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 274 YCAAPVVHAALANAPAemKAGIDHPVSAMVAG--AAPPEAvLARMEQmGFH---MVHVYGLTE-VYGPSAVCA-EKPEWD 346
Cdd:PRK05691 2427 LGFTPSYGSQLAQWLA--GQGEQLPVRMCITGgeALTGEH-LQRIRQ-AFApqlFFNAYGPTEtVVMPLACLApEQLEEG 2502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 347 ELSVEDRAAQKARQGVrntlqgaltVLDpETMEPVPADGktIGELMFRGNIVMKGYLKNPAETGKSF--------AGGWF 418
Cdd:PRK05691 2503 AASVPIGRVVGARVAY---------ILD-ADLALVPQGA--TGELYVGGAGLAQGYHDRPGLTAERFvadpfaadGGRLY 2570
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1092482886 419 HTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHP 462
Cdd:PRK05691 2571 RTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
416-530 |
4.34e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 46.27 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 416 GWFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPAVANVAVVALADEKWGEVPVAFVELKDDAQVSE 495
Cdd:PTZ00237 492 GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQS 571
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1092482886 496 EELDQYCRE----------RLAGFKrpKYYVFGELAKTATGKIQK 530
Cdd:PTZ00237 572 IDLNKLKNEinniitqdieSLAVLR--KIIIVNQLPKTKTGKIPR 614
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
25-296 |
4.50e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 46.33 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 25 LVRAHEvfGDDLAIVH----GSIRQ-NWTETYHRCRQMAAALRQNGADRGTTVATLLHNTPAMVEA-------G------ 86
Cdd:PRK03584 92 LLRHRR--DDRPAIIFrgedGPRRElSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAmlataslGaiwssc 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 87 ---FGVPmsgGVLlalnVR---LETEGLIYC--LQHGEAEFLLVDSefaphIPEIKKALPALKIIQVNDELGPKDVEPFS 158
Cdd:PRK03584 170 spdFGVQ---GVL----DRfgqIEPKVLIAVdgYRYGGKAFDRRAK-----VAELRAALPSLEHVVVVPYLGPAAAAAAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 159 D--IEYEGFLQSAEDLDN-----------WVLpkdewdaialnYTSGTTGNPKGVVYHHRGAALNAI-AQSLEFDMPKRP 224
Cdd:PRK03584 238 PgaLLWEDFLAPAEAAELefepvpfdhplWIL-----------YSSGTTGLPKCIVHGHGGILLEHLkELGLHCDLGPGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 225 VYLWtlplFHCNGWcFAWTIAARG---GVNVCLrkFD-------PKTCFDLIRQERVGFYCAAPVVHAALanapaeMKAG 294
Cdd:PRK03584 307 RFFW----YTTCGW-MMWNWLVSGllvGATLVL--YDgspfypdPNVLWDLAAEEGVTVFGTSAKYLDAC------EKAG 373
|
..
gi 1092482886 295 ID 296
Cdd:PRK03584 374 LV 375
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
189-530 |
1.46e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 189 YTSGTTGNPKGVVYHHRGAALN--------------AIAQ--SLEFDmpkrpVYLWTL---PLFHCNGWCFAWTIAargg 249
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNNqlskvpylalseadVIAQtaSQSFD-----ISVWQFlaaPLFGARVEIVPNAIA---- 3946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 250 vnvclrkFDPKTCFDLIRQERVGFYCAAPVVHAALAnapAEMKAGIDHPVSAMVAGAA-PPEAV---LARMEQMGfhmvh 325
Cdd:PRK05691 3947 -------HDPQGLLAHVQAQGITVLESVPSLIQGML---AEDRQALDGLRWMLPTGEAmPPELArqwLQRYPQIG----- 4011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 326 vygLTEVYGPsAVCAEKPEWDELSVEDRAAQKARQGVrNTLQGALTVLDpETMEPVPADGktIGELMFRGNIVMKGYLKN 405
Cdd:PRK05691 4012 ---LVNAYGP-AECSDDVAFFRVDLASTRGSYLPIGS-PTDNNRLYLLD-EALELVPLGA--VGELCVAGTGVGRGYVGD 4083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092482886 406 PAETGKSF------AGG--WFHTGDLGVLHPDGYAQIKDRSKDIIISGGENISSIEVEDVLYKHPaVANVAVVALADEKW 477
Cdd:PRK05691 4084 PLRTALAFvphpfgAPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQA-EVREAAVAVQEGVN 4162
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092482886 478 GEVPVAFVELKDDAQVSEEELDQyCRERLAGfKRPKYYV------FGELAKTATGKIQK 530
Cdd:PRK05691 4163 GKHLVGYLVPHQTVLAQGALLER-IKQRLRA-ELPDYMVplhwlwLDRLPLNANGKLDR 4219
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
389-449 |
2.27e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 40.86 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092482886 389 GELMFRGNIVMKGYLKNPAETGKSFA-GGWFHTGDLGVLHPDGYAQIKDRSKDII-ISGGENI 449
Cdd:PTZ00342 542 GELLIKSDSIFSGYFLEKEQTKNAFTeDGYFKTGDIVQINKNGSLTFLDRSKGLVkLSQGEYI 604
|
|
| |
