|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
7-678 |
0e+00 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 1023.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 7 PQIALYRTWLAEKRGLNFDSYEEMRQWSVRDLDGFWHAIWDYYDLQSPTPFAAVITERKMPGALWFPGAQVNYARQVFRH 86
Cdd:PRK03584 16 SRMTAFIRWLAARRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLAGRRMPGARWFPGARLNYAENLLRH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 87 vdaaDAAGLPAIVSCGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAP 166
Cdd:PRK03584 96 ----RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 167 DMAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVI----LHSEAAAPAAADALLSEiSATTGA 242
Cdd:PRK03584 172 DFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVvvpyLGPAAAAAALPGALLWE-DFLAPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 243 EIDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCsyhensfGERYHWYSSTGWIMWNSQV 322
Cdd:PRK03584 251 EAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGP-------GDRFFWYTTCGWMMWNWLV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 323 GGLLSGTTCCIFDGSPGgakdKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADT 402
Cdd:PRK03584 324 SGLLVGATLVLYDGSPF----YPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 403 QAWFNNRFAglsktngskaqADIWWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVIGEVGELVC 482
Cdd:PRK03584 400 FDWVYEHVK-----------ADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVC 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 483 TEPMPSMPLYFWNDKGGARYRASYFETYPDnfdgtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSA 562
Cdd:PRK03584 469 TKPFPSMPLGFWNDPDGSRYRDAYFDTFPG---------VWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 563 IEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPI 642
Cdd:PRK03584 540 VEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPV 619
|
650 660 670
....*....|....*....|....*....|....*.
gi 517269147 643 KKLLLGQPVEKVINREAMANPACLDWYLAFARDYLA 678
Cdd:PRK03584 620 KKLLHGRPVKKAVNRDALANPEALDWFADLAELRAA 655
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
9-669 |
0e+00 |
|
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: 898.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 9 IALYRTWLAEKRGLNFDSYEEMRQWSVRDLDGFWHAIWDYYDLQSPTPFA-AVITERKMPGALWFPGAQVNYARQVFRHV 87
Cdd:cd05943 1 MDAFRRWVNARHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDvVVVSGRIMPGARWFPGARLNYAENLLRHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 88 DAADAAglpAIVScGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPD 167
Cdd:cd05943 81 DADDPA---AIYA-AEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 168 MAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVIL-------HSEAAAPAAADALLSEISATT 240
Cdd:cd05943 157 FGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVvpytvaaGQPDLSKIAKALTLEDFLATG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 241 GAEIDAFEpaWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGcsyhensFGERYHWYSSTGWIMWNS 320
Cdd:cd05943 237 AAGELEFE--PLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLR-------PGDRLFYYTTCGWMMWNW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 321 QVGGLLSGTTCCIFDGSPGGakdkPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSA 400
Cdd:cd05943 308 LVSGLAVGATIVLYDGSPFY----PDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 401 DTQAWFNnrfaglsktngSKAQADIWWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVIGEVGEL 480
Cdd:cd05943 384 ESFDYVY-----------DHIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGEL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 481 VCTEPMPSMPLYFWNDKGGARYRASYFETYPdnfdgtgrgPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELY 560
Cdd:cd05943 453 VCTKPFPSMPVGFWNDPDGSRYRAAYFAKYP---------GVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIY 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 561 SAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQEL 640
Cdd:cd05943 524 RVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEV 603
|
650 660
....*....|....*....|....*....
gi 517269147 641 PIKKLLLGQPVEkviNREAMANPACLDWY 669
Cdd:cd05943 604 AVKKIIAGRPVK---NAGALANPESLDLF 629
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
8-674 |
0e+00 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 613.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 8 QIALYRTWLAEKRGLNFDSYEEMRQWSVRDLDGFWHAIWDYYDLQSPTPFAAVITERKMPGALWFPGAQVNYARQVFRHV 87
Cdd:TIGR01217 18 RMTRFQAWAGEHHGAAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVVDDRTMPGAQWFPGARLNYAENLLRAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 88 DAADAAglpaiVSCGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPD 167
Cdd:TIGR01217 98 GTEPAL-----LYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 168 MAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVIL------HSEAAAPAAADALLSEISATTG 241
Cdd:TIGR01217 173 FGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHipylgpRETEAPKIDGALDLEDFTAAAQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 242 AEIDAFEPawLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCsyhensfGERYHWYSSTGWIMWNSQ 321
Cdd:TIGR01217 253 AAELVFEQ--LPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGP-------GDRLFYYTTTGWMMWNWL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 322 VGGLLSGTTCCIFDGSPGgakdKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSAD 401
Cdd:TIGR01217 324 VSGLATGATLVLYDGSPG----FPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 402 TQAWFNNRFAglsktngskaqADIWWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVIGEVGELV 481
Cdd:TIGR01217 400 GFRWVYDEIK-----------ADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 482 CTEPMPSMPLYFWNDKGGARYRASYFETYPDnfdgtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYS 561
Cdd:TIGR01217 469 CTNPMPSMPIRFWNDPDGSKYRDAYFDTYPG---------VWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 562 AIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELP 641
Cdd:TIGR01217 540 AVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVA 619
|
650 660 670
....*....|....*....|....*....|...
gi 517269147 642 IKKLLLGQPVEkviNREAMANPACLDWYLAFAR 674
Cdd:TIGR01217 620 VKRVLQGTPVD---NPGAIDNPELLDLYEELAE 649
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
71-669 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 567.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 71 WFPGAQVNYARQVF-RHVDAADAAglPAIVSCGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETII 149
Cdd:COG0365 2 WFVGGRLNIAYNCLdRHAEGRGDK--VALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 150 AFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVIL--HSEAAAPA 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVvgRTGADVPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 228 AADALLSEISATTGAEidaFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLgcsyHEnsfGERY 307
Cdd:COG0365 160 EGDLDWDELLAAASAE---FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDL----KP---GDVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 308 HWYSSTGWIM--WNSQVGGLLSGTTCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDL 385
Cdd:COG0365 230 WCTADIGWATghSYIVYGPLLNGATVVLYEGRP----DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 386 SQLRCLGSTGSPLSADTQAWFNNRFaglsktngskaqaDIWWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEA 465
Cdd:COG0365 306 SSLRLLGSAGEPLNPEVWEWWYEAV-------------GVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 466 FDEQGRAVI-GEVGELVCTEPMPSMPLYFWNDKggARYRASYFETYPDnfdgtgrgpVWRHGDWLKVDPDGSCIIYGRSD 544
Cdd:COG0365 373 VDEDGNPVPpGEEGELVIKGPWPGMFRGYWNDP--ERYRETYFGRFPG---------WYRTGDGARRDEDGYFWILGRSD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 545 ATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIF 624
Cdd:COG0365 442 DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIE 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 517269147 625 AVAEIPRTLSGKKQELPIKKLLLGQPVEKvinREAMANPACLDWY 669
Cdd:COG0365 522 FVDELPKTRSGKIMRRLLRKIAEGRPLGD---TSTLEDPEALDEI 563
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-650 |
3.23e-100 |
|
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: 319.44 E-value: 3.23e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 22 LNFDSYEEMRQWSVRDLDGFWHAIWDYYDLQ-SPTPFAAVITERKMPGALWFPGAQVNYARQVFRHvDAADAAGLPAIVS 100
Cdd:cd05968 4 LGIPDLEAFLERSAEDNAWFWGEFVKDVGIEwYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDK-WLADTRTRPALRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 101 CGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQI 180
Cdd:cd05968 83 EGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 181 EPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVILH----SEAAAPAAADALLSEISATTGAEIDAFEPawlpfDH 256
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVrhlgNDFTPAKGRDLSYDEEKETAGDGAERTES-----ED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 257 PLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCsyhensfGERYHWYSSTGWIM--WnSQVGGLLSGTTCCIF 334
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKP-------GDLLTWFTDLGWMMgpW-LIFGGLILGATMVLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 335 DGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFnnrFAGLS 414
Cdd:cd05968 310 DGAP----DHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWL---FETVG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 415 KTNGSkaqadiwWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVIGEVGELVCTEPMPSMPLYFW 494
Cdd:cd05968 383 KGRNP-------IINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFW 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 495 NDKggaryrASYFETYPDNFDGtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLV 574
Cdd:cd05968 456 RDE------DRYLETYWSRFDN-----VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAA 524
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517269147 575 VDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKKLLLGQP 650
Cdd:cd05968 525 IGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKE 600
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
27-636 |
2.24e-79 |
|
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: 264.05 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 27 YEEMRQWSVRDLDGFWHAIWDYYDLQSP-TPFAAVITERKMPGALWFPGAQVNYARQ-VFRHV-DAADAAglpAIVSCGE 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPyQKVKNTSFAPGAPSIKWFEDATLNLAANaLDRHLrENGDRT---AIIYEGD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 104 DGRLCET-SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEP 182
Cdd:cd17634 78 DTSQSRTiSYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 183 KVLIACDAVTYAGRRHDRKDVLAE-LRRSLPTVEHVILHSEAAapaaadallSEISATTGAEID----------AFEPAW 251
Cdd:cd17634 158 RLLITADGGVRAGRSVPLKKNVDDaLNPNVTSVEHVIVLKRTG---------SDIDWQEGRDLWwrdliakaspEHQPEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 252 LPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCsyhensfGERYHWYSSTGWIMWNSQV--GGLLSGT 329
Cdd:cd17634 229 MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGP-------GDIYWCTADVGWVTGHSYLlyGPLACGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 330 TCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNR 409
Cdd:cd17634 302 TTLLYEGVP----NWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 410 FAGlsktnGSKAQADIWWanisgGTDFAGAFIGGNREL-PQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPMP 487
Cdd:cd17634 378 IGK-----EKCPVVDTWW-----QTETGGFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQpGGTEGNLVITDPWP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 488 SMPLYFWNDKggARYRASYFETypdnFDGtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALP 567
Cdd:cd17634 448 GQTRTLFGDH--ERFEQTYFST----FKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269147 568 EVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGK 585
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
25-636 |
6.31e-70 |
|
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: 239.00 E-value: 6.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 25 DSYEEMRQWSVRDLDGFWHAI-----WDyydlqspTPFAAVI-TERKMPGALWFPGAQVNYA-----RQVFRHVDAAdaa 93
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIakeldWF-------KPWDKVLdWSKGPPFIKWFEGGKLNISyncldRHLKERGDKV--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 94 glpAIVSCGEDGRLCET-SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPA 172
Cdd:cd05966 71 ---AIIWEGDEPDQSRTiTYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 173 VIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVI----LHSEAAAPAAADALLSEISATTGAEIdafE 248
Cdd:cd05966 148 LADRINDAQCKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLvvkrTGGEVPMTEGRDLWWHDLMAKQSPEC---E 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 PAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIiivvlaLLGLHndlgcSYHENSF----GERYHWYSSTGWIMWNSQV-- 322
Cdd:cd05966 225 PEWMDSEDPLFILYTSGSTGKPKGVVHTTGGY------LLYAA-----TTFKYVFdyhpDDIYWCTADIGWITGHSYIvy 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 323 GGLLSGTTCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADT 402
Cdd:cd05966 294 GPLANGATTVMFEGTP----TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 403 QAWFnNRFAGLSKTngskAQADIWWANISGG---TDFAGAFiggnrelPQTPGAMQCRLLGAAVEAFDEQGRAVIGEV-G 478
Cdd:cd05966 370 WMWY-YEVIGKERC----PIVDTWWQTETGGimiTPLPGAT-------PLKPGSATRPFFGIEPAILDEEGNEVEGEVeG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 479 ELVCTEPMPSMPLYFWNDKggARYRASYFETYPDnfdgtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSE 558
Cdd:cd05966 438 YLVIKRPWPGMARTIYGDH--ERYEDTYFSKFPG---------YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAE 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 559 LYSAIEALPEVLDSLVVDL--EYLGRDSYMplFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05966 507 VESALVAHPAVAEAAVVGRphDIKGEAIYA--FVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
27-651 |
3.51e-53 |
|
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: 193.30 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 27 YEEMRQWSVRDLDGFWHAIWDYYDLQspTPFAAVITERKMPGALWFPGAQVNYA-RQVFRHVDAADAAGLPAIVSCGEDG 105
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWF--KPPEKILDNSNPPFTRWFVGGRLNTCyNALDRHVEAGRGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 106 RLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVL 185
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 186 IACDAVTYAGRRHDRKDVLAE-LRRSLPTVEHVILHSEAAAPAAADALLSEIS-ATTGAEIDAFEPAWLPFDHPLWIVYS 263
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKaLELSGHKPHHVLVLNRPQVPADLTKPGRDLDwSELLAKAEPVDCVPVAATDPLYILYT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 264 SGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCsyhensfGERYHWYSSTGWIMWNSQV--GGLLSGTTCCIFDGSPGGA 341
Cdd:cd05967 239 SGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKP-------GDVWWAASDVGWVVGHSYIvyGPLLHGATTVLYEGKPVGT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 342 kdkPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVD--LVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFaglsktngS 419
Cdd:cd05967 312 ---PDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDgkYIKKYDLSSLRTLFLAGERLDPPTLEWAENTL--------G 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 420 KAQADIWWANISGGTDFAGAFigGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPM-PSMPLYFWNDK 497
Cdd:cd05967 381 VPVIDHWWQTETGWPITANPV--GLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVgPNELGNIVIKLPLpPGCLLTLWKND 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 498 GgaRYRASYFETYPdnfdgtgrgPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL 577
Cdd:cd05967 459 E--RFKKLYLSKFP---------GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGV 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 578 eylgRDSY---MPL-FVVLREGVafdGAMQAKINKAIEAgLSRRFL-----PNEIFAVAEIPRTLSGKKQELPIKKLLLG 648
Cdd:cd05967 528 ----RDELkgqVPLgLVVLKEGV---KITAEELEKELVA-LVREQIgpvaaFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
|
...
gi 517269147 649 QPV 651
Cdd:cd05967 600 EDY 602
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
16-636 |
3.42e-52 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 191.12 E-value: 3.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 16 LAEKRGLNFDSYEEMRQWSVRDLDGFW--HA---IWDyydlqspTPFAAVITERKmPGALWFPGAQVNYARQ-VFRHVDA 89
Cdd:PRK00174 8 FAANALIDMEQYKALYQESVEDPEGFWaeQAkrlDWF-------KPFDTVLDWNA-PFIKWFEDGELNVSYNcLDRHLKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 90 -ADAAglpAIVSCGEDGRLCET-SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPD 167
Cdd:PRK00174 80 rGDKV---AIIWEGDDPGDSRKiTYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 168 MAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTVEHVILHSeaaapaaadallseisaTTGAEI--- 244
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVR-----------------RTGGDVdwv 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 245 ---------------DAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIiivvlaLLGLHNDlgcsyHENSF----GE 305
Cdd:PRK00174 220 egrdlwwhelvagasDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGY------LVYAAMT-----MKYVFdykdGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 306 RYhWYSS-TGWIMWNSQV--GGLLSGTTCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAA 382
Cdd:PRK00174 289 VY-WCTAdVGWVTGHSYIvyGPLANGATTLMFEGVP----NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 383 GDLSQLRCLGSTGSPLSADTQAWFNNRFaGLSKTngskAQADIWWANISGG---TDFAGAFiggnrelPQTPGAMQCRLL 459
Cdd:PRK00174 364 YDLSSLRLLGSVGEPINPEAWEWYYKVV-GGERC----PIVDTWWQTETGGimiTPLPGAT-------PLKPGSATRPLP 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 460 GAAVEAFDEQGRAVIGEV-GELVCTEPMPSMPLYFWNDKggARYRASYFETYPDNFDGtgrgpvwrhGDWLKVDPDGSCI 538
Cdd:PRK00174 432 GIQPAVVDEEGNPLEGGEgGNLVIKDPWPGMMRTIYGDH--ERFVKTYFSTFKGMYFT---------GDGARRDEDGYYW 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 539 IYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVV----DLEylGRDSYMplFVVLREGVAFDGAMQAKINK--AIEA 612
Cdd:PRK00174 501 ITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVgrpdDIK--GQGIYA--FVTLKGGEEPSDELRKELRNwvRKEI 576
|
650 660
....*....|....*....|....*
gi 517269147 613 G-LSRrflPNEIFAVAEIPRTLSGK 636
Cdd:PRK00174 577 GpIAK---PDVIQFAPGLPKTRSGK 598
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
27-673 |
2.84e-51 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 188.95 E-value: 2.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 27 YEEMRQWSVRDLDGFWHAIWDYYDLQSPTPFAAVITE----RKMPGAL-WFPGAQVNYARQ-VFRHVDAADAAGLPAIVS 100
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSEnldvRKGPISIeWFKGGKTNICYNcLDRNVEAGNGDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 101 CGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQI 180
Cdd:PLN02654 112 GNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 181 EPKVLIACDAVTYAGRRHDRKDVlaelrrslptVEHVILHSEAAAPAAADALLSEISATTGAEIDAFEPA---------- 250
Cdd:PLN02654 192 KPKVVITCNAVKRGPKTINLKDI----------VDAALDESAKNGVSVGICLTYENQLAMKREDTKWQEGrdvwwqdvvp 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 251 ---------WLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDlgcsYHEnsfGERYHWYSSTGWIMWNSQ 321
Cdd:PLN02654 262 nyptkceveWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFD----YKP---TDVYWCTADCGWITGHSY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 322 V--GGLLSGTTCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLS 399
Cdd:PLN02654 335 VtyGPMLNGATVLVFEGAP----NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPIN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 400 ADTQAWFNNrFAGLSKTNGSkaqaDIWWANISGG---TDFAGAFiggnrelPQTPGAMQCRLLGAAVEAFDEQGRAVIGE 476
Cdd:PLN02654 411 PSAWRWFFN-VVGDSRCPIS----DTWWQTETGGfmiTPLPGAW-------PQKPGSATFPFFGVQPVIVDEKGKEIEGE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 477 VGELVCTEPmpSMPLYFWNDKGG-ARYRASYFETYPDnfdgtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMG 555
Cdd:PLN02654 479 CSGYLCVKK--SWPGAFRTLYGDhERYETTYFKPFAG---------YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 556 TSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSG 635
Cdd:PLN02654 548 TAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSG 627
|
650 660 670
....*....|....*....|....*....|....*...
gi 517269147 636 KKQELPIKKLLLGQpVEKVINREAMANPACLDWYLAFA 673
Cdd:PLN02654 628 KIMRRILRKIASRQ-LDELGDTSTLADPGVVDQLIALA 664
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
25-636 |
3.28e-41 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 159.34 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 25 DSYEEMRQWSVRDLDGFWHAIWDYYDLQspTPFAAVITERKMPGALWFPGAQVNYARQ-VFRHVDA-ADAAGLPAIVScg 102
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQ--TPFTQVLDYSNPPFARWFVGGRTNLCHNaVDRHLAKrPEQLALIAVST-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 103 EDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEP 182
Cdd:PRK10524 78 ETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 183 KVLIACDAVTYAGRRHDRKDVLAE-LRRSLPTVEHVILHSEAaapaaadalLSEISATTGAEID-----------AFEPA 250
Cdd:PRK10524 158 VLIVSADAGSRGGKVVPYKPLLDEaIALAQHKPRHVLLVDRG---------LAPMARVAGRDVDyatlraqhlgaRVPVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 251 WLPFDHPLWIVYSSGTTGLPKPIVHGHGGiIIVVLAllglhndlgcSYHENSF----GERYHWYSSTGWIMWNSQV--GG 324
Cdd:PRK10524 229 WLESNEPSYILYTSGTTGKPKGVQRDTGG-YAVALA----------TSMDTIFggkaGETFFCASDIGWVVGHSYIvyAP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 325 LLSGTTCCIFDGSPggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQA 404
Cdd:PRK10524 298 LLAGMATIMYEGLP----TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTAS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 405 WfnnrfagLSKTNGsKAQADIWWANISGGTDFAGAfiGGNRELPQTPGAMQCRLLGAAVEAFDEQ-GRAV-IGEVGELVC 482
Cdd:PRK10524 374 W-------ISEALG-VPVIDNYWQTETGWPILAIA--RGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCgPNEKGVLVI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 483 TEPMPSMPLY-FWNDKggARYRASYFETYpdnfdgtgRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYS 561
Cdd:PRK10524 444 EGPLPPGCMQtVWGDD--DRFVKTYWSLF--------GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 562 AIEALPEVLDSLVVDLEylgrDSY---MPL-FVVLREGVAFDG-----AMQAKINKAIEAGLSRRFLPNEIFAVAEIPRT 632
Cdd:PRK10524 514 SISSHPAVAEVAVVGVK----DALkgqVAVaFVVPKDSDSLADrearlALEKEIMALVDSQLGAVARPARVWFVSALPKT 589
|
....
gi 517269147 633 LSGK 636
Cdd:PRK10524 590 RSGK 593
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
256-638 |
2.99e-40 |
|
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: 150.51 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 256 HPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDlgcsyhenSFGERYHWYSSTGWI-MWNSQVGGLLSGTTCCIF 334
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL--------TEGDVFLSTLPLFHIgGLFGLLGALLAGGTVVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 335 DgspggakdKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAevDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFagls 414
Cdd:cd04433 73 P--------KFDPEAALELIEREKVTILLGVPTLLARLLKA--PESAGYDLSSLRALVSGGAPLPPELLERFEEAP---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 415 ktngskaqaDIWWANISGGTDFAGAFIGGNRELPQT-PGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPMPsMPLY 492
Cdd:cd04433 139 ---------GIKLVNGYGLTETGGTVATGPPDDDARkPGSVGRPVPGVEVRIVDPDGGELpPGEIGELVVRGPSV-MKGY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 493 fWNDkggaryrasYFETYPDNFDGtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDS 572
Cdd:cd04433 209 -WNN---------PEATAAVDEDG-----WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517269147 573 LV--VDLEYLGRDsyMPLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:cd04433 274 AVvgVPDPEWGER--VVAVVVLRPGADLD---AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
80-549 |
1.79e-36 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 142.07 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVsCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:pfam00501 2 ERQAARTPDK------TALE-VGEGRRL---TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWSLCAPDMAAPAVIDRFKQIEPKVLIAcdavtyagrrhDRKDVLAELRRSLPTVEHV--ILHSEAAAPAAADALLSEIS 237
Cdd:pfam00501 72 VYVPLNPRLPAEELAYILEDSGAKVLIT-----------DDALKLEELLEALGKLEVVklVLVLDRDPVLKEEPLPEEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 238 AttgAEIDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGcSYHENsfgERYHWYSSTGWIM 317
Cdd:pfam00501 141 P---ADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGF-GLGPD---DRVLSTLPLFHDF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 318 -WNSQV-GGLLSGTTCCIFDGSPggakdKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAevDLVAAGDLSQLRCLGSTG 395
Cdd:pfam00501 214 gLSLGLlGPLLAGATVVLPPGFP-----ALDPAALLELIERYKVTVLYGVPTLLNMLLEA--GAPKRALLSSLRLVLSGG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 396 SPLSADTQAWFNNRFAGlsktngskAQADIWWANISGGTDFAGAFIGGNRELPQTPGA----MQCRLLGaaveafDEQGR 471
Cdd:pfam00501 287 APLPPELARRFRELFGG--------ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRplpgTEVKIVD------DETGE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 472 AV-IGEVGELVCTEPMPsMPLYfWNDKGgaRYRASYFEtypdnfDGtgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINR 549
Cdd:pfam00501 353 PVpPGEPGELCVRGPGV-MKGY-LNDPE--LTAEAFDE------DG------WYRtGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
89-640 |
7.59e-34 |
|
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: 134.94 E-value: 7.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDM 168
Cdd:COG0318 9 AARHPDRPALVF--GGRRL---TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 AAPAVIDRFKQIEPKVLIACdavtyagrrhdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaeidafe 248
Cdd:COG0318 84 TAEELAYILEDSGARALVTA------------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 pawlpfdhplWIVYSSGTTGLPKPIVHGHGGII---IVVLALLGLHNDlgcsyhensfgERY-HW---YSSTGWIMWNsq 321
Cdd:COG0318 104 ----------LILYTSGTTGRPKGVMLTHRNLLanaAAIAAALGLTPG-----------DVVlVAlplFHVFGLTVGL-- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 322 VGGLLSGTTCCIFdgspggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEvdLVAAGDLSQLRCLGSTGSPLSAD 401
Cdd:COG0318 161 LAPLLAGATLVLL--------PRFDPERVLELIERERVTVLFGVPTMLARLLRHP--EFARYDLSSLRLVVSGGAPLPPE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 402 TQAWFNNRFA-------GLSKTNGskaqadiwwanisggtdfaGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV- 473
Cdd:COG0318 231 LLERFEERFGvrivegyGLTETSP-------------------VVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELp 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 474 IGEVGELVCTEPMPsMPLYfWNDkggaryrasyfetyPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLR 553
Cdd:COG0318 292 PGEVGEIVVRGPNV-MKGY-WND--------------PEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGEN 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 554 MGTSELYSAIEALPEVLDSLVVDL--EYLGRDSYmpLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPR 631
Cdd:COG0318 356 VYPAEVEEVLAAHPGVAEAAVVGVpdEKWGERVV--AFVVLRPGAELD---AEELRAFLRERLARYKVPRRVEFVDELPR 430
|
570
....*....|.
gi 517269147 632 TLSGK--KQEL 640
Cdd:COG0318 431 TASGKidRRAL 441
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
111-636 |
2.72e-32 |
|
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: 130.31 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI----WSLCAPDmaapAVIDRFKQIEPKVLI 186
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVicplFSAFGPE----AIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 187 ACDAVTyagRRHDRKDvlaelrrslptvehvilhseaaapaaadallseisattgaeidafepawlpfdhPLWIVYSSGT 266
Cdd:cd05969 78 TTEELY---ERTDPED------------------------------------------------------PTLLHYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 267 TGLPKPIVHGHGGIIIVVLA---LLGLHNDlGCSYHENSFGeryhWYSSTGWIMWnsqvGGLLSGTTCCIFDGSpggaKD 343
Cdd:cd05969 101 TGTPKGVLHVHDAMIFYYFTgkyVLDLHPD-DIYWCTADPG----WVTGTVYGIW----APWLNGVTNVVYEGR----FD 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 344 KPDWttlWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFaglsktngSKAQA 423
Cdd:cd05969 168 AESW---YGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF--------GVPIH 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 424 DIWWAnisggTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPMPSMPLYFWNDkgGARY 502
Cdd:cd05969 237 DTWWQ-----TETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELpPGTKGILALKPGWPSMFRGIWND--EERY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 503 RASYFETYpdnfdgtgrgpvWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGR 582
Cdd:cd05969 310 KNSFIDGW------------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLR 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 517269147 583 DSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05969 378 GEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
111-644 |
2.61e-29 |
|
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: 121.29 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIaCDA 190
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-TDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 vtyagrrhdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaeidafepawlpfDHPLWIVYSSGTTGLP 270
Cdd:cd05972 81 ----------------------------------------------------------------EDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 KPIVHGHG---GIIIVVLALLGLHNDlgcsyhensfgeRYHW-YSSTGWI--MWNSQVGGLLSGTTCCIFDGSPGGAKDK 344
Cdd:cd05972 97 KGVLHTHSyplGHIPTAAYWLGLRPD------------DIHWnIADPGWAkgAWSSFFGPWLLGATVFVYEGPRFDAERI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 345 PD---------WT---TLWRFVAQskatffgagaaffancakaeVDLvAAGDLSQLRCLGSTGSPLSADTQAWFNnRFAG 412
Cdd:cd05972 165 LEllerygvtsFCgppTAYRMLIK--------------------QDL-SSYKFSHLRLVVSAGEPLNPEVIEWWR-AATG 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 413 LSKTNGSkaqadiwwanisGGTDfAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVI-GEVGELVCTEPMPSMPL 491
Cdd:cd05972 223 LPIRDGY------------GQTE-TGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPpGEEGDIAIKLPPPGLFL 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 492 YFWNDKggARYRASYfetypdnfdgtgRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLD 571
Cdd:cd05972 290 GYVGDP--EKTEASI------------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAE 355
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517269147 572 SLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKK 644
Cdd:cd05972 356 AAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
104-636 |
2.77e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 118.30 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 104 DGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslcapdmAAPAVidrfkqiepk 183
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAI--------AVPLF---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 184 VLIACDAVtyagrrhdrkdvlaelrrslptvEHVILHSEAAApaaadaLLSEISattgaeidafepawlpfDHPLWIVYS 263
Cdd:cd05971 63 ALFGPEAL-----------------------EYRLSNSGASA------LVTDGS-----------------DDPALIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 264 SGTTGLPKPIVHGHggiiivvLALLGlHNDLGCSYHENSFGERYHWYSSTGWiMWnsqVGGLLSGTTCCIFDGSP--GGA 341
Cdd:cd05971 97 SGTTGPPKGALHAH-------RVLLG-HLPGVQFPFNLFPRDGDLYWTPADW-AW---IGGLLDVLLPSLYFGVPvlAHR 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 342 KDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGdlSQLRCLGSTGSPLSADTQAW----FN---NRFAGLS 414
Cdd:cd05971 165 MTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ--VKLRAIATGGESLGEELLGWareqFGvevNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 415 KTNgskaqadiwwanisggtdfagAFIGGNREL-PQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPMPSMPLY 492
Cdd:cd05971 243 ECN---------------------LVIGNCSALfPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 493 FWNDKGG--ARYRASYFETypdnfdgtgrgpvwrhGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVL 570
Cdd:cd05971 302 YWNNPSAteKKMAGDWLLT----------------GDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVL 365
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517269147 571 DSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05971 366 MAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
71-636 |
5.48e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 116.15 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 71 WFPGAQVNYARQ-VFRHVDAAdAAGLPAIVSCGEDGRLcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETII 149
Cdd:PRK04319 36 WLETGKVNIAYEaIDRHADGG-RKDKVALRYLDASRKE-KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 150 AFLASASIGAIWS-LCAPDMAAPaVIDRFKQIEPKVLIACDAVtyagrrHDRKDVlaelrRSLPTVEHVILHSEAAAPAA 228
Cdd:PRK04319 114 ALLGALKNGAIVGpLFEAFMEEA-VRDRLEDSEAKVLITTPAL------LERKPA-----DDLPSLKHVLLVGEDVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 229 A----DALLSEISattgaeiDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGII---IVVLALLGLHNDlgcsyhen 301
Cdd:PRK04319 182 GtldfNALMEQAS-------DEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLqhyQTGKYVLDLHED-------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 302 sfgERYHWYSSTGWIMWNSQ--VGGLLSGTTCCIFdgspGGAKDKPDWttlWRFVAQSKATFFGAGAAFFANCAKAEVDL 379
Cdd:PRK04319 247 ---DVYWCTADPGWVTGTSYgiFAPWLNGATNVID----GGRFSPERW---YRILEDYKVTVWYTAPTAIRMLMGAGDDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 380 VAAGDLSQLRCLGSTGSPLSADTQAW----FNNRFaglsktngskaqADIWWAnisggTDFAGAFIGGNRELPQTPGAMQ 455
Cdd:PRK04319 317 VKKYDLSSLRHILSVGEPLNPEVVRWgmkvFGLPI------------HDNWWM-----TETGGIMIANYPAMDIKPGSMG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 456 CRLLG--AAVEAFDEQGRAViGEVGELVCTEPMPSMPLYFWNDKggARYRaSYFetypdnfdgtgRGPVWRHGDWLKVDP 533
Cdd:PRK04319 380 KPLPGieAAIVDDQGNELPP-NRMGNLAIKKGWPSMMRGIWNNP--EKYE-SYF-----------AGDWYVSGDSAYMDE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 534 DGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAG 613
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKG 524
|
570 580
....*....|....*....|...
gi 517269147 614 LSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:PRK04319 525 LGAHAAPREIEFKDKLPKTRSGK 547
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
141-636 |
3.28e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 112.99 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 141 LPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIACDAVTYAGRRHDRKDVLAELRRS----LPTVE- 215
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAkaivLPAAGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 216 --HVILHSEAAAPAAADALLSEISATTGAEidaFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHggiiivvLALLGLHND 293
Cdd:PLN03051 81 pvAVPLREQDLSWCDFLGVAAAQGSVGGNE---YSPVYAPVESVTNILFSSGTTGEPKAIPWTH-------LSPLRCASD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 294 lGCSYHENSFGERYHWYSSTGWIMWNSQV-GGLLSGTTCCIFDGSPGGakdkPDWTtlwRFVAQSKATFFGAGAAFFANC 372
Cdd:PLN03051 151 -GWAHMDIQPGDVVCWPTNLGWMMGPWLLySAFLNGATLALYGGAPLG----RGFG---KFVQDAGVTVLGLVPSIVKAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 373 AKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWfnnrfagLSKTNGSKAQAdiwwANISGGTDFAGAFIGGNRELPQTPG 452
Cdd:PLN03051 223 RHTGAFAMEGLDWSKLRVFASTGEASAVDDVLW-------LSSVRGYYKPV----IEYCGGTELASGYISSTLLQPQAPG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 453 AMQCRLLGAAVEAFDEQG------RAVIGEVGelvctepmPSMPLYFWNDK-GGARYRASYFETYPdNFDGTGRgPVWRH 525
Cdd:PLN03051 292 AFSTASLGTRFVLLNDNGvpypddQPCVGEVA--------LAPPMLGASDRlLNADHDKVYYKGMP-MYGSKGM-PLRRH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 526 GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAI-EALPEVLDSLVVDLEYLGRDSYMpLFVVLREGVAFDG---- 600
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGPEL-LVIFLVLGEEKKGfdqa 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 517269147 601 ---AMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:PLN03051 441 rpeALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNK 479
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
16-636 |
5.44e-26 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 113.64 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 16 LAEKRGLNF---------DSYEEMRQWSVRDLDGFWHAIWDYYDLQSPTPFAAVI--TERKMPGALWFPGAQVNYARQVF 84
Cdd:PLN03052 102 LLEARGKELlgskykdpiSSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILdtSDESNPGGQWLPGAVLNVAECCL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 85 -----RHVDAadaaglPAIV--SCGEDGR-LCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASAS 156
Cdd:PLN03052 182 tpkpsKTDDS------IAIIwrDEGSDDLpVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIIL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 157 IGAIWSLCAPDMAAPAVIDRFKQIEPKVLIACDAVTYAGRRHD--RKDVLAELRRS--LPTVEHVILHSEAAAPAAADAL 232
Cdd:PLN03052 256 AGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPlySRVVEAKAPKAivLPADGKSVRVKLREGDMSWDDF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 233 LSEisATTGAEIDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHggiiivvlallglHNDLGCS-----YHENSFGERY 307
Cdd:PLN03052 336 LAR--ANGLRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQ-------------LTPLRAAadawaHLDIRKGDIV 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 308 HWYSSTGWIMWNSQV-GGLLSGTTCCIFDGSPGGakdkpdwTTLWRFVAQSKATF-----FGAGAAFFANCakaevdlVA 381
Cdd:PLN03052 401 CWPTNLGWMMGPWLVyASLLNGATLALYNGSPLG-------RGFAKFVQDAKVTMlgtvpSIVKTWKNTNC-------MA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 382 AGDLSQLRCLGSTGSPLSADTQAWfnnrfagLSktngSKAqadiWWANI---SGGTDFAGAFIGGNRELPQTPGAMQCRL 458
Cdd:PLN03052 467 GLDWSSIRCFGSTGEASSVDDYLW-------LM----SRA----GYKPIieyCGGTELGGGFVTGSLLQPQAFAAFSTPA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 459 LGAAVEAFDEQGRAVIGEVgelVCTEPMPSMPLYFwndkgGARYR---ASYFETYpdnFDGTgrgPVW------RHGDWL 529
Cdd:PLN03052 532 MGCKLFILDDSGNPYPDDA---PCTGELALFPLMF-----GASSTllnADHYKVY---FKGM---PVFngkilrRHGDIF 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 530 KVDPDGSCIIYGRSDATINRHGLRMGTSElysaIEALPEVLDSLVVDLEYLGrdsyMP----------LFVVLR--EGVA 597
Cdd:PLN03052 598 ERTSGGYYRAHGRADDTMNLGGIKVSSVE----IERVCNAADESVLETAAIG----VPppgggpeqlvIAAVLKdpPGSN 669
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 517269147 598 FDGAM-QAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:PLN03052 670 PDLNElKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNK 709
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
111-636 |
2.08e-25 |
|
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: 110.38 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIaCDa 190
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF-TD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 vtyagrrHDRKDVLAELRRSLPTVEHVILHSEAAAPAAADALLSEISATTgAEIDAFEPAWLPFDHPLWIVYSSGTTGLP 270
Cdd:cd05911 90 -------PDGLEKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLSPTLGE-EDEDLPPPLKDGKDDTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 KPIVHGHGGIIIvvlallglHNDLGCSYHENSFGERYHWYSSTG--WIMwnsqvgGLLSGTTCCIFdGSPGGAKDKPDWT 348
Cdd:cd05911 162 KGVCLSHRNLIA--------NLSQVQTFLYGNDGSNDVILGFLPlyHIY------GLFTTLASLLN-GATVIIMPKFDSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 349 TLWRFVAQSKATFFGAGAAFFANCAKAEvdLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFAGlsktngskaqadiWWA 428
Cdd:cd05911 227 LFLDLIEKYKITFLYLVPPIAAALAKSP--LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPN-------------ATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 429 NISGGTDFAGAFIGGNRELPQTPGA-------MQCRLLgaaveafDEQGRAV--IGEVGELVCTEPMPsMPLYFWNDKGG 499
Cdd:cd05911 292 KQGYGMTETGGILTVNPDGDDKPGSvgrllpnVEAKIV-------DDDGKDSlgPNEPGEICVRGPQV-MKGYYNNPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 500 ARYRASyfetypdnfDGtgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLe 578
Cdd:cd05911 364 KETFDE---------DG------WLHtGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGI- 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 579 YLGRDSYMPL-FVVLREG-VAFDGAMQAKINKAIEaglSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05911 428 PDEVSGELPRaYVVRKPGeKLTEKEVKDYVAKKVA---SYKQLRGGVVFVDEIPKSASGK 484
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-638 |
2.35e-24 |
|
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: 107.45 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 78 NYARQVFRHVDAADAaGLPAIVScgeDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASI 157
Cdd:cd05959 4 NAATLVDLNLNEGRG-DKTAFID---DAG--SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 158 GAIwslcapdmaaPAVIDRFKQIEPKVLIACD----AVTYAGRRHDRkdVLAELRRSLPTVEHVILhSEAAAPAAADALL 233
Cdd:cd05959 78 GIV----------PVPVNTLLTPDDYAYYLEDsrarVVVVSGELAPV--LAAALTKSEHTLVVLIV-SGGAGPEAGALLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 234 SEISAttgAEIDAFEPAWL-PFDHPLWIvYSSGTTGLPKPIVHGHGGIIIVVLA----LLGLHNDLGCSyhenSFGERYH 308
Cdd:cd05959 145 AELVA---AEAEQLKPAAThADDPAFWL-YSSGSTGRPKGVVHLHADIYWTAELyarnVLGIREDDVCF----SAAKLFF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 309 WYSstgwiMWNSQVGGLLSGTTCCIFDGSPggakdKPDwtTLWRFVAQSKATFFGAGAAFFANCAKAEVdlVAAGDLSQL 388
Cdd:cd05959 217 AYG-----LGNSLTFPLSVGATTVLMPERP-----TPA--AVFKRIRRYRPTVFFGVPTLYAAMLAAPN--LPSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 389 RCLGSTGSPLSADTQAWFNNRFaGLSKTNGSkaqadiwwanisGGTDFAGAFIGgNRELPQTPGAMQCRLLGAAVEAFDE 468
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARF-GLDILDGI------------GSTEMLHIFLS-NRPGRVRYGTTGKPVPGYEVELRDE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 469 QGRAV-IGEVGELVCTEPmpSMPLYFWNdkggaRYRASyfetyPDNFDGTgrgpvW-RHGDWLKVDPDGSCIIYGRSDAT 546
Cdd:cd05959 349 DGGDVaDGEPGELYVRGP--SSATMYWN-----NRDKT-----RDTFQGE-----WtRTGDKYVRDDDGFYTYAGRADDM 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 547 INRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAV 626
Cdd:cd05959 412 LKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFV 491
|
570
....*....|..
gi 517269147 627 AEIPRTLSGKKQ 638
Cdd:cd05959 492 DELPKTATGKIQ 503
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
80-273 |
3.76e-22 |
|
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: 100.61 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVscGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:COG1021 32 RRRAERHPDR------IAVV--DGERRL---SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IwslcaPDMAAPA----VIDRF-KQIEPKVLIACDAVtyagRRHDRKDVLAELRRSLPTVEHVILHSEAAAPAAADALLS 234
Cdd:COG1021 101 I-----PVFALPAhrraEISHFaEQSEAVAYIIPDRH----RGFDYRALARELQAEVPSLRHVLVVGDAGEFTSLDALLA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 517269147 235 EISATTGAEIDAFEPAWLpfdhplwiVYSSGTTGLPKPI 273
Cdd:COG1021 172 APADLSEPRPDPDDVAFF--------QLSGGTTGLPKLI 202
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
111-644 |
3.91e-22 |
|
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: 99.90 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLiacda 190
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 VTYAGRRHdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaEIDafepawlpfDHPLWIVYSSGTTGLP 270
Cdd:cd05973 77 VTDAANRH--------------------------------------------KLD---------SDPFVMMFTSGTTGLP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 KpivhghgGIIIVVLALLGLHndlgcSYHENSFGER---YHW-YSSTGWI--MWNSQVGGLLSGTTCCIFDGspgGAKDK 344
Cdd:cd05973 104 K-------GVPVPLRALAAFG-----AYLRDAVDLRpedSFWnAADPGWAygLYYAITGPLALGHPTILLEG---GFSVE 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 345 PDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAagdlsQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNGSKAQAD 424
Cdd:cd05973 169 STWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKG-----RLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 425 IWWANISGGTDfagafiggnrelPQTPGAMQCRLLGAAVEAFDEQGRavigevgelvctEPMPSMPLYFWNDKggARYRA 504
Cdd:cd05973 244 MVLANHHALEH------------PVHAGSAGRAMPGWRVAVLDDDGD------------ELGPGEPGRLAIDI--ANSPL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 505 SYFETYPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDS 584
Cdd:cd05973 298 MWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTE 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 585 YMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKK 644
Cdd:cd05973 378 VVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
109-638 |
3.67e-20 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 93.68 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIA- 187
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 188 CDAVTYagrrhdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaeidafepaWLpfdhplwivYSSGTT 267
Cdd:cd05919 90 ADDIAY---------------------------------------------------------LL---------YSSGTT 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 268 GLPKPIVHGHGGIIIVVLAL----LGLH-NDLGCSYHENSFGeryhwysstgWIMWNSQVGGLLSGTTCCIFDGSPggak 342
Cdd:cd05919 104 GPPKGVMHAHRDPLLFADAMareaLGLTpGDRVFSSAKMFFG----------YGLGNSLWFPLAVGASAVLNPGWP---- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 343 dKPD--WTTLWRFvaqsKATFFGAGAAFFANcAKAEVDLVAAgDLSQLRCLGSTGSPLSADT-QAWFNnrFAGLSKTNGS 419
Cdd:cd05919 170 -TAErvLATLARF----RPTVLYGVPTFYAN-LLDSCAGSPD-ALRSLRLCVSAGEALPRGLgERWME--HFGGPILDGI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 420 kaqadiwwanisGGTDFAGAFIGgNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTepMPSMPLYFWNDkg 498
Cdd:cd05919 241 ------------GATEVGHIFLS-NRPGAWRLGSTGRPVPGYEIRLVDEEGHTIpPGEEGDLLVR--GPSAAVGYWNN-- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 499 garyrasyfetyPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLE 578
Cdd:cd05919 304 ------------PEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP 371
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 579 YLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:cd05919 372 ESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
83-636 |
2.63e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 91.87 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 83 VFRHVdaADAAG-LPAIVsCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAiw 161
Cdd:PRK07798 8 LFEAV--ADAVPdRVALV-CGDR----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 162 slcapdmaAPAVID-RFKQIEPKVLIA-CDAVTYAgrrHDRK--DVLAELRRSLPTVEHVILHSEAAAPAAADALLS--E 235
Cdd:PRK07798 79 --------VPVNVNyRYVEDELRYLLDdSDAVALV---YEREfaPRVAEVLPRLPKLRTLVVVEDGSGNDLLPGAVDyeD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 236 ISATTGAEIDAFEPAwlPFDhpLWIVYSSGTTGLPKPIVHGHGGIiivVLALLGLHNDLGCSYHENSFG--ERYHWYSST 313
Cdd:PRK07798 148 ALAAGSPERDFGERS--PDD--LYLLYTGGTTGMPKGVMWRQEDI---FRVLLGGRDFATGEPIEDEEElaKRAAAGPGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 314 GWI----------MWNSqVGGLLSGTTCCIFDgspggaKDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAG 383
Cdd:PRK07798 221 RRFpapplmhgagQWAA-FAALFSGQTVVLLP------DVRFDADEVWRTIEREKVNVITIVGDAMARPLLDALEARGPY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 384 DLSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNGSKAQAdiwwanisggTDFAGAFIGGNRELPQTPGAMQcrlLGAAV 463
Cdd:PRK07798 294 DLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSE----------TGFGGSGTVAKGAVHTGGPRFT---IGPRT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 464 EAFDEQGRAV---IGEVGELVctePMPSMPLYFWNDKggARYRASYFEtypdnFDGTgrgpvwRH---GDWLKVDPDGSC 537
Cdd:PRK07798 361 VVLDEDGNPVepgSGEIGWIA---RRGHIPLGYYKDP--EKTAETFPT-----IDGV------RYaipGDRARVEADGTI 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 538 IIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVdleylGRDSymPLF-------VVLREGVAFDgamQAKINKAI 610
Cdd:PRK07798 425 TLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV-----GVPD--ERWgqevvavVQLREGARPD---LAELRAHC 494
|
570 580
....*....|....*....|....*.
gi 517269147 611 EAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:PRK07798 495 RSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
80-641 |
3.51e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.45 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVfrHVDAADAAGLPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:PRK07788 52 AGLV--AHAARRAPDRAALID--ERGTL---TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWSLCAPDMAAP---AVIDRFKQiepKVLIACDAVTyagrrhdrkDVLAELRRSLPTVEHVILHSEAAAPAAADAL-LSE 235
Cdd:PRK07788 125 RIILLNTGFSGPqlaEVAAREGV---KALVYDDEFT---------DLLSALPPDLGRLRAWGGNPDDDEPSGSTDEtLDD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 236 ISATTGAeidafEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLglhndlgcsyhensfgERYHW------ 309
Cdd:PRK07788 193 LIAGSST-----APLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLL----------------SRVPFragett 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 310 ------YSSTGWIMWNsqVGGLLSGTTCC--IFDgspggakdkPDwTTLwRFVAQSKATFFGAGAAFFANCAKAEVDLVA 381
Cdd:PRK07788 252 llpapmFHATGWAHLT--LAMALGSTVVLrrRFD---------PE-ATL-EDIAKHKATALVVVPVMLSRILDLGPEVLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 382 AGDLSQLRCLGSTGSPLSADTQAWFNNRFaglsktngskaqADIWWaNISGGTDFAGAFIGGNRELPQTPGAMQCRLLGA 461
Cdd:PRK07788 319 KYDTSSLKIIFVSGSALSPELATRALEAF------------GPVLY-NLYGSTEVAFATIATPEDLAEAPGTVGRPPKGV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 462 AVEAFDEQGRAV-IGEVGELVCTEPMPsmplyfwndkggaryrasyFETYPDnfdgtGRGPVWRH-----GDWLKVDPDG 535
Cdd:PRK07788 386 TVKILDENGNEVpRGVVGRIFVGNGFP-------------------FEGYTD-----GRDKQIIDgllssGDVGYFDEDG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 536 SCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVV---DLEYLGRdsyMPLFVVLREGVAFDGAMqakINKAIEA 612
Cdd:PRK07788 442 LLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIgvdDEEFGQR---LRAFVVKAPGAALDEDA---IKDYVRD 515
|
570 580 590
....*....|....*....|....*....|.
gi 517269147 613 GLSRRFLPNEIFAVAEIPRTLSGK--KQELP 641
Cdd:PRK07788 516 NLARYKVPRDVVFLDELPRNPTGKvlKRELR 546
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
79-636 |
8.24e-18 |
|
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: 87.01 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 79 YARQVFRHVDAadaaglPAIVScgeDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG 158
Cdd:cd17651 1 FERQAARTPDA------PALVA---EGR--RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 159 AIwslCAP-DMAAPAvidrfkqiEPKVLIACDAVTYAGRRHDRKDVLAELRRSLPTvehvilhseaaaPAAADALLSEIS 237
Cdd:cd17651 70 AA---YVPlDPAYPA--------ERLAFMLADAGPVLVLTHPALAGELAVELVAVT------------LLDQPGAAAGAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 238 ATTGAEIDAfepawlpfDHPLWIVYSSGTTGLPKPIVHGHGGiiivVLALLGLHndlgCSYHENSFGERYHWYSSTG--- 314
Cdd:cd17651 127 AEPDPALDA--------DDLAYVIYTSGSTGRPKGVVMPHRS----LANLVAWQ----ARASSLGPGARTLQFAGLGfdv 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 315 --WIMWnsqvGGLLSGTTCCIfdgspGGAKDKPDWTTLWRFVAQSKATFFGAGAAFFAncAKAEVDLVAAGDLSQLRCLG 392
Cdd:cd17651 191 svQEIF----STLCAGATLVL-----PPEEVRTDPPALAAWLDEQRISRVFLPTVALR--ALAEHGRPLGVRLAALRYLL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 393 STGSPLS--ADTQAWfnnrFAGLSKTNgskaqadiwWANISGGTD--FAGAfiggnRELPQTPGAMQCR------LLGAA 462
Cdd:cd17651 260 TGGEQLVltEDLREF----CAGLPGLR---------LHNHYGPTEthVVTA-----LSLPGDPAAWPAPppigrpIDNTR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 463 VEAFDEQGRAV-IGEVGElvctepmpsmpLYFwndkGGARYRASYF-------ETY-PDNFDGTGRgpVWRHGDWLKVDP 533
Cdd:cd17651 322 VYVLDAALRPVpPGVPGE-----------LYI----GGAGLARGYLnrpeltaERFvPDPFVPGAR--MYRTGDLARWLP 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 534 DGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamQAKINKAIEAG 613
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVD---AAELRAALATH 461
|
570 580
....*....|....*....|...
gi 517269147 614 LSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGK 484
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
103-646 |
1.55e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 86.39 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 103 EDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-----WSLCAPDMA-----Apa 172
Cdd:PRK06187 27 FDGR--RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlhpinIRLKPEEIAyilndA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 173 vidrfkqiEPKVLIACDAVTyagrrhdrkDVLAELRRSLPTVEHVILHSEAAAPAAADALLsEISATTGAEIDAFEpaWL 252
Cdd:PRK06187 103 --------EDRVVLVDSEFV---------PLLAAILPQLPTVRTVIVEGDGPAAPLAPEVG-EYEELLAAASDTFD--FP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 253 PFDH--PLWIVYSSGTTGLPKPIVHGHGGIIivvlallgLHNDLGCSyhensfgeryhwysstgWIMWNSQVGGLLS--- 327
Cdd:PRK06187 163 DIDEndAAAMLYTSGTTGHPKGVVLSHRNLF--------LHSLAVCA-----------------WLKLSRDDVYLVIvpm 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 328 ----GTTCC---IFDGSPGGAKDKPDWTTLWRFVAQSKATFFGagaaffanCAKAEV-DLVAA-----GDLSQLRCLGST 394
Cdd:PRK06187 218 fhvhAWGLPylaLMAGAKQVIPRRFDPENLLDLIETERVTFFF--------AVPTIWqMLLKAprayfVDFSSLRLVIYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 395 GSPLSADT-------------QAWfnnrfaGLSKTNGskaqadiwwanisggtdfAGAFiggNRELPQTPGAMQCR---- 457
Cdd:PRK06187 290 GAALPPALlrefkekfgidlvQGY------GMTETSP------------------VVSV---LPPEDQLPGQWTKRrsag 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 458 --LLGAAVEAFDEQGRAV---IGEVGELVCTEPmpsmplyfWNDKGgaryrasYFETyPDNFDGTgrgpvWRHGdWL--- 529
Cdd:PRK06187 343 rpLPGVEARIVDDDGDELppdGGEVGEIIVRGP--------WLMQG-------YWNR-PEATAET-----IDGG-WLhtg 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 530 ---KVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVV---DlEYLGRDsymPL-FVVLREGVAFDgam 602
Cdd:PRK06187 401 dvgYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvpD-EKWGER---PVaVVVLKPGATLD--- 473
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 517269147 603 qakiNKAIEAGLSRRF----LPNEIFAVAEIPRTLSGKKQelpiKKLL 646
Cdd:PRK06187 474 ----AKELRAFLRGRLakfkLPKRIAFVDELPRTSVGKIL----KRVL 513
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
89-636 |
1.73e-17 |
|
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: 85.35 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVscgEDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDM 168
Cdd:cd17631 5 ARRHPDRTALV---FGGR--SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 AAPAVIDRFKQIEPKVLiacdavtyagrrhdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaeidafe 248
Cdd:cd17631 80 TPPEVAYILADSGAKVL--------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 pawlpFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGlhnDLGCSYHENSF--GERYHWYSSTGWIMwnsqvGGLL 326
Cdd:cd17631 97 -----FDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALA---ALDLGPDDVLLvvAPLFHIGGLGVFTL-----PTLL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 327 SGTTCCIFdgspggakDKPDWTTLWRFVAQSKATFFGAgaaffancAKAEVDLVAA------GDLSQLRCLGSTGSPLSA 400
Cdd:cd17631 164 RGGTVVIL--------RKFDPETVLDLIERHRVTSFFL--------VPTMIQALLQhprfatTDLSSLRAVIYGGAPMPE 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 401 DT-QAW--FNNRFA---GLSKTngskaqadiwwaniSGGTDFAGAfiGGNRELPQTPGAmqcRLLGAAVEAFDEQGRAV- 473
Cdd:cd17631 228 RLlRALqaRGVKFVqgyGMTET--------------SPGVTFLSP--EDHRRKLGSAGR---PVFFVEVRIVDPDGREVp 288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 474 IGEVGELVCTEP--MPSmplyFWNDKggaryrasyfETYPDNF-DGtgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINR 549
Cdd:cd17631 289 PGEVGEIVVRGPhvMAG----YWNRP----------EATAAAFrDG------WFHtGDLGRLDEDGYLYIVDRKKDMIIS 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 550 HGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRdsyMPL-FVVLREGVAFDGamQAKINKAIEAgLSRRFLPNEIFAV 626
Cdd:cd17631 349 GGENVYPAEVEDVLYEHPAVAEVAVIGVpdEKWGE---AVVaVVVPRPGAELDE--DELIAHCRER-LARYKIPKSVEFV 422
|
570
....*....|
gi 517269147 627 AEIPRTLSGK 636
Cdd:cd17631 423 DALPRNATGK 432
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
96-636 |
3.74e-17 |
|
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: 84.50 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCAP-DMAAPAvi 174
Cdd:cd05930 4 VAVVD--GDQSL---TYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA---YVPlDPSYPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 175 DRFKQIepkvliacdavtyagrrhdrkdvlaeLRRSLPTVehVILHSeaaapaaadallseisattgaeidafepawlpf 254
Cdd:cd05930 74 ERLAYI--------------------------LEDSGAKL--VLTDP--------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 255 DHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGcsyhensfGERYHWYSSTGWIM-WNSQVGGLLSGTTCCI 333
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTP--------GDRVLQFTSFSFDVsVWEIFGALLAGATLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 334 FDgsPGGAKDKPDwttLWRFVAQSKATFFgagaaffaNC----AKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNR 409
Cdd:cd05930 165 LP--EEVRKDPEA---LADLLAEEGITVL--------HLtpslLRLLLQELELAALPSLRLVLVGGEALPPDLVRRWREL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 410 FAGLSKTNG---SKAQADIWWANISGGTDFAGAF-IGgnRELPQTpgamQCRLLgaaveafDEQGRAV-IGEVGELVCte 484
Cdd:cd05930 232 LPGARLVNLygpTEATVDATYYRVPPDDEEDGRVpIG--RPIPNT----RVYVL-------DENLRPVpPGVPGELYI-- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 485 pmpsmplyfwndkGG---AR-YR------ASYFEtyPDNFDGTGRgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRM 554
Cdd:cd05930 297 -------------GGaglARgYLnrpeltAERFV--PNPFGPGER--MYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 555 GTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLS 634
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDYMVPSAFVVLDALPLTPN 436
|
..
gi 517269147 635 GK 636
Cdd:cd05930 437 GK 438
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
103-288 |
1.77e-16 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 83.23 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 103 EDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslcapdmaaPAVI---DRFKQ 179
Cdd:COG1022 34 EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV----------TVPIyptSSAEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 180 I-------EPKVLIACDAVTYagrrhdrkDVLAELRRSLPTVEHVILHSEAAAPAAADAL-LSEISATtGAEI---DAFE 248
Cdd:COG1022 104 VayilndsGAKVLFVEDQEQL--------DKLLEVRDELPSLRHIVVLDPRGLRDDPRLLsLDELLAL-GREVadpAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517269147 249 PAW--LPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALL 288
Cdd:COG1022 175 ARRaaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALL 216
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
111-644 |
2.44e-15 |
|
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: 78.96 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCAPDMAApavidrfkqiepkvliacda 190
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---TNPILPF-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 vtyagrrHDRKDVLAELRRSLPTVehvilhseaaapaaadallseISATTgaEIDAFEPAWLPfDHPLWIVYSSGTTGLP 270
Cdd:cd05903 60 -------FREHELAFILRRAKAKV---------------------FVVPE--RFRQFDPAAMP-DAVALLLFTSGTTGEP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 KPIVHGHGGIIIVVlallglhndlgCSYHEN-SFGERyhwysstGWIMWNSQVG---GLLSGTTCCIFDGSPGGAKDkpD 346
Cdd:cd05903 109 KGVMHSHNTLSASI-----------RQYAERlGLGPG-------DVFLVASPMAhqtGFVYGFTLPLLLGAPVVLQD--I 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 347 WTTLW--RFVAQSKATFFGAGAAFFANCAKAEvdLVAAGDLSQLRCLGSTGSPLSADT--QAWfnnrfaglskTNGSKAQ 422
Cdd:cd05903 169 WDPDKalALMREHGVTFMMGATPFLTDLLNAV--EEAGEPLSRLRTFVCGGATVPRSLarRAA----------ELLGAKV 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 423 ADIWwanisGGTDFAGAFigGNRELPQTPGAMQ---CRLLGAAVEAFDEQGRAVI-GEVGELVCTEPmpsmplyfwndkg 498
Cdd:cd05903 237 CSAY-----GSTECPGAV--TSITPAPEDRRLYtdgRPLPGVEIKVVDDTGATLApGVEGELLSRGP------------- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 499 garyraSYFETYPDNFDGTGR---GPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVV 575
Cdd:cd05903 297 ------SVFLGYLDRPDLTADaapEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVV 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517269147 576 DL--EYLGRDSYMplFVVLREGVAFD-GAMQAKINKaieAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKK 644
Cdd:cd05903 371 ALpdERLGERACA--VVVTKSGALLTfDELVAYLDR---QGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-641 |
4.88e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 77.72 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslcapdmAAPavidrfkqIEPKvliac 188
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV--------LVP--------INTA----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 davtYAGrrhdrkdvlAELRrslptveHVILHSeaaapaaadallseisattgaeidafEPAWLPFDhPLWIVYSSGTTG 268
Cdd:cd05934 62 ----LRG---------DELA-------YIIDHS--------------------------GAQLVVVD-PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 269 LPKPIVHGH------------------GGIIIVVLALlglhndlgcsYHENSfgeryhwysstgwiMWNSQVGGLLSGTT 330
Cdd:cd05934 95 PPKGVVITHanltfagyysarrfglgeDDVYLTVLPL----------FHINA--------------QAVSVLAALSVGAT 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 331 CCIFDG-SPGGakdkpdwttLWRFVAQSKATffgagaafFANCAKAEVDLVAAGDLS------QLRCLGstGSPLSADTQ 403
Cdd:cd05934 151 LVLLPRfSASR---------FWSDVRRYGAT--------VTNYLGAMLSYLLAQPPSpddrahRLRAAY--GAPNPPELH 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 404 AWFNNRFaglsktnGSKAQAdiWWanisGGTDFAGAFIgGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVC 482
Cdd:cd05934 212 EEFEERF-------GVRLLE--GY----GMTETIVGVI-GPRDEPRRPGSIGRPAPGYEVRIVDDDGQELpAGEPGELVI 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 483 T-EPMPSMPLYFWND--KGGARYRASYFETypdnfdgtgrgpvwrhGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSEL 559
Cdd:cd05934 278 RgLRGWGFFKGYYNMpeATAEAMRNGWFHT----------------GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 560 YSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK--K 637
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLD---PEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKvaK 418
|
....
gi 517269147 638 QELP 641
Cdd:cd05934 419 AQLR 422
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
79-636 |
1.11e-14 |
|
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: 76.86 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 79 YARQVFRHVDAadaaglPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG 158
Cdd:cd12117 3 FEEQAARTPDA------VAVVY--GDRSL---TYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 159 AIWsLCApDMAAPAviDRFKQI----EPKVLIACDAVTyagrrhdrkDVLAELRRSLPTVEHvilhseaaapaaadalls 234
Cdd:cd12117 72 AAY-VPL-DPELPA--ERLAFMladaGAKVLLTDRSLA---------GRAGGLEVAVVIDEA------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 235 eisaTTGAEIDAFEPAWLPfDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVlallglhndLGCSYHENSFGERYHWYSSTG 314
Cdd:cd12117 121 ----LDAGPAGNPAVPVSP-DDLAYVMYTSGSTGRPKGVAVTHRGVVRLV---------KNTNYVTLGPDDRVLQTSPLA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 315 WI-----MWnsqvGGLLSGTTCCIFDGSPGgakdkPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLvaagdLSQLR 389
Cdd:cd12117 187 FDastfeIW----GALLNGARLVLAPKGTL-----LDPDALGALIAEEGVTVLWLTAALFNQLADEDPEC-----FAGLR 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 390 CLGSTGSPLSADTQAWFNNRFAGLSKTNGskaqadiwwaniSG---GTDFAGAFIGGNRELPQTP-------GAMQCRLL 459
Cdd:cd12117 253 ELLTGGEVVSPPHVRRVLAACPGLRLVNG------------YGpteNTTFTTSHVVTELDEVAGSipigrpiANTRVYVL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 460 gaaveafDEQGRAV-IGEVGEL------VCtepmpsmpLYFWNDKGGARYRasyFETYPdnFDGTGRgpVWRHGDWLKVD 532
Cdd:cd12117 321 -------DEDGRPVpPGVPGELyvggdgLA--------LGYLNRPALTAER---FVADP--FGPGER--LYRTGDLARWL 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 533 PDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamqakinkAIEA 612
Cdd:cd12117 379 PDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAA---------ELRA 449
|
570 580
....*....|....*....|....*...
gi 517269147 613 GLSRR----FLPNEIFAVAEIPRTLSGK 636
Cdd:cd12117 450 FLRERlpayMVPAAFVVLDELPLTANGK 477
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
111-636 |
1.45e-14 |
|
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: 76.56 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcAP-DMAAPAviDRFKQI----EPKVL 185
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAY---VPlDPDYPA--DRLRYIledaEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 186 IaCDAVTYAGrrhdrkdvlaeLRRSLPTVEHVILhseaaapaaadallseisATTGAEIDAFEPAwlPFDHPLWIVYSSG 265
Cdd:cd12116 89 L-TDDALPDR-----------LPAGLPVLLLALA------------------AAAAAPAAPRTPV--SPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 266 TTGLPKPIVHGHGGiiiVVLALLGLHNDLGcsyhensFGERYHWYSSTGW---IMWNSQVGGLLSGTTCCIfdGSPGGAK 342
Cdd:cd12116 137 STGRPKGVVVSHRN---LVNFLHSMRERLG-------LGPGDRLLAVTTYafdISLLELLLPLLAGARVVI--APRETQR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 343 D---------KPDWT------TLWRFvaqskatffgagaaffancakaevdLVAAG--DLSQLRCL-GstGSPLSADTQA 404
Cdd:cd12116 205 DpealarlieAHSITvmqatpATWRM-------------------------LLDAGwqGRAGLTALcG--GEALPPDLAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 405 WFNNRFAGLSKTNGSkAQADIW--WANISGGTdfAGAFIGGnrelpqtpgamqcRLLGAAVEAFDEQGRAV-IGEVGEL- 480
Cdd:cd12116 258 RLLSRVGSLWNLYGP-TETTIWstAARVTAAA--GPIPIGR-------------PLANTQVYVLDAALRPVpPGVPGELy 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 481 VCTepmPSMPLYFWNDkggaryRASYFETYPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELY 560
Cdd:cd12116 322 IGG---DGVAQGYLGR------PALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517269147 561 SAIEALPEVLDSLVVdLEYLGRDSYMPLFVVLREGVAFDGamqAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd12116 393 AALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDA---AALRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
82-636 |
4.17e-14 |
|
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: 75.06 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 82 QVFRHVDAADAAGLP-AIVSCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI 160
Cdd:cd05920 15 EPLGDLLARSAARHPdRIAVVDGDRRL---TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 161 wslcaPDMAAPAV----IDRF-KQIEPKVLIACDAVtyagRRHDRKDVLAELRRSLPTVEHVILhseaaapaaadallse 235
Cdd:cd05920 92 -----PVLALPSHrrseLSAFcAHAEAVAYIVPDRH----AGFDHRALARELAESIPEVALFLL---------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 236 isattgaeidafepawlpfdhplwivySSGTTGLPKPIVHGHGGIIIVVLALLGLhndlgCSYHENSfgeRY-------H 308
Cdd:cd05920 147 ---------------------------SGGTTGTPKLIPRTHNDYAYNVRASAEV-----CGLDQDT---VYlavlpaaH 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 309 WY--SSTGWImwnsqvGGLLSGTTCCIF-DGSPGGAKDkpdwttlwrFVAQSKATFFGAGAaffancAKAEVDLVAAG-- 383
Cdd:cd05920 192 NFplACPGVL------GTLLAGGRVVLApDPSPDAAFP---------LIEREGVTVTALVP------ALVSLWLDAAAsr 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 384 --DLSQLRCLGSTGSPLSADTQawfnnrfAGLSKTNGSKAQAdiwWANISGGT------DFAGAFIGGNRELPQTPgamq 455
Cdd:cd05920 251 raDLSSLRLLQVGGARLSPALA-------RRVPPVLGCTLQQ---VFGMAEGLlnytrlDDPDEVIIHTQGRPMSP---- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 456 crllGAAVEAFDEQGRAV-IGEVGELVCTEPMpSMPLYFWNDKGGARyrasYFEtyPDNFdgtgrgpvWRHGDWLKVDPD 534
Cdd:cd05920 317 ----DDEIRVVDEEGNPVpPGEEGELLTRGPY-TIRGYYRAPEHNAR----AFT--PDGF--------YRTGDLVRRTPD 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 535 GSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRDSYmpLFVVLRegvafDGAMQAKINKAI-- 610
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMpdELLGERSC--AFVVLR-----DPPPSAAQLRRFlr 450
|
570 580
....*....|....*....|....*.
gi 517269147 611 EAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05920 451 ERGLAAYKLPDRIEFVDSLPLTAVGK 476
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
85-277 |
1.41e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 73.87 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 85 RHVDAaDAaglPAIVsCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG-----A 159
Cdd:PRK10946 33 RHAAS-DA---IAVI-CGER----QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGvapvnA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWSLCAPDMAAPAvidrfKQIEPKVLIacdavtyAGRRHD---RKDVLAELRRSLPTVEHVILHSEaaapAAADALLSEI 236
Cdd:PRK10946 104 LFSHQRSELNAYA-----SQIEPALLI-------ADRQHAlfsDDDFLNTLVAEHSSLRVVLLLND----DGEHSLDDAI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517269147 237 SatTGAEIDAFEPAwlPFDHPLWIVYSSGTTGLPKPIVHGH 277
Cdd:PRK10946 168 N--HPAEDFTATPS--PADEVAFFQLSGGSTGTPKLIPRTH 204
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
114-638 |
1.62e-13 |
|
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: 73.50 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCAP---DMAAPAVIDRFKQIEPKVLIACDA 190
Cdd:cd05926 19 DLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAV---VAPlnpAYKKAEFEFYLADLGSKLVLTPKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 VTYAgrrhdrkDVLAELRRSLPTVEHVILHSEAAAPAAADALLSEISATTGAeidAFEPAWLPFDHPLwIVYSSGTTGLP 270
Cdd:cd05926 96 ELGP-------ASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNA---KSEGVPLPDDLAL-ILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 K--PIVHGHggiiIVVLAllglHNDlgCSYHENSFGER-------YHwysstgwimWNSQVGGLLSGTTCcifdgspGGA 341
Cdd:cd05926 165 KgvPLTHRN----LAASA----TNI--TNTYKLTPDDRtlvvmplFH---------VHGLVASLLSTLAA-------GGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 342 ---KDKPDWTTLWRFVAQSKAT-FFGAGAAFFANCAKAEVDLVAAgdLSQLRCLGSTGSPLSADTQAWFNNRFA------ 411
Cdd:cd05926 219 vvlPPRFSASTFWPDVRDYNATwYTAVPTIHQILLNRPEPNPESP--PPKLRFIRSCSASLPPAVLEALEATFGapvlea 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 412 -GLSKTNgskAQAdiwwanisggtdFAGAFIGGNRElPQTPGamqcRLLGAAVEAFDEQGRAV-IGEVGElVCTEpmpsm 489
Cdd:cd05926 297 yGMTEAA---HQM------------TSNPLPPGPRK-PGSVG----KPVGVEVRILDEDGEILpPGVVGE-ICLR----- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 490 plyfwndkgGARYRASYFETYPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEV 569
Cdd:cd05926 351 ---------GPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517269147 570 LDSLVVDL--EYLGRDsyMPLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:cd05926 422 LEAVAFGVpdEKYGEE--VAAAVVLREGASVT---EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
80-636 |
1.91e-13 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 73.08 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVscGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:cd17646 5 AEQAARTPDA------PAVV--DEGRTL---TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWslcAP-DMAAPAviDRFKQI----EPKVLIACDAVTYAGRRHDRKDVLAElrrslptvehvilhseaaapaaadalls 234
Cdd:cd17646 74 AY---LPlDPGYPA--DRLAYMladaGPAVVLTTADLAARLPAGGDVALLGD---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 235 eiSATTGAEIDAFEPAWLPfDHPLWIVYSSGTTGLPKPIVHGHGGIiivVLALLGLHNDLGC-----SYHENSFGeryhw 309
Cdd:cd17646 121 --EALAAPPATPPLVPPRP-DNLAYVIYTSGSTGRPKGVMVTHAGI---VNRLLWMQDEYPLgpgdrVLQKTPLS----- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 310 YSSTGW-IMWNSQVGGllsgttcCIFDGSPGGAKDkPDWttLWRFVAQSKATFFGAGAAFFAncakAEVDLVAAGDLSQL 388
Cdd:cd17646 190 FDVSVWeLFWPLVAGA-------RLVVARPGGHRD-PAY--LAALIREHGVTTCHFVPSMLR----VFLAEPAAGSCASL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 389 RCLGSTGSPLSADTQAWFNNRFaGLSKTNG---SKAQADIWWANISGGTDFAGAFIGgnRELPQTpgamQCRLLgaavea 465
Cdd:cd17646 256 RRVFCSGEALPPELAARFLALP-GAELHNLygpTEAAIDVTHWPVRGPAETPSVPIG--RPVPNT----RLYVL------ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 466 fDEQGRAV-IGEVGELVCtepmpsmplyfwndkGGARYRASYF-------ETY-PDNFDGTGRgpVWRHGDWLKVDPDGS 536
Cdd:cd17646 323 -DDALRPVpVGVPGELYL---------------GGVQLARGYLgrpaltaERFvPDPFGPGSR--MYRTGDLARWRPDGA 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 537 CIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAF--DGAMQAKINKAieagL 614
Cdd:cd17646 385 LEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpdTAALRAHLAER----L 460
|
570 580
....*....|....*....|..
gi 517269147 615 SRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd17646 461 PEYMVPAAFVVLDALPLTANGK 482
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
97-643 |
2.23e-13 |
|
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: 73.30 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 97 AIVSCGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwSLCAPDMAAPA-VID 175
Cdd:cd05970 35 ALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAI-AIPATHQLTAKdIVY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 RFKQIEPKVLIACDavtyagrRHDRKDVLAELRRSLPTVEHVIL--HSEAAAPAAADALLSEISATtgaeidaFEP---- 249
Cdd:cd05970 114 RIESADIKMIVAIA-------EDNIPEEIEKAAPECPSKPKLVWvgDPVPEGWIDFRKLIKNASPD-------FERptan 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 250 AWLPFDHPLWIVYSSGTTGLPKPIVHGHggiiivvLALLGlHNDLGCSYHENSFGERYHWYSSTGW--IMWNSQVGGLLS 327
Cdd:cd05970 180 SYPCGEDILLVYFSSGTTGMPKMVEHDF-------TYPLG-HIVTAKYWQNVREGGLHLTVADTGWgkAVWGKIYGQWIA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 328 GTTCCIFDgspggaKDKPDWTTLWRFVAQSKATFFgagaaffanCAKAEV-------DLvAAGDLSQLRCLGSTGSPLSA 400
Cdd:cd05970 252 GAAVFVYD------YDKFDPKALLEKLSKYGVTTF---------CAPPTIyrflireDL-SRYDLSSLRYCTTAGEALNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 401 DTqawFNN--RFAGLSKTNG-SKAQADIWWANISGgtdfagafiggnreLPQTPGAMQCRLLGAAVEAFDEQGRAV-IGE 476
Cdd:cd05970 316 EV---FNTfkEKTGIKLMEGfGQTETTLTIATFPW--------------MEPKPGSMGKPAPGYEIDLIDREGRSCeAGE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 477 VGElVCTEPMPSMPLYFWNDKGGARYRASyfETYpdnFDGtgrgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGT 556
Cdd:cd05970 379 EGE-IVIRTSKGKPVGLFGGYYKDAEKTA--EVW---HDG-----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 557 SELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05970 448 FEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGK 527
|
....*..
gi 517269147 637 KQELPIK 643
Cdd:cd05970 528 IRRVEIR 534
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
114-574 |
4.90e-13 |
|
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: 71.53 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALHLK-EKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSlcaP-DMAAPAviDRFKQI----EPKVLIA 187
Cdd:TIGR01733 4 ELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYV---PlDPAYPA--ERLAFIledaGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 188 CDAvtyagrrhdrkdvLAELRRSLPTVEHVILHSEaaapaaadallseiSATTGAEIDAFEPAWLPF-DHPLWIVYSSGT 266
Cdd:TIGR01733 79 DSA-------------LASRLAGLVLPVILLDPLE--------------LAALDDAPAPPPPDAPSGpDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 267 TGLPKPIVHGHGGIIIVVLALLglhndlgcsyHENSFGERYHWYSSTG-------WIMWnsqvGGLLSGTTCCIFDGSPG 339
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVNLLAWLA----------RRYGLDPDDRVLQFASlsfdasvEEIF----GALLAGATLVVPPEDEE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 340 GAKDKpdwttLW-RFVAQSKATFFGAGAAFFancakAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNG 418
Cdd:TIGR01733 198 RDDAA-----LLaALIAEHPVTVLNLTPSLL-----ALLAAALPPALASLRLVILGGEALTPALVDRWRARGPGARLINL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 419 -SKAQADIWwaniSGGTDFAGAFIGGNRELP-QTP-GAMQCRLLgaaveafDEQGRAV-IGEVGELVCTEpmPSMPLYFW 494
Cdd:TIGR01733 268 yGPTETTVW----STATLVDPDDAPRESPVPiGRPlANTRLYVL-------DDDLRPVpVGVVGELYIGG--PGVARGYL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 495 NDKG--GARYRasyfetyPDNFDGTGRGPVWRHGDWLKVDPDGsCIIY-GRSDATINRHGLRMGTSELYSAIEALPEVLD 571
Cdd:TIGR01733 335 NRPEltAERFV-------PDPFAGGDGARLYRTGDLVRYLPDG-NLEFlGRIDDQVKIRGYRIELGEIEAALLRHPGVRE 406
|
...
gi 517269147 572 SLV 574
Cdd:TIGR01733 407 AVV 409
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
89-639 |
5.74e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 71.73 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDM 168
Cdd:PRK12583 28 VARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 AAPAVIDRFKQIEPKVLIACDAVtyagRRHDRKDVLAELRRSL-------------PTVEHVILH--SEAAAPAAADALL 233
Cdd:PRK12583 105 RASELEYALGQSGVRWVICADAF----KTSDYHAMLQELLPGLaegqpgalacerlPELRGVVSLapAPPPGFLAWHELQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 234 SEISATTGAEIDAFEpAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGII----IVVLAL-LGLHNDLgCS----YHenSFG 304
Cdd:PRK12583 181 ARGETVSREALAERQ-ASLDRDDPINIQYTSGTTGFPKGATLSHHNILnngyFVAESLgLTEHDRL-CVpvplYH--CFG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 305 eryhwysstgwiMWNSQVGGLLSGtTCCIFdgsPGGAKDkPDWTTlwRFVAQSKATFFGAGAAFFAncakAEVDLVAAG- 383
Cdd:PRK12583 257 ------------MVLANLGCMTVG-ACLVY---PNEAFD-PLATL--QAVEEERCTALYGVPTMFI----AELDHPQRGn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 384 -DLSQLRCLGSTGSPLSADTqawfnnrfagLSKTNGSKAQADIwwaNISGGTDFAGAFI---GGNRELP---QTPGAMQC 456
Cdd:PRK12583 314 fDLSSLRTGIMAGAPCPIEV----------MRRVMDEMHMAEV---QIAYGMTETSPVSlqtTAADDLErrvETVGRTQP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 457 RLlgaAVEAFDEQGRAV-IGEVGELvCTEPMPSMPLYFWNDKGGAryrasyfetypDNFDGTGrgpvWRH-GDWLKVDPD 534
Cdd:PRK12583 381 HL---EVKVVDPDGATVpRGEIGEL-CTRGYSVMKGYWNNPEATA-----------ESIDEDG----WMHtGDLATMDEQ 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 535 GSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRDsyMPLFVVLREGVAfdgAMQAKINKAIEA 612
Cdd:PRK12583 442 GYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVpdEKYGEE--IVAWVRLHPGHA---ASEEELREFCKA 516
|
570 580
....*....|....*....|....*..
gi 517269147 613 GLSRRFLPNEIFAVAEIPRTLSGKKQE 639
Cdd:PRK12583 517 RIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
131-646 |
6.92e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 71.70 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 131 IKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIACD-------AVTYAGrrhDRKDV 203
Cdd:PTZ00237 114 ISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNygilndeIITFTP---NLKEA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 204 LaELRRSLPTveHVILH----SEAAAPAAADALLSEISATTG--AEIDAF-EPAWLPF--------DHPLWIVYSSGTTG 268
Cdd:PTZ00237 191 I-ELSTFKPS--NVITLfrndITSESDLKKIETIPTIPNTLSwyDEIKKIkENNQSPFyeyvpvesSHPLYILYTSGTTG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 269 LPKPIVHGHGGIIIvvlallglhndlGCSYHENSFGE-----RYHWYSSTGWIMWNSQVGGLLS-GTTCCIFDGspGGAK 342
Cdd:PTZ00237 268 NSKAVVRSNGPHLV------------GLKYYWRSIIEkdiptVVFSHSSIGWVSFHGFLYGSLSlGNTFVMFEG--GIIK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 343 DKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVD---LVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFAglSKTNGS 419
Cdd:PTZ00237 334 NKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEatiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLK--IKSSRG 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 420 KAQADIWWANIsggtdfagaFIGGNRELPQTPGAMQCRLLGAAVeaFDEQGRAV-IGEVGELVCTEPM-PSMPLYFWndK 497
Cdd:PTZ00237 412 YGQTEIGITYL---------YCYGHINIPYNATGVPSIFIKPSI--LSEDGKELnVNEIGEVAFKLPMpPSFATTFY--K 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 498 GGARYRaSYFETYPDNFDGtgrgpvwrhGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL 577
Cdd:PTZ00237 479 NDEKFK-QLFSKFPGYYNS---------GDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517269147 578 EYLGRDSYMPLFVVLREGVAFDGA----MQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKKLL 646
Cdd:PTZ00237 549 YDPDCYNVPIGLLVLKQDQSNQSIdlnkLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFL 621
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
96-271 |
1.86e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 70.32 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVscgeDGRLcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVID 175
Cdd:PRK07656 22 EAYV----FGDQ-RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 RFKQIEPKVLIACDA---VTYAGrrHDRkdvlaelrrsLPTVEHVILHSEAAAPAAADALLSEISATTGAEIDAFEPAWL 252
Cdd:PRK07656 97 ILARGDAKALFVLGLflgVDYSA--TTR----------LPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD 164
|
170
....*....|....*....
gi 517269147 253 PfDHPLWIVYSSGTTGLPK 271
Cdd:PRK07656 165 P-DDVADILFTSGTTGRPK 182
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
78-271 |
2.89e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.84 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 78 NYARQVFRHVDAadaaglPAIVSCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASI 157
Cdd:PRK08315 21 LLDRTAARYPDR------EALVYRDQGLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 158 GAI--------------WSLCAPDMAAPAVIDRFKQiepkvliacdavtyagrrHDRKDVLAELR-------------RS 210
Cdd:PRK08315 92 GAIlvtinpayrlseleYALNQSGCKALIAADGFKD------------------SDYVAMLYELApelatcepgqlqsAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517269147 211 LPTVEHVIL--HSEAAAPAAADALLSEISATTGAEIDAFEPAwLPFDHPLWIVYSSGTTGLPK 271
Cdd:PRK08315 154 LPELRRVIFlgDEKHPGMLNFDELLALGRAVDDAELAARQAT-LDPDDPINIQYTSGTTGFPK 215
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
109-277 |
3.18e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 69.43 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEK-GIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIa 187
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 188 CDAVTyagrrhdrKDVLAELRRSLPTVEHVILHSEAAAPAAADALLSEISATT-GAEIDA----FEPAWLPFDHPLWIVY 262
Cdd:PRK05620 117 ADPRL--------AEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYSyEALLDGrstvYDWPELDETTAAAICY 188
|
170
....*....|....*
gi 517269147 263 SSGTTGLPKPIVHGH 277
Cdd:PRK05620 189 STGTTGAPKGVVYSH 203
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
86-410 |
3.26e-12 |
|
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: 69.19 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 86 HVDAADAAGLPAIVScGEDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCA 165
Cdd:cd05904 12 FLFASAHPSRPALID-AATGR--ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 166 PDmAAPAVIDrfKQIE---PKVLIACDAvtyagrrhdrkdVLAELRRSLPTVehVILHSEAAAPAAADALLSEISATtga 242
Cdd:cd05904 89 PL-STPAEIA--KQVKdsgAKLAFTTAE------------LAEKLASLALPV--VLLDSAEFDSLSFSDLLFEADEA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 243 eiDAFEPAwLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIivvlALLGLHNDLgcsyhENSFGER----------YHWYSS 312
Cdd:cd05904 149 --EPPVVV-IKQDDVAALLYSSGTTGRSKGVMLTHRNLI----AMVAQFVAG-----EGSNSDSedvflcvlpmFHIYGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 313 TGWIMwnsqvGGLLSGTTCCIFdgspggakDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAevDLVAAGDLSQLRCLG 392
Cdd:cd05904 217 SSFAL-----GLLRLGATVVVM--------PRFDLEELLAAIERYKVTHLPVVPPIVLALVKS--PIVDKYDLSSLRQIM 281
|
330
....*....|....*...
gi 517269147 393 STGSPLSADTQAWFNNRF 410
Cdd:cd05904 282 SGAAPLGKELIEAFRAKF 299
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
96-281 |
3.45e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 69.30 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVSCGEdgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVID 175
Cdd:PRK06178 50 PAIIFYGH-----VITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 RFKQIEPKVLIACDAVTYAGR--------RHDRKDVLAELRRSLPTVEHVILHSEAAAPAAADA-LLSEISATTGAEIDa 246
Cdd:PRK06178 125 ELNDAGAEVLLALDQLAPVVEqvraetslRHVIVTSLADVLPAEPTLPLPDSLRAPRLAAAGAIdLLPALRACTAPVPL- 203
|
170 180 190
....*....|....*....|....*....|....*
gi 517269147 247 fEPAWLpfDHPLWIVYSSGTTGLPKPIVHGHGGII 281
Cdd:PRK06178 204 -PPPAL--DALAALNYTGGTTGMPKGCEHTQRDMV 235
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
89-640 |
6.52e-12 |
|
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: 68.43 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPdm 168
Cdd:cd12119 5 AARLHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 aapavidRF--KQIEPKVLIACDAVTYAGRrhDRKDVLAELRRSLPTVEHVILHSEAAApaaadallSEISATTGAE--- 243
Cdd:cd12119 83 -------RLfpEQIAYIINHAEDRVVFVDR--DFLPLLEAIAPRLPTVEHVVVMTDDAA--------MPEPAGVGVLaye 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 244 --IDAFEP--AWLPFDH--PLWIVYSSGTTGLPKPIVHGHGGIIIVVLALlgLHND-LGCS-----------YHENSfge 305
Cdd:cd12119 146 elLAAESPeyDWPDFDEntAAAICYTSGTTGNPKGVVYSHRSLVLHAMAA--LLTDgLGLSesdvvlpvvpmFHVNA--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 306 ryhwysstgwimWNSQVGGLLSGTTCCIFDGSPGGA-------KDKPDWT----TLWRFVAQSkatffgagaaffancak 374
Cdd:cd12119 221 ------------WGLPYAAAMVGAKLVLPGPYLDPAslaelieREGVTFAagvpTVWQGLLDH----------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 375 aevdLVAAG-DLSQLRCLGSTGSPLSADTQAWFNNRfaGLSKTNGskaqadiWwanisGGTDFA--GAFIGGNRELPQTP 451
Cdd:cd12119 272 ----LEANGrDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHA-------W-----GMTETSplGTVARPPSEHSNLS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 452 GAMQCRLL--------GAAVEAFDEQGRAVI---GEVGELVCTEP--MPSmplYFWNDKGGARYRAsyfetypdnfDGtg 518
Cdd:cd12119 334 EDEQLALRakqgrpvpGVELRIVDDDGRELPwdgKAVGELQVRGPwvTKS---YYKNDEESEALTE----------DG-- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 519 rgpvW-RHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDleylgrdsyMP---------L 588
Cdd:cd12119 399 ----WlRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIG---------VPhpkwgerplA 465
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 517269147 589 FVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK--KQEL 640
Cdd:cd12119 466 VVVLKEGATVT---AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKidKKAL 516
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
89-636 |
7.07e-12 |
|
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: 68.30 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEDGRLCETswpELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslcapdm 168
Cdd:cd05923 11 ASRAPDACAIADPARGLRLTYS---ELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 aaPAVID-RFKQIEPKVLIACDAVTYAGRRHDRkdvlaelrrsLPTVEHVILHSEAAAPAAADALLSEISATTGAEIDAF 247
Cdd:cd05923 80 --PALINpRLKAAELAELIERGEMTAAVIAVDA----------QVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 248 EPAwlpfdHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLA-------LLGLHND-LGCS--YHENSFgeryhwysstgwim 317
Cdd:cd05923 148 EPE-----QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFmstqaglRHGRHNVvLGLMplYHVIGF-------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 318 WNSQVGGL-LSGTTCCIFDGSPGGAkdkpdwttlWRFVAQSKATFFGAGAAFFANCAKAEvdLVAAGDLSQLRCLGSTGS 396
Cdd:cd05923 209 FAVLVAALaLDGTYVVVEEFDPADA---------LKLIEQERVTSLFATPTHLDALAAAA--EFAGLKLSSLRHVTFAGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 397 PLSADTQAWFNNRFAGLsKTN---GSKAQADIWWANISGGTDFAGAFIGGNRELpqtpgamqcRLLGAAVEAfdeqgrAV 473
Cdd:cd05923 278 TMPDAVLERVNQHLPGE-KVNiygTTEAMNSLYMRDARTGTEMRPGFFSEVRIV---------RIGGSPDEA------LA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 474 IGEVGELVCtepmpsmplyfwndkggARYRASYFETYPDNFDGTGRGPV---WRHGDWLKVDPDGSCIIYGRSDATINRH 550
Cdd:cd05923 342 NGEEGELIV-----------------AAAADAAFTGYLNQPEATAKKLQdgwYRTGDVGYVDPSGDVRILGRVDDMIISG 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 551 GLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRdsYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRrflPNEIFAVAE 628
Cdd:cd05923 405 GENIHPSEIERVLSRHPGVTEVVVIGVadERWGQ--SVTACVVPREGTLSADELDQFCRASELADFKR---PRRYFFLDE 479
|
....*...
gi 517269147 629 IPRTLSGK 636
Cdd:cd05923 480 LPKNAMNK 487
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
114-644 |
7.08e-12 |
|
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: 68.26 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALhlKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIACDAVTy 193
Cdd:cd05928 49 SLSRKAANVLS--GACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELA- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 194 agrrhdrkdvlaelrrslPTVEHVILHSEAAAPAAadaLLSEISattgaeidafEPAWLPF---------DH-------- 256
Cdd:cd05928 126 ------------------PEVDSVASECPSLKTKL---LVSEKS----------RDGWLNFkellneastEHhcvetgsq 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 257 -PLWIVYSSGTTGLPKPIVHGHGgiiivvlaLLGLHNDLGCSYHENSFGERYHW-YSSTGWIM--WNSQVGGLLSGttCC 332
Cdd:cd05928 175 ePMAIYFTSGTTGSPKMAEHSHS--------SLGLGLKVNGRYWLDLTASDIMWnTSDTGWIKsaWSSLFEPWIQG--AC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 333 IFDGSpggakdkpdwttLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLR------CLgSTGSPLSADTQAWF 406
Cdd:cd05928 245 VFVHH------------LPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKfpslqhCV-TGGEPLNPEVLEKW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 407 NNRfAGLSKTNGSkaqadiwwanisGGTDfAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGElVCTEP 485
Cdd:cd05928 312 KAQ-TGLDIYEGY------------GQTE-TGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLpPGTEGD-IGIRV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 486 MPSMPLYFWndkggaryraSYFETYPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEA 565
Cdd:cd05928 377 KPIRPFGLF----------SGYVDNPEKTAATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 566 LPEVLDSLVVDLEYLGRDSYMPLFVVLreGVAFDGAMQAKINKAIEAGLSRRF----LPNEIFAVAEIPRTLSGKKQELP 641
Cdd:cd05928 447 HPAVVESAVVSSPDPIRGEVVKAFVVL--APQFLSHDPEQLTKELQQHVKSVTapykYPRKVEFVQELPKTVTGKIQRNE 524
|
...
gi 517269147 642 IKK 644
Cdd:cd05928 525 LRD 527
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
96-636 |
1.27e-11 |
|
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: 67.39 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVsCGEdgrlCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAApavid 175
Cdd:cd17649 4 VALV-FGD----QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 rfkqiepkvliacdavtyagrrhdrkdvlAELRRSLPTVEHVILHSEAAapaaadallseisattgaeidafepawlpfD 255
Cdd:cd17649 74 -----------------------------ERLRYMLEDSGAGLLLTHHP------------------------------R 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 256 HPLWIVYSSGTTGLPKPIVHGHGGIII---VVLALLGLHNDlGCSYHENSFG-----ERyhWYSstgwimwnsqvgGLLS 327
Cdd:cd17649 95 QLAYVIYTSGSTGTPKGVAVSHGPLAAhcqATAERYGLTPG-DRELQFASFNfdgahEQ--LLP------------PLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 328 GTTCCIFDGSPGGAKDkpdwtTLWRFVAQSKATFFGAGAAFFANCAKaEVDLVAAGDLSQLRCLGSTGSPLSADT-QAWF 406
Cdd:cd17649 160 GACVVLRPDELWASAD-----ELAEMVRELGVTVLDLPPAYLQQLAE-EADRTGDGRPPSLRLYIFGGEALSPELlRRWL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 407 nnrfaglsktngskaQADIWWANISGGTD---FAGAFIGGNRELPQTPGAMQCRLLGA-AVEAFDEQGRAV-IGEVGELv 481
Cdd:cd17649 234 ---------------KAPVRLFNAYGPTEatvTPLVWKCEAGAARAGASMPIGRPLGGrSAYILDADLNPVpVGVTGEL- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 482 ctepmpsmplyFWNDKGGAR-Y------RASYFetYPDNFDGTGrGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRM 554
Cdd:cd17649 298 -----------YIGGEGLARgYlgrpelTAERF--VPDPFGAPG-SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 555 GTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPlFVVLREGVAfDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLS 634
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVALDGAGGKQLVA-YVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
..
gi 517269147 635 GK 636
Cdd:cd17649 442 GK 443
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
58-638 |
1.56e-11 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 67.48 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 58 AAVITERKMPGALwfpgaqvnyARQvfrhvdAADAAGLPAIVSCGEdgrlcETSWPELRRKAAALALHLKEKGIKPGDRV 137
Cdd:PRK06155 15 PLPPSERTLPAML---------ARQ------AERYPDRPLLVFGGT-----RWTYAEAARAAAAAAHALAAAGVKRGDRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 138 AAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIAcDAvtyagrrhdrkDVLAELRRSLPTV--- 214
Cdd:PRK06155 75 ALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVV-EA-----------ALLAALEAADPGDlpl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 215 EHVILHSEAAAPAAADALLSEISATTGAEIDAFEPAwlPFDhPLWIVYSSGTTGLPKPIVHGHGGII---IVVLALLGL- 290
Cdd:PRK06155 143 PAVWLLDAPASVSVPAGWSTAPLPPLDAPAPAAAVQ--PGD-TAAILYTSGTTGPSKGVCCPHAQFYwwgRNSAEDLEIg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 291 ------------HND----------LGCSYHensFGERyhwYSSTGWimW------NSQVGGLLsGTTCCIFDGSPGGAK 342
Cdd:PRK06155 220 addvlyttlplfHTNalnaffqallAGATYV---LEPR---FSASGF--WpavrrhGATVTYLL-GAMVSILLSQPARES 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 343 DKPdwttlwrfvaqskatffgagaaffancakaevdlvaagdlSQLRCLGSTGSPlsADTQAWFNNRFaGLSKTNGskaq 422
Cdd:PRK06155 291 DRA----------------------------------------HRVRVALGPGVP--AALHAAFRERF-GVDLLDG---- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 423 adiwwaniSGGTDfAGAFIGGNRElPQTPGAMqcrllGAAVEAF-----DEQGRAV-IGEVGELV--CTEP--------- 485
Cdd:PRK06155 324 --------YGSTE-TNFVIAVTHG-SQRPGSM-----GRLAPGFearvvDEHDQELpDGEPGELLlrADEPfafatgyfg 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 486 MPSMPLYFWNDkggaryrasyfetypdnfdgtgrgpVWRH-GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIE 564
Cdd:PRK06155 389 MPEKTVEAWRN-------------------------LWFHtGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLL 443
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517269147 565 ALPEVLDSLVVDLEY-LGRDSYMpLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:PRK06155 444 SHPAVAAAAVFPVPSeLGEDEVM-AAVVLRDGTALE---PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQ 514
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
78-277 |
1.80e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 67.11 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 78 NYARQVFRHVDAADAAglPAIVSCGEDgrlceTSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASI 157
Cdd:PRK07786 18 NWVNQLARHALMQPDA--PALRFLGNT-----TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 158 GAIWSLCAPDMAAPAVIDRFKQIEPKVLIACDAVTyagrrhdrkDVLAELRRSLPTVEHVILHSEAAAPAAADalLSEIS 237
Cdd:PRK07786 91 GAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALA---------PVATAVRDIVPLLSTVVVAGGSSDDSVLG--YEDLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517269147 238 ATTGAeidAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGH 277
Cdd:PRK07786 160 AEAGP---AHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-636 |
3.45e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 65.92 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 117 RKAAALALHLKEKGIKPGDRVAAYLPNIPEtiiaflasasigAIWSLCAPDMAAPAVIDRFKQIEPkvLIACDAVTYAGR 196
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFT------------YIELSFAVAYAGGRLGLVFVPLNP--TLKESVLRYLVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 197 RHDRKDVLAELrrslPTVEHVILHSEAAAPAAADALLSEISATtGAEIDAFEPAwlpFDHPLWIVYSSGTTGLPKPIVHG 276
Cdd:cd05922 67 DAGGRIVLADA----GAADRLRDALPASPDPGTVLDADGIRAA-RASAPAHEVS---HEDLALLLYTSGSTGSPKLVRLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 277 HGGIII---VVLALLGLHND------LGCSYhensfgeryhwysSTGWIMWNSQvggLLSGTTCCIfdgSPGGAKDKpdw 347
Cdd:cd05922 139 HQNLLAnarSIAEYLGITADdraltvLPLSY-------------DYGLSVLNTH---LLRGATLVL---TNDGVLDD--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 348 tTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAagdLSQLRCLGSTGSPLSADTQAWFNNRFAGlsktngskaqADIWW 427
Cdd:cd05922 197 -AFWEDLREHGATGLAGVPSTYAMLTRLGFDPAK---LPSLRYLTQAGGRLPQETIARLRELLPG----------AQVYV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 428 anISGGTD-FAG-AFIGGNRELpQTPGAMQCRLLGAAVEAFDEQG-RAVIGEVGELVCTEPMPSMplYFWNDKGGARyra 504
Cdd:cd05922 263 --MYGQTEaTRRmTYLPPERIL-EKPGSIGLAIPGGEFEILDDDGtPTPPGEPGEIVHRGPNVMK--GYWNDPPYRR--- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 505 syfetypdnfDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLE-YLGRD 583
Cdd:cd05922 335 ----------KEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPdPLGEK 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 517269147 584 syMPLFVVLREGVAFDGAMqakinKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd05922 405 --LALFVTAPDKIDPKDVL-----RSLAERLPPYKVPATVRVVDELPLTASGK 450
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
96-636 |
4.56e-11 |
|
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: 65.76 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVsCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcAP-DMAAPAvi 174
Cdd:cd12114 4 TAVI-CGDG----TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY---VPvDIDQPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 175 DRFKQIepkvLIACDAVTyagrrhdrkdvlaelrrslptvehVILHSEAAAPAAADALLSEISATTGAEIDAFEPAWLPF 254
Cdd:cd12114 74 ARREAI----LADAGARL------------------------VLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 255 DHPLWIVYSSGTTGLPKPIVHGHGGII---------------IVVLALLGLHNDLgcsyhensfgeryhwysSTGWIMwn 319
Cdd:cd12114 126 DDLAYVIFTSGSTGTPKGVMISHRAALntildinrrfavgpdDRVLALSSLSFDL-----------------SVYDIF-- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 320 sqvGGLLSGTTCCIfdgsPGGAKDK-PDwttLW-RFVAQSKATffgagaafFANCAKAEVDLV------AAGDLSQLRCL 391
Cdd:cd12114 187 ---GALSAGATLVL----PDEARRRdPA---HWaELIERHGVT--------LWNSVPALLEMLldvleaAQALLPSLRLV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 392 GSTGS--PLS-ADT--QAWFNNRFAGLsktnGSKAQADIW------------WANISGGTDFAGafiggnrelpqtpgaM 454
Cdd:cd12114 249 LLSGDwiPLDlPARlrALAPDARLISL----GGATEASIWsiyhpidevppdWRSIPYGRPLAN---------------Q 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 455 QCRLLgaaveafDEQGRAV-IGEVGELVCTEpmPSMPLYFWNDkgGARYRASYFEtypdnfDGTGRGpVWRHGDWLKVDP 533
Cdd:cd12114 310 RYRVL-------DPRGRDCpDWVPGELWIGG--RGVALGYLGD--PELTAARFVT------HPDGER-LYRTGDLGRYRP 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 534 DGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL-EYLGRDSYmpLFVVLREGVAfdGAMQAKINKAIEA 612
Cdd:cd12114 372 DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLgDPGGKRLA--AFVVPDNDGT--PIAPDALRAFLAQ 447
|
570 580
....*....|....*....|....
gi 517269147 613 GLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd12114 448 TLPAYMIPSRVIALEALPLTANGK 471
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
109-281 |
6.72e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 65.41 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIAC 188
Cdd:PRK05605 57 TTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 DAVTyagrrhdrkDVLAELRRSLPtVEHVI-----------------------------LHSEAAAPAAADALLSeiSAT 239
Cdd:PRK05605 137 DKVA---------PTVERLRRTTP-LETIVsvnmiaampllqrlalrlpipalrkaraaLTGPAPGTVPWETLVD--AAI 204
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517269147 240 TGAEIDAFEPAWLPFDHPLwIVYSSGTTGLPKPIVHGHGGII 281
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVAL-ILYTSGTTGKPKGAQLTHRNLF 245
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
89-635 |
1.03e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 64.76 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEDGRLceTSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSlcapdm 168
Cdd:PRK06164 17 DAHARARPDAVALIDEDRP--LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 aapAVIDRFKQIEPKVLIA---CDAVTYAGRRH--DRKDVLAELRRS-LPTVEHVILHSEAAAPAAADALLSEISA---T 239
Cdd:PRK06164 89 ---AVNTRYRSHEVAHILGrgrARWLVVWPGFKgiDFAAILAAVPPDaLPPLRAIAVVDDAADATPAPAPGARVQLfalP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 240 TGAEIDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVH------GHGGIIIVVLALLGLHNDLGCSYHENSFGeryhwysst 313
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHrqatllRHARAIARAYGYDPGAVLLAALPFCGVFG--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 314 gwimWNSQVGGLLSGTTCC---IFDGSPggakdkpdwtTLwRFVAQSKATFFGAGAAFFANCAKAEvdlVAAGDLSQLRC 390
Cdd:PRK06164 237 ----FSTLLGALAGGAPLVcepVFDAAR----------TA-RALRRHRVTHTFGNDEMLRRILDTA---GERADFPSARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 391 LG-STGSPLSADTQAWFNNRFAGLSKTNGSK---AQADIWWANisggTDFAGAFIGGNRelPQTPgamqcrllGAAVEAF 466
Cdd:PRK06164 299 FGfASFAPALGELAALARARGVPLTGLYGSSevqALVALQPAT----DPVSVRIEGGGR--PASP--------EARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 467 DEQGRAVI--GEVGELVCTEPmpsmplyfwndkggaryraSYFETYPDNFDGTGRGPV----WRHGDWLKVDPDGSCIIY 540
Cdd:PRK06164 365 DPQDGALLpdGESGEIEIRAP-------------------SLMRGYLDNPDATARALTddgyFRTGDLGYTRGDGQFVYQ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 541 GRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPlFVVLREGVAFDgamQAKINKAIEAGLSRRFLP 620
Cdd:PRK06164 426 TRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVA-FVIPTDGASPD---EAGLMAACREALAGFKVP 501
|
570
....*....|....*
gi 517269147 621 NEIFAVAEIPRTLSG 635
Cdd:PRK06164 502 ARVQVVEAFPVTESA 516
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
114-640 |
1.33e-10 |
|
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: 64.12 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIaCDavty 193
Cdd:cd05936 29 ELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI-VA---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 194 agrrHDRKDVLAELRRSLPTVEhvilhseaaapaaadallseisattgaeidafepawLPFDHPLWIVYSSGTTGLPKPI 273
Cdd:cd05936 104 ----VSFTDLLAAGAPLGERVA------------------------------------LTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 274 VHGHGGIiivvlallgLHNDLGCSYHENSFGER----------YHWYSST-----GWIMWNSQV----------GGLLSG 328
Cdd:cd05936 144 MLTHRNL---------VANALQIKAWLEDLLEGddvvlaalplFHVFGLTvalllPLALGATIVliprfrpigvLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 329 TTCCIFDGSPggakdkPDWTTLWRFVAQSKAtffgagaaffancakaevdlvaagDLSQLRCLGSTGSPLSADTQAWFNN 408
Cdd:cd05936 215 HRVTIFPGVP------TMYIALLNAPEFKKR------------------------DFSSLRLCISGGAPLPVEVAERFEE 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 409 RFA-------GLSKTngSKAQAdiwwANISGGTDFAGAfIGgnreLPqtpgamqcrLLGAAVEAFDEQGRAV-IGEVGEL 480
Cdd:cd05936 265 LTGvpivegyGLTET--SPVVA----VNPLDGPRKPGS-IG----IP---------LPGTEVKIVDDDGEELpPGEVGEL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 481 VCTEPMpSMPLYfWNDKGgaryrasyfETYPDNFDGtgrgpvW-RHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSEL 559
Cdd:cd05936 325 WVRGPQ-VMKGY-WNRPE---------ETAEAFVDG------WlRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREV 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 560 YSAIEALPEVLDSLVVDL--EYLGRDsyMPLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK- 636
Cdd:cd05936 388 EEVLYEHPAVAEAAVVGVpdPYSGEA--VKAFVVLKEGASLT---EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKi 462
|
....*
gi 517269147 637 -KQEL 640
Cdd:cd05936 463 lRREL 467
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
111-284 |
1.37e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 64.29 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcapdmaapaVIDRFKQIEPKV------ 184
Cdd:PRK07470 34 TWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVW-----------VPTNFRQTPDEVaylaea 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 185 ----LIACDAvtyagrrhDRKDVLAELRRSLPTVEHVILHSEAAAPAAADALlseISATTGAeidAFEPAWLPFDHPLWI 260
Cdd:PRK07470 103 sgarAMICHA--------DFPEHAAAVRAASPDLTHVVAIGGARAGLDYEAL---VARHLGA---RVANAAVDHDDPCWF 168
|
170 180
....*....|....*....|....
gi 517269147 261 VYSSGTTGLPKPIVHGHGGIIIVV 284
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTHGQMAFVI 192
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
96-651 |
1.38e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 64.30 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVSCGEDGRLCET-SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSlcaPDMaaPAVI 174
Cdd:PRK13295 41 TAVTAVRLGTGAPRRfTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLN---PLM--PIFR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 175 DR-----FKQIEPKVLIacdaVTYAGRRHDRKDVLAELRRSLPTVEHVIlhseaaapaaadallseisATTGAEIDAFE- 248
Cdd:PRK13295 116 ERelsfmLKHAESKVLV----VPKTFRGFDHAAMARRLRPELPALRHVV-------------------VVGGDGADSFEa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 ----PAW--LPFDHPLW------------IVYSSGTTGLPKPIVHGHGGI---IIVVLALLGLHND---LGCS--YHENs 302
Cdd:PRK13295 173 llitPAWeqEPDAPAILarlrpgpddvtqLIYTSGTTGEPKGVMHTANTLmanIVPYAERLGLGADdviLMASpmAHQT- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 303 fgeryhwysstgwimwnsqvgGLLSGTTCCIFDGSPGGAKDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAeVDLvAA 382
Cdd:PRK13295 252 ---------------------GFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRA-VKE-SG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 383 GDLSQLRCLGSTGSPLSAD--TQAWfnnrfAGLSKTNGSkaqadIWwanisGGTDFAGAFIGGNRELPQ----TPGamqC 456
Cdd:PRK13295 309 RPVSSLRTFLCAGAPIPGAlvERAR-----AALGAKIVS-----AW-----GMTENGAVTLTKLDDPDErastTDG---C 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 457 RLLGAAVEAFDEQGRAV-IGEVGELVCTEPmpsmplyfwNDKGGARYRAsyfETYPDNFDGtgrgpvW-RHGDWLKVDPD 534
Cdd:PRK13295 371 PLPGVEVRVVDADGAPLpAGQIGRLQVRGC---------SNFGGYLKRP---QLNGTDADG------WfDTGDLARIDAD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 535 GSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRDSYMplFVVLREGVAFD-GAMQAKINkaiE 611
Cdd:PRK13295 433 GYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYpdERLGERACA--FVVPRPGQSLDfEEMVEFLK---A 507
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 517269147 612 AGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKKLLLGQPV 651
Cdd:PRK13295 508 QKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
27-80 |
1.52e-10 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 56.71 E-value: 1.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 517269147 27 YEEMRQWSVRDLDGFWHAIWDyyDLQSPTPFAAVITERKMPGALWFPGAQVNYA 80
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAK--ELDWFKPFDKVLDGSNGPFAKWFVGGKLNVC 52
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
99-636 |
1.59e-10 |
|
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: 63.87 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 99 VSCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcAP-DMAAPAviDRf 177
Cdd:cd17643 6 VVDEDR----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAY---VPiDPAYPV--ER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 178 kqiepkvliacdavtyagRRHdrkdVLAELRRSLptvehvilhseaaapaaadaLLSEIsattgaeidafepawlpfDHP 257
Cdd:cd17643 76 ------------------IAF----ILADSGPSL--------------------LLTDP------------------DDL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 258 LWIVYSSGTTGLPKPIVHGHGGiiivVLALLGlhndlGCSyHENSFGER-----YHWYS---STgWIMWnsqvGGLLSGT 329
Cdd:cd17643 96 AYVIYTSGSTGRPKGVVVSHAN----VLALFA-----ATQ-RWFGFNEDdvwtlFHSYAfdfSV-WEIW----GALLHGG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 330 TCCIFdgspggakdkPDWTT-----LWRFVAQSKATFFGAGAAFFAncAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQA 404
Cdd:cd17643 161 RLVVV----------PYEVArspedFARLLRDEGVTVLNQTPSAFY--QLVEAADRDGRDPLALRYVIFGGEALEAAMLR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 405 WFNNRFA----------GLSKTNGSKAQADIWWANISGGtdfAGAFIGgnRELPQTpgamQCRLLgaaveafDEQGRAV- 473
Cdd:cd17643 229 PWAGRFGldrpqlvnmyGITETTVHVTFRPLDAADLPAA---AASPIG--RPLPGL----RVYVL-------DADGRPVp 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 474 IGEVGELVCTEPmpsmplyfwndkGGAR-Y------RASYFETYPDNFDGTGRgpvWRHGDWLKVDPDGSCIIYGRSDAT 546
Cdd:cd17643 293 PGVVGELYVSGA------------GVARgYlgrpelTAERFVANPFGGPGSRM---YRTGDLARRLPDGELEYLGRADEQ 357
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 547 INRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAmqakinkAIEAGLSRRF----LPNE 622
Cdd:cd17643 358 VKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIA-------ELRALLKELLpdymVPAR 430
|
570
....*....|....
gi 517269147 623 IFAVAEIPRTLSGK 636
Cdd:cd17643 431 YVPLDALPLTVNGK 444
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
89-636 |
3.03e-10 |
|
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: 63.03 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVscGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAiwslcapdm 168
Cdd:cd05945 1 AAANPDRPAVV--EGGRTL---TYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGH--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 aapavidrfkqiepkVLIACDAVTYAGRrhdrkdvlaelrrslptVEHVIlhseaaapaaadallsEISATTGAEIDAFE 248
Cdd:cd05945 67 ---------------AYVPLDASSPAER-----------------IREIL----------------DAAKPALLIADGDD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 PAWlpfdhplwIVYSSGTTGLPKPIVHGHGGII-----IVVLALLGLHNDLGCSYHensfgerYHWYSSTGWIMwnsqvG 323
Cdd:cd05945 99 NAY--------IIFTSGSTGRPKGVQISHDNLVsftnwMLSDFPLGPGDVFLNQAP-------FSFDLSVMDLY-----P 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 324 GLLSGTTCCIFDgspggaKD-KPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAgdLSQLRCLGSTGSPLS-AD 401
Cdd:cd05945 159 ALASGATLVPVP------RDaTADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPES--LPSLRHFLFCGEVLPhKT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 402 TQAWFNnRFAGlsktngskaqADIWwaNISGGTDFAGAFIGgnRELPQTPGAMQCRL------LGAAVEAFDEQGRAVI- 474
Cdd:cd05945 231 ARALQQ-RFPD----------ARIY--NTYGPTEATVAVTY--IEVTPEVLDGYDRLpigyakPGAKLVILDEDGRPVPp 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 475 GEVGELVCTEPmpSMPLYFWNDKGGARYRasyfetypdNFDGTGRgPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRM 554
Cdd:cd05945 296 GEKGELVISGP--SVSKGYLNNPEKTAAA---------FFPDEGQ-RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 555 GTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMqakinkAIEAGLSRR----FLPNEIFAVAEIP 630
Cdd:cd05945 364 ELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTK------AIKAELAERlppyMIPRRFVYLDELP 437
|
....*.
gi 517269147 631 RTLSGK 636
Cdd:cd05945 438 LNANGK 443
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
96-636 |
3.58e-10 |
|
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: 62.95 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIvsCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslCAPDMAAPAviD 175
Cdd:cd05918 16 PAV--CAWDGSL---TYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAF--VPLDPSHPL--Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 RFKQIepkvLIACDAvtyagrrhdrkdvlaelrrslptveHVILHSEAaapaaadallseisattgaeidafepawlpfD 255
Cdd:cd05918 87 RLQEI----LQDTGA-------------------------KVVLTSSP-------------------------------S 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 256 HPLWIVYSSGTTGLPKPIVHGHGgiiIVVLALLGLHNDLGcsYHENSfgeRYHWYSSTGW-IMWNSQVGGLLSGTTCCIf 334
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHR---ALSTSALAHGRALG--LTSES---RVLQFASYTFdVSILEIFTTLAAGGCLCI- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 335 dgspggAKDKPDWTTLWRFVAQSKATFfgagaaffancakaeVDL---VAA----GDLSQLRCLGSTGSPLSADtqawfn 407
Cdd:cd05918 178 ------PSEEDRLNDLAGFINRLRVTW---------------AFLtpsVARlldpEDVPSLRTLVLGGEALTQS------ 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 408 nrfaglsktngskaQADIWWANIS-----GGTDfagAFIGGNRELPQTPGamQCRLLGAA-------VEAFDEQGRAVIG 475
Cdd:cd05918 231 --------------DVDTWADRVRlinayGPAE---CTIAATVSPVVPST--DPRNIGRPlgatcwvVDPDNHDRLVPIG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 476 EVGELVCTEPMPSMplYFWNDKGgaRYRASYFETYPD--NFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLR 553
Cdd:cd05918 292 AVGELLIEGPILAR--GYLNDPE--KTAAAFIEDPAWlkQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQR 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 554 MGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPL---FVVLREGVAFDGAMQAKIN----------KAIEAGLSRRF-- 618
Cdd:cd05918 368 VELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlvaFVVLDGSSSGSGDGDSLFLepsdefralvAELRSKLRQRLps 447
|
570 580
....*....|....*....|
gi 517269147 619 --LPNEIFAVAEIPRTLSGK 636
Cdd:cd05918 448 ymVPSVFLPLSHLPLTASGK 467
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
111-281 |
1.07e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 61.98 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcAP-DMAAPavIDRFKQI----EPKVL 185
Cdd:PRK10252 485 SYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAW---LPlDTGYP--DDRLKMMledaRPSLL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 186 IACDAVtyAGRRHDRKDVLAELRRSLPTVehvilhseaaapaaadallseisattgaeiDAFEPAWLPF-DHPLWIVYSS 264
Cdd:PRK10252 560 ITTADQ--LPRFADVPDLTSLCYNAPLAP------------------------------QGAAPLQLSQpHHTAYIIFTS 607
|
170
....*....|....*..
gi 517269147 265 GTTGLPKPIVHGHGGII 281
Cdd:PRK10252 608 GSTGRPKGVMVGQTAIV 624
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
260-638 |
1.95e-09 |
|
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: 60.18 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 260 IVYSSGTTGLPKPIVHGHGGIIIVV----LALLGLH-NDLGCSYHENSFGeryhwYSSTGWIMWNSQVGGllsgtTCCIF 334
Cdd:cd05958 102 LAFTSGTTGAPKATMHFHRDPLASAdryaVNVLRLReDDRFVGSPPLAFT-----FGLGGVLLFPFGVGA-----SGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 335 DGSpggakdKPDwtTLWRFVAQSKATFFGAGAAFFAncAKAEVDLVAAGDLSQLRCLGSTGSPLSADT-QAWFnnrfagl 413
Cdd:cd05958 172 EEA------TPD--LLLSAIARYKPTVLFTAPTAYR--AMLAHPDAAGPDLSSLRKCVSAGEALPAALhRAWK------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 414 sKTNGSKAQADIwwanisGGTDFAGAFIGgNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPMpsmply 492
Cdd:cd05958 235 -EATGIPIIDGI------GSTEMFHIFIS-ARPGDARPGATGKPVPGYEAKVVDDEGNPVpDGTIGRLAVRGPT------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 493 fwndkgGARYRASyfETYPDNFDGTgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLD 571
Cdd:cd05958 301 ------GCRYLAD--KRQRTYVQGG-----WNItGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAE 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517269147 572 SLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:cd05958 368 CAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
111-647 |
2.53e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 60.21 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-----WSLCAPDMAapAVIDRfkqIEPKVL 185
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIyvplnWRLSASELD--ALLQD---AEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 186 IACDAVtyAGRRHDRKDvLAELRrslptvehvilhseaaapaaadallseisattgAEIDAFEPA---WLPFDHPLWIVY 262
Cdd:PRK09088 99 LGDDAV--AAGRTDVED-LAAFI---------------------------------ASADALEPAdtpSIPPERVSLILF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 263 SSGTTGLPKpivhghgGIIIVVLALLGL-HN--DLGCSYHENSFGERYHWYSSTGWImwNSQVGGLLSGTTCCIFDGSPG 339
Cdd:PRK09088 143 TSGTSGQPK-------GVMLSERNLQQTaHNfgVLGRVDAHSSFLCDAPMFHIIGLI--TSVRPVLAVGGSILVSNGFEP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 340 GAkdkpdwtTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGdLSQLRCLGSTGSP-LSADTQAWFNnrfAGLSKTNG 418
Cdd:PRK09088 214 KR-------TLGRLGDPALGITHYFCVPQMAQAFRAQPGFDAAA-LRHLTALFTGGAPhAAEDILGWLD---DGIPMVDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 419 SkaqadiwwanisgGTDFAGAFIGgnreLPQTPGAMQCRLLGAAVEA-------FDEQGRAV-IGEVGELVCTEpmPSMP 490
Cdd:PRK09088 283 F-------------GMSEAGTVFG----MSVDCDVIRAKAGAAGIPTptvqtrvVDDQGNDCpAGVPGELLLRG--PNLS 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 491 LYFWNDKggaryrasyfETYPDNFDGTGrgpvW-RHGDWLKVDPDGSCIIYGR-SDATINrhglrmGTSELYSA-IEAL- 566
Cdd:PRK09088 344 PGYWRRP----------QATARAFTGDG----WfRTGDIARRDADGFFWVVDRkKDMFIS------GGENVYPAeIEAVl 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 567 ---PEVLDSLVVDL--EYLGRDSYmpLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELP 641
Cdd:PRK09088 404 adhPGIRECAVVGMadAQWGEVGY--LAIVPADGAPLD---LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKAR 478
|
....*.
gi 517269147 642 IKKLLL 647
Cdd:PRK09088 479 LRDALA 484
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
116-284 |
3.05e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 59.99 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 116 RRKAAALALHlkekGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPdMAAPAVIdrFKQIEpkvliACDA---VT 192
Cdd:PLN02246 61 RRVAAGLHKL----GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP-FYTPAEI--AKQAK-----ASGAkliIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 193 YAgrrhdrkdVLAELRRSLPTVEHVILHSEAAAPAAADAlLSEISATTGAEIDAFE-----PAWLPfdhplwivYSSGTT 267
Cdd:PLN02246 129 QS--------CYVDKLKGLAEDDGVTVVTIDDPPEGCLH-FSELTQADENELPEVEispddVVALP--------YSSGTT 191
|
170
....*....|....*..
gi 517269147 268 GLPKPIVHGHGGIIIVV 284
Cdd:PLN02246 192 GLPKGVMLTHKGLVTSV 208
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
109-640 |
5.46e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 59.10 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLK-EKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-----WSLcapdmaAPAVID-RFKQIE 181
Cdd:PRK06839 27 EMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIavplnIRL------TENELIfQLKDSG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 182 PKVLiaCDAVTYAGrrhdrkdvLAELRRSLPTVEHVILhseaaapaaadalLSEISATTGAEIDAFEPAwlPFDHPLWIV 261
Cdd:PRK06839 101 TTVL--FVEKTFQN--------MALSMQKVSYVQRVIS-------------ITSLKEIEDRKIDNFVEK--NESASFIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 262 YSSGTTGLPKPIVhghggIIIVVLALLGLHNDLgcsyhenSFGERYHWYSSTGWIMWNsqVGGLLSGTTCCIFDGSPGGA 341
Cdd:PRK06839 156 YTSGTTGKPKGAV-----LTQENMFWNALNNTF-------AIDLTMHDRSIVLLPLFH--IGGIGLFAFPTLFAGGVIIV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 342 KDKPDWTTLWRFVAQSKATFFGAGAAFFAncAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNR---FA---GLSK 415
Cdd:PRK06839 222 PRKFEPTKALSMIEKHKVTVVMGVPTIHQ--ALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRgflFGqgfGMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 416 TNGSkaqadiwwanisggtdfagAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVGELVCTEPmPSMPLYFW 494
Cdd:PRK06839 300 TSPT-------------------VFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVeVGEVGELLIRGP-NVMKEYWN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 495 NDKGGAryrasyfETYPDNfdgtgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSL 573
Cdd:PRK06839 360 RPDATE-------ETIQDG---------WLCtGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVA 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517269147 574 VVDLEYLGRDSYMPLFVVLREGVAFdgaMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGK--KQEL 640
Cdd:PRK06839 424 VVGRQHVKWGEIPIAFIVKKSSSVL---IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKiqKAQL 489
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-278 |
7.67e-09 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 58.73 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDM 168
Cdd:PRK08279 47 AARHPDRPALLF--EDQSI---SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 AAPAVIDRFKQIEPKVLIAcdavtyagrRHDRKDVLAELRRSLPtvEHVILHSEAAAPAAADALLSEIsATTGAEIDAFE 248
Cdd:PRK08279 122 RGAVLAHSLNLVDAKHLIV---------GEELVEAFEEARADLA--RPPRLWVAGGDTLDDPEGYEDL-AAAAAGAPTTN 189
|
170 180 190
....*....|....*....|....*....|...
gi 517269147 249 PAW---LPFDHPLWIVYSSGTTGLPKPIVHGHG 278
Cdd:PRK08279 190 PASrsgVTAKDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
80-597 |
1.25e-08 |
|
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: 58.33 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:COG1020 483 EAQAARTPDA------VAVVF--GDQSL---TYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWslcAP-DMAAPAviDRFKQI----EPKVLIACDAvtyagrrhdrkdvlaeLRRSLP--TVEHVILHSEAAAPAAADAL 232
Cdd:COG1020 552 AY---VPlDPAYPA--ERLAYMledaGARLVLTQSA----------------LAARLPelGVPVLALDALALAAEPATNP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 233 LSEISAttgaeidafepawlpfDHPLWIVYSSGTTGLPKPIVHGHGGiiiVVLALLGLHNDLGCSYhensfGERYHWYSS 312
Cdd:COG1020 611 PVPVTP----------------DDLAYVIYTSGSTGRPKGVMVEHRA---LVNLLAWMQRRYGLGP-----GDRVLQFAS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 313 TG-----WIMWnsqvGGLLSGTTCCIFDgsPGGAKDkPDwtTLWRFVAQSKATFfgagaaffancakaeVDLV------- 380
Cdd:COG1020 667 LSfdasvWEIF----GALLSGATLVLAP--PEARRD-PA--ALAELLARHRVTV---------------LNLTpsllral 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 381 ---AAGDLSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNG-------------SKAQADIWWANISggtdfagafIGgn 444
Cdd:COG1020 723 ldaAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLygptettvdstyyEVTPPDADGGSVP---------IG-- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 445 RELPQTpgamQCRLLgaaveafDEQGRAV-IGEVGELVCtepmpsmplyfwndkGG---AR-YR------ASYFETYPDN 513
Cdd:COG1020 792 RPIANT----RVYVL-------DAHLQPVpVGVPGELYI---------------GGaglARgYLnrpeltAERFVADPFG 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 514 FDGtGRgpVWRHGDWLKVDPDGScIIY-GRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVL 592
Cdd:COG1020 846 FPG-AR--LYRTGDLARWLPDGN-LEFlGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP 921
|
....*
gi 517269147 593 REGVA 597
Cdd:COG1020 922 EAGAA 926
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
109-274 |
1.30e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 58.10 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwSLCAPDMAAPAVIDRFKQIepkvliaC 188
Cdd:PRK05857 41 ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI-AVMADGNLPIAAIERFCQI-------T 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 DAVTYAGRRHDRKDvlaelRRSLPTvehvILHSEAAAPAAADALLSEISATTGAEIDAFEPAwLPFDHPLWIVYSSGTTG 268
Cdd:PRK05857 113 DPAAALVAPGSKMA-----SSAVPE----ALHSIPVIAVDIAAVTRESEHSLDAASLAGNAD-QGSEDPLAMIFTSGTTG 182
|
....*.
gi 517269147 269 LPKPIV 274
Cdd:PRK05857 183 EPKAVL 188
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-636 |
1.80e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 57.01 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 258 LWIVYSSGTTGLPKPIVHGHGGIIIVVL--ALLGLHNDLGCSYHENSFGERyhwySSTGWIM---------WNSQVGGLL 326
Cdd:cd05924 6 LYILYTGGTTGMPKGVMWRQEDIFRMLMggADFGTGEFTPSEDAHKAAAAA----AGTVMFPapplmhgtgSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 327 SGTTCCIFDgspggakDKPDWTTLWRFVAQSKATFFGAGAAFFancAKAEVD-LVAAG--DLSQLRCLGSTGSPLSADTQ 403
Cdd:cd05924 82 GGQTVVLPD-------DRFDPEEVWRTIEKHKVTSMTIVGDAM---ARPLIDaLRDAGpyDLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 404 AWFnnrfaglsktngSKAQADIWWANISGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVeaFDEQGRAVIGEVGELVCT 483
Cdd:cd05924 152 QGL------------LELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 484 EPMPSMPLYFWND----------KGGARYRASyfetypdnfdgtgrgpvwrhGDWLKVDPDGSCIIYGRSDATINRHGLR 553
Cdd:cd05924 218 ARRGHIPLGYYGDeaktaetfpeVDGVRYAVP--------------------GDRATVEADGTVTLLGRGSVCINTGGEK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 554 MGTSELYSAIEALPEVLDSLVVDL--EYLGrdSYMPLFVVLREGVAFDGAmqakinkAIEAGLSRRF----LPNEIFAVA 627
Cdd:cd05924 278 VFPEEVEEALKSHPAVYDVLVVGRpdERWG--QEVVAVVQLREGAGVDLE-------ELREHCRTRIarykLPKQVVFVD 348
|
....*....
gi 517269147 628 EIPRTLSGK 636
Cdd:cd05924 349 EIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
257-638 |
1.90e-08 |
|
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: 56.89 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 257 PLWIVYSSGTTGLPKPIVHGHGGIIIVVlallglhndlgcsyhENSFGERYHWYSS--TGWIMWNSQVGGLLSGTTCCIF 334
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVP---------------DILQKEGLNWVVGdvTYLPLPATHIGGLWWILTCLIH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 335 DGSPGGAKDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAagDLSQLRCLGSTGS-PLSADTQ--AWFNNrfa 411
Cdd:cd17635 68 GGLCVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANA--TVPSLRLIGYGGSrAIAADVRfiEATGL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 412 glskTNgskaqadiwWANISGGTDFAGA-FIGGNRELPQTpGAMQCRLLGAAVEAFDEQGRAVI-GEVGELVCTEPMpSM 489
Cdd:cd17635 143 ----TN---------TAQVYGLSETGTAlCLPTDDDSIEI-NAVGRPYPGVDVYLAATDGIAGPsASFGTIWIKSPA-NM 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 490 PLYFWNDKGGA-RYRASYFETypdnfdgtgrgpvwrhGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPE 568
Cdd:cd17635 208 LGYWNNPERTAeVLIDGWVNT----------------GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSG 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517269147 569 VLDSLVVDLEylgrDSYMPLFV---VLREGVAFDGAMQAKINKaIEAGLSRRFLPNEIFAVAEIPRTLSGKKQ 638
Cdd:cd17635 272 VQECACYEIS----DEEFGELVglaVVASAELDENAIRALKHT-IRRELEPYARPSTIVIVTDIPRTQSGKVK 339
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-281 |
3.28e-08 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 56.68 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIAcdAVTY 193
Cdd:PRK06087 54 ALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA--PTLF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 194 AGRRHDrkDVLAELRRSLPTVEHVILHSEaaapaaadaLLSEISATTGAEI-DAFEPAWLPF----DHPLWIVYSSGTTG 268
Cdd:PRK06087 132 KQTRPV--DLILPLQNQLPQLQQIVGVDK---------LAPATSSLSLSQIiADYEPLTTAItthgDELAAVLFTSGTEG 200
|
170
....*....|...
gi 517269147 269 LPKPIVHGHGGII 281
Cdd:PRK06087 201 LPKGVMLTHNNIL 213
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
111-645 |
5.29e-08 |
|
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: 55.65 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFkQIEPKVLIACDA 190
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 VTYAgrrhdrkdvlaelrrslptvehvilhseaaapaaadallseisattgaeidafepawlpfDHPLWIVYSSGTTGLP 270
Cdd:cd05974 81 NTHA------------------------------------------------------------DDPMLLYFTSGTTSKP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 271 KPIVHGHGGIIIVVLALL---GLH-NDLgcsyhensfgeryHW-YSSTGWI--MWNSQVGGLLSGTTCCIFDGSPGGAK- 342
Cdd:cd05974 101 KLVEHTHRSYPVGHLSTMywiGLKpGDV-------------HWnISSPGWAkhAWSCFFAPWNAGATVFLFNYARFDAKr 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 343 -----DKPDWTTL------WRFVAQSkatffgagaaffaNCAKAEVdlvaagdlsQLRCLGSTGSPLSADT-----QAWf 406
Cdd:cd05974 168 vlaalVRYGVTTLcapptvWRMLIQQ-------------DLASFDV---------KLREVVGAGEPLNPEVieqvrRAW- 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 407 nnrfaGLSKTNGSkaqadiwwanisGGTDFAgAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAVI-GEVG-ELVCTE 484
Cdd:cd05974 225 -----GLTIRDGY------------GQTETT-ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATeGEVAlDLGDTR 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 485 PMPSMPLYFWNdkggaryrasyfetyPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIE 564
Cdd:cd05974 287 PVGLMKGYAGD---------------PDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLI 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 565 ALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLS-----RRFlpneifAVAEIPRTLSGKKQE 639
Cdd:cd05974 352 EHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLApykriRRL------EFAELPKTISGKIRR 425
|
....*.
gi 517269147 640 LPIKKL 645
Cdd:cd05974 426 VELRRR 431
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
119-667 |
6.67e-08 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.81 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 119 AAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMaapaviDRFKQIEPKVLIACDAVTYAGRRH 198
Cdd:PRK06060 40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL------HRDDHALAARNTEPALVVTSDALR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 199 DRkdvlaelRRSLPTVEHVILHSEaaapaaadallseisaTTGAEIDAFEPawLPFDHPLWIVYSSGTTGLPKPIVHGHG 278
Cdd:PRK06060 114 DR-------FQPSRVAEAAELMSE----------------AARVAPGGYEP--MGGDALAYATYTSGTTGPPKAAIHRHA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 279 GIIIVVLAL----LGLH-NDLGCSyhensfGERYHWYSSTGWIMWNSqvggLLSGTTCCIfDGSPGGAKDKPDWTTlwRF 353
Cdd:PRK06060 169 DPLTFVDAMcrkaLRLTpEDTGLC------SARMYFAYGLGNSVWFP----LATGGSAVI-NSAPVTPEAAAILSA--RF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 354 vaqskatfFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNGskaqadiwwaniSGG 433
Cdd:PRK06060 236 --------GPSVLYGVPNFFARVIDSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDG------------IGS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 434 TDFAGAFIgGNRELPQTPGAMQCRLLGAAVEAFDEQGrAVIGEVGELVCTEPMPSMPLYFWNdkggaryrasyfetYPDn 513
Cdd:PRK06060 296 TEVGQTFV-SNRVDEWRLGTLGRVLPPYEIRVVAPDG-TTAGPGVEGDLWVRGPAIAKGYWN--------------RPD- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 514 fdgtgrgPVWRHGDWL------KVDPDGsCIIYG-RSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYM 586
Cdd:PRK06060 359 -------SPVANEGWLdtrdrvCIDSDG-WVTYRcRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTL 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 587 PLFVVLREGVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKqelpIKKLLLGQPVEKVINREAMAN---- 662
Cdd:PRK06060 431 QAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKL----VRGALRKQSPTKPIWELSLTEpgsg 506
|
....*.
gi 517269147 663 -PACLD 667
Cdd:PRK06060 507 vRAQRD 512
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
111-279 |
7.75e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 55.34 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIAcda 190
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 vtyagrrhDR------KDVLAELRRSLPTVEHVILhSEAAAPAAADALLSEISATTGAEidAFEPAWlPFDHplW----I 260
Cdd:PRK08162 122 --------DTefaevaREALALLPGPKPLVIDVDD-PEYPGGRFIGALDYEAFLASGDP--DFAWTL-PADE--WdaiaL 187
|
170
....*....|....*....
gi 517269147 261 VYSSGTTGLPKPIVHGHGG 279
Cdd:PRK08162 188 NYTSGTTGNPKGVVYHHRG 206
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
96-288 |
8.29e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 55.38 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 96 PAIVscGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPdMAAPAviD 175
Cdd:PRK06188 29 PALV--LGDTRL---TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHP-LGSLD--D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 176 RFKQI---EPKVLIAcDAVTYAGRRhdrkdvlAELRRSLPTVEHVILHSEaaapaaadallSEISATTGAEIDAFEPAWL 252
Cdd:PRK06188 101 HAYVLedaGISTLIV-DPAPFVERA-------LALLARVPSLKHVLTLGP-----------VPDGVDLLAAAAKFGPAPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517269147 253 -PFDHP---LWIVYSSGTTGLPKPIVHGHGGIIIVVLALL 288
Cdd:PRK06188 162 vAAALPpdiAGLAYTGGTTGKPKGVMGTHRSIATMAQIQL 201
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
121-286 |
1.61e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 54.42 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 121 ALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-------WSLcapDMAAPAVidrfKQIEPKVLIACDAVTY 193
Cdd:PLN02860 44 SLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIvaplnyrWSF---EEAKSAM----LLVRPVMLVTDETCSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 194 AGRRHDRKDvlaelrrsLPTVE-HVILH--SEAAAPAAADALLSEISATTGAEIDAFEPAWLPFDHPLwIVYSSGTTGLP 270
Cdd:PLN02860 117 WYEELQNDR--------LPSLMwQVFLEspSSSVFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVL-ICFTSGTTGRP 187
|
170
....*....|....*.
gi 517269147 271 KPIVHGHGGIIIVVLA 286
Cdd:PLN02860 188 KGVTISHSALIVQSLA 203
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
109-636 |
2.19e-07 |
|
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: 53.64 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPdMAAPavidrfkqiepkvliac 188
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP-MLKE----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 davtyagrrhdrkdvlAELrrslptvEHVILHSEAAapaaadallseiSATTGAEIDafEPAWLPfdhplwivYSSGTTG 268
Cdd:cd05935 63 ----------------REL-------EYILNDSGAK------------VAVVGSELD--DLALIP--------YTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 269 LPKPIVHGHGGIIIVVLAlLGLHNDLGCSYHENSFGERYHwysSTGwiMWNSQVGGLLSGTTCCIFdgspggakDKPDWT 348
Cdd:cd05935 98 LPKGCMHTHFSAAANALQ-SAVWTGLTPSDVILACLPLFH---VTG--FVGSLNTAVYVGGTYVLM--------ARWDRE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 349 TLWRFVAQSKATffgagaaFFANCAKAEVDLVA-----AGDLSQLRCLGSTGSPLSA-------DTQAWFNNRFAGLSKT 416
Cdd:cd05935 164 TALELIEKYKVT-------FWTNIPTMLVDLLAtpefkTRDLSSLKVLTGGGAPMPPavaekllKLTGLRFVEGYGLTET 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 417 ngskaqadiwwanisggtdfagafiggnreLPQT----PGAMQCRLLGAAVEAFD------EQGRAV-IGEVGELVCTEp 485
Cdd:cd05935 237 ------------------------------MSQThtnpPLRPKLQCLGIP*FGVDarvidiETGRELpPNEVGEIVVRG- 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 486 mPSMPLYFWNDKggARYRASYFETYPDNFdgtgrgpvWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEA 565
Cdd:cd05935 286 -PQIFKGYWNRP--EETEESFIEIKGRRF--------FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517269147 566 LPEVLDSLVVDL--EYLGRDsyMPLFVVLREGvafdgaMQAKINKAIEAGLSRRFL-----PNEIFAVAEIPRTLSGK 636
Cdd:cd05935 355 HPAI*EVCVISVpdERVGEE--VKAFIVLRPE------YRGKVTEEDIIEWAREQMaaykyPREVEFVDELPRSASGK 424
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
111-160 |
2.98e-07 |
|
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: 53.37 E-value: 2.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI 160
Cdd:cd05907 7 TWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV 56
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
89-412 |
3.05e-07 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 53.40 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIV----SCGEDGRLcetSWPELRRKAAALALHLKEKGiKPGDRVAAYLPNIPETIIAFLASASIGAIwSLC 164
Cdd:cd05931 3 AAARPDRPAYTflddEGGREETL---TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI-AVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 165 APDMAAPAVIDR----FKQIEPKVLIACDAVtyagrrhdrkdvLAELRRSLptvehvilhSEAAAPAAADALLSEISATT 240
Cdd:cd05931 78 LPPPTPGRHAERlaaiLADAGPRVVLTTAAA------------LAAVRAFA---------ASRPAAGTPRLLVVDLLPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 241 GAeiDAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLglhndlgcsyhensfgERYHWYSSTGWIMWNS 320
Cdd:cd05931 137 SA--ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIR----------------RAYGLDPGDVVVSWLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 321 Q------VGGLL----SGTTCCIFdgSPGGAKDKPdwtTLW-RFVAQSKATFFGAGAAFFANCAKA--EVDLvAAGDLSQ 387
Cdd:cd05931 199 LyhdmglIGGLLtplySGGPSVLM--SPAAFLRRP---LRWlRLISRYRATISAAPNFAYDLCVRRvrDEDL-EGLDLSS 272
|
330 340
....*....|....*....|....*
gi 517269147 388 LRCLGSTGSPLSADTQAWFNNRFAG 412
Cdd:cd05931 273 WRVALNGAEPVRPATLRRFAEAFAP 297
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-280 |
4.68e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.04 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 87 VDAADAAGLPAIVSCGEdgrlcETSWPELRRKAAALALHLKEK-GIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCA 165
Cdd:PRK08314 18 VSARRYPDKTAIVFYGR-----AISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 166 PdMAAPaviDRFKQI----EPKVLIAcdAVTYAGRrhdrkdvLAELRRSLPtVEHVILHSeaaapaaadaLLSEISATTG 241
Cdd:PRK08314 93 P-MNRE---EELAHYvtdsGARVAIV--GSELAPK-------VAPAVGNLR-LRHVIVAQ----------YSDYLPAEPE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517269147 242 AEIdafePAWLPFDHPL----------W----------------------IVYSSGTTGLPKPIVHGHGGI 280
Cdd:PRK08314 149 IAV----PAWLRAEPPLqalapggvvaWkealaaglappphtagpddlavLPYTSGTTGVPKGCMHTHRTV 215
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
73-641 |
4.76e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 53.08 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 73 PGAQVNYARQVFR---------HVDAADAAGLPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPN 143
Cdd:PRK13383 20 PRAVLRLLREASRggtnpytllAVTAARWPGRTAIID--DDGAL---SYRELQRATESLARRLTRDGVAPGRAVGVMCRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 144 IPETIIAFLASASIGAIWSLCAPDMAApavidrfkqiepkvliacDAVTYAGRRHDRKDVLAE---LRRSLPTVEHVILH 220
Cdd:PRK13383 95 GRGFVTAVFAVGLLGADVVPISTEFRS------------------DALAAALRAHHISTVVADnefAERIAGADDAVAVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 221 SeaaapaaadallseiSATTGAEIDAFEPAWLPfdhPLWIVY-SSGTTGLPK-----PIVHGHGGIIIVVLALLGLHNDL 294
Cdd:PRK13383 157 D---------------PATAGAEESGGRPAVAA---PGRIVLlTSGTTGKPKgvpraPQLRSAVGVWVTILDRTRLRTGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 295 GCS-----YHENSFGeryhwysstgWIMWNSQVGGLLsgTTCCIFDGSPGGAKdkpdwTTLWRFVAQSKATFFGAGAAFF 369
Cdd:PRK13383 219 RISvampmFHGLGLG----------MLMLTIALGGTV--LTHRHFDAEAALAQ-----ASLHRADAFTAVPVVLARILEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 370 ANCAKAEvdlvaaGDLSQLRCLGSTGSPLSADtqawFNNRFAglsktngsKAQADIWWaNISGGTDFAGAFIGGNRELPQ 449
Cdd:PRK13383 282 PPRVRAR------NPLPQLRVVMSSGDRLDPT----LGQRFM--------DTYGDILY-NGYGSTEVGIGALATPADLRD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 450 TPGAMQCRLLGAAVEAFDEQGRAVigevgelvctEPMPSMPLYFWNDKGGARYRASYFETYPDNFDGTGrgpvwrhgDWL 529
Cdd:PRK13383 343 APETVGKPVAGCPVRILDRNNRPV----------GPRVTGRIFVGGELAGTRYTDGGGKAVVDGMTSTG--------DMG 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 530 KVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRDsyMPLFVVLREGVAFDGamqAKIN 607
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVpdERFGHR--LAAFVVLHPGSGVDA---AQLR 479
|
570 580 590
....*....|....*....|....*....|....*.
gi 517269147 608 KAIEAGLSRRFLPNEIFAVAEIPRTLSGK--KQELP 641
Cdd:PRK13383 480 DYLKDRVSRFEQPRDINIVSSIPRNPTGKvlRKELP 515
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
109-281 |
5.24e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 52.63 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWP--ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-----WSLCAPDMAapAVIDrfkQIE 181
Cdd:PRK08316 34 DRSWTyaELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVhvpvnFMLTGEELA--YILD---HSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 182 PKVLIACDAVTYAGRRHDRKDVLA--ELRRSLPTVEHvilhsEAAAPAAADALLSEISATTGAEIDAfepawlpfDHPLW 259
Cdd:PRK08316 109 ARAFLVDPALAPTAEAALALLPVDtlILSLVLGGREA-----PGGWLDFADWAEAGSVAEPDVELAD--------DDLAQ 175
|
170 180
....*....|....*....|..
gi 517269147 260 IVYSSGTTGLPKPIVHGHGGII 281
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALI 197
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
514-636 |
5.53e-07 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 52.02 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 514 FDGTGRGPVWRHGDWLKV------DPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEylgrDSY-- 585
Cdd:cd17633 195 FSGYVRGGFSNPDGWMSVgdigyvDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIP----DARfg 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 517269147 586 -MPLFVVLREGVAfDGAMQAKINKAieagLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd17633 271 eIAVALYSGDKLT-YKQLKRFLKQK----LSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
259-636 |
6.52e-07 |
|
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: 52.40 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 259 WIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCSYHENSFGERYHWYSSTgwimwNSQVGGLLSGTTCCIFDGSp 338
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFV-----EQMTLALLNGQKLVVPPDE- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 339 ggakDKPDWTTLWRFVAQSKATFFgagaaffaNCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNG 418
Cdd:cd17648 172 ----MRFDPDRFYAYINREKVTYL--------SGTPSVLQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 419 SKAQADIWWANI--SGGTDFAGAfIGgnRELPQTpgamQCRLLGAAVEafdeqgRAVIGEVGEL----VCTEPMpsmply 492
Cdd:cd17648 240 GPTETTVTNHKRffPGDQRFDKS-LG--RPVRNT----KCYVLNDAMK------RVPVGAVGELylggDGVARG------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 493 FWN--DKGGARYRASYFETYPDNFDGTgRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVL 570
Cdd:cd17648 301 YLNrpELTAERFLPNPFQTEQERARGR-NARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVR 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517269147 571 DSLVVDLEYLG-----RDSYMPLFVVLREGVAFDGAMQAkinkAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd17648 380 ECAVVAKEDASqaqsrIQKYLVGYYLPEPGHVPESDLLS----FLRAKLPRYMVPARLVRLEGIPVTINGK 446
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
109-281 |
6.62e-07 |
|
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: 52.43 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPKVLIAC 188
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 DavtyagrrHDRKDVLAELRRSLPTVEHVILHSEAAAPAAADALLSEIS--ATTGAEIDAFEP-------AWLPFDHPLW 259
Cdd:cd17641 91 D--------EEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPRLISFEdvVALGRALDRRDPglyerevAAGKGEDVAV 162
|
170 180
....*....|....*....|..
gi 517269147 260 IVYSSGTTGLPKPIVHGHGGII 281
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFL 184
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
72-278 |
1.47e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 51.44 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 72 FPGAQVNYARQVfrhVDAA----DAAGLPAIVSCGEDGRLC--ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIP 145
Cdd:PRK09274 1 MMASMANIARHL---PRAAqerpDQLAVAVPGGRGADGKLAydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 146 ETIIAFLASASIGAIWSLCAPDMAapavIDRFKQI----EPKVLIACDAVTyAGRRHdrkdvlaeLRRSLPTVEHVILHS 221
Cdd:PRK09274 78 EFFALTFALFKAGAVPVLVDPGMG----IKNLKQClaeaQPDAFIGIPKAH-LARRL--------FGWGKPSVRRLVTVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517269147 222 EAAAPAAADalLSEISATTGAEidAFEPAWLPFDHPLWIVYSSGTTGLPKPIVHGHG 278
Cdd:PRK09274 145 GRLLWGGTT--LATLLRDGAAA--PFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG 197
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
109-636 |
1.99e-06 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 50.93 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAApavidrfkqiepkvliac 188
Cdd:cd17650 12 QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPA------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 davtyagrrhDRKDVLAElrrslptvehvilHSeaaapaaadallseisattGAEIDAFEPawlpfDHPLWIVYSSGTTG 268
Cdd:cd17650 74 ----------ERLQYMLE-------------DS-------------------GAKLLLTQP-----EDLAYVIYTSGTTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 269 LPKPIVHGHGGIIIVVLALLGlhndlgcSYHENSFGERYHWYSSTGWIMWNSQVG-GLLSGTTCCIfdgSPGGAKDKPdw 347
Cdd:cd17650 107 KPKGVMVEHRNVAHAAHAWRR-------EYELDSFPVRLLQMASFSFDVFAGDFArSLLNGGTLVI---CPDEVKLDP-- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 348 TTLWRFVAQSKATFFGAGAAFfancAKAEVDLVAAG--DLSQLRCL--GSTGSPlsADTQAWFNNRF-AGLSKTNG---S 419
Cdd:cd17650 175 AALYDLILKSRITLMESTPAL----IRPVMAYVYRNglDLSAMRLLivGSDGCK--AQDFKTLAARFgQGMRIINSygvT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 420 KAQADIWWANISGGTDFAGAFIGGNRELPQTpgamqcrllgaAVEAFDEQGRAV-IGEVGELVCtepmpsmplyfwndkG 498
Cdd:cd17650 249 EATIDSTYYEEGRDPLGDSANVPIGRPLPNT-----------AMYVLDERLQPQpVGVAGELYI---------------G 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 499 GARYRASYF-------ETY-PDNFDGTGRgpVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVL 570
Cdd:cd17650 303 GAGVARGYLnrpeltaERFvENPFAPGER--MYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAID 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517269147 571 DSLVVDLEYLGRDSYMPLFVVLRegvafdgamqAKIN-KAIEAGLSRRF----LPNEIFAVAEIPRTLSGK 636
Cdd:cd17650 381 EAVVAVREDKGGEARLCAYVVAA----------ATLNtAELRAFLAKELpsymIPSYYVQLDALPLTPNGK 441
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
103-293 |
2.05e-06 |
|
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: 50.75 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 103 EDGRLC-ETSWPELRRKAAALALHLkekGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIE 181
Cdd:cd05938 2 EGETYTyRDVDRRSNQAARALLAHA---GLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 182 PKVLIAcDAvtyagrrhdrkDVLAELRRSLPTVE----HVILHSEAAAPAAADALLSEISATTGAEIDAFEPAWLPFDHP 257
Cdd:cd05938 79 AKVLVV-AP-----------ELQEAVEEVLPALRadgvSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSP 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 517269147 258 LWIVYSSGTTGLPKPIVHGHGGIIIV--VLALLGLHND 293
Cdd:cd05938 147 ALYIYTSGTTGLPKAARISHLRVLQCsgFLSLCGVTAD 184
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
459-646 |
2.47e-06 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 50.45 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 459 LGAAVEAFDEQGRAV-IGEVGELvCTEPMPS---MPLYFWNDKGGARYrasyfetypdnFDGTGrgpvWRH-GDWLKVDP 533
Cdd:PRK08008 347 FCYEAEIRDDHNRPLpAGEIGEI-CIKGVPGktiFKEYYLDPKATAKV-----------LEADG----WLHtGDTGYVDE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 534 DGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamQAKINKAIEAG 613
Cdd:PRK08008 411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLS---EEEFFAFCEQN 487
|
170 180 190
....*....|....*....|....*....|...
gi 517269147 614 LSRRFLPNEIFAVAEIPRTLSGKKqelpIKKLL 646
Cdd:PRK08008 488 MAKFKVPSYLEIRKDLPRNCSGKI----IKKNL 516
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
111-280 |
4.39e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 49.89 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCAPDMAAPAVIDRfkqiepkvliaCDA 190
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV---VVPLDPALPIAEQ-----------RVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 VTYAGRRHDRKDVLAELRRSLPTVEH--VILHSEAAAPAAADALLSEISATTGAEIDAFEPAWLPFDHPLwIVYSSGTTG 268
Cdd:PRK05852 111 SQAAGARVVLIDADGPHDRAEPTTRWwpLTVNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDAM-IMFTGGTTG 189
|
170
....*....|..
gi 517269147 269 LPKPIVHGHGGI 280
Cdd:PRK05852 190 LPKMVPWTHANI 201
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
80-636 |
5.54e-06 |
|
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: 49.24 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVScgEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:cd12115 6 EAQAARTPDA------IALVC--GDESL---TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWslcAP-DMAAPAVIDRFkqiepkvlIACDAvtyagrrhdrkdvlaelrrslpTVEHVIlhseaaapaaadallseisa 238
Cdd:cd12115 75 AY---VPlDPAYPPERLRF--------ILEDA----------------------QARLVL-------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 239 TTGaeidafepawlpfDHPLWIVYSSGTTGLPKPIVHGHGGIIivvlALLGlhndlgcsYHENSFGEryhwysstgwimw 318
Cdd:cd12115 102 TDP-------------DDLAYVIYTSGSTGRPKGVAIEHRNAA----AFLQ--------WAAAAFSA------------- 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 319 nSQVGGLLSGTTCCiFDGS---------PGG-------AKDKPDW-----TTLWRFVAQskatffgagaaffancAKAEv 377
Cdd:cd12115 144 -EELAGVLASTSIC-FDLSvfelfgplaTGGkvvladnVLALPDLpaaaeVTLINTVPS----------------AAAE- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 378 dLVAAGDLSQ-LRCLGSTGSPLSADTQAwfnnRFAGlsKTNGSKAqadiwwANISG---GTDFAGAfiggnreLPQTPGA 453
Cdd:cd12115 205 -LLRHDALPAsVRVVNLAGEPLPRDLVQ----RLYA--RLQVERV------VNLYGpseDTTYSTV-------APVPPGA 264
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 454 MQC-----RLLGAAVEAFDEQGRAV-IGEVGELVCTEPmpSMPLYFWNDKG--GARYRasyfetyPDNFDGTGRgpVWRH 525
Cdd:cd12115 265 SGEvsigrPLANTQAYVLDRALQPVpLGVPGELYIGGA--GVARGYLGRPGltAERFL-------PDPFGPGAR--LYRT 333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 526 GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamQAK 605
Cdd:cd12115 334 GDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGL---VED 410
|
570 580 590
....*....|....*....|....*....|.
gi 517269147 606 INKAIEAGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:cd12115 411 LRRHLGTRLPAYMVPSRFVRLDALPLTPNGK 441
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
467-638 |
6.32e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 48.81 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 467 DEQGRAV--IGEVGELvCTEPMPSMPLYfWNDKGGARyrasyfETypdnFDGTGrgpvWRH-GDWLKVDPDGSCIIYGRS 543
Cdd:cd05917 189 DPEGGIVppVGVPGEL-CIRGYSVMKGY-WNDPEKTA------EA----IDGDG----WLHtGDLAVMDEDGYCRIVGRI 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 544 DATINRHGLRMGTSELYSAIEALPEVLDSLVVDL--EYLGRDsyMPLFVVLREGVAFDGAmqaKINKAIEAGLSRRFLPN 621
Cdd:cd05917 253 KDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVpdERYGEE--VCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPR 327
|
170
....*....|....*..
gi 517269147 622 EIFAVAEIPRTLSGKKQ 638
Cdd:cd05917 328 YVFFVDEFPLTVSGKIQ 344
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
111-281 |
1.05e-05 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 48.80 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCA--PDMAAPAVIDRFKQIEPKVLiac 188
Cdd:PRK07529 60 TYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA---NPinPLLEPEQIAELLRAAGAKVL--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 daVTYAGR-RHDRKDVLAELRRSLPTVEHVI---LHSEAAAPAAADALLSEISATTG-----AEIDAFEPAWLPFDHPLW 259
Cdd:PRK07529 134 --VTLGPFpGTDIWQKVAEVLAALPELRTVVevdLARYLPGPKRLAVPLIRRKAHARildfdAELARQPGDRLFSGRPIG 211
|
170 180
....*....|....*....|....*...
gi 517269147 260 I------VYSSGTTGLPKPIVHGHGGII 281
Cdd:PRK07529 212 PddvaayFHTGGTTGMPKLAQHTHGNEV 239
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
111-278 |
1.15e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 48.33 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwslCAPDMAAPavidrfkqiePKVLiacda 190
Cdd:PRK09029 30 TWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGAR---VLPLNPQL----------PQPL----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 191 vtyagrrhdrkdvLAELRRSLpTVEHVI-LHSEAAAPAAADALLSEISATTGAEIDAFEPAWLPFdhplwivySSGTTGL 269
Cdd:PRK09029 92 -------------LEELLPSL-TLDFALvLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTL--------TSGSTGL 149
|
....*....
gi 517269147 270 PKPIVHGHG 278
Cdd:PRK09029 150 PKAAVHTAQ 158
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
84-274 |
1.95e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 47.76 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 84 FRHVDAADAAGLPAIVSCGEDGRLcetSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG----A 159
Cdd:PRK13391 2 YPGIHAQTTPDKPAVIMASTGEVV---TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGlyytC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWSLCAPDMAAPAVIDRfkqiEPKVLIAcdavtyagrRHDRKDVLAELRRSLPTVEHVILHSEAAAPAAADALlseisat 239
Cdd:PRK13391 79 VNSHLTPAEAAYIVDDS----GARALIT---------SAAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGY------- 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 517269147 240 tgAEIDAFEPAWLPFDHPLW--IVYSSGTTGLPKPIV 274
Cdd:PRK13391 139 --AEAVAGLPATPIADESLGtdMLYSSGTTGRPKGIK 173
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
111-271 |
2.01e-05 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 47.56 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWslcAPDMAA--PAVIDRFKQ-IEPKVLIa 187
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVF---LPLNTAytLAELDYFIGdAEPALVV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 188 CDAVTYAGRRHdrkdvLAElRRSLPTVEhvILHSEAAAPaaadalLSEISATTGaeiDAFEPAWLPFDHPLWIVYSSGTT 267
Cdd:PRK07514 106 CDPANFAWLSK-----IAA-AAGAPHVE--TLDADGTGS------LLEAAAAAP---DDFETVPRGADDLAAILYTSGTT 168
|
....
gi 517269147 268 GLPK 271
Cdd:PRK07514 169 GRSK 172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
79-578 |
3.56e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 47.26 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 79 YARQVFRH-VDAADAAGLP-AI-VSCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASA 155
Cdd:PRK12316 1999 YPRGPGVHqRIAEQAARAPeAIaVVFGDQ----HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 156 SIGAIWSLCAPDmaapavidrfkqiepkvliacdavtYAGRRhdrkdvLAelrrslptveHVILHSEAAAPAAADALLSE 235
Cdd:PRK12316 2075 KAGGAYVPLDPN-------------------------YPAER------LA----------YMLEDSGAALLLTQRHLLER 2113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 236 ISATTGAEIDAFE-PAWL---PFDHPL---------WIVYSSGTTGLPKPIVHGHGGIIIVVLAlLGLHNDLG---CSYH 299
Cdd:PRK12316 2114 LPLPAGVARLPLDrDAEWadyPDTAPAvqlagenlaYVIYTSGSTGLPKGVAVSHGALVAHCQA-AGERYELSpadCELQ 2192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 300 ENSFG-ERYHWysstGWiMWNsqvggLLSGTTCCIFDGSpggakdkpDWTT--LWRFVAQSKATFFGAGAAFFANCAK-A 375
Cdd:PRK12316 2193 FMSFSfDGAHE----QW-FHP-----LLNGARVLIRDDE--------LWDPeqLYDEMERHGVTILDFPPVYLQQLAEhA 2254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 376 EVDlvaaGDLSQLR--CLGSTGSPLSADTQAWFNNRFAGLSKTNG-SKAQAD--IWWANISGGTDFAGAFIGgnrelpQT 450
Cdd:PRK12316 2255 ERD----GRPPAVRvyCFGGEAVPAASLRLAWEALRPVYLFNGYGpTEAVVTplLWKCRPQDPCGAAYVPIG------RA 2324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 451 PGAMQCRLLGAAVEAFdeqgraVIGEVGElvctepmpsmpLYFwndkGGARYRASYFET--------YPDNFDGTGrGPV 522
Cdd:PRK12316 2325 LGNRRAYILDADLNLL------APGMAGE-----------LYL----GGEGLARGYLNRpgltaerfVPDPFSASG-ERL 2382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 517269147 523 WRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLE 578
Cdd:PRK12316 2383 YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQD 2438
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
104-278 |
4.58e-05 |
|
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: 46.69 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 104 DGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDMAAPAVIDRFKQIEPK 183
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 184 VLIacdavtyAGRRHDRKDVLAELRRSLPTVEhVILHSEAAAPAAADALLseisattgAEIDAFEPAWLPFDHPLW-IVY 262
Cdd:cd05932 81 ALF-------VGKLDDWKAMAPGVPEGLISIS-LPPPSAANCQYQWDDLI--------AQHPPLEERPTRFPEQLAtLIY 144
|
170
....*....|....*.
gi 517269147 263 SSGTTGLPKPIVHGHG 278
Cdd:cd05932 145 TSGTTGQPKGVMLTFG 160
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
100-270 |
5.21e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 46.27 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 100 SCGEDGRLCETSWPELRRKAAALALHLkEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIW-SLCAPDMAAPAviDR-- 176
Cdd:PRK12476 59 SHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAvPLFAPELPGHA--ERld 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 177 --FKQIEPKVLIACDAVtyagrrhdrKDVLAELRRSLPTVE--HVIlhseaaapaaadaLLSEISATTGAeidAFEPAWL 252
Cdd:PRK12476 136 taLRDAEPTVVLTTTAA---------AEAVEGFLRNLPRLRrpRVI-------------AIDAIPDSAGE---SFVPVEL 190
|
170
....*....|....*...
gi 517269147 253 PFDHPLWIVYSSGTTGLP 270
Cdd:PRK12476 191 DTDDVSHLQYTSGSTRPP 208
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
388-641 |
6.18e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 46.29 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 388 LRCLGSTGSPLSADTQAWFNNRFAGLSKTNGSKAQADiwWANISGGTDFagafiggnRELPQTPG--AMqcrllGAAVEA 465
Cdd:PRK13382 314 LRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG--MIATATPADL--------RAAPDTAGrpAE-----GTEIRI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 466 FDEQGRAV-IGEVGELvctepmpsmplYFWNDkggaryraSYFETYPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSD 544
Cdd:PRK13382 379 LDQDFREVpTGEVGTI-----------FVRND--------TQFDGYTSGSTKDFHDGFMASGDVGYLDENGRLFVVGRDD 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 545 ATINRHGLRMGTSELYSAIEALPEVLDSLV--VDLEYLGRDsyMPLFVVLREGVAfdgAMQAKINKAIEAGLSRRFLPNE 622
Cdd:PRK13382 440 EMIVSGGENVYPIEVEKTLATHPDVAEAAVigVDDEQYGQR--LAAFVVLKPGAS---ATPETLKQHVRDNLANYKVPRD 514
|
250 260
....*....|....*....|.
gi 517269147 623 IFAVAEIPRTLSGK--KQELP 641
Cdd:PRK13382 515 IVVLDELPRGATGKilRRELQ 535
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
111-286 |
6.47e-05 |
|
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: 46.14 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIwsLCAPD--MAAPAVIDRFKQIEPKVLIAC 188
Cdd:cd12118 31 TWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV--LNALNtrLDAEEIAFILRHSEAKVLFVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 DAVTYagrrhdrKDVLAELRRSlptvehvilhseaaapaaadallseisattgaeidaFEPAWlPFDH--PLWIVYSSGT 266
Cdd:cd12118 109 REFEY-------EDLLAEGDPD------------------------------------FEWIP-PADEwdPIALNYTSGT 144
|
170 180
....*....|....*....|
gi 517269147 267 TGLPKPIVHGHGGIIIVVLA 286
Cdd:cd12118 145 TGRPKGVVYHHRGAYLNALA 164
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
114-636 |
8.34e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 45.84 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 114 ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-----WSLcAPDMAAPAVIDRfkqiEPKVLIAc 188
Cdd:PRK12406 16 ELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYavpvnWHF-KPEEIAYILEDS----GARVLIA- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 189 davtyagrrHDrkDVLAELRRSLPtvEHV-ILHSEAAAPAAADALLSEISATTGAEIDAFEpAWLPfDHPLW-------- 259
Cdd:PRK12406 90 ---------HA--DLLHGLASALP--AGVtVLSVPTPPEIAAAYRISPALLTPPAGAIDWE-GWLA-QQEPYdgppvpqp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 260 --IVYSSGTTGLPK------PIVHGHGGIIIVVLALLGLHNDL-----GCSYHE--NSFGERyhwysstgwimwNSQVGG 324
Cdd:PRK12406 155 qsMIYTSGTTGHPKgvrraaPTPEQAAAAEQMRALIYGLKPGIralltGPLYHSapNAYGLR------------AGRLGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 325 LLSgttccifdgspggAKDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDLVAAGDLSQLRCLGSTGSPLSADTQa 404
Cdd:PRK12406 223 VLV-------------LQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVK- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 405 wfnnrfaglsktngskaQADI-WWANI----SGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQGRAV-IGEVG 478
Cdd:PRK12406 289 -----------------RAMIeWWGPViyeyYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLpQGEIG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 479 ELVCTepMPSMPLYFWNDKggaryrasyfetyPDNFDGTGRGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSE 558
Cdd:PRK12406 352 EIYSR--IAGNPDFTYHNK-------------PEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 559 LYSAIEALPEVLDSLVV---DLEYlgRDSYMpLFVVLREGVAFDgamQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSG 635
Cdd:PRK12406 417 IEAVLHAVPGVHDCAVFgipDAEF--GEALM-AVVEPQPGATLD---EADIRAQLKARLAGYKVPKHIEIMAELPREDSG 490
|
.
gi 517269147 636 K 636
Cdd:PRK12406 491 K 491
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
526-646 |
1.24e-04 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 45.25 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 526 GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYlgrdsymPLF-------VVLREGVAF 598
Cdd:PRK07514 382 GDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPH-------PDFgegvtavVVPKPGAAL 454
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 517269147 599 DGAmqakinkAIEAGLSRRF----LPNEIFAVAEIPRTLSGKKQelpiKKLL 646
Cdd:PRK07514 455 DEA-------AILAALKGRLarfkQPKRVFFVDELPRNTMGKVQ----KNLL 495
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
504-641 |
1.73e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 504 ASYFETYPDNFDGtgrGPVWRHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVdleYLGRD 583
Cdd:PRK12467 876 AERFVPDPFGADG---GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL---AQPGD 949
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517269147 584 SYMPLFVVLREGVAFDGAMQAKINKAIEAGLSRRF----LPNEIFAVAEIPRTLSGK--KQELP 641
Cdd:PRK12467 950 AGLQLVAYLVPAAVADGAEHQATRDELKAQLRQVLpdymVPAHLLLLDSLPLTPNGKldRKALP 1013
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
111-160 |
2.61e-04 |
|
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: 43.97 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI 160
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAI 58
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
102-338 |
2.83e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 44.27 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 102 GEDGRLCETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI-------WSLCAPDMAapavi 174
Cdd:PRK12582 73 PGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPaapvspaYSLMSHDHA----- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 175 dRFKQI----EPKVLIACDAVTYAGrrhdrkdVLAELRRSLPTVEHVILHSEAAAPAAadalLSEISATT-GAEIDAFEP 249
Cdd:PRK12582 148 -KLKHLfdlvKPRVVFAQSGAPFAR-------ALAALDLLDVTVVHVTGPGEGIASIA----FADLAATPpTAAVAAAIA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 250 AWLPfDHPLWIVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCSYHENSFgeryhwysstGWIMWNSQVGG----- 324
Cdd:PRK12582 216 AITP-DTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSL----------DWMPWNHTMGGnanfn 284
|
250
....*....|....*.
gi 517269147 325 --LLSGTTCCIFDGSP 338
Cdd:PRK12582 285 glLWGGGTLYIDDGKP 300
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
111-163 |
3.05e-04 |
|
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: 43.88 E-value: 3.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSL 163
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAAL 57
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
89-299 |
5.11e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.62 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEdgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDM 168
Cdd:PRK05691 2198 AARTPQAPALTFAGQ-----TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEY 2272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 AapavIDRFK-QIEPK--VLIACDAVTYagrrhdrkDVLAELRRSlptVEHVILHSEaaapaaadallseisattGAEID 245
Cdd:PRK05691 2273 P----LERLHyMIEDSgiGLLLSDRALF--------EALGELPAG---VARWCLEDD------------------AAALA 2319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517269147 246 AFEPAWLPF----DHPLWIVYSSGTTGLPKPIVHGHGGIII---VVLALLGLHNDlGCSYH 299
Cdd:PRK05691 2320 AYSDAPLPFlslpQHQAYLIYTSGSTGKPKGVVVSHGEIAMhcqAVIERFGMRAD-DCELH 2379
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
262-569 |
6.95e-04 |
|
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: 42.47 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 262 YSSGTTGLPKPIVHGHGGIiiVVLALLGLHNDLgcsyhensfgeryhwYSSTGWIMWNS---QVGGLLSGTTCCIFDG-- 336
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNE--VYNAWMLALNSL---------------FDPDDVLLCGLplfHVNGSVVTLLTPLASGah 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 337 ----SPGGAKDKPDWTTLWRFVAQSKATFFGAGAAFFANCAKAEVDlvaaGDLSQLRCLGSTGSPLSADTQAWFNNRfAG 412
Cdd:cd05944 72 vvlaGPAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVN----ADISSLRFAMSGAAPLPVELRARFEDA-TG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 413 LSKTNGSkaqadiwwanisGGTDFAGAFIGGNRELPQTPGAMQCRLLGAAVEAFDEQG------RAVIGEVGELVCTEPm 486
Cdd:cd05944 147 LPVVEGY------------GLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllrDCAPDEVGEICVAGP- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 487 psmplyfwNDKGGAryrasyfeTYPDNFDGTGRGPVW-RHGDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEA 565
Cdd:cd05944 214 --------GVFGGY--------LYTEGNKNAFVADGWlNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLR 277
|
....
gi 517269147 566 LPEV 569
Cdd:cd05944 278 HPAV 281
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
80-641 |
7.31e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 43.23 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 80 ARQVFRHVDAadaaglPAIVsCGEDgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGA 159
Cdd:PRK12467 3102 EAQVARTPEA------PALV-FGDQ----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGG 3170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 160 IWSLCAPDMAApaviDRFK-QIEP---KVLIAcdavtyagrrhdrkdvLAELRRSLPtvehvILHSEAAAPAAADALLSE 235
Cdd:PRK12467 3171 AYVPLDPEYPR----ERLAyMIEDsgvKLLLT----------------QAHLLEQLP-----APAGDTALTLDRLDLNGY 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 236 ISATTGAEIDAFEPAWlpfdhplwIVYSSGTTGLPKPIVHGHGGIII---VVLALLGLHND----LGCSYHENSFGERYH 308
Cdd:PRK12467 3226 SENNPSTRVMGENLAY--------VIYTSGSTGKPKGVGVRHGALANhlcWIAEAYELDANdrvlLFMSFSFDGAQERFL 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 309 WysstgwimwnsqvgGLLSGTTCCIFDGspggakDKPDWTTLWRFVAQSKATFFgagaaffaNCAKAEVDLVAA----GD 384
Cdd:PRK12467 3298 W--------------TLICGGCLVVRDN------DLWDPEELWQAIHAHRISIA--------CFPPAYLQQFAEdaggAD 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 385 LSQLRCLGSTGSPLSADTQAWFNNRFAGLSKTNG---SKAQADI--WWANISGGTDFAGAFIGgnRELPqtpgamqcrll 459
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGygpTEAVVTVtlWKCGGDAVCEAPYAPIG--RPVA----------- 3416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 460 GAAVEAFDEQGRAV-IGEVGELvctepmpsmplyFWNDKGGARyraSYFET--------YPDNFDGTGrGPVWRHGDWLK 530
Cdd:PRK12467 3417 GRSIYVLDGQLNPVpVGVAGEL------------YIGGVGLAR---GYHQRpsltaerfVADPFSGSG-GRLYRTGDLAR 3480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 531 VDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGrDSYMPLFVVLRegvAFDGAMQAKINKAI 610
Cdd:PRK12467 3481 YRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAG-GKQLVAYVVPA---DPQGDWRETLRDHL 3556
|
570 580 590
....*....|....*....|....*....|...
gi 517269147 611 EAGLSRRFLPNEIFAVAEIPRTLSGK--KQELP 641
Cdd:PRK12467 3557 AASLPDYMVPAQLLVLAAMPLGPNGKvdRKALP 3589
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
558-636 |
1.01e-03 |
|
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: 38.29 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 558 ELYSAIEALPEVLDSLVV--DLEYLGRdsyMPL-FVVLREGVAfdgAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLS 634
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVgvPDELKGE---APVaFVVLKPGVE---LLEEELVAHVREELGPYAVPKEVVFVDELPKTRS 74
|
..
gi 517269147 635 GK 636
Cdd:pfam13193 75 GK 76
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
260-307 |
1.03e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 42.27 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 517269147 260 IVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGCSYHEnsfGERY 307
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEE---DETY 313
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
79-641 |
1.06e-03 |
|
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: 42.16 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 79 YARQVFRHVDAadaaglPAIVSCGEdgrlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG 158
Cdd:cd17645 4 FEEQVERTPDH------VAVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 159 AIWSLCAPDmaapavidrfkqiepkvliacdavtYAGRRhdrkdvlaelrrslptvehvilhseaaapaaadalLSEISA 238
Cdd:cd17645 73 GAYVPIDPD-------------------------YPGER-----------------------------------IAYMLA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 239 TTGAEIDAFEPawlpfDHPLWIVYSSGTTGLPKpivhghgGIIIVVLALLGLhndlgCSYHENSFG----ERYHWYSSTG 314
Cdd:cd17645 93 DSSAKILLTNP-----DDLAYVIYTSGSTGLPK-------GVMIEHHNLVNL-----CEWHRPYFGvtpaDKSLVYASFS 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 315 -----WIMWNSqvggLLSGTTCCIFDgspggAKDKPDWTTLWRFVAQSKATFFGAGAAFfancakaeVDLVAAGDLSQLR 389
Cdd:cd17645 156 fdasaWEIFPH----LTAGAALHVVP-----SERRLDLDALNDYFNQEGITISFLPTGA--------AEQFMQLDNQSLR 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 390 CLGSTGSPLSADTQAWF---NNRFAGLSKTNGSKAQADIWWANISGGTDFAgafiggNRELPQTPGAMQCRLLGAAVEAF 466
Cdd:cd17645 219 VLLTGGDKLKKIERKGYklvNNYGPTENTVVATSFEIDKPYANIPIGKPID------NTRVYILDEALQLQPIGVAGELC 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 467 deqgraVIGEvgelvctepmpsmplyfwndkGGARYRASYFETYPDNFDGTGRGP---VWRHGDWLKVDPDGSCIIYGRS 543
Cdd:cd17645 293 ------IAGE---------------------GLARGYLNRPELTAEKFIVHPFVPgerMYRTGDLAKFLPDGNIEFLGRL 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 544 DATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDgamqaKINKAIEAGLSRRFLPNEI 623
Cdd:cd17645 346 DQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHE-----ELREWLKNDLPDYMIPTYF 420
|
570 580
....*....|....*....|
gi 517269147 624 FAVAEIPRTLSGK--KQELP 641
Cdd:cd17645 421 VHLKALPLTANGKvdRKALP 440
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
97-273 |
1.38e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 41.81 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 97 AIVSCGEDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIG----AI-WSLCAPDmAAP 171
Cdd:PRK08276 1 PAVIMAPSGE--VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGlyytPInWHLTAAE-IAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 172 AVIDRfkqiEPKVLIACDAVtyagrrhdrKDVLAELRRSLPtvEHVilhseaaapaaadallsEISATTGAEIDAFEP-- 249
Cdd:PRK08276 78 IVDDS----GAKVLIVSAAL---------ADTAAELAAELP--AGV-----------------PLLLVVAGPVPGFRSye 125
|
170 180 190
....*....|....*....|....*....|...
gi 517269147 250 AWL-------PFDHPLW--IVYSSGTTGLPKPI 273
Cdd:PRK08276 126 EALaaqpdtpIADETAGadMLYSSGTTGRPKGI 158
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
532-636 |
3.26e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 40.40 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 532 DPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVvdleYLGRDSYMPLFVVLREgVAFDGAMQAKINKAIE 611
Cdd:PRK08308 302 SERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV----YRGKDPVAGERVKAKV-ISHEEIDPVQLREWCI 376
|
90 100
....*....|....*....|....*
gi 517269147 612 AGLSRRFLPNEIFAVAEIPRTLSGK 636
Cdd:PRK08308 377 QHLAPYQVPHEIESVTEIPKNANGK 401
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
109-160 |
4.49e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 40.02 E-value: 4.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 517269147 109 ETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI 160
Cdd:PRK06710 49 DITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGI 100
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
89-641 |
4.56e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 40.71 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 89 AADAAGLPAIVSCGEDGRlcETSWPELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAIWSLCAPDm 168
Cdd:PRK12316 4558 AERARMTPDAVAVVFDEE--KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPE- 4634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 169 aapavidrfkqiepkvliacdavtYAGRRhdrkdvLAelrrslptveHVILHSEAAAPAAADALLSEISATTGAEIDAFE 248
Cdd:PRK12316 4635 ------------------------YPRER------LA----------YMMEDSGAALLLTQSHLLQRLPIPDGLASLALD 4674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 249 PA--WLPF-----------DHPLWIVYSSGTTGLPKPIVHGHGGI---IIVVLALLGLHNDlGCSYHENSF---GERYHW 309
Cdd:PRK12316 4675 RDedWEGFpahdpavrlhpDNLAYVIYTSGSTGRPKGVAVSHGSLvnhLHATGERYELTPD-DRVLQFMSFsfdGSHEGL 4753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 310 YsstgwimwnsqvGGLLSGTTCCIfdgSPGGAKDkPDwtTLWRFVAQSKATFFGAGAAFFANCAKaevDLVAAGDLSQLR 389
Cdd:PRK12316 4754 Y------------HPLINGASVVI---RDDSLWD-PE--RLYAEIHEHRVTVLVFPPVYLQQLAE---HAERDGEPPSLR 4812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 390 --CLGSTGSPLSADTQAWFNNRFAGLSKTNGSKAQADIWWANISGGTDFAGAF---IGGnrelpqtpgamqcRLLGAAVE 464
Cdd:PRK12316 4813 vyCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAympIGT-------------PLGNRSGY 4879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 465 AFDEQGRAV-IGEVGELVCtepmpsmplyfwndkGGARYRASYFET--------YPDNFDGTGrGPVWRHGDWLKVDPDG 535
Cdd:PRK12316 4880 VLDGQLNPLpVGVAGELYL---------------GGEGVARGYLERpaltaerfVPDPFGAPG-GRLYRTGDLARYRADG 4943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 536 SCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLVVDLEYLGRDSYMPLFVVLREGVAFDGAMQAKINKAIEAGLS 615
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALR 5023
|
570 580 590
....*....|....*....|....*....|..
gi 517269147 616 RRF----LPNEIFAVAEIPRTLSGK--KQELP 641
Cdd:PRK12316 5024 ERLpeymVPAHLVFLARMPLTPNGKldRKALP 5055
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
498-646 |
5.06e-03 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 39.62 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 498 GGARYRASYF--ETYPDNFDGTgrgpvWRH-GDWLKVDPDGSCIIYGRSDATINRHGLRMGTSELYSAIEALPEVLDSLV 574
Cdd:cd17630 184 GGASLAMGYLrgQLVPEFNEDG-----WFTtKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFV 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517269147 575 VDL--EYLGRdsyMPLFVVlregVAFDGAMQAKINKAIEAGLSRRFLPNEIFAVAEIPRTLSGKKQELPIKKLL 646
Cdd:cd17630 259 VGVpdEELGQ---RPVAVI----VGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
114-160 |
5.50e-03 |
|
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: 39.64 E-value: 5.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 517269147 114 ELRRKAAALALHLKEKGIKPGDRVAAYLPNIPETIIAFLASASIGAI 160
Cdd:cd05912 6 ELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE 52
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
111-338 |
7.42e-03 |
|
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: 39.34 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 111 SWPELRRKAAALALHLKEKGIKPGDRVAAYLPN-IPETIIAFLA------SASIGAIWSLCAPDMAAPAVIdrFKQIEPK 183
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNsIEHALMALAAmyagvpAAPVSPAYSLMSQDLAKLKHL--FELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 184 VLIACDAVTYAgrrhdrkDVLAELRRSLPTVehviLHSEAAAPAAADALLSEISATT-GAEIDAFEPAWLPfDHPLWIVY 262
Cdd:cd05921 105 LVFAQDAAPFA-------RALAAIFPLGTPL----VVSRNAVAGRGAISFAELAATPpTAAVDAAFAAVGP-DTVAKFLF 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517269147 263 SSGTTGLPKPIVHGHGGIIIVVLALLGLHNDLGcsyHENSfgeryhwySSTGWIMWNSQVGG-------LLSGTTCCIFD 335
Cdd:cd05921 173 TSGSTGLPKAVINTQRMLCANQAMLEQTYPFFG---EEPP--------VLVDWLPWNHTFGGnhnfnlvLYNGGTLYIDD 241
|
...
gi 517269147 336 GSP 338
Cdd:cd05921 242 GKP 244
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
260-294 |
9.79e-03 |
|
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: 39.12 E-value: 9.79e-03
10 20 30
....*....|....*....|....*....|....*
gi 517269147 260 IVYSSGTTGLPKPIVHGHGGIIIVVLALLGLHNDL 294
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEL 127
|
|
| |
