|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-837 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 606.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRID-RVHFENGSVGVDRFYCNRGGFIPEV-KFDPANFGL 78
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDaDAYYDPDPDAPGKTYVRWGGFLDDVdEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 79 LPVAIEGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGN--YAgpgatraieivrtgeqiasilkdLLPHLNE 156
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSndYA-----------------------LLLLADP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 157 EEIDkvkkefqvrkgrfgADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHV 236
Cdd:COG3321 138 EAID--------------AYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 237 GQNAAFWSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:COG3321 204 MLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDAslPKAG---IGTVKSNIGHAMPASGIAGLIK 393
Cdd:COG3321 284 AQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGR--PADQpcaIGSVKSNIGHLEAAAGVAGLIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 394 TSLALYHNVLPPTLHCEQ--PLAQLKETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVLEGYKANNAEQSSVlin 471
Cdd:COG3321 362 AVLALRHGVLPPTLHFETpnPHIDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAA--- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 472 RKTDEVLLIARHSHEAL-------LDALEAK-DKDPGE-----------GKYRIAVFDPTPERIKKAVKIAgknIPWRNK 532
Cdd:COG3321 439 ARPPQLLVLSAKTEEALralaarlAAFLEAHpDLDLADvaytlatgrahFEHRLAVVASSREELAAKLRAL---AAGEAA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 533 QELWYTNEPilsNGGKVAFVFPG--------LDGLAGGE------VHSVAEHFKiTHQESSgsggLLDEALKILEKSSIL 598
Cdd:COG3321 516 PGVVTGAAA---AAPKVAFLFPGqgsqyvgmGRELYETEpvfraaLDECDALLR-PHLGWS----LREVLFPDEEESRLD 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 599 DTA----------------LKKLGVLPDMNAGHSLGEWLAARSSEL----------AEESSVMQllnylnpetfELKDS- 651
Cdd:COG3321 588 RTEvaqpalfaveyalarlWRSWGVRPDAVIGHSVGEYAAACVAGVlsledalrlvAARGRLMQ----------ALPGGg 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 652 RFIAVGCGIDKLQPIIGNIEQLYLSNDNCPQQVILCGTNTALDELVPLLRTKQIFHQILPFQSGFHSPFVADKLDVMLEG 731
Cdd:COG3321 658 AMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAA 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 732 MKDMQFRKTKFPLWSATTLELYPEGfEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSGG-LIGFIDDTLRGKNY 810
Cdd:COG3321 738 LAGVTPRAPRIPLISNVTGTWLTGE-ALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPvLTGLVRQCLAAAGD 816
|
890 900
....*....|....*....|....*...
gi 1273038340 811 S-AVSSNVPIRSGIGQLQRVLAALFIEG 837
Cdd:COG3321 817 AvVLPSLRRGEDELAQLLTALAQLWVAG 844
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-455 |
9.26e-153 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 468.96 E-value: 9.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 4 TDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRIDRVHFENGSVGVDRFYCNRGGFIPEV-KFDPANFGLLPVA 82
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFLDDVdAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 83 IEGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGNYagpgatraieivrtgeqiasilkDLLPHLNEEEIDKv 162
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSS-----------------------DYLELLARDPDEI- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 163 kkefqvrkgrfGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAF 242
Cdd:cd00833 137 -----------DAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 243 WSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAI 322
Cdd:cd00833 206 FVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 323 TQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFG-NDASLPKAGIGTVKSNIGHAMPASGIAGLIKTSLALYHN 401
Cdd:cd00833 286 RRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGgSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHG 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1273038340 402 VLPPTLHCEQPLAQLK--ETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00833 366 VIPPNLHFETPNPKIDfeESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-808 |
5.59e-126 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 434.82 E-value: 5.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADR--IDRVHFENGSVGvDRFYCNRGGFIPEVKFDPANFGL 78
Cdd:TIGR02813 4 LKDMPIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHwaKDDYYDSDKSEA-DKSYCKRGGFLPEVDFNPMEFGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 79 LPVAIEGTEPDHLLTLALVQKALEDAGVFEkNVSLDKTGIIIGKGnyagpGATRAIEIVRTGEQiASILKDLLPH--LNE 156
Cdd:TIGR02813 83 PPNILELTDISQLLSLVVAKEVLNDAGLPD-GYDRDKIGITLGVG-----GGQKQSSSLNARLQ-YPVLKKVFKAsgVED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 157 EEIDKVKKEFQVRKGRFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHV 236
Cdd:TIGR02813 156 EDSEMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 237 GQNAAFWSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:TIGR02813 236 DNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGND-ASLPKAGIGTVKSNIGHAMPASGIAGLIKTS 395
Cdd:TIGR02813 316 GQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 396 LALYHNVLPPTLHCEQPLAQL--KETRFKAIQEARNW--DDSGLPRIAGVNAFGFGGINAHAVLEGYKANNAEQSSVLIn 471
Cdd:TIGR02813 396 LALHHKVLPPTINVDQPNPKLdiENSPFYLNTETRPWmqREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQ- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 472 RKTDEVLLIARHSHEALLDALEAKD-----------------------KDPGEGKYRIAVFDPTPERIKKAVKIAGKNIP 528
Cdd:TIGR02813 475 RAVAQTLLFTAANEKALVSSLKDWKnklsakaddqpyafnalaventlRTIAVALARLGFVAKNADELITMLEQAITQLE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 529 WRNKQE------LWYTNEPILSNGGKVAFVFPGLDGLAGGEVHSVAEHFKITHQE---------SSGSGGLL-------- 585
Cdd:TIGR02813 555 AKSCEEwqlpsgISYRKSALVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAaadmdsvftQAGKGALSpvlypipv 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 586 --DEALKILE---------KSSI--LDTALKKL----GVLPDMNAGHSLGEWLAARSSELAEESSVMQLL----NYLNPE 644
Cdd:TIGR02813 635 fnDESRKAQEealtntqhaQSAIgtLSMGQYKLftqaGFKADMTAGHSFGELSALCAAGVISDDDYMMLAfsrgQAMAAP 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 645 TFELKDSRFIAVGCGIDKLQPIIGN----IEQLYLSNDNCPQQVILCGTNTALDELVPLLrTKQIFHQI-LPFQSGFHSP 719
Cdd:TIGR02813 715 TGEADIGFMYAVILAVVGSPTVIANcikdFEGVSIANYNSPTQLVIAGVSTQIQIAAKAL-KEKGFKAIpLPVSGAFHTP 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 720 FVADKLDVMLEGMKDMQFRKTKFPLWSATTLELYPEGFEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSGG-LI 798
Cdd:TIGR02813 794 LVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNiLQ 873
|
890
....*....|
gi 1273038340 799 GFIDDTLRGK 808
Cdd:TIGR02813 874 KLVENTLKDK 883
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
6-456 |
3.60e-89 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 291.54 E-value: 3.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 6 VAVVGMSCIFPGASDVETFWHNIINKVDstqvvpadridrvhfengsvGVDRFycnrggfipevkfDPANFGLLPVAIEG 85
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLD--------------------DVDLF-------------DAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 86 TEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGkgnyagpgatraieivrtgeqiasilkdllphlneeeidkvkke 165
Cdd:smart00825 48 MDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVG-------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 166 fqvrkgRFGADTAMglipnlvaslvanrlnlggvayTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFWSI 245
Cdd:smart00825 84 ------VSSSDYSV----------------------TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVG 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 246 FTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIkaitqa 325
Cdd:smart00825 136 LSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQL------ 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 326 wenagidlkdigyieahgtgtplgdktevetllqffgndaslpkaGIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPP 405
Cdd:smart00825 210 ---------------------------------------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPP 244
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1273038340 406 TLHCEQ--PLAQLKETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVLE 456
Cdd:smart00825 245 TLHFETpnPHIDLEESPLRVPTELTPWPPPGRPRRAGVSSFGFGGTNAHVILE 297
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-285 |
5.18e-53 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 186.30 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 5 DVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRIDRV-HFENGSVGVDRFYCNRGGFIPEVKFDPANFGLLPVAI 83
Cdd:pfam00109 2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDkLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 84 EGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGNyagpgatraieivrtGEQIASILkdllphLNEEEIDkvk 163
Cdd:pfam00109 82 ERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGI---------------GDYAALLL------LDEDGGP--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 164 kefqvRKGRFGAdtaMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFW 243
Cdd:pfam00109 138 -----RRGSPFA---VGTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1273038340 244 SIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDA 285
Cdd:pfam00109 210 AGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-460 |
1.93e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 184.82 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRidrvhfengsvgVDRFYCNRGGFIPEVKFDP-ANF--G 77
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFP------------VGDLATKIGGQVPDLAEDAeAGFdpD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 78 LLPVAIEGTEPDHLLTLALV--QKALEDAGVFEKNVS-LDKTGIIIGkgnyAGPGATRAI-EIVRTGEQiasilkdllph 153
Cdd:PRK06333 69 RYLDPKDQRKMDRFILFAMAaaKEALAQAGWDPDTLEdRERTATIIG----SGVGGFPAIaEAVRTLDS----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 154 lneeeidkvkkefqvrKG--RFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVA 231
Cdd:PRK06333 134 ----------------RGprRLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 232 GGVHVGQNAAFWSIFTQLGALSKKGKIA------PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDG 305
Cdd:PRK06333 198 GGTEAAIDRVSLAGFAAARALSTRFNDApeqasrPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 306 SGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLpkaGIGTVKSNIGHAMPA 385
Cdd:PRK06333 278 YHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGL---AVSSTKSATGHLLGA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273038340 386 SGIAGLIKTSLALYHNVLPPTLHCEQPLAQLKETRFKAiQEARNWDdsglPRIAGVNAFGFGGINAHAVLEGYKA 460
Cdd:PRK06333 355 AGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVA-NKARPMD----MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| Sfp |
COG2091 |
Phosphopantetheinyl transferase [Coenzyme transport and metabolism]; |
1240-1396 |
2.42e-27 |
|
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
Pssm-ID: 441694 Cd Length: 177 Bit Score: 110.05 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1240 LKRYFNQDEKKHHNSLL-PNKRKEWMISRVAVKDAVRNLLNRTkkeayfPIAFEIRSDEFRKPYPHGDmtdGVHISIAH- 1317
Cdd:COG2091 25 LLALLSEDERARAARFRsEKRRRRFLAGRALLRELLARLLGLP------PADLEFAYDPHGKPYLADP---GLHFSLSHs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1318 KGTDAVGIAQyDRPVGIDIEKIEPRSE-GFSELVFSEEERLLLA---DKDMAEWATRFWVAKEAYGKCLSKGLQGNPKAY 1393
Cdd:COG2091 96 GGLAAVAVSR-GGPVGVDIERIRPRIDlALARRFFSPEERAWLAalpQDDRLEAFTRLWTLKEALLKATGTGLSLPLRAL 174
|
...
gi 1273038340 1394 TIQ 1396
Cdd:COG2091 175 AVE 177
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1331-1386 |
2.91e-11 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 61.86 E-value: 2.91e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273038340 1331 PVGIDIEKI-------EPRSEGFSELVFSEEERLLLA--DKDMAEWATRFWVAKEAYGKCLSKGL 1386
Cdd:pfam01648 1 GVGIDIEEIarirrpiERLGERLAERIFTPEERALLAslPAEARRAFARLWTAKEAVFKALGPGL 65
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1331-1421 |
4.14e-07 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 50.51 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1331 PVGIDIEKIEP------RSEGFSELVFSEEER---LLLADKDMAEWATRFWVAKEAYGKCLSKGLQGNPKAYTIQEIR-- 1399
Cdd:TIGR00556 4 GIGIDIVEIKRiaeqieRSGTFAERFFTPSEIedyCKLSPKSQTESLAGRWAAKEAFIKALGKGISLGELLFTDIEIVkd 83
|
90 100
....*....|....*....|....*
gi 1273038340 1400 ---GEELRindiFIKTIKHKNYIIG 1421
Cdd:TIGR00556 84 lkgAPRVC----LIGEAAKDAEKLG 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-837 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 606.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRID-RVHFENGSVGVDRFYCNRGGFIPEV-KFDPANFGL 78
Cdd:COG3321 1 AADEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDaDAYYDPDPDAPGKTYVRWGGFLDDVdEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 79 LPVAIEGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGN--YAgpgatraieivrtgeqiasilkdLLPHLNE 156
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSndYA-----------------------LLLLADP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 157 EEIDkvkkefqvrkgrfgADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHV 236
Cdd:COG3321 138 EAID--------------AYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 237 GQNAAFWSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:COG3321 204 MLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDAslPKAG---IGTVKSNIGHAMPASGIAGLIK 393
Cdd:COG3321 284 AQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGR--PADQpcaIGSVKSNIGHLEAAAGVAGLIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 394 TSLALYHNVLPPTLHCEQ--PLAQLKETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVLEGYKANNAEQSSVlin 471
Cdd:COG3321 362 AVLALRHGVLPPTLHFETpnPHIDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAA--- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 472 RKTDEVLLIARHSHEAL-------LDALEAK-DKDPGE-----------GKYRIAVFDPTPERIKKAVKIAgknIPWRNK 532
Cdd:COG3321 439 ARPPQLLVLSAKTEEALralaarlAAFLEAHpDLDLADvaytlatgrahFEHRLAVVASSREELAAKLRAL---AAGEAA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 533 QELWYTNEPilsNGGKVAFVFPG--------LDGLAGGE------VHSVAEHFKiTHQESSgsggLLDEALKILEKSSIL 598
Cdd:COG3321 516 PGVVTGAAA---AAPKVAFLFPGqgsqyvgmGRELYETEpvfraaLDECDALLR-PHLGWS----LREVLFPDEEESRLD 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 599 DTA----------------LKKLGVLPDMNAGHSLGEWLAARSSEL----------AEESSVMQllnylnpetfELKDS- 651
Cdd:COG3321 588 RTEvaqpalfaveyalarlWRSWGVRPDAVIGHSVGEYAAACVAGVlsledalrlvAARGRLMQ----------ALPGGg 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 652 RFIAVGCGIDKLQPIIGNIEQLYLSNDNCPQQVILCGTNTALDELVPLLRTKQIFHQILPFQSGFHSPFVADKLDVMLEG 731
Cdd:COG3321 658 AMLAVGLSEEEVEALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAA 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 732 MKDMQFRKTKFPLWSATTLELYPEGfEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSGG-LIGFIDDTLRGKNY 810
Cdd:COG3321 738 LAGVTPRAPRIPLISNVTGTWLTGE-ALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPvLTGLVRQCLAAAGD 816
|
890 900
....*....|....*....|....*...
gi 1273038340 811 S-AVSSNVPIRSGIGQLQRVLAALFIEG 837
Cdd:COG3321 817 AvVLPSLRRGEDELAQLLTALAQLWVAG 844
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-455 |
9.26e-153 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 468.96 E-value: 9.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 4 TDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRIDRVHFENGSVGVDRFYCNRGGFIPEV-KFDPANFGLLPVA 82
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFLDDVdAFDAAFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 83 IEGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGNYagpgatraieivrtgeqiasilkDLLPHLNEEEIDKv 162
Cdd:cd00833 81 AEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSS-----------------------DYLELLARDPDEI- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 163 kkefqvrkgrfGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAF 242
Cdd:cd00833 137 -----------DAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 243 WSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAI 322
Cdd:cd00833 206 FVGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 323 TQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFG-NDASLPKAGIGTVKSNIGHAMPASGIAGLIKTSLALYHN 401
Cdd:cd00833 286 RRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGgSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHG 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1273038340 402 VLPPTLHCEQPLAQLK--ETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00833 366 VIPPNLHFETPNPKIDfeESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-808 |
5.59e-126 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 434.82 E-value: 5.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADR--IDRVHFENGSVGvDRFYCNRGGFIPEVKFDPANFGL 78
Cdd:TIGR02813 4 LKDMPIAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHwaKDDYYDSDKSEA-DKSYCKRGGFLPEVDFNPMEFGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 79 LPVAIEGTEPDHLLTLALVQKALEDAGVFEkNVSLDKTGIIIGKGnyagpGATRAIEIVRTGEQiASILKDLLPH--LNE 156
Cdd:TIGR02813 83 PPNILELTDISQLLSLVVAKEVLNDAGLPD-GYDRDKIGITLGVG-----GGQKQSSSLNARLQ-YPVLKKVFKAsgVED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 157 EEIDKVKKEFQVRKGRFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHV 236
Cdd:TIGR02813 156 EDSEMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 237 GQNAAFWSIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:TIGR02813 236 DNSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGND-ASLPKAGIGTVKSNIGHAMPASGIAGLIKTS 395
Cdd:TIGR02813 316 GQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 396 LALYHNVLPPTLHCEQPLAQL--KETRFKAIQEARNW--DDSGLPRIAGVNAFGFGGINAHAVLEGYKANNAEQSSVLIn 471
Cdd:TIGR02813 396 LALHHKVLPPTINVDQPNPKLdiENSPFYLNTETRPWmqREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQ- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 472 RKTDEVLLIARHSHEALLDALEAKD-----------------------KDPGEGKYRIAVFDPTPERIKKAVKIAGKNIP 528
Cdd:TIGR02813 475 RAVAQTLLFTAANEKALVSSLKDWKnklsakaddqpyafnalaventlRTIAVALARLGFVAKNADELITMLEQAITQLE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 529 WRNKQE------LWYTNEPILSNGGKVAFVFPGLDGLAGGEVHSVAEHFKITHQE---------SSGSGGLL-------- 585
Cdd:TIGR02813 555 AKSCEEwqlpsgISYRKSALVVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAaadmdsvftQAGKGALSpvlypipv 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 586 --DEALKILE---------KSSI--LDTALKKL----GVLPDMNAGHSLGEWLAARSSELAEESSVMQLL----NYLNPE 644
Cdd:TIGR02813 635 fnDESRKAQEealtntqhaQSAIgtLSMGQYKLftqaGFKADMTAGHSFGELSALCAAGVISDDDYMMLAfsrgQAMAAP 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 645 TFELKDSRFIAVGCGIDKLQPIIGN----IEQLYLSNDNCPQQVILCGTNTALDELVPLLrTKQIFHQI-LPFQSGFHSP 719
Cdd:TIGR02813 715 TGEADIGFMYAVILAVVGSPTVIANcikdFEGVSIANYNSPTQLVIAGVSTQIQIAAKAL-KEKGFKAIpLPVSGAFHTP 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 720 FVADKLDVMLEGMKDMQFRKTKFPLWSATTLELYPEGFEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSGG-LI 798
Cdd:TIGR02813 794 LVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNiLQ 873
|
890
....*....|
gi 1273038340 799 GFIDDTLRGK 808
Cdd:TIGR02813 874 KLVENTLKDK 883
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
6-456 |
3.60e-89 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 291.54 E-value: 3.60e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 6 VAVVGMSCIFPGASDVETFWHNIINKVDstqvvpadridrvhfengsvGVDRFycnrggfipevkfDPANFGLLPVAIEG 85
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLD--------------------DVDLF-------------DAAFFGISPREAEA 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 86 TEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGkgnyagpgatraieivrtgeqiasilkdllphlneeeidkvkke 165
Cdd:smart00825 48 MDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVG-------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 166 fqvrkgRFGADTAMglipnlvaslvanrlnlggvayTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFWSI 245
Cdd:smart00825 84 ------VSSSDYSV----------------------TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVG 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 246 FTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIkaitqa 325
Cdd:smart00825 136 LSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQL------ 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 326 wenagidlkdigyieahgtgtplgdktevetllqffgndaslpkaGIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPP 405
Cdd:smart00825 210 ---------------------------------------------LIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPP 244
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1273038340 406 TLHCEQ--PLAQLKETRFKAIQEARNWDDSGLPRIAGVNAFGFGGINAHAVLE 456
Cdd:smart00825 245 TLHFETpnPHIDLEESPLRVPTELTPWPPPGRPRRAGVSSFGFGGTNAHVILE 297
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-451 |
6.27e-78 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 263.88 E-value: 6.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 4 TDVAVVGMSCIFPGASDVETFWHNIINKVdsTQVVPADRIDrvhfengsvgVDRFYCNRGGFIPEvkFDPANFgLLPVAI 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGR--SGIRPITRFD----------ASGLPVRIAGEVKD--FDPEEY-LDRKEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 84 EGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGkgnyAGPGATRAIEivrtgeqiasilkdllphlneEEIDKVK 163
Cdd:COG0304 66 RRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIG----SGIGGLDTLE---------------------EAYRALL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 164 KEfqvRKGRFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFW 243
Cdd:COG0304 121 EK---GPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 244 SIFTQLGALSKKG---KIA--PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQ 318
Cdd:COG0304 198 AGFDALGALSTRNddpEKAsrPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 319 IKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLPKagIGTVKSNIGHAMPASGIAGLIKTSLAL 398
Cdd:COG0304 278 ARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYKVP--VSSTKSMTGHLLGAAGAIEAIASVLAL 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1273038340 399 YHNVLPPTLHCEQPLAqlkETRFKAI-QEARNWDdsglPRIAGVNAFGFGGINA 451
Cdd:COG0304 356 RDGVIPPTINLENPDP---ECDLDYVpNEAREAK----IDYALSNSFGFGGHNA 402
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
6-451 |
8.90e-77 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 260.55 E-value: 8.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 6 VAVVGMSCIFPGASDVETFWHNIINKVdsTQVVPADRIDRvhfengsvgvDRFYCNRGGFIPEvkFDPANFGLLPVAIEG 85
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAGR--SGIRPITRFDA----------SGFPSRIAGEVPD--FDPEDYLDRKELRRM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 86 TePDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGkgnyAGPGATRAIEivrtgeqiasilkDLLPHLNEEEIDKVKkE 165
Cdd:cd00834 69 D-RFAQFALAAAEEALADAGLDPEELDPERIGVVIG----SGIGGLATIE-------------EAYRALLEKGPRRVS-P 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 166 FQVRKgrfgadtamgLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFWSI 245
Cdd:cd00834 130 FFVPM----------ALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 246 FTQLGALSKKGKIA-----PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIK 320
Cdd:cd00834 200 FAALRALSTRNDDPekasrPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAAR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 321 AITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLPKagIGTVKSNIGHAMPASGIAGLIKTSLALYH 400
Cdd:cd00834 280 AMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKVP--VSSTKSMTGHLLGAAGAVEAIATLLALRD 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1273038340 401 NVLPPTLHCEQP--LAQLKETRfkaiQEARNWDDsglpRIAGVNAFGFGGINA 451
Cdd:cd00834 358 GVLPPTINLEEPdpECDLDYVP----NEAREAPI----RYALSNSFGFGGHNA 402
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-285 |
5.18e-53 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 186.30 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 5 DVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRIDRV-HFENGSVGVDRFYCNRGGFIPEVKFDPANFGLLPVAI 83
Cdd:pfam00109 2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDkLYDPPSRIAGKIYTKWGGLDDIFDFDPLFFGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 84 EGTEPDHLLTLALVQKALEDAGVFEKNVSLDKTGIIIGKGNyagpgatraieivrtGEQIASILkdllphLNEEEIDkvk 163
Cdd:pfam00109 82 ERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGI---------------GDYAALLL------LDEDGGP--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 164 kefqvRKGRFGAdtaMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFW 243
Cdd:pfam00109 138 -----RRGSPFA---VGTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGF 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1273038340 244 SIFTQLGALSKKGKIAPFDEGADGLLIGEGCGFVVLKRLEDA 285
Cdd:pfam00109 210 AGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-460 |
1.93e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 184.82 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVDSTQVVPADRidrvhfengsvgVDRFYCNRGGFIPEVKFDP-ANF--G 77
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFP------------VGDLATKIGGQVPDLAEDAeAGFdpD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 78 LLPVAIEGTEPDHLLTLALV--QKALEDAGVFEKNVS-LDKTGIIIGkgnyAGPGATRAI-EIVRTGEQiasilkdllph 153
Cdd:PRK06333 69 RYLDPKDQRKMDRFILFAMAaaKEALAQAGWDPDTLEdRERTATIIG----SGVGGFPAIaEAVRTLDS----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 154 lneeeidkvkkefqvrKG--RFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVA 231
Cdd:PRK06333 134 ----------------RGprRLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVC 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 232 GGVHVGQNAAFWSIFTQLGALSKKGKIA------PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDG 305
Cdd:PRK06333 198 GGTEAAIDRVSLAGFAAARALSTRFNDApeqasrPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 306 SGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLpkaGIGTVKSNIGHAMPA 385
Cdd:PRK06333 278 YHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSGL---AVSSTKSATGHLLGA 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273038340 386 SGIAGLIKTSLALYHNVLPPTLHCEQPLAQLKETRFKAiQEARNWDdsglPRIAGVNAFGFGGINAHAVLEGYKA 460
Cdd:PRK06333 355 AGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVA-NKARPMD----MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
186-455 |
2.27e-50 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 181.68 E-value: 2.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 186 VASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVgqNAAFWSIFTQLG--ALSKKGKIAPFDE 263
Cdd:cd00825 75 ASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEE--LAAPMDCEFDAMgaLSTPEKASRTFDA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 264 GADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHG 343
Cdd:cd00825 153 AADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 344 TGTPLGDKTEVETLLQFFGnDASLPkagIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCEQPLAQLKETRFKA 423
Cdd:cd00825 233 TGTPIGDVKELKLLRSEFG-DKSPA---VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTET 308
|
250 260 270
....*....|....*....|....*....|..
gi 1273038340 424 IQEArnwddsglPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00825 309 TPRE--------LRTALLNGFGLGGTNATLVL 332
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
20-451 |
7.47e-50 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 182.97 E-value: 7.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 20 DVETFWHNIINK---VDSTQVVPADRIDRV-HFENGSVGVDRFYCNRGGFIPEVKFDPANFgllpvAIEGTEPDHL-LTL 94
Cdd:PTZ00050 8 GAESTWEALIAGksgIRKLTEFPKFLPDCIpEQKALENLVAAMPCQIAAEVDQSEFDPSDF-----APTKRESRAThFAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 95 ALVQKALEDAGVFEKNVSL-DKTGIIIGKGNyagPGATRAIEIVRTgeqiasilkdllphLNEEEIDKVKKEFQVRkgrf 173
Cdd:PTZ00050 83 AAAREALADAKLDILSEKDqERIGVNIGSGI---GSLADLTDEMKT--------------LYEKGHSRVSPYFIPK---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 174 gadtamgLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFWSIFTQLGALS 253
Cdd:PTZ00050 142 -------ILGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALC 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 254 KK----GKIA--PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAITQAWE 327
Cdd:PTZ00050 215 TKynddPQRAsrPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 328 NAG-IDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASlPKAGIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPT 406
Cdd:PTZ00050 295 DGAnININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGA-PKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPT 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1273038340 407 LHCEQPL--AQLKETRFKAIQEARNWDdsglprIAGVNAFGFGGINA 451
Cdd:PTZ00050 374 INLENPDaeCDLNLVQGKTAHPLQSID------AVLSTSFGFGGVNT 414
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
91-455 |
2.84e-48 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 178.02 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 91 LLTLALVQKALEDAGV-FEKNVSLDKTGIIIGKGnYAGPGATRaieivrtgeqiaSILKDLLPHLNEEEIDKvkkefqvr 169
Cdd:cd00828 74 LLALVATEEALADAGItDPYEVHPSEVGVVVGSG-MGGLRFLR------------RGGKLDARAVNPYVSPK-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 170 kgrfgadtaMGLIPNLVASLVANRLNLG-GVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVH-VGQNAAFWsiFT 247
Cdd:cd00828 133 ---------WMLSPNTVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEdPLEEGLSG--FA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 248 QLGALSKKGK-----IAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPsVKGQIKAI 322
Cdd:cd00828 202 NMGALSTAEEepeemSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 323 TQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGN-DASLPkagIGTVKSNIGHAMPASGIAGLIKTSLALYHN 401
Cdd:cd00828 281 RTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGAlGAPLP---VTAQKALFGHSKGAAGALQLIGALQSLEHG 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1273038340 402 VLPPTLHCEQPLAQLKETRFkaIQEARnwDDSGLPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00828 358 LIPPTANLDDVDPDVEHLSV--VGLSR--DLNLKVRAALVNAFGFGGSNAALVL 407
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
293-410 |
1.07e-46 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 163.12 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 293 YSVLKGIGVSSDGSGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLPKAGI 372
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1273038340 373 GTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCE 410
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
6-459 |
1.41e-46 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 173.44 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 6 VAVVGMSCIFPGASDVETFWHNIINKVDStqvvpADRIDrvHFEngsvgVDRFYCNRGGfipEVK-FDPANFgllpvaIE 84
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVESTWKNLLAGKSG-----IGPIT--HFD-----TSDLAVKIAG---EVKdFNPDDY------MS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 85 GTEPDH-----LLTLALVQKALEDAGVFEKNVSLDKTGIIIGkgnyAGPGATRAIEivrtgEQIASilkdllphLNEEEI 159
Cdd:PRK07314 63 RKEARRmdrfiQYGIAAAKQAVEDAGLEITEENADRIGVIIG----SGIGGLETIE-----EQHIT--------LLEKGP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 160 DKVKKEFqvrkgrfgadtAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQN 239
Cdd:PRK07314 126 RRVSPFF-----------VPMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAIT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 240 AAFWSIFTQLGALSKKG---KIA--PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPS 314
Cdd:PRK07314 195 PLGIAGFAAARALSTRNddpERAsrPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 315 VKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASlpKAGIGTVKSNIGHAMPASGIAGLIKT 394
Cdd:PRK07314 275 GEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAY--KVAVSSTKSMTGHLLGAAGAVEAIFS 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1273038340 395 SLALYHNVLPPTLHCEQPLAQLK------ETRFKAIQEARNwddsglpriagvNAFGFGGINAHAVLEGYK 459
Cdd:PRK07314 353 VLAIRDQVIPPTINLDNPDEECDldyvpnEARERKIDYALS------------NSFGFGGTNASLVFKRYE 411
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
189-456 |
1.06e-40 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 155.96 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 189 LVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNR--CNMVVAGGVHVGqnaaFWSI--FTQLGALSKKGKIA----- 259
Cdd:PRK07103 149 LCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSvdACIAVGALMDLS----YWECqaLRSLGAMGSDRFADepeaa 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 260 --PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGsgTSVMSPSVKGQIKAITQAWENAGIDLKDIG 337
Cdd:PRK07103 225 crPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA--NRGPDPSLEGEMRVIRAALRRAGLGPEDID 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 338 YIEAHGTGTPLGDKTEVETLlqfFGndASLPKAGIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCEQPL-AQL 416
Cdd:PRK07103 303 YVNPHGTGSPLGDETELAAL---FA--SGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIdERF 377
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1273038340 417 KETRFKAIQeARNwddsglpRIAGVNAFGFGGINAHAVLE 456
Cdd:PRK07103 378 RWVGSTAES-ARI-------RYALSLSFGFGGINTALVLE 409
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
79-455 |
2.35e-40 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 154.05 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 79 LPVAIEGTEPDHL--LTLALVQKALEDAGVfekNVSLDKTGIIIGkgnyagpgATRAIEivRTGEQIASilKDLLPHLNE 156
Cdd:PRK05952 44 LPLGLIGNQPSSLedLTKTVVTAALKDAGL---TPPLTDCGVVIG--------SSRGCQ--GQWEKLAR--QMYQGDDSP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 157 EEIDKVKKEFQVrkgrfgadtamglIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHV 236
Cdd:PRK05952 109 DEELDLENWLDT-------------LPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 237 GQNAAFWSIFTQLGALSKKGkIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:PRK05952 176 PITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGndaslPKAGIGTVKSNIGHAMPASGIAGLIKTSL 396
Cdd:PRK05952 255 SAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFP-----HRVAVSSTKGATGHTLGASGALGVAFSLL 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1273038340 397 ALYHNVLPPTLHCEQPLAQLketrfKAIQEARNwddSGLPRIAGVnAFGFGGINAHAVL 455
Cdd:PRK05952 330 ALRHQQLPPCVGLQEPEFDL-----NFVRQAQQ---SPLQNVLCL-SFGFGGQNAAIAL 379
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
6-455 |
5.81e-40 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 154.56 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 6 VAVVGMSCIFPGASDVETFWHNIIN-KVDSTQVVPADRIDRVHFENGSVGV-DRFYCNRGGFIPEVKFDPANFGLLPVAI 83
Cdd:PLN02836 8 VVVTGLGLVTPLGCGVETTWRRLIAgECGVRALTQDDLKMKSEDEETQLYTlDQLPSRVAALVPRGTGPGDFDEELWLNS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 84 EGTEPDHLLTLALVQKALEDAG-VFEKNVSLDKTGIIIGkgnyAGPGATRaiEIVRTGEQIasilkdllphlNEEEIDKV 162
Cdd:PLN02836 88 RSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIG----GGIGSIT--DILEAAQLI-----------CEKRLRRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 163 KKEFQVRkgrfgadtamgLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAF 242
Cdd:PLN02836 151 SPFFVPR-----------ILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 243 WSIFTQLGALSKKGKIAP------FDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVK 316
Cdd:PLN02836 220 IAGFSRSRALSTKFNSCPteasrpFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 317 GQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLPKAGIGTVKSNIGHAMPASGIAGLIKTSL 396
Cdd:PLN02836 300 GAVLAMTRALQQSGLHPNQVDYVNAHATSTPLGDAVEARAIKTVFSEHATSGGLAFSSTKGATGHLLGAAGAVEAIFSVL 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 397 ALYHNVLPPTLHCEQPLAQLKeTRFKAIQEARNwddsgLPRIAGV-NAFGFGGINAHAVL 455
Cdd:PLN02836 380 AIHHGIAPPTLNLERPDPIFD-DGFVPLTASKA-----MLIRAALsNSFGFGGTNASLLF 433
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
98-460 |
1.09e-36 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 144.04 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 98 QKALEDAGVFEKNVSLDKTGIIIGkgnyAGPGATR----AIEIVRTGEQIASIlkdllphlneeeidkvkkefqvrkGRF 173
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGLIAG----SGGGSTRnqveAADAMRGPRGPKRV------------------------GPY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 174 GADTAMGlipNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGvhvGQNAAfWSI---FTQLG 250
Cdd:PRK07967 132 AVTKAMA---STVSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGG---GEELD-WEMsclFDAMG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 251 ALSKKGKIAP------FDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSgtSVMSPSVKGQIKAITQ 324
Cdd:PRK07967 205 ALSTKYNDTPekasraYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGY--DMVAPSGEGAVRCMQM 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 325 AWenAGIDLKdIGYIEAHGTGTPLGDKTEVETLLQFFGNDAslPKagIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLP 404
Cdd:PRK07967 283 AL--ATVDTP-IDYINTHGTSTPVGDVKELGAIREVFGDKS--PA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIA 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1273038340 405 PTLHCEQ--PLAQ----LKETRfkaiqearnwDDSGLPRIAGvNAFGFGGINAHAVLEGYKA 460
Cdd:PRK07967 356 PSANIEEldPQAAgmpiVTETT----------DNAELTTVMS-NSFGFGGTNATLVFRRYKG 406
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
173-455 |
4.70e-33 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 129.10 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 173 FGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVgqnaafwsiftqlgal 252
Cdd:cd00327 34 VGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 253 skkgkiapfdegadgLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMsPSVKGQIKAITQAWENAGID 332
Cdd:cd00327 98 ---------------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPA-VSGEGLARAARKALEGAGLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 333 LKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLPKAGigtvKSNIGHAMPASGIAGLIKTSLALYHNVLPPTlhceqp 412
Cdd:cd00327 162 PSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSPAVSAT----LIMTGHPLGAAGLAILDELLLMLEHEFIPPT------ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1273038340 413 laqlketrfkaiqearnwdDSGlPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00327 232 -------------------PRE-PRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
186-451 |
8.83e-33 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 132.27 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 186 VASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHvgqnaafwSI-------FTQLGALSKkGKI 258
Cdd:PRK09185 139 LADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVD--------SLcrltlngFNSLESLSP-QPC 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 259 APFDEGADGLLIGEGCGFVVLKRLEDAIVdgdriysVLKGIGVSSDGSGTSVMSPSVKGQIKAITQAWENAGIDLKDIGY 338
Cdd:PRK09185 210 RPFSANRDGINIGEAAAFFLLEREDDAAV-------ALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGY 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 339 IEAHGTGTPLGDKTEVETLLQFFGNdaSLPKAGigtVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCEQPLAQLKE 418
Cdd:PRK09185 283 INLHGTATPLNDAMESRAVAAVFGD--GVPCSS---TKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPP 357
|
250 260 270
....*....|....*....|....*....|...
gi 1273038340 419 TRFKAIQEARNwddsglPRIAGVNAFGFGGINA 451
Cdd:PRK09185 358 LYLVENAQALA------IRYVLSNSFAFGGNNC 384
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
120-460 |
2.67e-31 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 128.59 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 120 IGKGNYAGP--GATRAIEI---------VRTGEQIASILKDLLPHLNEEEIDKVKKEFQvrkgrFGAdtamglipnlVAS 188
Cdd:PRK06501 92 IGKGDFPGPlfLAAPPVELewparfalaAAVGDNDAPSYDRLLRAARGGRFDALHERFQ-----FGS----------IAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 189 LVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVHVGQNAAFWSIFTQLGALSKKGKIA-----PFDE 263
Cdd:PRK06501 157 RLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPekaskPFSK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 264 GADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHG 343
Cdd:PRK06501 237 DRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 344 TGTPLGDKTEVETLLQFFGND-ASLPkagIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCEQPLAqlketrfk 422
Cdd:PRK06501 317 TSTPENDKMEYLGLSAVFGERlASIP---VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDP-------- 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1273038340 423 AI------QEARNwddsglPRIAGV--NAFGFGGINAHAVLEGYKA 460
Cdd:PRK06501 386 AIpldvvpNVARD------ARVTAVlsNSFGFGGQNASLVLTAEPA 425
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-450 |
2.00e-30 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 125.89 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINkvDSTQVVPADRIDRVHFENGSVGVDRfycnrgGFIPEVKFDPANFGLLP 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLA--GQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 81 VAIEgtepdhlLTLALVQKALEDAG--VFEKNVSldKTGIIIGKGnyagpgaTRAIEIVRTGEQIasilkdllphLNEEE 158
Cdd:PRK08722 73 LFIQ-------YGIAAGIQALDDSGleVTEENAH--RIGVAIGSG-------IGGLGLIEAGHQA----------LVEKG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 159 IDKVKKEFqvrkgrfgadtamglIPNLVASLVANRLN----LGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGV 234
Cdd:PRK08722 127 PRKVSPFF---------------VPSTIVNMIAGNLSimrgLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 235 HVGQNAAFWSIFTQLGALSKKGK-----IAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTS 309
Cdd:PRK08722 192 EKASTPLGMAGFGAAKALSTRNDepqkaSRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 310 VMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASlPKAGIGTVKSNIGHAMPASGIA 389
Cdd:PRK08722 272 SPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGS-KQVLVSSTKSMTGHLLGAAGSV 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1273038340 390 GLIKTSLALYHNVLPPTLHCEQPLAQLKETRFKaiQEARNWDDSglpRIAGVNAFGFGGIN 450
Cdd:PRK08722 351 EAIITVMSLVDQIVPPTINLDDPEEGLDIDLVP--HTARKVESM---EYAICNSFGFGGTN 406
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
50-450 |
4.09e-30 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 124.85 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 50 NGSVGVDRFYCnrggfipevkFDPANFgllPVAIEG----------------TEPDHLLTLAL--VQKALEDAGVFEKNV 111
Cdd:PRK08439 28 NGECGIKKITL----------FDASDF---PVQIAGeitdfdptevmdpkevKKADRFIQLGLkaAREAMKDAGFLPEEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 112 SLDKTGIIIGkgnyAGPGATRAIEIvrtgeqiASILkdllphLNEEEIDKVKKEFqvrkgrfgadtamglIP----NLVA 187
Cdd:PRK08439 95 DAERFGVSSA----SGIGGLPNIEK-------NSII------CFEKGPRKISPFF---------------IPsalvNMLG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 188 SLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRC-NMVVaggvhVGQNAAFWSI----FTQLGALSKKG---KIA 259
Cdd:PRK08439 143 GFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGAdKMLV-----VGAESAICPVgiggFAAMKALSTRNddpKKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 260 --PFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSgtSVMSPSVKGQIKAITQAWENAGIDlkDIG 337
Cdd:PRK08439 218 srPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDAN--HITSPAPEGPLRAMKAALEMAGNP--KID 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 338 YIEAHGTGTPLGDKTEVETLLQFFGNDASLPKagIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLPPTLHCEQPLaqlK 417
Cdd:PRK08439 294 YINAHGTSTPYNDKNETAALKELFGSKEKVPP--VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPD---P 368
|
410 420 430
....*....|....*....|....*....|....
gi 1273038340 418 ETRFKAI-QEARNWDdsglPRIAGVNAFGFGGIN 450
Cdd:PRK08439 369 ECDLDYIpNVARKAE----LNVVMSNSFGFGGTN 398
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-450 |
2.15e-29 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 122.92 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 5 DVAVVGMSCIFPGASDVETFWHNIINkvdstqvvpadridrvhfenGSVGVDRFycnRGGFIPEvkFDpanfglLPVAIE 84
Cdd:PRK07910 13 NVVVTGIAMTTALATDAETTWKLLLD--------------------GQSGIRTL---DDPFVEE--FD------LPVRIG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 85 G---TEPDHLLT------LALVQK--------ALEDAGVFEknVSLDKTGIIIGkgnyAGPGATRAieivrtgeqiasiL 147
Cdd:PRK07910 62 GhllEEFDHQLTrvelrrMSYLQRmstvlgrrVWENAGSPE--VDTNRLMVSIG----TGLGSAEE-------------L 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 148 KDLLPHLNEEEIDKVKKeFQVRKgrfgadtamgLIPNLVASLVA-NRLNLGGVAyTLDAACASSLIAIDHAVQELNSNRC 226
Cdd:PRK07910 123 VFAYDDMRARGLRAVSP-LAVQM----------YMPNGPAAAVGlERHAKAGVI-TPVSACASGSEAIAQAWRQIVLGEA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 227 NMVVAGGVHVGQNAAFWSIFTQLGA-LSKK-----GKIAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIG 300
Cdd:PRK07910 191 DIAICGGVETRIEAVPIAGFAQMRIvMSTNnddpaGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGAS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 301 VSSDGSGTSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDaslpKAGIGTVKSNIG 380
Cdd:PRK07910 271 ITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGH----RPAVYAPKSALG 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1273038340 381 HAMPASGIAGLIKTSLALYHNVLPPTLHCEQPLAQL------KETRFKAIQEARNwddsglpriagvNAFGFGGIN 450
Cdd:PRK07910 347 HSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIdldvvaGEPRPGNYRYAIN------------NSFGFGGHN 410
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-459 |
9.18e-29 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 122.78 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1 MKKTDVAVVGMSCIFPGASDVETFWHNIINKVdsTQVVPADRIDRVHFENGSVGVDRFYCNRGGFIPEVKFDPANFGLlp 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGV--SGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFML-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 81 vaiegtepdHLLTLAlvQKALEDAGVFEKNVS-LDKT--GIIIGKGNYAGPGATRAIEIVRtgeqiasilkdllphLNEE 157
Cdd:PLN02787 202 ---------YLLTAG--KKALADGGITEDVMKeLDKTkcGVLIGSAMGGMKVFNDAIEALR---------------ISYR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 158 EIDKVKKEFqvrkgrfgADTAMGlipnlvASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGvhvg 237
Cdd:PLN02787 256 KMNPFCVPF--------ATTNMG------SAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGG---- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 238 QNAAFWSI----FTQLGALSKKGK-----IAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGT 308
Cdd:PLN02787 318 SDAAIIPIglggFVACRALSQRNDdptkaSRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHM 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 309 SVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDaslPKAGIGTVKSNIGHAMPASGI 388
Cdd:PLN02787 398 TEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQN---PELRVNSTKSMIGHLLGAAGA 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1273038340 389 AGLIKTSLALYHNVLPPTLHCEQPlAQLKETRFKAIQEARNWDdsglPRIAGVNAFGFGGINAHAVLEGYK 459
Cdd:PLN02787 475 VEAIATVQAIRTGWVHPNINLENP-ESGVDTKVLVGPKKERLD----IKVALSNSFGFGGHNSSILFAPYK 540
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
195-450 |
1.51e-27 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 117.01 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 195 NLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGVH--VGQNAAfwsIFTQLGALSKKGKI-----APFDEGADG 267
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEelCPTEAA---VFDTLFATSTRNDApeltpRPFDANRDG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 268 LLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSgtSVMSPSVKGQIKAITQAWENAGIDLKDIGYIEAHGTGTP 347
Cdd:PRK09116 229 LVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGA--HVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 348 LGDKTEVETLLQFFGNdaSLPkagIGTVKSNIGHAMpasGIAGLIKTSLAL---YHNVLPPTLHCEQPLAQLKETRFkAI 424
Cdd:PRK09116 307 RGDIAESQATAAVFGA--RMP---ISSLKSYFGHTL---GACGALEAWMSIemmNEGWFAPTLNLTQVDPACGALDY-IM 377
|
250 260
....*....|....*....|....*.
gi 1273038340 425 QEARNWDdsglPRIAGVNAFGFGGIN 450
Cdd:PRK09116 378 GEAREID----TEYVMSNNFAFGGIN 399
|
|
| Sfp |
COG2091 |
Phosphopantetheinyl transferase [Coenzyme transport and metabolism]; |
1240-1396 |
2.42e-27 |
|
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
Pssm-ID: 441694 Cd Length: 177 Bit Score: 110.05 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1240 LKRYFNQDEKKHHNSLL-PNKRKEWMISRVAVKDAVRNLLNRTkkeayfPIAFEIRSDEFRKPYPHGDmtdGVHISIAH- 1317
Cdd:COG2091 25 LLALLSEDERARAARFRsEKRRRRFLAGRALLRELLARLLGLP------PADLEFAYDPHGKPYLADP---GLHFSLSHs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1318 KGTDAVGIAQyDRPVGIDIEKIEPRSE-GFSELVFSEEERLLLA---DKDMAEWATRFWVAKEAYGKCLSKGLQGNPKAY 1393
Cdd:COG2091 96 GGLAAVAVSR-GGPVGVDIERIRPRIDlALARRFFSPEERAWLAalpQDDRLEAFTRLWTLKEALLKATGTGLSLPLRAL 174
|
...
gi 1273038340 1394 TIQ 1396
Cdd:COG2091 175 AVE 177
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
172-456 |
2.62e-27 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 114.83 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 172 RFGADTAMGLIPNLVASLVANRLNLGGVAYTLDAACASSLIAIDHAVQELNSNRCNMVVAGG-------VHVGQNAAFWS 244
Cdd:PRK14691 56 RLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGaeavidtVSLAGFAAARA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 245 IFTQLGALSKKGKiAPFDEGADGLLIGEGCGFVVLKRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPSVKGQIKAITQ 324
Cdd:PRK14691 136 LSTHFNSTPEKAS-RPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 325 AWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQFFGNDASLpkaGIGTVKSNIGHAMPASGIAGLIKTSLALYHNVLP 404
Cdd:PRK14691 215 ALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNAL---AITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1273038340 405 PTLHCEQPLAQLKETRFKAiQEARNWDDSglprIAGVNAFGFGGINAHAVLE 456
Cdd:PRK14691 292 ATLNLENPDPAAKGLNIIA-GNAQPHDMT----YALSNGFGFAGVNASILLK 338
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
547-815 |
4.16e-24 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 104.44 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 547 GKVAFVFPG--------LDGLAggEVHSVAEH----------FKITH--QESSgsggllDEALK--------ILEKSSIL 598
Cdd:COG0331 1 MKLAFLFPGqgsqyvgmGKDLY--ENFPVAREvfeeasealgYDLSAlcFEGP------EEELNltentqpaILAASVAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 599 DTALKKLGVLPDMNAGHSLGEWLAARSSE-LAEESSV---------MQllnylnpETFELKDSRFIAV-GCGIDKLQPII 667
Cdd:COG0331 73 YRALEEEGIRPDAVAGHSLGEYSALVAAGaLSFEDALrlvrlrgrlMQ-------EAVPAGPGGMAAVlGLDDEEVEALC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 668 ---GNIEQLYLSNDNCPQQVILCGTNTALDELVPLLRTKQIfHQILPFQ-SG-FHSPFVADKLDVMLEGMKDMQFRKTKF 742
Cdd:COG0331 146 aeaAQGEVVEIANYNSPGQIVISGEKEAVEAAAELAKEAGA-KRAVPLPvSGpFHTPLMAPAAEKLAEALAAVTFADPKI 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1273038340 743 PLWSATTLELYPEGfEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSGG-LIGFIDDTLRGKNYSAVSS 815
Cdd:COG0331 225 PVVSNVDAAPVTDP-EEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKvLSGLVKRIDPGVEVLAVED 297
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
548-805 |
9.48e-17 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 82.52 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 548 KVAFVFPGLDGLAGGEVHSVAEHFKITHQessgsggLLDEALKILEKS----------------------------SILD 599
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKE-------LFDQASEALGYDlkklcqegpaeelnktqytqpalyvvsaILYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 600 TALKKLGVLPDMNAGHSLGEWLAARSSELAEESSVMQLLNylnpetfelKDSRFI--AVGCGIDKLQPIIG-NIEQL--- 673
Cdd:TIGR00128 75 KLKEQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVK---------KRGELMqeAVPEGGGAMAAVIGlDEEQLaqa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 674 ---------YLSNDNCPQQVILCGTNTALDELVPLLRTKQIFHQI-LPFQSGFHSPFV---ADKLDVMLEGmkdMQFRKT 740
Cdd:TIGR00128 146 ceeatendvDLANFNSPGQVVISGTKDGVEAAAALFKEMGAKRAVpLEVSGAFHSRFMkpaAEKFAETLEA---CQFNDP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1273038340 741 KFPLWSATTLELYPEGfEAIRALSVEHLIKPVRFRELTERLYNEGARVFVQIGSG----GLIGFIDDTL 805
Cdd:TIGR00128 223 TVPVISNVDAKPYTNG-DRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGkvltGLIKRIKNDL 290
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
208-455 |
4.95e-15 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 78.94 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 208 ASSLIAIDHAVQELNSNRCnMVVAGGVhvgqNAAF--WSIFTQL--GALSKKGKIA----PFDEGADGLLIGEGCGFVVL 279
Cdd:cd00832 162 AGGLDALAQARRLVRRGTP-LVVSGGV----DSALcpWGWVAQLssGRLSTSDDPAraylPFDAAAAGYVPGEGGAILVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 280 KRLEDAIVDGDRIYSVLKGIGVSSDGSGTSVMSPsvkGQIKAITQAWENAGIDLKDIGYIEAHGTGTPLGDKTEVETLLQ 359
Cdd:cd00832 237 EDAAAARERGARVYGEIAGYAATFDPPPGSGRPP---GLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAA 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 360 FFGNDA---SLPKAGIGTVKSNighAMPASGIAGLiktsLALYHNVLPPTLHCEQP---------LAQLKETRfkaiqea 427
Cdd:cd00832 314 VFGPRGvpvTAPKTMTGRLYAG---GAPLDVATAL----LALRDGVIPPTVNVTDVppaygldlvTGRPRPAA------- 379
|
250 260
....*....|....*....|....*...
gi 1273038340 428 rnwddsglPRIAGVNAFGFGGINAHAVL 455
Cdd:cd00832 380 --------LRTALVLARGRGGFNSALVV 399
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
571-792 |
1.35e-14 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 76.36 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 571 FKITHQESSGSGGLLDE------ALKILEKSSILDtaLKKLGVLPDMNAGHSLGEWLAARS-SELAEESSVMQLLNYlNP 643
Cdd:pfam00698 42 FSVSDVLRNNPEGTLDGtqfvqpALFAMQIALAAL--LQSYGVRPDAVVGHSLGEYAAAVVaGALSPEEALLAAVLR-SR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 644 ETFELKDSRFIAvGCGIDKLQPIIGNIEQLYLSNDNCPQQVILCGTNTALDELVPLLRTKQIFHQILPFQSGFHSPFVAD 723
Cdd:pfam00698 119 LMMQLAGPGGMA-AVELSAEEVEQRWPDDVVGAVVNSPRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1273038340 724 KLDVMLEGMKDMQFRKTKFPLWSATTLE--LYPEGFEAIralSVEHLIKPVRFRELTERLYNEGARVFVQI 792
Cdd:pfam00698 198 IAPALLSALADIAPRTPRVPFISSTSIDpsDQRTLSAEY---WVRNLRSPVRFAEAILSAAEPGPLVFIEI 265
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1331-1386 |
2.91e-11 |
|
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pfam00550. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: The ACPS type and the Sfp type. The structure of the Sfp type is known, which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Pssm-ID: 426364 [Multi-domain] Cd Length: 111 Bit Score: 61.86 E-value: 2.91e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273038340 1331 PVGIDIEKI-------EPRSEGFSELVFSEEERLLLA--DKDMAEWATRFWVAKEAYGKCLSKGL 1386
Cdd:pfam01648 1 GVGIDIEEIarirrpiERLGERLAERIFTPEERALLAslPAEARRAFARLWTAKEAVFKALGPGL 65
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
416-499 |
2.18e-09 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 56.40 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 416 LKETRFKAIQEARNWDDsglpRIAGVNAFGFGGINAHAVLEGY---KANNAEQSS----VLINRKTDEVLliarhshEAL 488
Cdd:pfam16197 8 LLDGRLKVVTEPTPWPG----GIVGVNSFGFGGANAHVILKSNpkpKIPPESPDNlprlVLLSGRTEEAV-------KAL 76
|
90
....*....|.
gi 1273038340 489 LDALEAKDKDP 499
Cdd:pfam16197 77 LEKLENHLDDA 87
|
|
| EntD |
COG2977 |
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ... |
1290-1383 |
1.21e-07 |
|
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442216 [Multi-domain] Cd Length: 205 Bit Score: 53.77 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1290 AFEIRSDEFRKP-YPhgdmtDGVHISIAHKGTDA---VGIAQYDRPVGIDIEKI--EPRSEGFSELVFSEEERLLLAD-- 1361
Cdd:COG2977 49 PAPILIGEDRAPlWP-----AGVVGSISHSDGYAaavVAPASDVRGLGIDIEPLldEPLAEELLPSILTPAERALLAAls 123
|
90 100
....*....|....*....|...
gi 1273038340 1362 -KDMAEWATRFWVAKEAYGKCLS 1383
Cdd:COG2977 124 pLPFAHALTLLFSAKESLYKALY 146
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1331-1421 |
4.14e-07 |
|
phosphopantetheine--protein transferase domain; This model models a domain active in transferring the phophopantetheine prosthetic group to its attachment site on enzymes and carrier proteins. Many members of this family are small proteins that act on the acyl carrier protein involved in fatty acid biosynthesis. Some members are domains of larger proteins involved specialized pathways for the synthesis of unusual molecules including polyketides, atypical fatty acids, and antibiotics. [Protein fate, Protein modification and repair]
Pssm-ID: 273136 [Multi-domain] Cd Length: 128 Bit Score: 50.51 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273038340 1331 PVGIDIEKIEP------RSEGFSELVFSEEER---LLLADKDMAEWATRFWVAKEAYGKCLSKGLQGNPKAYTIQEIR-- 1399
Cdd:TIGR00556 4 GIGIDIVEIKRiaeqieRSGTFAERFFTPSEIedyCKLSPKSQTESLAGRWAAKEAFIKALGKGISLGELLFTDIEIVkd 83
|
90 100
....*....|....*....|....*
gi 1273038340 1400 ---GEELRindiFIKTIKHKNYIIG 1421
Cdd:TIGR00556 84 lkgAPRVC----LIGEAAKDAEKLG 104
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1332-1386 |
1.06e-03 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 40.50 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1273038340 1332 VGIDIEKIEpR--------SEGFSELVFSEEER-LLLADKDMAE-WATRFwVAKEAYGKCLSKGL 1386
Cdd:COG0736 2 IGIDIVEIA-RieralerhGERFLERVFTPAERaYCQSRKRPAEfLAGRF-AAKEAVSKALGTGI 64
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
200-234 |
4.14e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 41.21 E-value: 4.14e-03
10 20 30
....*....|....*....|....*....|....*
gi 1273038340 200 AYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGV 234
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGV 115
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
200-234 |
4.34e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 41.31 E-value: 4.34e-03
10 20 30
....*....|....*....|....*....|....*
gi 1273038340 200 AYTLDAACASSLIAIDHAVQELNSNRCNMVVAGGV 234
Cdd:cd00751 77 ATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
|
|
| |
