|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
12-1388 |
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: 596.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVD--AEVDVAGFGVMPNSV 88
Cdd:COG3321 6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDAdAYYDPDPDAPGKTYVRWGGFLDdvDEFDALFFGISPREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 89 PGTEPDQLIALHVAAASLADAGgeaVLPA--DRERVGVILGrGGYLTPGLVRLDQRvrtanqvvktlrevvpdldderve 166
Cdd:COG3321 86 EAMDPQQRLLLEVAWEALEDAG---YDPEslAGSRTGVFVG-ASSNDYALLLLADP------------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 167 avraafveqlGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDI 246
Cdd:COG3321 138 ----------EAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 247 TLWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQAR 326
Cdd:COG3321 208 ESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 327 AVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA----ALGSVKSMIGHAMPAAGIAGLIKAAL 402
Cdd:COG3321 288 VIRRALADAGVDPAT---VDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpcAIGSVKSNIGHLEAAAGVAGLIKAVL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 403 ALHHRVLPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVLTE---PAPARVEVVEPV 477
Cdd:COG3321 365 ALRHGVLPPTLHFETPNPHIdfENSPFYVNTELRPW--PAGGGPRRAGVSSFGFGGTNAHVVLEEapaAAPAAAAAARPP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 478 RVLRLAAATPRELGELLA------AGDPGLD--------ERARTTEPCRLGVVEPTPRKLKLAAKAIAKGVPWSGrsdVW 543
Cdd:COG3321 443 QLLVLSAKTEEALRALAArlaaflEAHPDLDladvaytlATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPG---VV 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 544 FAPEPLPGRTAFVFPG--------------LEAEFEPEVADVAALFG--LPWSTGEASVGDIGR---HGTAVFQ-----V 599
Cdd:COG3321 520 TGAAAAAPKVAFLFPGqgsqyvgmgrelyeTEPVFRAALDECDALLRphLGWSLREVLFPDEEEsrlDRTEVAQpalfaV 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 600 GRLLDAALRRLGVVPDAVAGHSVGEWTAMAAGGIhaadevdafLETFDPDSLVV----------PGVAFAVLGMPAAEVL 669
Cdd:COG3321 600 EYALARLWRSWGVRPDAVIGHSVGEYAAACVAGV---------LSLEDALRLVAargrlmqalpGGGAMLAVGLSEEEVE 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 670 AVLPEHPEVVLSHDNAPSQAMVCGPREQVEALVTRMRvQEGVLGRILPFQSGFHTPMLAPYLGPIRDAAQTYTLNPQATP 749
Cdd:COG3321 671 ALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLE-ARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIP 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 750 VWSATTAAPYPaEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ-LGSLVDDTLAGRPHTTV-----SAHG 823
Cdd:COG3321 750 LISNVTGTWLT-GEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPvLTGLVRQCLAAAGDAVVlpslrRGED 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 824 GLLQLRKVVTALWVDGADPDASPLLPAGtaaavapaarrpkvklalGSPLVSLP--PEQRPVARPRVPAAQAFAGLETTA 901
Cdd:COG3321 829 ELAQLLTALAQLWVAGVPVDWSALYPGR------------------GRRRVPLPtyPFQREDAAAALLAAALAAALAAAA 890
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 902 HPIAAELSALLHDTAGVAAELIGAASGRRALPARPPATPAHLPAPPPPAPPVRPTPPVPPSGAVPASLRFDVESMPYLLD 981
Cdd:COG3321 891 ALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAA 970
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 982 HCFFRQPDDWPDPADRWPVVPATTVVTHLMRIAEQAVPGTRAVGLRDVRLLKWIVAEPAAEVPVTARVLGPDRVEVTLVG 1061
Cdd:COG3321 971 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1062 CSQATVELAPAPGAPPAAWPVPDDDRVPERGVEVLYDERWMFHGPRFQGVAEITGIGARHVRGVLTGLAAPGALLDNVGQ 1141
Cdd:COG3321 1051 LAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAAL 1130
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1142 LFGYWIMAVLPERTTVFPVRMERVGFHGSEPV-------PGERLDCLIRITEVTAGTVTADMQLSRGGVVWAQFTGWTDR 1214
Cdd:COG3321 1131 LAAAAAAAALAAAAAAAAALALAAAAAALAAAlaaallaAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLA 1210
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1215 RFDTDPGIRAMDRWPGRNTLSTVDEDGVAVVHERWPDLATRELIMRNNLAGAERDAYDAQPPNRRRQFLLGRIAAKDAAR 1294
Cdd:COG3321 1211 LALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAA 1290
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1295 TALWRAGAGEVYPAELAITNDATGKPVLRGVHGRDPGGLTVSIAHCREVGVGIAATGPCGVDVEEVVARPDRTVDAACDP 1374
Cdd:COG3321 1291 AAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAA 1370
|
1450
....*....|....
gi 1132615381 1375 AERALLDGLGGDRA 1388
Cdd:COG3321 1371 AAAAALALAALAAA 1384
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
12-463 |
2.91e-151 |
|
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: 466.26 E-value: 2.91e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDPGFFGTGERRADRVYCRRGGFVD--AEVDVAGFGVMPNSVP 89
Cdd:cd00833 3 IAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFLDdvDAFDAAFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 90 GTEPDQLIALHVAAASLADAGgEAVLPADRERVGVILGRGGYLTPGLVrldqrvrtanqvvktlrevvpdldderveavr 169
Cdd:cd00833 83 AMDPQQRLLLEVAWEALEDAG-YSPESLAGSRTGVFVGASSSDYLELL-------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 170 aafVEQLGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLW 249
Cdd:cd00833 130 ---ARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 250 STFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQARAVR 329
Cdd:cd00833 207 VGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 330 RAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGT----PAALGSVKSMIGHAMPAAGIAGLIKAALALH 405
Cdd:cd00833 287 RAYARAGVDPSD---IDYVEAHGTGTPLGDPIEVEALAKVFGGSRsadqPLLIGSVKSNIGHLEAAAGLAGLIKVVLALE 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 406 HRVLPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVL 463
Cdd:cd00833 364 HGVIPPNLHFETPNPKIdfEESPLRVPTEARPW--PAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
12-814 |
1.49e-135 |
|
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: 464.48 E-value: 1.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVdAEVDV--AGFGVMPNSV 88
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKdDYYDSDKSEADKSYCKRGGFL-PEVDFnpMEFGLPPNIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 89 PGTEPDQLIALHVAAASLADAGgeavLPA--DRERVGVILGRGG---YLTPGLVRLDQRVrtANQVVKTlrevvPDLDDE 163
Cdd:TIGR02813 88 ELTDISQLLSLVVAKEVLNDAG----LPDgyDRDKIGITLGVGGgqkQSSSLNARLQYPV--LKKVFKA-----SGVEDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 164 RVEAVRAAFVEQLGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHC 243
Cdd:TIGR02813 157 DSEMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 244 HDITLWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAG 323
Cdd:TIGR02813 237 NSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 324 QARAVRRAWDAAGLDPRdpdSVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA----ALGSVKSMIGHAMPAAGIAGLIK 399
Cdd:TIGR02813 317 QAKALKRAYDDAGFAPH---TCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhiALGSVKSQIGHTKSTAGTAGMIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 400 AALALHHRVLPPTLHCDDPNPA--VARTRFAPLAEATPWRAPDSGAPRRAGVNAFGFGGINAHVVLTEPAPARVEVV--- 474
Cdd:TIGR02813 394 AVLALHHKVLPPTINVDQPNPKldIENSPFYLNTETRPWMQREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDqyr 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 475 --EPVRVLRLAAATPRELGELLAAGDPGLDERA----------------RTTEP--CRLGVVEPTPRKL-KLAAKAIAK- 532
Cdd:TIGR02813 474 qrAVAQTLLFTAANEKALVSSLKDWKNKLSAKAddqpyafnalaventlRTIAValARLGFVAKNADELiTMLEQAITQl 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 533 ----GVPWSGRSDVWFAPEPL---PGRTAFVFPGLEAEFE----------PEVADVAA-----------------LFGLP 578
Cdd:TIGR02813 554 eaksCEEWQLPSGISYRKSALvveSGKVAALFAGQGSQYLnmgrelacnfPEVRQAAAdmdsvftqagkgalspvLYPIP 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 579 WSTGEA-SVGDIGRHGTAVFQ--VGRL---LDAALRRLGVVPDAVAGHSVGEWTAMAAGGIHAADEVD--AFLE------ 644
Cdd:TIGR02813 634 VFNDESrKAQEEALTNTQHAQsaIGTLsmgQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMmlAFSRgqamaa 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 645 -TFDPDSLVVPGVAFAVLGMPAAEVlAVLPEHPEVVLSHDNAPSQAMVCGPREQVeALVTRMRVQEGVLGRILPFQSGFH 723
Cdd:TIGR02813 714 pTGEADIGFMYAVILAVVGSPTVIA-NCIKDFEGVSIANYNSPTQLVIAGVSTQI-QIAAKALKEKGFKAIPLPVSGAFH 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 724 TPMLAPYLGPIRDAAQTYTLNPQATPVWSATTAAPYPAEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ- 802
Cdd:TIGR02813 792 TPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNi 871
|
890
....*....|..
gi 1132615381 803 LGSLVDDTLAGR 814
Cdd:TIGR02813 872 LQKLVENTLKDK 883
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
12-465 |
1.45e-80 |
|
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: 267.27 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAItdvpaDRWDPGFFGTGERRADRvycrrggfvdaevdvagfgvmpnsvpgT 91
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDV-----DLFDAAFFGISPREAEA---------------------------M 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLADAGgeavLPADR---ERVGVILGRGGyltpglvrldqrvrtanqvvktlrevvpdldderveav 168
Cdd:smart00825 49 DPQQRLLLEVAWEALEDAG----IDPESlrgSRTGVFVGVSS-------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 169 raafveqlgpaapesaiglvpnlaasrvanrldlRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITL 248
Cdd:smart00825 87 ----------------------------------SDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDT 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 249 WSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQarav 328
Cdd:smart00825 133 FVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ---- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 329 rrawdaagldprdpdsvglieahgtatpagdaaelstlaevfgpgtpAALGSVKSMIGHAMPAAGIAGLIKAALALHHRV 408
Cdd:smart00825 209 -----------------------------------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGV 241
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1132615381 409 LPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVLTE 465
Cdd:smart00825 242 IPPTLHFETPNPHIdlEESPLRVPTELTPW--PPPGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
12-291 |
5.72e-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: 5.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVDAE-VDVAGFGVMPNSVP 89
Cdd:pfam00109 3 VAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPdKLYDPPSRIAGKIYTKWGGLDDIFdFDPLFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 90 GTEPDQLIALHVAAASLADAGgeaVLPA--DRERVGVILGRGGYLTPGLVRLDqrvrtanqvvktlrevvpdlDDERVEA 167
Cdd:pfam00109 83 RMDPQQRLLLEAAWEALEDAG---ITPDslDGSRTGVFIGSGIGDYAALLLLD--------------------EDGGPRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 168 VRAAFVeqlgpaapesaiGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDIT 247
Cdd:pfam00109 140 GSPFAV------------GTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPL 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1132615381 248 LWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADA 291
Cdd:pfam00109 208 GFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
12-463 |
6.97e-53 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 192.14 E-value: 6.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRwdpgffgtgerrADRVYCRRGGFVDAEVDVAGFGVMPN-SVPG 90
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFP------------VGDLATKIGGQVPDLAEDAEAGFDPDrYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 91 TEP---DQLIALHVAAA--SLADAGGEAVLPADRERVGVILGRGgylTPGLVRLDQRVRTanqvvktlrevvpdldderv 165
Cdd:PRK06333 74 KDQrkmDRFILFAMAAAkeALAQAGWDPDTLEDRERTATIIGSG---VGGFPAIAEAVRT-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 166 eavraafVEQLGP--AAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHC 243
Cdd:PRK06333 131 -------LDSRGPrrLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 244 HDITLWSTFSQLGALS------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLL 317
Cdd:PRK06333 204 IDRVSLAGFAAARALStrfndaPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 318 NPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPAALGSVKSMIGHAMPAAGIAGL 397
Cdd:PRK06333 284 PEDGEGARRAMLIALRQAGIPPEE---VQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEA 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1132615381 398 IKAALALHHRVLPPTLHCDDPNPAVARTRFAPLaEATPWRApdsgapRRAGVNAFGFGGINAHVVL 463
Cdd:PRK06333 361 IFTILALRDQIAPPTLNLENPDPAAEGLDVVAN-KARPMDM------DYALSNGFGFGGVNASILF 419
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1352-1456 |
1.50e-14 |
|
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: 71.10 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1352 PCGVDVEEV-------VARPDRTVDAACDPAERALLDGLGGDRALWFTRFWAAKEAVAKARGTGLGGR--PQSFRVVHAT 1422
Cdd:pfam01648 1 GVGIDIEEIarirrpiERLGERLAERIFTPEERALLASLPAEARRAFARLWTAKEAVFKALGPGLSKLldFDDIEVLLDP 80
|
90 100 110
....*....|....*....|....*....|....
gi 1132615381 1423 AERLRVQVEGAVHVVRVRSAENppglpARDYVVA 1456
Cdd:pfam01648 81 DGRPTLRLLGEAADLAWRFEVL-----AGDYALA 109
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1351-1434 |
3.27e-06 |
|
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: 47.82 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1351 GPCGVDVEEV------VARPDRTVDAACDPAERALLDGL-GGDRALWFTRFWAAKEAVAKARGTGLGGRPQSFRVVHATA 1423
Cdd:TIGR00556 3 VGIGIDIVEIkriaeqIERSGTFAERFFTPSEIEDYCKLsPKSQTESLAGRWAAKEAFIKALGKGISLGELLFTDIEIVK 82
|
90
....*....|....
gi 1132615381 1424 ERL---RVQVEGAV 1434
Cdd:TIGR00556 83 DLKgapRVCLIGEA 96
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1354-1436 |
6.12e-05 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 43.96 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1354 GVDV------EEVVARP-DRTVDAACDPAERALLDGLGgDRALWFTRFWAAKEAVAKARGTGLG---------------G 1411
Cdd:COG0736 3 GIDIveiariERALERHgERFLERVFTPAERAYCQSRK-RPAEFLAGRFAAKEAVSKALGTGIGkgvswrdievlndpsG 81
|
90 100
....*....|....*....|....*
gi 1132615381 1412 RPQsFRVVHATAERLRVQVEGAVHV 1436
Cdd:COG0736 82 KPT-VRLSGRAAELAAELGITRIHL 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
12-1388 |
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: 596.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVD--AEVDVAGFGVMPNSV 88
Cdd:COG3321 6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPADRWDAdAYYDPDPDAPGKTYVRWGGFLDdvDEFDALFFGISPREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 89 PGTEPDQLIALHVAAASLADAGgeaVLPA--DRERVGVILGrGGYLTPGLVRLDQRvrtanqvvktlrevvpdldderve 166
Cdd:COG3321 86 EAMDPQQRLLLEVAWEALEDAG---YDPEslAGSRTGVFVG-ASSNDYALLLLADP------------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 167 avraafveqlGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDI 246
Cdd:COG3321 138 ----------EAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 247 TLWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQAR 326
Cdd:COG3321 208 ESFILFSKGGMLSPDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 327 AVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA----ALGSVKSMIGHAMPAAGIAGLIKAAL 402
Cdd:COG3321 288 VIRRALADAGVDPAT---VDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpcAIGSVKSNIGHLEAAAGVAGLIKAVL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 403 ALHHRVLPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVLTE---PAPARVEVVEPV 477
Cdd:COG3321 365 ALRHGVLPPTLHFETPNPHIdfENSPFYVNTELRPW--PAGGGPRRAGVSSFGFGGTNAHVVLEEapaAAPAAAAAARPP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 478 RVLRLAAATPRELGELLA------AGDPGLD--------ERARTTEPCRLGVVEPTPRKLKLAAKAIAKGVPWSGrsdVW 543
Cdd:COG3321 443 QLLVLSAKTEEALRALAArlaaflEAHPDLDladvaytlATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPG---VV 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 544 FAPEPLPGRTAFVFPG--------------LEAEFEPEVADVAALFG--LPWSTGEASVGDIGR---HGTAVFQ-----V 599
Cdd:COG3321 520 TGAAAAAPKVAFLFPGqgsqyvgmgrelyeTEPVFRAALDECDALLRphLGWSLREVLFPDEEEsrlDRTEVAQpalfaV 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 600 GRLLDAALRRLGVVPDAVAGHSVGEWTAMAAGGIhaadevdafLETFDPDSLVV----------PGVAFAVLGMPAAEVL 669
Cdd:COG3321 600 EYALARLWRSWGVRPDAVIGHSVGEYAAACVAGV---------LSLEDALRLVAargrlmqalpGGGAMLAVGLSEEEVE 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 670 AVLPEHPEVVLSHDNAPSQAMVCGPREQVEALVTRMRvQEGVLGRILPFQSGFHTPMLAPYLGPIRDAAQTYTLNPQATP 749
Cdd:COG3321 671 ALLAGYDGVSIAAVNGPRSTVVSGPAEAVEALAARLE-ARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIP 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 750 VWSATTAAPYPaEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ-LGSLVDDTLAGRPHTTV-----SAHG 823
Cdd:COG3321 750 LISNVTGTWLT-GEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPvLTGLVRQCLAAAGDAVVlpslrRGED 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 824 GLLQLRKVVTALWVDGADPDASPLLPAGtaaavapaarrpkvklalGSPLVSLP--PEQRPVARPRVPAAQAFAGLETTA 901
Cdd:COG3321 829 ELAQLLTALAQLWVAGVPVDWSALYPGR------------------GRRRVPLPtyPFQREDAAAALLAAALAAALAAAA 890
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 902 HPIAAELSALLHDTAGVAAELIGAASGRRALPARPPATPAHLPAPPPPAPPVRPTPPVPPSGAVPASLRFDVESMPYLLD 981
Cdd:COG3321 891 ALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAA 970
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 982 HCFFRQPDDWPDPADRWPVVPATTVVTHLMRIAEQAVPGTRAVGLRDVRLLKWIVAEPAAEVPVTARVLGPDRVEVTLVG 1061
Cdd:COG3321 971 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1062 CSQATVELAPAPGAPPAAWPVPDDDRVPERGVEVLYDERWMFHGPRFQGVAEITGIGARHVRGVLTGLAAPGALLDNVGQ 1141
Cdd:COG3321 1051 LAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAAL 1130
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1142 LFGYWIMAVLPERTTVFPVRMERVGFHGSEPV-------PGERLDCLIRITEVTAGTVTADMQLSRGGVVWAQFTGWTDR 1214
Cdd:COG3321 1131 LAAAAAAAALAAAAAAAAALALAAAAAALAAAlaaallaAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLA 1210
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1215 RFDTDPGIRAMDRWPGRNTLSTVDEDGVAVVHERWPDLATRELIMRNNLAGAERDAYDAQPPNRRRQFLLGRIAAKDAAR 1294
Cdd:COG3321 1211 LALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAA 1290
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1295 TALWRAGAGEVYPAELAITNDATGKPVLRGVHGRDPGGLTVSIAHCREVGVGIAATGPCGVDVEEVVARPDRTVDAACDP 1374
Cdd:COG3321 1291 AAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAA 1370
|
1450
....*....|....
gi 1132615381 1375 AERALLDGLGGDRA 1388
Cdd:COG3321 1371 AAAAALALAALAAA 1384
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
12-463 |
2.91e-151 |
|
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: 466.26 E-value: 2.91e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDPGFFGTGERRADRVYCRRGGFVD--AEVDVAGFGVMPNSVP 89
Cdd:cd00833 3 IAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFLDdvDAFDAAFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 90 GTEPDQLIALHVAAASLADAGgEAVLPADRERVGVILGRGGYLTPGLVrldqrvrtanqvvktlrevvpdldderveavr 169
Cdd:cd00833 83 AMDPQQRLLLEVAWEALEDAG-YSPESLAGSRTGVFVGASSSDYLELL-------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 170 aafVEQLGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLW 249
Cdd:cd00833 130 ---ARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 250 STFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQARAVR 329
Cdd:cd00833 207 VGFSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 330 RAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGT----PAALGSVKSMIGHAMPAAGIAGLIKAALALH 405
Cdd:cd00833 287 RAYARAGVDPSD---IDYVEAHGTGTPLGDPIEVEALAKVFGGSRsadqPLLIGSVKSNIGHLEAAAGLAGLIKVVLALE 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 406 HRVLPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVL 463
Cdd:cd00833 364 HGVIPPNLHFETPNPKIdfEESPLRVPTEARPW--PAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
12-814 |
1.49e-135 |
|
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: 464.48 E-value: 1.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVdAEVDV--AGFGVMPNSV 88
Cdd:TIGR02813 9 IAIVGMASIFANSRYLNKFWDLIFEKIDAITDVPSDHWAKdDYYDSDKSEADKSYCKRGGFL-PEVDFnpMEFGLPPNIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 89 PGTEPDQLIALHVAAASLADAGgeavLPA--DRERVGVILGRGG---YLTPGLVRLDQRVrtANQVVKTlrevvPDLDDE 163
Cdd:TIGR02813 88 ELTDISQLLSLVVAKEVLNDAG----LPDgyDRDKIGITLGVGGgqkQSSSLNARLQYPV--LKKVFKA-----SGVEDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 164 RVEAVRAAFVEQLGPAAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHC 243
Cdd:TIGR02813 157 DSEMLIKKFQDQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 244 HDITLWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAG 323
Cdd:TIGR02813 237 NSPFMYMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 324 QARAVRRAWDAAGLDPRdpdSVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA----ALGSVKSMIGHAMPAAGIAGLIK 399
Cdd:TIGR02813 317 QAKALKRAYDDAGFAPH---TCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhiALGSVKSQIGHTKSTAGTAGMIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 400 AALALHHRVLPPTLHCDDPNPA--VARTRFAPLAEATPWRAPDSGAPRRAGVNAFGFGGINAHVVLTEPAPARVEVV--- 474
Cdd:TIGR02813 394 AVLALHHKVLPPTINVDQPNPKldIENSPFYLNTETRPWMQREDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDqyr 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 475 --EPVRVLRLAAATPRELGELLAAGDPGLDERA----------------RTTEP--CRLGVVEPTPRKL-KLAAKAIAK- 532
Cdd:TIGR02813 474 qrAVAQTLLFTAANEKALVSSLKDWKNKLSAKAddqpyafnalaventlRTIAValARLGFVAKNADELiTMLEQAITQl 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 533 ----GVPWSGRSDVWFAPEPL---PGRTAFVFPGLEAEFE----------PEVADVAA-----------------LFGLP 578
Cdd:TIGR02813 554 eaksCEEWQLPSGISYRKSALvveSGKVAALFAGQGSQYLnmgrelacnfPEVRQAAAdmdsvftqagkgalspvLYPIP 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 579 WSTGEA-SVGDIGRHGTAVFQ--VGRL---LDAALRRLGVVPDAVAGHSVGEWTAMAAGGIHAADEVD--AFLE------ 644
Cdd:TIGR02813 634 VFNDESrKAQEEALTNTQHAQsaIGTLsmgQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMmlAFSRgqamaa 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 645 -TFDPDSLVVPGVAFAVLGMPAAEVlAVLPEHPEVVLSHDNAPSQAMVCGPREQVeALVTRMRVQEGVLGRILPFQSGFH 723
Cdd:TIGR02813 714 pTGEADIGFMYAVILAVVGSPTVIA-NCIKDFEGVSIANYNSPTQLVIAGVSTQI-QIAAKALKEKGFKAIPLPVSGAFH 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 724 TPMLAPYLGPIRDAAQTYTLNPQATPVWSATTAAPYPAEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ- 802
Cdd:TIGR02813 792 TPLVAHAQKPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNi 871
|
890
....*....|..
gi 1132615381 803 LGSLVDDTLAGR 814
Cdd:TIGR02813 872 LQKLVENTLKDK 883
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
12-465 |
1.45e-80 |
|
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: 267.27 E-value: 1.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAItdvpaDRWDPGFFGTGERRADRvycrrggfvdaevdvagfgvmpnsvpgT 91
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDV-----DLFDAAFFGISPREAEA---------------------------M 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLADAGgeavLPADR---ERVGVILGRGGyltpglvrldqrvrtanqvvktlrevvpdldderveav 168
Cdd:smart00825 49 DPQQRLLLEVAWEALEDAG----IDPESlrgSRTGVFVGVSS-------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 169 raafveqlgpaapesaiglvpnlaasrvanrldlRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITL 248
Cdd:smart00825 87 ----------------------------------SDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDT 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 249 WSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQarav 328
Cdd:smart00825 133 FVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ---- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 329 rrawdaagldprdpdsvglieahgtatpagdaaelstlaevfgpgtpAALGSVKSMIGHAMPAAGIAGLIKAALALHHRV 408
Cdd:smart00825 209 -----------------------------------------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGV 241
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1132615381 409 LPPTLHCDDPNPAV--ARTRFAPLAEATPWraPDSGAPRRAGVNAFGFGGINAHVVLTE 465
Cdd:smart00825 242 IPPTLHFETPNPHIdlEESPLRVPTELTPW--PPPGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
12-463 |
5.65e-75 |
|
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: 255.54 E-value: 5.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITdvPADRWDPGFFgtgerradrvYCRRGGFVDAEVDVAGFGvmPNSVPGT 91
Cdd:cd00834 3 VVITGLGAVTPLGNGVEEFWEALLAGRSGIR--PITRFDASGF----------PSRIAGEVPDFDPEDYLD--RKELRRM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLADAGGEAVlPADRERVGVILGRGgylTPGLVRLDQRVRTanqvvktlrevvpdLDDERVEAVRAA 171
Cdd:cd00834 69 DRFAQFALAAAEEALADAGLDPE-ELDPERIGVVIGSG---IGGLATIEEAYRA--------------LLEKGPRRVSPF 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 172 FVEQLgpaapesaiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVH-HCHDITLWS 250
Cdd:cd00834 131 FVPMA-----------LPNMAAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 251 tFSQLGALSPSQRI-----RPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQA 325
Cdd:cd00834 200 -FAALRALSTRNDDpekasRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 326 RAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTP-AALGSVKSMIGHAMPAAGIAGLIKAALAL 404
Cdd:cd00834 279 RAMRAALADAGLSPED---IDYINAHGTSTPLNDAAESKAIKRVFGEHAKkVPVSSTKSMTGHLLGAAGAVEAIATLLAL 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1132615381 405 HHRVLPPTLHCDDPNPAVArTRFAPlAEATPWRApdsgapRRAGVNAFGFGGINAHVVL 463
Cdd:cd00834 356 RDGVLPPTINLEEPDPECD-LDYVP-NEAREAPI------RYALSNSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
12-464 |
8.92e-74 |
|
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: 252.32 E-value: 8.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITdvPADRWDPGFFGtgerradrvyCRRGGFVDaEVDVAGFgVMPNSVPGT 91
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIR--PITRFDASGLP----------VRIAGEVK-DFDPEEY-LDRKELRRM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLADAGGEAVlPADRERVGVILG--RGGyltpglvrldqrvrtanqvVKTLREVVPDLDDERVEAVR 169
Cdd:COG0304 69 DRFTQYALAAAREALADAGLDLD-EVDPDRTGVIIGsgIGG-------------------LDTLEEAYRALLEKGPRRVS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 170 AAFVEQLgpaapesaiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLW 249
Cdd:COG0304 129 PFFVPMM-----------MPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 250 STFSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQ 324
Cdd:COG0304 198 AGFDALGALStrnddPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 325 ARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA-ALGSVKSMIGHAMPAAGIAGLIKAALA 403
Cdd:COG0304 278 ARAMRAALKDAGLSPED---IDYINAHGTSTPLGDAAETKAIKRVFGDHAYKvPVSSTKSMTGHLLGAAGAIEAIASVLA 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132615381 404 LHHRVLPPTLHCDDPNPAvartrfAPL----AEATPWRapdsgaPRRAGVNAFGFGGINAHVVLT 464
Cdd:COG0304 355 LRDGVIPPTINLENPDPE------CDLdyvpNEAREAK------IDYALSNSFGFGGHNASLVFK 407
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
12-291 |
5.72e-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: 5.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRWDP-GFFGTGERRADRVYCRRGGFVDAE-VDVAGFGVMPNSVP 89
Cdd:pfam00109 3 VAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPdKLYDPPSRIAGKIYTKWGGLDDIFdFDPLFFGISPREAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 90 GTEPDQLIALHVAAASLADAGgeaVLPA--DRERVGVILGRGGYLTPGLVRLDqrvrtanqvvktlrevvpdlDDERVEA 167
Cdd:pfam00109 83 RMDPQQRLLLEAAWEALEDAG---ITPDslDGSRTGVFIGSGIGDYAALLLLD--------------------EDGGPRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 168 VRAAFVeqlgpaapesaiGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDIT 247
Cdd:pfam00109 140 GSPFAV------------GTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPL 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1132615381 248 LWSTFSQLGALSPSQRIRPFHRGADGVLIAEGTGVVVLKRLADA 291
Cdd:pfam00109 208 GFAGFSAAGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
12-463 |
6.97e-53 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 192.14 E-value: 6.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVPADRwdpgffgtgerrADRVYCRRGGFVDAEVDVAGFGVMPN-SVPG 90
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFP------------VGDLATKIGGQVPDLAEDAEAGFDPDrYLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 91 TEP---DQLIALHVAAA--SLADAGGEAVLPADRERVGVILGRGgylTPGLVRLDQRVRTanqvvktlrevvpdldderv 165
Cdd:PRK06333 74 KDQrkmDRFILFAMAAAkeALAQAGWDPDTLEDRERTATIIGSG---VGGFPAIAEAVRT-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 166 eavraafVEQLGP--AAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHC 243
Cdd:PRK06333 131 -------LDSRGPrrLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 244 HDITLWSTFSQLGALS------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLL 317
Cdd:PRK06333 204 IDRVSLAGFAAARALStrfndaPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 318 NPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPAALGSVKSMIGHAMPAAGIAGL 397
Cdd:PRK06333 284 PEDGEGARRAMLIALRQAGIPPEE---VQHLNAHATSTPVGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEA 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1132615381 398 IKAALALHHRVLPPTLHCDDPNPAVARTRFAPLaEATPWRApdsgapRRAGVNAFGFGGINAHVVL 463
Cdd:PRK06333 361 IFTILALRDQIAPPTLNLENPDPAAEGLDVVAN-KARPMDM------DYALSNGFGFGGVNASILF 419
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
12-463 |
1.07e-51 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 188.08 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITdvPADRWDPGFFGtgerradrvycrrggfvdaeVDVAGfgvmpnSVPGT 91
Cdd:TIGR03150 3 VVVTGLGAVTPLGNGVEEFWENLLAGKSGIG--PITRFDASDLP--------------------VKIAG------EVKDF 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLI--------------ALHVAAASLADAGGEaVLPADRERVGVILGRG-GyltpGLVRLDQRVRTanqvvktLREV 156
Cdd:TIGR03150 55 DPEDYIdkkearrmdrfiqyALAAAKEAVEDSGLD-IEEEDAERVGVIIGSGiG----GLETIEEQHIV-------LLEK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 157 VPDlddeRVeavraafveqlgpaAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMF 236
Cdd:TIGR03150 123 GPR----RV--------------SPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMI 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 237 AGGVHHChdITLWST--FSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVAS 309
Cdd:TIGR03150 185 AGGAEAA--ITPLGIagFAAMKALStrnddPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 310 DGRSASLLNPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTP-AALGSVKSMIGHA 388
Cdd:TIGR03150 263 DAYHITAPAPEGEGAARAMRAALKDAGINPED---VDYINAHGTSTPLGDKAETKAIKKVFGDHAYkLAVSSTKSMTGHL 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132615381 389 MPAAGIAGLIKAALALHHRVLPPTLHCDDPNPAVARTrFAPLaEATPWRapdsgaPRRAGVNAFGFGGINAHVVL 463
Cdd:TIGR03150 340 LGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLD-YVPN-EAREAK------IDYALSNSFGFGGTNASLVF 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
12-466 |
4.19e-51 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 187.31 E-value: 4.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDV-PADRWDPGFFGTGERRA-DRVYCRRGGFVDAEVDVAGFGVMP-NSV 88
Cdd:PLN02836 8 VVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtQDDLKMKSEDEETQLYTlDQLPSRVAALVPRGTGPGDFDEELwLNS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 89 PGTEPDQLIALHVAAASLADAGGEAVLPADRERVGVILGRGGYLTPGLVRLDQRVRTanqvvKTLREVVPdldderveav 168
Cdd:PLN02836 88 RSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICE-----KRLRRLSP---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 169 raAFVEQLgpaapesaiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITL 248
Cdd:PLN02836 153 --FFVPRI-----------LINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 249 WSTFSQLGALS------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPA 322
Cdd:PLN02836 220 IAGFSRSRALStkfnscPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 323 GQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPA---ALGSVKSMIGHAMPAAGIAGLIK 399
Cdd:PLN02836 300 GAVLAMTRALQQSGLHPNQ---VDYVNAHATSTPLGDAVEARAIKTVFSEHATSgglAFSSTKGATGHLLGAAGAVEAIF 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132615381 400 AALALHHRVLPPTLHCDDPNPaVARTRFAPLAEAtpwrapdSGAPRRAGV-NAFGFGGINAHVVLTEP 466
Cdd:PLN02836 377 SVLAIHHGIAPPTLNLERPDP-IFDDGFVPLTAS-------KAMLIRAALsNSFGFGGTNASLLFTSP 436
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
12-463 |
4.80e-49 |
|
"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: 180.33 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFP---GAPDLDAYWRNIAAGTDAIT--DVPADRWDPGFFGTgerradrvycRRGGFVDAEvDVAGFGVMPn 86
Cdd:cd00828 3 VVITGIGVVSPhgeGCDEVEEFWEALREGRSGIApvARLKSRFDRGVAGQ----------IPTGDIPGW-DAKRTGIVD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 87 svpgtePDQLIALHVAAASLADAGGEAVLPADRERVGVILGRG-GYLTPGLVRLDQRVRTANQVVKTLREvvpdldderv 165
Cdd:cd00828 71 ------RTTLLALVATEEALADAGITDPYEVHPSEVGVVVGSGmGGLRFLRRGGKLDARAVNPYVSPKWM---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 166 eavraafveqlgpaapesaigLVPNLAASRVANRLDL-RGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGvhhCH 244
Cdd:cd00828 135 ---------------------LSPNTVAGWVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGG---VE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 245 DITLWST--FSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLL 317
Cdd:cd00828 191 DPLEEGLsgFANMGALStaeeePEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 318 NPDPaGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGP-GTPAALGSVKSMIGHAMPAAGIAG 396
Cdd:cd00828 271 AGGK-GIARAIRTALAKAGLSLDD---LDVISAHGTSTPANDVAESRAIAEVAGAlGAPLPVTAQKALFGHSKGAAGALQ 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1132615381 397 LIKAALALHHRVLPPTLHCDDPNPAVARTRFAPLAEatpwraPDSGAPRRAGVNAFGFGGINAHVVL 463
Cdd:cd00828 347 LIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSR------DLNLKVRAALVNAFGFGGSNAALVL 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
12-463 |
1.28e-48 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 179.21 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITdvPADRWDpgffgtgerrADRVYCRRGGfvdaevdvagfgvmpnSVPGT 91
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVESTWKNLLAGKSGIG--PITHFD----------TSDLAVKIAG----------------EVKDF 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLI--------------ALHVAAASLADAGGEaVLPADRERVGVILGRG-GyltpGLVRLDQRVRTANQvvKTLREV 156
Cdd:PRK07314 56 NPDDYMsrkearrmdrfiqyGIAAAKQAVEDAGLE-ITEENADRIGVIIGSGiG----GLETIEEQHITLLE--KGPRRV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 157 VPdldderveavraAFVeqlgPAApesaiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMF 236
Cdd:PRK07314 129 SP------------FFV----PMA-------IINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 237 AGGVHHChdITLWST--FSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVAS 309
Cdd:PRK07314 186 AGGAEAA--ITPLGIagFAAARALStrnddPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 310 DGRSASLLNPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTP-AALGSVKSMIGHA 388
Cdd:PRK07314 264 DAYHMTAPAPDGEGAARAMKLALKDAGINPED---IDYINAHGTSTPAGDKAETQAIKRVFGEHAYkVAVSSTKSMTGHL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 389 MPAAGIAGLIKAALALHHRVLPPTLHCDDPNPAVArTRFAPlaeatpwrapdsGAPRRAGV-----NAFGFGGINAHVVL 463
Cdd:PRK07314 341 LGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD-LDYVP------------NEARERKIdyalsNSFGFGGTNASLVF 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
31-464 |
4.37e-48 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 177.96 E-value: 4.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 31 WRNIAAG---TDAITDVPADRwdPGFFGTGERRADRVY---CRRGGFVDAEVDVAgfgvmPNSVPGTEPDQLIALHVAAA 104
Cdd:PTZ00050 13 WEALIAGksgIRKLTEFPKFL--PDCIPEQKALENLVAampCQIAAEVDQSEFDP-----SDFAPTKRESRATHFAMAAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 105 SLA--DAGGEAVLPADRERVGVILGRGgylTPGLVRLDQrvrtanqVVKTLREvvpdlddERVEAVRAAFVEQLgpaape 182
Cdd:PTZ00050 86 REAlaDAKLDILSEKDQERIGVNIGSG---IGSLADLTD-------EMKTLYE-------KGHSRVSPYFIPKI------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 183 saiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLWSTFSQLGALS--- 259
Cdd:PTZ00050 143 -----LGNMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtky 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 260 ---PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQARAVRRAW-DAA 335
Cdd:PTZ00050 218 nddPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALkDGA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 336 GLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGT--PAALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPT- 412
Cdd:PTZ00050 298 NININD---VDYVNAHATSTPIGDKIELKAIKKVFGDSGapKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTi 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1132615381 413 -LHCDDPNPAVARTRFAPLAEATPWRAPDSgaprragvNAFGFGGINAHVVLT 464
Cdd:PTZ00050 375 nLENPDAECDLNLVQGKTAHPLQSIDAVLS--------TSFGFGGVNTALLFT 419
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
181-463 |
5.85e-44 |
|
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: 163.19 E-value: 5.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 181 PESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLWSTFSQLGALSP 260
Cdd:cd00825 64 PYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 261 SQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQARAVRRAWDAAGLDPR 340
Cdd:cd00825 144 EKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVW 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 341 DPDSVgliEAHGTATPAGDAAELSTLAEVFGPGTPaALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDPNP 420
Cdd:cd00825 224 DIDYL---VAHGTGTPIGDVKELKLLRSEFGDKSP-AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE 299
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1132615381 421 AVARTrfapLAEATPWRapdsgaPRRAGVNAFGFGGINAHVVL 463
Cdd:cd00825 300 AGLNI----VTETTPRE------LRTALLNGFGLGGTNATLVL 332
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
299-416 |
2.66e-43 |
|
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: 153.49 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 299 YAVVSGTGVASDGRSASLLNPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGT---P 375
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPED---VDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1132615381 376 AALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCD 416
Cdd:pfam02801 78 LAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
196-463 |
2.89e-40 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 154.23 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 196 VANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLWStFSQLGALSPsQRIRPFHRGADGVL 275
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNG-FNSLESLSP-QPCRPFSANRDGIN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 276 IAEGTGVVVLKRLADAErdgdrvyAVVSGTGVASDGRSASLLNPDPAGQARAVRRAWDAAGLDPRDpdsVGLIEAHGTAT 355
Cdd:PRK09185 221 IGEAAAFFLLEREDDAA-------VALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPAD---IGYINLHGTAT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 356 PAGDAAELSTLAEVFGPGTPAAlgSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDPNPAvartrFAPLAEATP 435
Cdd:PRK09185 291 PLNDAMESRAVAAVFGDGVPCS--STKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPA-----LPPLYLVEN 363
|
250 260
....*....|....*....|....*...
gi 1132615381 436 WRAPdsgAPRRAGVNAFGFGGINAHVVL 463
Cdd:PRK09185 364 AQAL---AIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
101-463 |
3.99e-40 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 154.42 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 101 VAAASLADAGGEAVL-PADRERVGVILGrGGYLTPglvRLDQRVRTANQvvktlrevvpdlddERVEAVRAAFVEQlgpA 179
Cdd:PRK07103 83 AALAAAREAWRDAALgPVDPDRIGLVVG-GSNLQQ---REQALVHETYR--------------DRPAFLRPSYGLS---F 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 180 APESAIGLVPNLaasrvanrLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVhhCHDITLWS--TFSQLGA 257
Cdd:PRK07103 142 MDTDLVGLCSEQ--------FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGA--LMDLSYWEcqALRSLGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 258 LS-------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASllNPDPAGQARAVRR 330
Cdd:PRK07103 212 MGsdrfadePEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGP--DPSLEGEMRVIRA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 331 AWDAAGLDPRDPDSVgliEAHGTATPAGDAAELSTLaevFGPGTPAA-LGSVKSMIGHAMPAAGIAGLIKAALALHHRVL 409
Cdd:PRK07103 290 ALRRAGLGPEDIDYV---NPHGTGSPLGDETELAAL---FASGLAHAwINATKSLTGHGLSAAGIVELIATLLQMRAGFL 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1132615381 410 PPTLHCDDPNPAVARtrfaplaeatpW--RAPDSGAPRRAGVNAFGFGGINAHVVL 463
Cdd:PRK07103 364 HPSRNLDEPIDERFR-----------WvgSTAESARIRYALSLSFGFGGINTALVL 408
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
105-463 |
2.99e-37 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 145.97 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 105 SLADAGGEAVLPADrERVGVILGRGGyltpglvrldqrVRTANQVvktlrevvpdlddERVEAVRAAF-VEQLGPAApes 183
Cdd:PRK07967 82 AIADAGLSEEQVSN-PRTGLIAGSGG------------GSTRNQV-------------EAADAMRGPRgPKRVGPYA--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 184 aiglVPNLAASRV----ANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGvHHCHDITLWSTFSQLGALS 259
Cdd:PRK07967 133 ----VTKAMASTVsaclATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGG-GEELDWEMSCLFDAMGALS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 260 ------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGrsASLLNPDPAGQARAVRRAwd 333
Cdd:PRK07967 208 tkyndtPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDG--YDMVAPSGEGAVRCMQMA-- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 334 AAGLDPRdpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPAaLGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTL 413
Cdd:PRK07967 284 LATVDTP----IDYINTHGTSTPVGDVKELGAIREVFGDKSPA-ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSA 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1132615381 414 HCDDPNPAVA-------RTRFAPLAEATPwrapdsgaprragvNAFGFGGINAHVVL 463
Cdd:PRK07967 359 NIEELDPQAAgmpivteTTDNAELTTVMS--------------NSFGFGGTNATLVF 401
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
12-463 |
8.75e-37 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 144.76 E-value: 8.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVpaDRWDPGFFGTgerradrvycRRGGFVDaEVDVAGFGVMPNSvpgT 91
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNI--EHFDTTNFST----------RFAGLVK-DFNCEEYMSKKDA---R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLA-DAGGEAVLPADRERVGVILGRGgylTPGLvrldqrvrtanqvvktlrevvpdlddERVEAVRA 170
Cdd:PRK08722 70 KMDLFIQYGIAAGIQAlDDSGLEVTEENAHRIGVAIGSG---IGGL--------------------------GLIEAGHQ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 171 AFVEQlGP--AAPESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITL 248
Cdd:PRK08722 121 ALVEK-GPrkVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 249 WSTFSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAG 323
Cdd:PRK08722 200 MAGFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 324 QARAVRRAWDAAGLdprDPDSVGLIEAHGTATPAGDAAELSTLAEVFG-PGTPAAL-GSVKSMIGHAMPAAGIAGLIKAA 401
Cdd:PRK08722 280 GALAMEAAMRDAGV---TGEQIGYVNAHGTSTPAGDVAEIKGIKRALGeAGSKQVLvSSTKSMTGHLLGAAGSVEAIITV 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1132615381 402 LALHHRVLPPTLHCDDPNPAVArtrfaplAEATPWRAPDSGAPRRAGVNAFGFGGINAHVVL 463
Cdd:PRK08722 357 MSLVDQIVPPTINLDDPEEGLD-------IDLVPHTARKVESMEYAICNSFGFGGTNGSLIF 411
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
193-467 |
8.78e-35 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 139.00 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 193 ASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFA----GGVHHCHDITlwstFSQLGALS-----PSQR 263
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCiatdGSVSAEALIR----FSLLSALStqndpPEKA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 264 IRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDG--RSASllNPDPAGQARAVRRAWDAAGLDPrd 341
Cdd:PRK06501 231 SKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSfhRTRS--SPDGSPAIGAIRAALADAGLTP-- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 342 pDSVGLIEAHGTATPAGDAAELSTLAEVFG---PGTPaaLGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDP 418
Cdd:PRK06501 307 -EQIDYINAHGTSTPENDKMEYLGLSAVFGerlASIP--VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNP 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1132615381 419 NPAVartrfaPLaEATPWRAPDsgAPRRAGV-NAFGFGGINAHVVLT-EPA 467
Cdd:PRK06501 384 DPAI------PL-DVVPNVARD--ARVTAVLsNSFGFGGQNASLVLTaEPA 425
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
167-463 |
6.35e-34 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 134.47 E-value: 6.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 167 AVRAAfvEQLGPA--APESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCH 244
Cdd:PRK14691 45 AVRTS--DSRGPKrlSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 245 DITLWSTFSQLGALS------PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLN 318
Cdd:PRK14691 123 DTVSLAGFAAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 319 PDPAGQARAVRRAWDAAGLDPrdpDSVGLIEAHGTATPAGDAAELSTLAEVFGPGTPAALGSVKSMIGHAMPAAGIAGLI 398
Cdd:PRK14691 203 EDGDGAYRAMKIALRQAGITP---EQVQHLNAHATSTPVGDLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETI 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132615381 399 KAALALHHRVLPPTLHCDDPNPAvARTRFAPLAEATPWRAPdsgaprRAGVNAFGFGGINAHVVL 463
Cdd:PRK14691 280 FTVLALRDQIVPATLNLENPDPA-AKGLNIIAGNAQPHDMT------YALSNGFGFAGVNASILL 337
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
551-820 |
2.06e-32 |
|
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: 128.71 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 551 GRTAFVFPG-----------LEAEFePEVADVAAlfglpwstgEAS------VGDIGRHG-------TAVFQ-----VGR 601
Cdd:COG0331 1 MKLAFLFPGqgsqyvgmgkdLYENF-PVAREVFE---------EASealgydLSALCFEGpeeelnlTENTQpailaASV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 602 LLDAALRRLGVVPDAVAGHSVGEWTAMAAGGihAADEVDAFletfdpdSLV-------------VPGVAFAVLGMPAAEV 668
Cdd:COG0331 71 AAYRALEEEGIRPDAVAGHSLGEYSALVAAG--ALSFEDAL-------RLVrlrgrlmqeavpaGPGGMAAVLGLDDEEV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 669 LAVLPEHPE---VVLSHDNAPSQAMVCGPREQVEALVTRMRvqEGVLGRILPFQ-SG-FHTPMLAPYLGPIRDAAQTYTL 743
Cdd:COG0331 142 EALCAEAAQgevVEIANYNSPGQIVISGEKEAVEAAAELAK--EAGAKRAVPLPvSGpFHTPLMAPAAEKLAEALAAVTF 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132615381 744 NPQATPVWSATTAAPYpAEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ-LGSLVDDTLAGRPHTTVS 820
Cdd:COG0331 220 ADPKIPVVSNVDAAPV-TDPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKvLSGLVKRIDPGVEVLAVE 296
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
183-458 |
7.61e-31 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 127.03 E-value: 7.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 183 SAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHChDITLWSTFSQLGALS--- 259
Cdd:PRK09116 134 TYVRMMPHTTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEEL-CPTEAAVFDTLFATStrn 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 260 --PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGrsASLLNPDPAGQARAVRRAWDAAGL 337
Cdd:PRK09116 213 daPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDG--AHVTQPQAETMQIAMELALKDAGL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 338 DPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPaaLGSVKSMIGHAMpaaGIAGLIKAALAL---HHRVLPPTLH 414
Cdd:PRK09116 291 APED---IGYVNAHGTATDRGDIAESQATAAVFGARMP--ISSLKSYFGHTL---GACGALEAWMSIemmNEGWFAPTLN 362
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1132615381 415 CDDPNPAVARTRFAplaeatpwrapdSGAPRRAGV-----NAFGFGGIN 458
Cdd:PRK09116 363 LTQVDPACGALDYI------------MGEAREIDTeyvmsNNFAFGGIN 399
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
120-458 |
9.38e-31 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 126.77 E-value: 9.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 120 ERVGVILGRGGYLTPGLVRLDQR-----VRTANQVVKTLREVVPDLDDERVEAVRAAFVEQLGPAAPESAIGLvpnlaas 194
Cdd:PRK07910 84 QRMSTVLGRRVWENAGSPEVDTNrlmvsIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGL------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 195 rvanRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLWSTFSQLGAL------SPSQRIRPFH 268
Cdd:PRK07910 157 ----ERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVmstnndDPAGACRPFD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 269 RGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSasLLNPDPAGQ--ARAVRRAWDAAGLDPRDpdsVG 346
Cdd:PRK07910 233 KDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFH--MVAPDPNGEraGHAMTRAIELAGLTPGD---ID 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 347 LIEAHGTATPAGDAAELSTLAEVFGPGTPAALGSvKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDPNPAVARTR 426
Cdd:PRK07910 308 HVNAHATGTSVGDVAEGKAINNALGGHRPAVYAP-KSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDV 386
|
330 340 350
....*....|....*....|....*....|..
gi 1132615381 427 FAplaeatpwRAPDSGAPRRAGVNAFGFGGIN 458
Cdd:PRK07910 387 VA--------GEPRPGNYRYAINNSFGFGGHN 410
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
181-463 |
4.10e-29 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 121.31 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 181 PESAIGLVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHH-CHDITLwSTFSQLGALS 259
Cdd:PRK05952 114 LENWLDTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApITPLTL-AGFQQMGALA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 260 PsQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPAGQARAVRRAWDAAGLDP 339
Cdd:PRK05952 193 K-TGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 340 RDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTpaALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDPN 419
Cdd:PRK05952 272 ED---IDYIHAHGTATRLNDQREANLIQALFPHRV--AVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1132615381 420 PA---VARTRFAPLaeatpwrapdsgapRRAGVNAFGFGGINAHVVL 463
Cdd:PRK05952 347 FDlnfVRQAQQSPL--------------QNVLCLSFGFGGQNAAIAL 379
|
|
| Sfp |
COG2091 |
Phosphopantetheinyl transferase [Coenzyme transport and metabolism]; |
1233-1416 |
1.95e-28 |
|
Phosphopantetheinyl transferase [Coenzyme transport and metabolism];
Pssm-ID: 441694 Cd Length: 177 Bit Score: 113.14 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1233 TLSTVDEDGVAVVHERWPDLATRELimRNNLAGAERDAYDA-QPPNRRRQFLLGRIAAKDAARTALwragagEVYPAELA 1311
Cdd:COG2091 1 PLLSTIPGEVHVWFIRLDEEDLDEL--LALLSEDERARAARfRSEKRRRRFLAGRALLRELLARLL------GLPPADLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1312 ITNDATGKPVLRGvhgrdpGGLTVSIAHCRE-VGVGIAATGPCGVDVEEVVARPD-RTVDAACDPAERALLDGLGG-DRA 1388
Cdd:COG2091 73 FAYDPHGKPYLAD------PGLHFSLSHSGGlAAVAVSRGGPVGVDIERIRPRIDlALARRFFSPEERAWLAALPQdDRL 146
|
170 180
....*....|....*....|....*...
gi 1132615381 1389 LWFTRFWAAKEAVAKARGTGLGGRPQSF 1416
Cdd:COG2091 147 EAFTRLWTLKEALLKATGTGLSLPLRAL 174
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
199-463 |
2.30e-28 |
|
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: 119.39 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 199 RLDLRGPAYTVDAACASSLIAVDHAVRELAEGrADVMFAGGVhhchDITL--WSTFSQL--GALS----PSQRIRPFHRG 270
Cdd:cd00832 147 RHGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGV----DSALcpWGWVAQLssGRLStsddPARAYLPFDAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 271 ADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASllnPDPAGQARAVRRAWDAAGLDPRDPDSVgliEA 350
Cdd:cd00832 222 AAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGS---GRPPGLARAIRLALADAGLTPEDVDVV---FA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 351 HGTATPAGDAAELSTLAEVFGP-GTPAAlgSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLHCDDPNPAVArtrfAP 429
Cdd:cd00832 296 DAAGVPELDRAEAAALAAVFGPrGVPVT--APKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG----LD 369
|
250 260 270
....*....|....*....|....*....|....
gi 1132615381 430 LAEATPWRApdsgAPRRAGVNAFGFGGINAHVVL 463
Cdd:cd00832 370 LVTGRPRPA----ALRTALVLARGRGGFNSALVV 399
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
192-463 |
2.42e-28 |
|
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: 115.62 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 192 AASRVANRLDLR-GPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHChditlwstfsqlgalspsqrirpfhrg 270
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 271 adgvLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLnPDPAGQARAVRRAWDAAGLDPRDPDsvgLIEA 350
Cdd:cd00327 99 ----VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPA-VSGEGLARAARKALEGAGLTPSDID---YVEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 351 HGTATPAGDAAELSTLAEVFGPGTPaALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTlhcddpnPAVARTrfapl 430
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRSP-AVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-------PREPRT----- 237
|
250 260 270
....*....|....*....|....*....|...
gi 1132615381 431 aeatpwrapdsgaprrAGVNAFGFGGINAHVVL 463
Cdd:cd00327 238 ----------------VLLLGFGLGGTNAAVVL 254
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
202-462 |
1.82e-27 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 116.76 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 202 LRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDITLWSTFSQLGALS-----PSQRIRPFHRGADGVLI 276
Cdd:PRK08439 151 LKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStrnddPKKASRPFDKDRDGFVM 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 277 AEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDgrSASLLNPDPAGQARAVRRAWDAAGLDPrdpdsVGLIEAHGTATP 356
Cdd:PRK08439 231 GEGAGALVLEEYESAKKRGAKIYAEIIGFGESGD--ANHITSPAPEGPLRAMKAALEMAGNPK-----IDYINAHGTSTP 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 357 AGDAAELSTLAEVFGPGTPAAL-GSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTLH-------CD-DPNPAVARTrf 427
Cdd:PRK08439 304 YNDKNETAALKELFGSKEKVPPvSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINqetpdpeCDlDYIPNVARK-- 381
|
250 260 270
....*....|....*....|....*....|....*
gi 1132615381 428 aplAEATPwrapdsgaprrAGVNAFGFGGINAHVV 462
Cdd:PRK08439 382 ---AELNV-----------VMSNSFGFGGTNGVVI 402
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
12-463 |
2.50e-26 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 115.46 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 12 VAIVGMAALFPGAPDLDAYWRNIAAGTDAITDVpaDRWDPGFFGTgerradrvycRRGGFVDAeVDVAGFgVMPNSVPGT 91
Cdd:PLN02787 131 VVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEI--ERFDCSQFPT----------RIAGEIKS-FSTDGW-VAPKLSKRM 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 92 EPDQLIALHVAAASLADAG--GEAVLPADRERVGVILGR--GGYltpglvrldqrvrtanQVVktlrevvpdldDERVEA 167
Cdd:PLN02787 197 DKFMLYLLTAGKKALADGGitEDVMKELDKTKCGVLIGSamGGM----------------KVF-----------NDAIEA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 168 VRAAFvEQLGPAAPESAiglVPNLAASRVANRLDLRGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHHCHDIT 247
Cdd:PLN02787 250 LRISY-RKMNPFCVPFA---TTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 248 LWSTFSQLGALS-----PSQRIRPFHRGADGVLIAEGTGVVVLKRLADAERDGDRVYAVVSGTGVASDGRSASLLNPDPA 322
Cdd:PLN02787 326 GLGGFVACRALSqrnddPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 323 GQARAVRRAWDAAGLDPRDpdsVGLIEAHGTATPAGDAAELSTLAEVFGPGTPAALGSVKSMIGHAMPAAGIAGLIKAAL 402
Cdd:PLN02787 406 GVILCIEKALAQSGVSKED---VNYINAHATSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQ 482
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1132615381 403 ALHHRVLPPTLHCDDPNPAV-ARTRFAPLAEATPWRAPDSgaprragvNAFGFGGINAHVVL 463
Cdd:PLN02787 483 AIRTGWVHPNINLENPESGVdTKVLVGPKKERLDIKVALS--------NSFGFGGHNSSILF 536
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
607-819 |
1.42e-24 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 105.56 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 607 LRRLGVVPDAVAGHSVGEWTAM-AAGGIHAADEVdafletfdpdSLVV----------PGVAFAVLGMPAAEVLAVLPEH 675
Cdd:smart00827 76 LRSWGVRPDAVVGHSSGEIAAAyVAGVLSLEDAA----------RLVAargrlmqalpGGGAMLAVGLSEEEVEPLLAGV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 676 P-EVVLSHDNAPSQAMVCGPREQVEALVTRMRvQEGVLGRILPFQSGFHTPMLAPYLGPIRDAAQTYTLNPQATPVWSAT 754
Cdd:smart00827 146 PdRVSVAAVNSPSSVVLSGDEDAVDELAARLE-AEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTV 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1132615381 755 TAAPYPAEPEAVRELFVRHLLEPVRFRQLVLAMHDA-GFRTFLQLGAGQ-LGSLVDDTLAGRPHTTV 819
Cdd:smart00827 225 TGTLIDGAELDDADYWVRNLREPVRFADAVRALLAEgGVTVFLEVGPHPvLTGPIKQTLAAAGSAVV 291
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
611-801 |
9.65e-19 |
|
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: 88.29 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 611 GVVPDAVAGHSVGEWTA-MAAGGIHAADEVDAFLETFDPDSLVVP---GVAFAVLGMPAAEVLAVLPEHPE--VVLSHDN 684
Cdd:TIGR00128 81 GLKPDFAAGHSLGEYSAlVAAGALDFETALKLVKKRGELMQEAVPeggGAMAAVIGLDEEQLAQACEEATEndVDLANFN 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 685 APSQAMVCGPREQVEALvtRMRVQEGVLGRILPFQ-SG-FHTPMLAPYLGPIRDAAQTYTLNPQATPVWSATTAAPYpAE 762
Cdd:TIGR00128 161 SPGQVVISGTKDGVEAA--AALFKEMGAKRAVPLEvSGaFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPY-TN 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 1132615381 763 PEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAG 801
Cdd:TIGR00128 238 GDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPG 276
|
|
| ACPS |
pfam01648 |
4'-phosphopantetheinyl transferase superfamily; Members of this family transfers the 4 ... |
1352-1456 |
1.50e-14 |
|
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: 71.10 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1352 PCGVDVEEV-------VARPDRTVDAACDPAERALLDGLGGDRALWFTRFWAAKEAVAKARGTGLGGR--PQSFRVVHAT 1422
Cdd:pfam01648 1 GVGIDIEEIarirrpiERLGERLAERIFTPEERALLASLPAEARRAFARLWTAKEAVFKALGPGLSKLldFDDIEVLLDP 80
|
90 100 110
....*....|....*....|....*....|....
gi 1132615381 1423 AERLRVQVEGAVHVVRVRSAENppglpARDYVVA 1456
Cdd:pfam01648 81 DGRPTLRLLGEAADLAWRFEVL-----AGDYALA 109
|
|
| EntD |
COG2977 |
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites ... |
1263-1404 |
1.96e-14 |
|
4'-phosphopantetheinyl transferase EntD (siderophore biosynthesis) [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442216 [Multi-domain] Cd Length: 205 Bit Score: 73.80 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1263 LAGAERDAYDAQPPNRRRQFLLGRIaakdAARTALWRAGAGEVypaelAITNDATGKPVLrgvhgrdPGGLTVSIAHCRe 1342
Cdd:COG2977 12 LGPPEPAALARAVPKRRAEFLAGRL----CARRALAELGVPPA-----PILIGEDRAPLW-------PAGVVGSISHSD- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1132615381 1343 vGVGIAATGPC------GVDVEEVVA--RPDRTVDAACDPAERALLDGLGG-DRALWFTRFWAAKEAVAKA 1404
Cdd:COG2977 75 -GYAAAVVAPAsdvrglGIDIEPLLDepLAEELLPSILTPAERALLAALSPlPFAHALTLLFSAKESLYKA 144
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
595-798 |
2.38e-14 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 75.97 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 595 AVFQVGRLLDAALRRLGVVPDAVAGHSVGEWTAMAAGGihAADEVDAFLETFDPDSLVVPGV---AFAVLGMPAAEVLAV 671
Cdd:pfam00698 65 ALFAMQIALAALLQSYGVRPDAVVGHSLGEYAAAVVAG--ALSPEEALLAAVLRSRLMMQLAgpgGMAAVELSAEEVEQR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 672 LPehPEVVLSHDNAPSQAMVCGPREQVEALVTRMRvQEGVLGRILPFQSGFHTPMLAPYLGPIRDAAQTYTLNPQATPVW 751
Cdd:pfam00698 143 WP--DDVVGAVVNSPRSVVISGPQEAVRELVERVS-KEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFI 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1132615381 752 SATTAAPYpAEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQL 798
Cdd:pfam00698 220 SSTSIDPS-DQRTLSAEYWVRNLRSPVRFAEAILSAAEPGPLVFIEI 265
|
|
| PS-DH |
pfam14765 |
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ... |
970-1216 |
3.34e-14 |
|
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.
Pssm-ID: 434191 Cd Length: 296 Bit Score: 75.10 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 970 RFDVESMPYLLDHCFFRQPddwpdpadrwpVVPATTVVTHLMRIAEQAVPGTRAVGLRDVRLLKWIVAEP--AAEVPVTA 1047
Cdd:pfam14765 21 RLRLADLPWLRDHRVGGTV-----------VLPGAGYLEMALEAARQLFGGSGAVALRDVSILKALVLPEddPVEVQTSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1048 RVLGPDR---VEVTLVGCS----------QATVELAPAPGAPPAAWPVPDDDRVPERGVEVLYDERW--------MFHGP 1106
Cdd:pfam14765 90 TPEEDGAdswWEFEIFSRAgggwewtlhaTGTVRLAPGEPAAPVDLESLPARCAQPADPRSVSSAEFyerlaargLFYGP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1107 RFQGVAEI-TGIGARHVRGVLTGLAAPG--------ALLDNVGQLFGYWIMAVLP-ERTTVFPVRMERVGFHGSEPvPGE 1176
Cdd:pfam14765 170 AFQGLRRIwRGDGEALAEARLPEAAAGGespyllhpALLDAALQLLGAALPAEAEhADQAYLPVGIERLRIYRSLP-PGE 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1132615381 1177 RLDCLIRITEVTAGTVTADMQLS-RGGVVWAQFTGWTDRRF 1216
Cdd:pfam14765 249 PLWVHARLERRGGRTIVGDLTLVdEDGRVVARIEGLRLRRV 289
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
605-802 |
5.13e-13 |
|
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon subunit of malonate decarboxylase. This subunit has malonyl-CoA/dephospho-CoA acyltransferase activity. Malonate decarboxylase may be a soluble enzyme, or linked to membrane subunits and active as a sodium pump. The epsilon subunit is closely related to the malonyl CoA-acyl carrier protein (ACP) transacylase family described by TIGR00128, but acts on an ACP subunit of malonate decarboxylase that has an unusual coenzyme A derivative as its prothetic group.
Pssm-ID: 132175 Cd Length: 295 Bit Score: 71.57 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 605 AALRRLGVVPDAVAGHSVGEWTA-MAAGGIHAADEVDAFLETFDPDSLVVPGVA--FAVLGMPAAEVLAVLPEHpEVVLS 681
Cdd:TIGR03131 68 RALLALLPRPSAVAGYSVGEYAAaVVAGVLTFDDALRLVALRAALMDQAVPGGYgmLAVLGLDLAAVEALIAKH-GVYLA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 682 HDNAPSQAMVCGPREQVEALVTRMRVQEGVLGRILPFQSGFHTPMLAPYLGPIRDAAQTYTLNPQATPVWSATTAAPYpA 761
Cdd:TIGR03131 147 IINAPDQVVIAGSRAALRAVAELARAAGASRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLV-R 225
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1132615381 762 EPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ 802
Cdd:TIGR03131 226 DAAQIRDDLARQIATPVDWHDCMQAAYERGARLVIELGPGD 266
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
418-488 |
1.58e-08 |
|
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: 54.09 E-value: 1.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1132615381 418 PNP---AVARTRFAPLAEATPWRapdsgaPRRAGVNAFGFGGINAHVVLTEPAPARVEVVEPVRVLRLAAATPR 488
Cdd:pfam16197 1 PNPdipALLDGRLKVVTEPTPWP------GGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRLVLLSGR 68
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
615-802 |
5.01e-07 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 53.61 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 615 DAVAGHSVGEWTAMA-AGGI---HAADEVDAFLETFDPDSLVVPGVAFAVLGMPAAEVLAVLPE-----HPEVVLSHDN- 684
Cdd:PLN02752 126 DVCAGLSLGEYTALVfAGALsfeDGLKLVKLRGEAMQAAADAGPSGMVSVIGLDSDKVQELCAAaneevGEDDVVQIANy 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 685 -APSQAMVCGPR---EQVEALVT----RMRVQEGVLGrilpfqsGFHTPMLAPYLGPIRDAAQTYTLNPQATPVWSATTA 756
Cdd:PLN02752 206 lCPGNYAVSGGKkgiDAVEAKAKsfkaRMTVRLAVAG-------AFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDA 278
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1132615381 757 APYpAEPEAVRELFVRHLLEPVRFRQLVLAMHDAGFRTFLQLGAGQ 802
Cdd:PLN02752 279 QPH-SDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGK 323
|
|
| pantethn_trn |
TIGR00556 |
phosphopantetheine--protein transferase domain; This model models a domain active in ... |
1351-1434 |
3.27e-06 |
|
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: 47.82 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1351 GPCGVDVEEV------VARPDRTVDAACDPAERALLDGL-GGDRALWFTRFWAAKEAVAKARGTGLGGRPQSFRVVHATA 1423
Cdd:TIGR00556 3 VGIGIDIVEIkriaeqIERSGTFAERFFTPSEIEDYCKLsPKSQTESLAGRWAAKEAFIKALGKGISLGELLFTDIEIVK 82
|
90
....*....|....
gi 1132615381 1424 ERL---RVQVEGAV 1434
Cdd:TIGR00556 83 DLKgapRVCLIGEA 96
|
|
| PRK10251 |
PRK10251 |
enterobactin synthase subunit EntD; |
1274-1444 |
1.63e-05 |
|
enterobactin synthase subunit EntD;
Pssm-ID: 182334 [Multi-domain] Cd Length: 207 Bit Score: 47.55 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1274 QPPNRRRQ--FLLGRIAAKDAARTALWRA--GAGEVYpaelaitndatgKPVLrgvhgrdPGGLTVSIAHCREVGVGIAA 1349
Cdd:PRK10251 43 QHAGRKRKaeHLAGRIAAVYALREYGYKCvpAIGELR------------QPVW-------PAGVYGSISHCGTTALAVVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1350 TGPCGVDVEEVVARPDRT--VDAACDPAERALLDGLGGDRALWFTRFWAAKEAVAKARGTGLGGRPQSFRVVHATAERLR 1427
Cdd:PRK10251 104 RQPIGIDIEEIFSAQTATelTDNIITPAEHERLADCGLAFPLALTLAFSAKESAFKASEIQTLAGFLDYQIISWNKQQII 183
|
170
....*....|....*..
gi 1132615381 1428 VQVEGAVHVVRVRSAEN 1444
Cdd:PRK10251 184 IHRENEFFAVHWQIKEK 200
|
|
| AcpS |
COG0736 |
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism]; |
1354-1436 |
6.12e-05 |
|
Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid transport and metabolism];
Pssm-ID: 440499 [Multi-domain] Cd Length: 122 Bit Score: 43.96 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 1354 GVDV------EEVVARP-DRTVDAACDPAERALLDGLGgDRALWFTRFWAAKEAVAKARGTGLG---------------G 1411
Cdd:COG0736 3 GIDIveiariERALERHgERFLERVFTPAERAYCQSRK-RPAEFLAGRFAAKEAVSKALGTGIGkgvswrdievlndpsG 81
|
90 100
....*....|....*....|....*
gi 1132615381 1412 RPQsFRVVHATAERLRVQVEGAVHV 1436
Cdd:COG0736 82 KPT-VRLSGRAAELAAELGITRIHL 105
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
205-242 |
6.18e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 47.02 E-value: 6.18e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1132615381 205 PAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHH 242
Cdd:PRK06445 87 PAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEH 124
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
205-240 |
1.10e-04 |
|
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: 46.21 E-value: 1.10e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1132615381 205 PAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGV 240
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGV 115
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
205-240 |
2.06e-04 |
|
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: 45.55 E-value: 2.06e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1132615381 205 PAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGV 240
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGV 111
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
205-242 |
3.74e-04 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 44.53 E-value: 3.74e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1132615381 205 PAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGVHH 242
Cdd:TIGR01930 75 PAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVES 112
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
178-240 |
6.66e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 43.85 E-value: 6.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1132615381 178 PAAPESAIGLVpnlaasrVANRLDL--RGPAYTVDAACASSLIAVDHAVRELAEGRADVMFAGGV 240
Cdd:PRK08170 59 PSPDEANIARV-------VALRLGCgeKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGV 116
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
165-345 |
7.66e-04 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 43.79 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 165 VEAVRAAFVE-QLGPAAPESAI------GLVPNLAASRVANRLDLRG-PAYTVDAACASSLIAVDHAVRELAEGRADVMF 236
Cdd:cd00829 21 AEAARAALDDaGLEPADIDAVVvgnaagGRFQSFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 237 AGGVHHCHDITLWSTF-SQLGALSPSQRIRPF---------------------------------HRGA----------- 271
Cdd:cd00829 101 VVGAEKMSDVPTGDEAgGRASDLEWEGPEPPGgltppalyalaarrymhrygttredlakvavknHRNAarnpyaqfrkp 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 272 -------------------DGVLIAEGTGVVVLKRLADAERDGDRvYAVVSGTGVASDGRSAS--LLNPDPAGQARAVRR 330
Cdd:cd00829 181 itvedvlnsrmiadplrllDCCPVSDGAAAVVLASEERARELTDR-PVWILGVGAASDTPSLSerDDFLSLDAARLAARR 259
|
250
....*....|....*
gi 1132615381 331 AWDAAGLDPRDPDSV 345
Cdd:cd00829 260 AYKMAGITPDDIDVA 274
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
143-240 |
2.84e-03 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 41.91 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 143 VRTANQVVKTLREV---VPDLDDERVEAVRAafveqlGPAAPESAIGLvpNLAasRVAnrLDLRG-----PAYTVDAACA 214
Cdd:PRK09052 29 TRPDDLLAHVLRSAvaqVPGLDPKLIEDAIV------GCAMPEAEQGL--NVA--RIG--ALLAGlpnsvGGVTVNRFCA 96
|
90 100
....*....|....*....|....*.
gi 1132615381 215 SSLIAVDHAVRELAEGRADVMFAGGV 240
Cdd:PRK09052 97 SGLQAVAMAADRIRVGEADVMIAAGV 122
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
207-240 |
3.30e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 41.53 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|....
gi 1132615381 207 YTVDAACASSLIAVDHAVRELAEGRADVMFAGGV 240
Cdd:PRK06366 82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGM 115
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
214-453 |
8.77e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 40.32 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 214 ASSLIAVDHAVRELAEGRADVMFAGGVHHCH--DITLWSTFSQL---GALSPSQRIRPFHRGadGVLIAEGTGVVVLKRL 288
Cdd:PRK06519 176 SAGVSAIEIAFARIASGQSDHALVGGAYNAErpDMLLLYELGGLllkGGWAPVWSRGGEDGG--GFILGSGGAFLVLESR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 289 ADAERDGDRVYAVVSGtgVASDgRSASllnpDPAGQARAVRRAWDAAGLDPRDpdsvGLIEAHGTATPAGDAAELSTLAE 368
Cdd:PRK06519 254 EHAEARGARPYARISG--VESD-RARR----APGDLEASLERLLKPAGGLAAP----TAVISGATGAHPATAEEKAALEA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132615381 369 VFgpgtPAALGSVKSMIGHAMPAAGIAGLIKAALALHHRVLPPTlhcddpnpavartrFAPLAEatpwrAPDSGAPRRAG 448
Cdd:PRK06519 323 AL----AGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPP--------------FDASGE-----KPMSGAAREAV 379
|
....*
gi 1132615381 449 VNAFG 453
Cdd:PRK06519 380 VTTVG 384
|
|
| |
