|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
34-1427 |
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: 1134.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 34 TEPVAIIGMSCRFPGgVRSPEQLWDLVAAGGDAMAPFPDDRgWHLDALYDTDPASRGTSYVREGGFLPDAGDFDPAFFGI 113
Cdd:COG3321 3 DEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADR-WDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 114 SPREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQgDYAALLAGVGGGVEGYLGTGSAAAVASGRISY 193
Cdd:COG3321 81 SPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSN-DYALLLLADPEAIDAYALTGNAKSVLAGRISY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 194 ALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAAADGTGWSE 273
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 274 GVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPI 353
Cdd:COG3321 240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 354 EAQALLATYGRQRPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDWSAGAVTLLTGTTP 433
Cdd:COG3321 320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 434 WPATGRPRRAGVSAFGVSGTNAHTIVEQADPADagtARPAGTPAPAGPWIVSARSAPALAGQARRLLAHLAAHPELRPAD 513
Cdd:COG3321 400 WPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAA---PAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 514 VAYSLVTTRAALPHRAVVTGDDADALRAGLRAVAEDAAHPHVVRGVARPAGKLAVLFTGQGAQRPGMGAELHRRFPVFAA 593
Cdd:COG3321 477 VAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 594 AFDEVAAELDRHLTHPLREVVFaaaGTPQAALLDRTEFTQPALFAYEVAAYRLVTAWGLRPQQLLGHSVGELAAAHVAGV 673
Cdd:COG3321 557 ALDECDALLRPHLGWSLREVLF---PDEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 674 LSLADAAALVAARGRLMQALPEGGAMLAVRATEAEVTPLLGA--GVALAAVNGPTSVVLSGDADAVLAAGDRLTAQGRQV 751
Cdd:COG3321 634 LSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAGydGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRA 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 752 RRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGAVLTaAEATDPGYWVDHVRDTVRFHAGMATLAAAGAG 831
Cdd:COG3321 714 RRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLT-GEALDADYWVRHLRQPVRFADAVEALLADGVR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 832 TFLELGPDGALTALARECLPDAEAAAFVPVGRRDQPEAATLLAALAAVDLRGAGVDWAALFAGTDATRVELPTYAFDHQr 911
Cdd:COG3321 793 VFLEVGPGPVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGRRRVPLPTYPFQRE- 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 912 yWPEPVVLDLDPRPAADTADGEFWAAVESDEPAALAAVLGVDAERGAALADLLPALAAYRGRRRRRDELDALRYRGTWTR 991
Cdd:COG3321 872 -DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 992 VDPPPAVAPAGACLVVADPDAATGTLLAALAAAGLSPVRVSPDDLPAAVAGATPALVLSLLAVDTTSRDGGVAGPLAGTA 1071
Cdd:COG3321 951 AAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAA 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1072 TLVRVLADAGCTAPVWCVTRGAVAVDADDAAPDVAGACLWGLGRVLALEAPRLWGGLVDLPADPDAAAYAALARAVTGDG 1151
Cdd:COG3321 1031 AAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLA 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1152 GEDQLAVRAGGLHARRLERAPTGPASDEDWRPRGAVLVHGTAAVRAPHLLRRLAEHGAPHLLLAGPDAPADLGVEVTVLD 1231
Cdd:COG3321 1111 LLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALA 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1232 DPAALPAALDRLAAAGTPVRTVVHVADSGGAGDPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWG 1311
Cdd:COG3321 1191 GLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAG 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1312 SGGAAVTAATGAGLAALAAHRRAAGRPATVLAWVPWADEVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVD 1391
Cdd:COG3321 1271 LAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAA 1350
|
1370 1380 1390
....*....|....*....|....*....|....*.
gi 1215099124 1392 WPTFTPAFTAVRPSALLRGVPEAVVEPSGRDGAEPA 1427
Cdd:COG3321 1351 AAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
35-459 |
0e+00 |
|
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: 628.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 35 EPVAIIGMSCRFPGGVrSPEQLWDLVAAGGDAMAPFPDDRGWHldALYDTDPASRGTSYVREGGFLPDAGDFDPAFFGIS 114
Cdd:cd00833 1 EPIAIVGMACRFPGAA-DPDEFWENLLEGRDAISEIPEDRWDA--DGYYPDPGKPGKTYTRRGGFLDDVDAFDAAFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 115 PREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQgDYAALLAGVGGGVEGYLGTGSAAAVASGRISYA 194
Cdd:cd00833 78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSS-DYLELLARDPDEIDAYAATGTSRAFLANRISYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 195 LGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAAADGTGWSEG 274
Cdd:cd00833 157 FDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 275 VGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPIE 354
Cdd:cd00833 237 VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 355 AQALLATYGRQRPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDWSAGAVTLLTGTTPW 434
Cdd:cd00833 317 VEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPW 396
|
410 420
....*....|....*....|....*
gi 1215099124 435 PATGRPRRAGVSAFGVSGTNAHTIV 459
Cdd:cd00833 397 PAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
37-461 |
3.99e-173 |
|
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: 525.36 E-value: 3.99e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 37 VAIIGMSCRFPGgVRSPEQLWDLVAAGgdamapfpddrgwhldalydtdpasrgtsyvreggfLPDAGDFDPAFFGISPR 116
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------------------LDDVDLFDAAFFGISPR 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 117 EALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQgDYAallagvgggvegylgtgsaaavasgrisyalg 196
Cdd:smart00825 44 EAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSS-DYS-------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 197 legpaVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAAADGTGWSEGVG 276
Cdd:smart00825 91 -----VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 277 MLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQrrvitqalanaglsadeidvveahgtgttlgdpieaq 356
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 357 allatygrqrpadrpLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDWSAGAVTLLTGTTPWPA 436
Cdd:smart00825 209 ---------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPP 273
|
410 420
....*....|....*....|....*
gi 1215099124 437 TGRPRRAGVSAFGVSGTNAHTIVEQ 461
Cdd:smart00825 274 PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
37-915 |
1.71e-171 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 565.70 E-value: 1.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 37 VAIIGMSCRFPGGVRSPEQLWDLVAAGGDAMAPFPDDRgWhldALYDTDP--ASRGTSYVREGGFLPDAGDFDPAFFGIS 114
Cdd:NF040607 102 IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGR-W---SEFAADPriAERVAKANTRGGYLDDIKGFDAEFFALS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 115 PREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQgDYAALLAGVGGGVEGYLGTGSAAAVASGRISYA 194
Cdd:NF040607 178 PLEAENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNN-DYQMLAVADPAEAHPYALTGTSSSIIANRVSYF 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 195 LGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRG-LATDGRCKSFAAAADGTGWSE 273
Cdd:NF040607 257 FDFRGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDELGGvLAPDGRIKAFSSDADGMVRSE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 274 GVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPI 353
Cdd:NF040607 337 GGGVVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPI 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 354 EAQALLATYGRQRPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDWSAGAVTLLTGTTP 433
Cdd:NF040607 417 EADALGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 434 WPA-TGRPrRAGVSAFGVSGTNAHTIVEQADPADAGTAR----------PAGTPAPAGPWIVSARSAPALAGQA------ 496
Cdd:NF040607 497 WPRySGHA-VAGVSGFGFGGTNAHVVVREVLPADLVEPEaqpdedteaeLAGLTAEAKRLLAEAELAAEFAPAApegpvv 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 497 ------------RRLLAHLAAHPElRPADVAYSLVTTRAALPH------RAVVTGDDADALRAGLRAVAEDAAHPHVVRG 558
Cdd:NF040607 576 plpvsgflpsrrRAAAADLADWLE-SEEGRATPLADVARALARrnhgrsRAVVLAHTHEEAIKGLRAVAEGKPGPGVFSA 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 559 VArPAGKLAV-LFTGQGAQRPGMGAELHRRFPVFAAAFDEVAAELDRHLTHPLREVVFAAAGTPQaalldrTEFTQPALF 637
Cdd:NF040607 655 DA-PAANGPVwVLSGFGSQHRKMAKQLYLENPVFAARIDEVDELVQDESGYSIVELILDDEQTYD------IETAQVGIF 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 638 AYEVAAYRLVTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLM----QALPEG--GAMLAVRATEAEVTP 711
Cdd:NF040607 728 AIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMgegeAMLPGDdiRLMALVEYSAEEIET 807
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 712 LLG--AGVALAAVNGPTSVVLSGDADAVLAAGDRLTAQGRQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLV 789
Cdd:NF040607 808 VLAdfPDLEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTSQMDPLLGELAAELAGIEPQPLTVGLY 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 790 S--DRtGAVLTAAEAT--DPGYWVDHVRDTVRFHAGMATLAAAGAGTFLELGPDG------ALTALAREcLPDAEaaaFV 859
Cdd:NF040607 888 SsvDR-GTFYRPGHEPihDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPvalmsvAATTFAAG-LHDAQ---LI 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1215099124 860 PVGRRDQPEAATLLAALAAVDLRGAGVDWAALFagTDATRVELPTYAFDHQRYWPE 915
Cdd:NF040607 963 PTLKRKEDESESVLNALAQLYVHGHDVDLRSLF--GAGDYADIPRTRFKRKPYWLD 1016
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
569-865 |
1.04e-104 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 337.07 E-value: 1.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 569 LFTGQGAQRPGMGAELHRRFPVFAAAFDEVAAELDRHLTHPLREVVFaaaGTPQAALLDRTEFTQPALFAYEVAAYRLVT 648
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLL---GEDGAASLLDTEVAQPALFAVQVALARLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 649 AWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLMQALPEGGAMLAVRATEAEVTPLL---GAGVALAAVNGP 725
Cdd:smart00827 78 SWGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLagvPDRVSVAAVNSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 726 TSVVLSGDADAVLAAGDRLTAQGRQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGAVLTAAEATDP 805
Cdd:smart00827 158 SSVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215099124 806 GYWVDHVRDTVRFHAG-MATLAAAGAGTFLELGPDGALTALARECLPDAEAAAFVPVGRRD 865
Cdd:smart00827 238 DYWVRNLREPVRFADAvRALLAEGGVTVFLEVGPHPVLTGPIKQTLAAAGSAVVLPSLRRG 298
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
36-854 |
4.37e-102 |
|
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: 365.87 E-value: 4.37e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 36 PVAIIGMSCRFpGGVRSPEQLWDLVAAGGDAMAPFPDDRgWHLDALYDTDPASRGTSYVREGGFLPDAgDFDPAFFGISP 115
Cdd:TIGR02813 8 PIAIVGMASIF-ANSRYLNKFWDLIFEKIDAITDVPSDH-WAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 116 REALAMDPQQRLLLETAWEAFERAGIDPTTLR---GAPTGVYAATSSQGDYAALLAG-------VGGGVE---------- 175
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGLPDGYDRdkiGITLGVGGGQKQSSSLNARLQYpvlkkvfKASGVEdedsemlikk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 176 ---GYLG------TGSAAAVASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVE 246
Cdd:TIGR02813 165 fqdQYIHweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 247 FSRQRGLATDGRCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQA 326
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 327 LANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGRQRPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLP 406
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 407 PTLHVDAPTPHVDWSAGAVTLLTGTTPWPA--TGRPRRAGVSAFGVSGTNAHTIVEQADPADAGTARPAGTPAPAgPWIV 484
Cdd:TIGR02813 405 PTINVDQPNPKLDIENSPFYLNTETRPWMQreDGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQ-TLLF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 485 SARSAPALAGQARRLLAHLAAHPELRPAD-----VAYSLVTTRAALPHRAVVTGDDADALRAGLRAV----AEDAAHPHV 555
Cdd:TIGR02813 484 TAANEKALVSSLKDWKNKLSAKADDQPYAfnalaVENTLRTIAVALARLGFVAKNADELITMLEQAItqleAKSCEEWQL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 556 VRGVA-------RPAGKLAVLFTGQGAQRPGMGAELHRRFPVFAAAFDEVAAELDRHLTHPLREVVFA------AAGTPQ 622
Cdd:TIGR02813 564 PSGISyrksalvVESGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTQAGKGALSPVLYPipvfndESRKAQ 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 623 AALLDRTEFTQPALFAYEVAAYRLVTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLMQALPEGGA---- 698
Cdd:TIGR02813 644 EEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAPTGEADigfm 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 699 ---MLAVRATEAEVTPLLGA--GVALAAVNGPTSVVLSGDADAVLAAGDRLTAQGRQVRRLRVSHAFHSARMDAVLADFR 773
Cdd:TIGR02813 724 yavILAVVGSPTVIANCIKDfeGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQKPFS 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 774 VVAEKVTWHPPTLPLVSDRTGAVLTAAEATDPGYWVDHVRDTVRFHAGMATLAAAGAGTFLELGPDGALTALARECLPDA 853
Cdd:TIGR02813 804 AAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENTLKDK 883
|
.
gi 1215099124 854 E 854
Cdd:TIGR02813 884 E 884
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
35-286 |
1.32e-97 |
|
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: 314.96 E-value: 1.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 35 EPVAIIGMSCRFPGGVrSPEQLWDLVAAGGDAMAPFPDDRgWHLDALYDTDPASRGTSYVREGGfLPDAGDFDPAFFGIS 114
Cdd:pfam00109 1 EPVAIVGMGCRFPGGN-DPEEFWENLLEGRDGISEIPADR-WDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 115 PREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSqGDYAAL--LAGVGGGVEGY-LGTGSAAAVASGRI 191
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGI-GDYAALllLDEDGGPRRGSpFAVGTMPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 192 SYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAAADGTGW 271
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVR 236
|
250
....*....|....*
gi 1215099124 272 SEGVGMLLVERLSDA 286
Cdd:pfam00109 237 GEGVGAVVLKRLSDA 251
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1601-1811 |
1.49e-77 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 255.61 E-value: 1.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1601 VCCCTMSLLSGPHEYARVAAGFRGRRDVWALPNPGFGVGEELPADLPALLRVHADTVRRTVGDGPFVLAGHSGGAMVANV 1680
Cdd:smart00824 1 ICFPSTAAPSGPHEYARLAAALRGRRDVSALPLPGFGPGEPLPASADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLAHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1681 LARELERQGRPPAAVVLMDTYPADSEVLGGWTSQLLDGMVERDSAYTPMDDYRTTAWAGYLPLFLDWQPAPMDAATLLVR 1760
Cdd:smart00824 81 VAARLEARGIPPAAVVLLDTYPPGDPAPEGWLPELLRGVFEREDSFVPMDDARLTAMGAYLRLFGGWTPGPVAAPTLLVR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1215099124 1761 ASRPLGEWTGE-PDGWRSRWPYPHEAVDAAGDHFTMVGERGPELAATVDEWL 1811
Cdd:smart00824 161 ASEPLAEWPDEdPDGWRAHWPLPHTVVDVPGDHFTMMEEHAAATARAVHDWL 212
|
|
| KR_1_SDR_x |
cd08952 |
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
978-1414 |
1.10e-72 |
|
ketoreductase (KR), subgroup 1, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the single KR domain of SpiF, the first KR domains of SpiE,-G,H,-I,and #J, the third KR domain of SpiG, and the second KR domain of SpiH. The second KR domains of SpiE,-G, I, and #J, and the KR domains of SpiD, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187655 [Multi-domain] Cd Length: 480 Bit Score: 252.09 E-value: 1.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 978 DELDALRYRGTWTRVDPPPAVAPAGACLVVA---DPDAATGTLLAALAAAGLSPVRVSPDD----------LPAAVAGAT 1044
Cdd:cd08952 9 AAVDSWRYRVTWRPLPDPPAARLTGTWLVVVpagADDALAAAVARALAAAGAEVVVLEVDAadadaaaaaaLAAAAAGGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1045 PALVLSLLAVDTTSRDG--GVAGPLAGTATLVRVLADAGCTAPVWCVTRGAVAVDADDAAPDVAGACLWGLGRVLALEAP 1122
Cdd:cd08952 89 VAGVLSLLALDERPHPDhpAVPAGLAATLALVQALGDAGVDAPLWCVTRGAVAVGPDDPLPDPAQAAVWGLGRVAALEHP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1123 RLWGGLVDLPADPDAAAYAALARAVTGDGGEDQLAVRAGGLHARRLERAPTGPASDEDWRPRGAVLVHGTAAVRAPHLLR 1202
Cdd:cd08952 169 DRWGGLVDLPADLDARALRRLAAVLAGAGGEDQVAVRASGVFARRLVRAPAPAPAARPWRPRGTVLVTGGTGALGAHVAR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1203 RLAEHGAPHLLLA---GPDAP---------ADLGVEVTV----LDDPAALPAALDRLaAAGTPVRTVVHVADSGGAGdPV 1266
Cdd:cd08952 249 WLARRGAEHLVLTsrrGPDAPgaaelvaelTALGARVTVaacdVADRDALAALLAAL-PAGHPLTAVVHAAGVLDDG-PL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1267 TATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAGLAALAAHRRAAGRPATVLAWVP 1346
Cdd:cd08952 327 DDLTPERLAEVLRAKVAGARHLDELTRDRDLDAFVLFSSIAGVWGSGGQGAYAAANAYLDALAERRRARGLPATSVAWGP 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215099124 1347 WAD----EVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVDWPTFTPAFTAVRPSALLRGVPEA 1414
Cdd:cd08952 407 WAGggmaAGAAAERLRRRGLRPMDPELALAALRRALDHDETAVVVADVDWERFAPAFTAARPSPLLDELPEA 478
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
36-455 |
1.37e-61 |
|
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: 217.02 E-value: 1.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 36 PVAIIGMSCRFPGGVrSPEQLWDLVAAGGDAMAPFPDDRgwhldalydtdpasRGTSYVREGGFLPDagdfDPAFFGISP 115
Cdd:cd00834 2 RVVITGLGAVTPLGN-GVEEFWEALLAGRSGIRPITRFD--------------ASGFPSRIAGEVPD----FDPEDYLDR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 116 REALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSS------QGDYAALLAGVGGGVEGYLGTGSAAAVASG 189
Cdd:cd00834 63 KELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSGIgglatiEEAYRALLEKGPRRVSPFFVPMALPNMAAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 190 RISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDG-----RCKSFAA 264
Cdd:cd00834 143 QVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNddpekASRPFDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 265 AADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHG 344
Cdd:cd00834 223 DRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 345 TGTTLGDPIEAQALLATYGrqrPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDwsaga 424
Cdd:cd00834 303 TSTPLNDAAESKAIKRVFG---EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD----- 374
|
410 420 430
....*....|....*....|....*....|..
gi 1215099124 425 vtllTGTTPWPATGRPRRAGVS-AFGVSGTNA 455
Cdd:cd00834 375 ----LDYVPNEAREAPIRYALSnSFGFGGHNA 402
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
124-459 |
5.46e-58 |
|
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: 204.41 E-value: 5.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 124 QQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSqGDYAALLAGVGG--GVEGYLGTGSAAAVASGRISYALGLEGPA 201
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGG-GSPRFQVFGADAmrAVGPYVVTKAMFPGASGQIATPLGIHGPA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 202 VTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAAADGTGWSEGVGMLLVE 281
Cdd:cd00825 90 YDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 282 RLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPIEAQALLAT 361
Cdd:cd00825 170 ELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 362 YGrqrpaDRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDWSAGAVTlltgttpwpaTGRPR 441
Cdd:cd00825 250 FG-----DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETT----------PRELR 314
|
330
....*....|....*...
gi 1215099124 442 RAGVSAFGVSGTNAHTIV 459
Cdd:cd00825 315 TALLNGFGLGGTNATLVL 332
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
564-857 |
5.69e-58 |
|
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: 203.05 E-value: 5.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 564 GKLAVLFTGQGAQRPGMGAELHRRFPVFAAAFDEVAAELDRhlthPLREVVFAAAgtpqAALLDRTEFTQPALFAYEVAA 643
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGY----DLSALCFEGP----EEELNLTENTQPAILAASVAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 644 YRLVTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLMQ-ALPEG-GAMLAVR-ATEAEVTPLL-----GA 715
Cdd:COG0331 73 YRALEEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQeAVPAGpGGMAAVLgLDDEEVEALCaeaaqGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 716 GVALAAVNGPTSVVLSGDADAVLAAGDRLTAQG-RQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTG 794
Cdd:COG0331 153 VVEIANYNSPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215099124 795 AVLTAAEATdPGYWVDHVRDTVRFHAGMATLAAAGAGTFLELGPDGALTALARECLPDAEAAA 857
Cdd:COG0331 233 APVTDPEEI-RELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRIDPGVEVLA 294
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
105-455 |
4.68e-57 |
|
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: 204.17 E-value: 4.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 105 DFDPAFFgISPREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQG------DYAALLAGVGGGVEGYL 178
Cdd:COG0304 53 DFDPEEY-LDRKELRRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGldtleeAYRALLEKGPRRVSPFF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 179 GTGSAAAVASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLAT--- 255
Cdd:COG0304 132 VPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrnd 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 256 --DGRCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLS 333
Cdd:COG0304 212 dpEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 334 ADEIDVVEAHGTGTTLGDPIEAQALLATYGrqrPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDA 413
Cdd:COG0304 292 PEDIDYINAHGTSTPLGDAAETKAIKRVFG---DHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLEN 368
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1215099124 414 PTPHVDwsagaVTLLTGTtpwpATGRPRRAGVS-AFGVSGTNA 455
Cdd:COG0304 369 PDPECD-----LDYVPNE----AREAKIDYALSnSFGFGGHNA 402
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
294-412 |
1.25e-51 |
|
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: 177.38 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 294 LAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGRQRPaDRPLL 373
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR-KQPLA 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1215099124 374 LGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVD 412
Cdd:pfam02801 80 IGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
35-459 |
1.05e-44 |
|
"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: 168.00 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 35 EPVAIIGMSCRFPGG--VRSPEQLWDLVAAGGDAMAPFPddrgwhldalydtdpASRGTSYVREGGFLPDaGDFDPAFfg 112
Cdd:cd00828 1 SRVVITGIGVVSPHGegCDEVEEFWEALREGRSGIAPVA---------------RLKSRFDRGVAGQIPT-GDIPGWD-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 113 isPREALAMDPQQRLLLETAWEAFERAGI-DPTTLRGAPTGVYAaTSSQGDYAAL---LAGVGGGVEGYLGTG--SAAAV 186
Cdd:cd00828 63 --AKRTGIVDRTTLLALVATEEALADAGItDPYEVHPSEVGVVV-GSGMGGLRFLrrgGKLDARAVNPYVSPKwmLSPNT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 187 ASGRISYALGLE-GPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMaTPTVFVEFSRQRGLATD-----GRCK 260
Cdd:cd00828 140 VAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALSTAeeepeEMSR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 261 SFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPnGPSQRRVITQALANAGLSADEIDVV 340
Cdd:cd00828 219 PFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 341 EAHGTGTTLGDPIEAQALLATYGrqrPADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDw 420
Cdd:cd00828 298 SAHGTSTPANDVAESRAIAEVAG---ALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVE- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1215099124 421 sagavTLLTGTTPWPATGRPRRAGVSAFGVSGTNAHTIV 459
Cdd:cd00828 374 -----HLSVVGLSRDLNLKVRAALVNAFGFGGSNAALVL 407
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
569-867 |
9.92e-43 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 159.56 E-value: 9.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 569 LFTGQGAQRPGMGAELHRRFPVFAAAFDE----VAAELDRHLTHPLREvvfaaagtPQAALLDRTEFTQPALFAYEVAAY 644
Cdd:pfam00698 3 VFSGQGSQWAGMGMQLLKTSPAFAAVIDRadeaFKPQYGFSVSDVLRN--------NPEGTLDGTQFVQPALFAMQIALA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 645 RLVTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLMQALPEGGAMLAVRATEAEVTPLLGAGVALAAVNG 724
Cdd:pfam00698 75 ALLQSYGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPDDVVGAVVNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 725 PTSVVLSGDADAVLAAGDRLTAQGRQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGAVLTAAEaTD 804
Cdd:pfam00698 155 PRSVVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRT-LS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215099124 805 PGYWVDHVRDTVRFHAGMATLAAAGAGTFLELGPDGALTALARECL---PDAEAAAFVPVGRRDQP 867
Cdd:pfam00698 234 AEYWVRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLksaSDGKVATLVGTLIRDQT 299
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
187-455 |
2.02e-34 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 138.29 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 187 ASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLAT------DGRCK 260
Cdd:PTZ00050 147 AAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkynddpQRASR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 261 SFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAG-LSADEIDV 339
Cdd:PTZ00050 227 PFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDY 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 340 VEAHGTGTTLGDPIEAQALLATYGRQrpADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVD 419
Cdd:PTZ00050 307 VNAHATSTPIGDKIELKAIKKVFGDS--GAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD 384
|
250 260 270
....*....|....*....|....*....|....*..
gi 1215099124 420 wsagaVTLLTGTTPWPATGrpRRAGVS-AFGVSGTNA 455
Cdd:PTZ00050 385 -----LNLVQGKTAHPLQS--IDAVLStSFGFGGVNT 414
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
152-459 |
3.98e-34 |
|
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: 132.57 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 152 GVYAATSSQGDYAALLAGVGGGVEGYLGTGSAAAVASGRISYALGL-EGPAVTVDTACSSSLVALHLACQALRLGECTLA 230
Cdd:cd00327 11 GFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIsGGPAYSVNQACATGLTALALAVQQVQNGKADIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 231 LAGGVSVMATptvfvefsrqrglatdgrcksfaaaadgtgwSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSG 310
Cdd:cd00327 91 LAGGSEEFVF-------------------------------GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 311 lTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGrqrpaDRPLLLGSVKSNIGHTQAAAGV 390
Cdd:cd00327 140 -PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDG-----VRSPAVSATLIMTGHPLGAAGL 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215099124 391 AGVIKMVLAMRHGVLPPTlhvdaptphvdwsagavtlltgttpwpaTGRPRRAGVSAFGVSGTNAHTIV 459
Cdd:cd00327 214 AILDELLLMLEHEFIPPT----------------------------PREPRTVLLLGFGLGGTNAAVVL 254
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
565-853 |
4.82e-33 |
|
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: 130.67 E-value: 4.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 565 KLAVLFTGQGAQRPGMGAELHRRFPVFAAAFDEVaaelDRHLTHPLREVVFAAagtpQAALLDRTEFTQPALFAYEVAAY 644
Cdd:TIGR00128 2 KIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQA----SEALGYDLKKLCQEG----PAEELNKTQYTQPALYVVSAILY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 645 RL-VTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLMQ-ALPEG-GAMLAVRATEAE-VTPLLG----AG 716
Cdd:TIGR00128 74 LKlKEQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQeAVPEGgGAMAAVIGLDEEqLAQACEeateND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 717 VALAAVNGPTSVVLSGDADAVLAAGDRLTAQG-RQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGA 795
Cdd:TIGR00128 154 VDLANFNSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215099124 796 VLT-AAEATDPgyWVDHVRDTVRFHAGMATLAAAGAGTFLELGPDGALTALARECLPDA 853
Cdd:TIGR00128 234 PYTnGDRIKEK--LSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRIKNDL 290
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
103-416 |
9.00e-33 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 133.22 E-value: 9.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 103 AGDFDpaFFGISPREALAMdpQQRLLLETAWEAFERAGIDPTTLRG-----AP-----------TGVYAATSSQGDYAAL 166
Cdd:PRK06501 58 AGTVD--FLPESPFGASAL--SEALARLAAEEALAQAGIGKGDFPGplflaAPpvelewparfaLAAAVGDNDAPSYDRL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 167 LAGVGGGV-EGYLGTGSAAAVASgRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFV 245
Cdd:PRK06501 134 LRAARGGRfDALHERFQFGSIAD-RLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 246 EFSRQRGLAT-----DGRCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQR 320
Cdd:PRK06501 213 RFSLLSALSTqndppEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 321 RVITQALANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGrQRPADRPllLGSVKSNIGHTQAAAGVAGVIKMVLAM 400
Cdd:PRK06501 293 GAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFG-ERLASIP--VSSNKSMIGHTLTAAGAVEAVFSLLTI 369
|
330
....*....|....*.
gi 1215099124 401 RHGVLPPTLHVDAPTP 416
Cdd:PRK06501 370 QTGRLPPTINYDNPDP 385
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
187-455 |
1.26e-32 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 133.38 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 187 ASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLAT------DGRCK 260
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfnscpTEASR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 261 SFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVV 340
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 341 EAHGTGTTLGDPIEAQALLATYGRQRPADRpLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPhvdw 420
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATSGG-LAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP---- 397
|
250 260 270
....*....|....*....|....*....|....*..
gi 1215099124 421 sagavTLLTGTTPWPATGR-PRRAGVS-AFGVSGTNA 455
Cdd:PLN02836 398 -----IFDDGFVPLTASKAmLIRAALSnSFGFGGTNA 429
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
94-419 |
6.40e-32 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 130.68 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 94 VREGGFLPDagdFDPAFFgISPREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATssqgdyaallaGVGGG 173
Cdd:PRK07314 46 VKIAGEVKD---FNPDDY-MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIGS-----------GIGGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 174 ---VEGYL-----GT---------GSAAAVASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVS 236
Cdd:PRK07314 111 etiEEQHItllekGPrrvspffvpMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 237 VMATPTVFVEFSRQRGLATD-----GRCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSavnqdGASSG- 310
Cdd:PRK07314 191 AAITPLGIAGFAAARALSTRnddpeRASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGY-----GMTGDa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 311 --LTAP--NGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGRqrpADRPLLLGSVKSNIGHTQA 386
Cdd:PRK07314 266 yhMTAPapDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGE---HAYKVAVSSTKSMTGHLLG 342
|
330 340 350
....*....|....*....|....*....|...
gi 1215099124 387 AAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVD 419
Cdd:PRK07314 343 AAGAVEAIFSVLAIRDQVIPPTINLDNPDEECD 375
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
37-455 |
2.68e-29 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 123.18 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 37 VAIIGMscrfpgGVRSP-----EQLWDLVAAGGDAMAPFPDDrgwhldalYDTDPASRGTSYVREGGFLPDAGdFDPAFF 111
Cdd:PRK06333 6 IVVTGM------GAVSPlgcgvETFWQRLLAGQSGIRTLTDF--------PVGDLATKIGGQVPDLAEDAEAG-FDPDRY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 112 gISPREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAP-TGVYAAtssqgdyaallAGVGG------GVEGYLGTGSA- 183
Cdd:PRK06333 71 -LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEDRErTATIIG-----------SGVGGfpaiaeAVRTLDSRGPRr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 184 ----------AAVASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGL 253
Cdd:PRK06333 139 lspftipsflTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 254 ATDGR------CKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQAL 327
Cdd:PRK06333 219 STRFNdapeqaSRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 328 ANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGRqrpaDRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPP 407
Cdd:PRK06333 299 RQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGH----VSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPP 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1215099124 408 TLHVDAPTPhvdwSAGAVTLLTGTT-PWPATgrprRAGVSAFGVSGTNA 455
Cdd:PRK06333 375 TLNLENPDP----AAEGLDVVANKArPMDMD----YALSNGFGFGGVNA 415
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1437-1522 |
2.90e-28 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 109.65 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1437 LAGSAAVDRHRILLDLVRAHVATVLGHASPGAIEADRDFLELGFDSLTALELRDALRQDTGAELSATLLFDHPTPSALAR 1516
Cdd:smart00823 1 LAALPPAERRRLLLDLVREQVAAVLGHAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
....*.
gi 1215099124 1517 HLLDRI 1522
Cdd:smart00823 81 HLAAEL 86
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
566-858 |
1.24e-27 |
|
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: 115.10 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 566 LAVLFTGQGAQRPGMGAELhRRFPVFAAAFDEVAaeldrhlthplrEVVFAAAGTPQAAL-LDRTEFTQPALFAYEVAAY 644
Cdd:TIGR03131 1 IALLFPGQGSQRAGMLAEL-PDHPAVAAVLAEAS------------DVLGIDPRELDDAEaLASTRSAQLCILAAGVAAW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 645 RLVTAWGLRPQQLLGHSVGELAAAHVAGVLSLADAAALVAARGRLM-QALPEGGAMLAVR-ATEAEVTPLL-GAGVALAA 721
Cdd:TIGR03131 68 RALLALLPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMdQAVPGGYGMLAVLgLDLAAVEALIaKHGVYLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 722 VNGPTSVVLSGDADAVLAAGDRLTAQG-RQVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGAVL--T 798
Cdd:TIGR03131 148 INAPDQVVIAGSRAALRAVAELARAAGaSRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVrdA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 799 AAEATDPGYWVDHvrdTVRFHAGMATLAAAGAGTFLELGPDGALTALARECLPDAEAAAF 858
Cdd:TIGR03131 228 AQIRDDLARQIAT---PVDWHDCMQAAYERGARLVIELGPGDVLTKLANEAFPELPARSA 284
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
189-460 |
2.33e-27 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 117.05 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 189 GRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGG---------------VSVMATPTvfveFSRQRGL 253
Cdd:PRK07103 148 GLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGalmdlsywecqalrsLGAMGSDR----FADEPEA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 254 AtdgrCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSglTAPNGPSQRRVITQALANAGLS 333
Cdd:PRK07103 224 A----CRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRG--PDPSLEGEMRVIRAALRRAGLG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 334 ADEIDVVEAHGTGTTLGDPIEAQALLATYGRQrpadrpLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDA 413
Cdd:PRK07103 298 PEDIDYVNPHGTGSPLGDETELAALFASGLAH------AWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDE 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1215099124 414 P-TPHVDWsagavtllTGTTPWPAtgRPRRAGVSAFGVSGTNAHTIVE 460
Cdd:PRK07103 372 PiDERFRW--------VGSTAESA--RIRYALSLSFGFGGINTALVLE 409
|
|
| KR_FAS_SDR_x |
cd05274 |
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ... |
1048-1391 |
6.59e-27 |
|
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187582 [Multi-domain] Cd Length: 375 Bit Score: 114.79 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1048 VLSLLAVDTTSRDGGVAGPLAGTATLVRVLADAGCT--APVWCVTRGAVAVDADDAAPDVAGaCLWGLGRVLALEAPRLW 1125
Cdd:cd05274 11 ALSLLAVAPACGAADAVLALAALLALVAALLAAYAStgPPLWLVTRGAEAVSADDVAALAQA-ALWGLLRVLALEHPELW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1126 GGLVDLPADPDAAAYAALARAVTGDGGEDQLAVRAGGLHARRLERAPTGPA--SDEDWRPRGAVLVHGTAAVRAPHLLRR 1203
Cdd:cd05274 90 GGLVDLDAADAADEAAALAALLAGAPGEDELALRGGQRLVPRLVRAPAAALelAAAPGGLDGTYLITGGLGGLGLLVARW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1204 LAEHGAPHLLLAGPDAPAD-----------LGVEVTVLD----DPAALPAALDRLaAAGTPVRTVVHVADSGGAGdPVTA 1268
Cdd:cd05274 170 LAARGARHLVLLSRRGPAPraaaraallraGGARVSVVRcdvtDPAALAALLAEL-AAGGPLAGVIHAAGVLRDA-LLAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1269 TDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAGLAALAAHRRAAGRPATVLAWVPWA 1348
Cdd:cd05274 248 LTPAAFAAVLAAKVAGALNLHELTPDLPLDFFVLFSSVAALLGGAGQAAYAAANAFLDALAAQRRRRGLPATSVQWGAWA 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1215099124 1349 DEVADSAP-----LRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVD 1391
Cdd:cd05274 328 GGGMAAAAalrarLARSGLGPLAPAEALEALEALLASDAPQAVVASVD 375
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
174-454 |
1.08e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 115.21 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 174 VEGYLGTGSAAAVASGRisyalGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQR-G 252
Cdd:PRK07910 142 VQMYMPNGPAAAVGLER-----HAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRiV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 253 LATD-----GRCKSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQAL 327
Cdd:PRK07910 217 MSTNnddpaGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 328 ANAGLSADEIDVVEAHGTGTTLGDPIEAQALLATYGRQRPAdrpllLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPP 407
Cdd:PRK07910 297 ELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGHRPA-----VYAPKSALGHSVGAVGAVESILTVLALRDGVIPP 371
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1215099124 408 TLHVDAPTPHVDwsagavtlLTGTTPWPATGRPRRAGVSAFGVSGTN 454
Cdd:PRK07910 372 TLNLENLDPEID--------LDVVAGEPRPGNYRYAINNSFGFGGHN 410
|
|
| KR_2_FAS_SDR_x |
cd08955 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); ... |
1038-1392 |
7.44e-26 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 2, complex (x); Ketoreductase, a module of the multidomain polyketide synthase, has 2 subdomains, each corresponding to a short-chain dehydrogenases/reductase (SDR) family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerizes but is composed of 2 subdomains, each resembling an SDR monomer. In some instances, as in porcine FAS, an enoyl reductase (a Rossman fold NAD binding domain of the MDR family) module is inserted between the sub-domains. The active site resembles that of typical SDRs, except that the usual positions of the catalytic asparagine and tyrosine are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular polyketide synthases are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) fatty acid synthase. In some instances, such as porcine FAS , an enoyl reductase module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER). Polyketide syntheses also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes the KR domain of the Lyngbya majuscule Jam J, -K, and #L which are encoded on the jam gene cluster and are involved in the synthesis of the Jamaicamides (neurotoxins); Lyngbya majuscule Jam P belongs to a different KR_FAS_SDR_x subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187658 [Multi-domain] Cd Length: 376 Bit Score: 111.61 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1038 AAVAGATPALVLSLLAVDTTSRDGGVAGP-LAGTAT---LVRVLADAGCT--APVWCVTRGAVAVDADDAAPDVAGACLW 1111
Cdd:cd08955 1 ALLGSAPLAGVVHLWSLDAPREEPADAASqELGCASalhLVQALSKAGLRraPRLWLVTRGAQSVLADGEPVSPAQAPLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1112 GLGRVLALEAPRLWGGLVDLPADPDAAAYAAL-ARAVTGDGGEDQLAVRAGGLHARRLERAPTGPAsdedwRPRGAVLVH 1190
Cdd:cd08955 81 GLGRVIALEHPELRCGLVDLDPEATAAEEAEAlLAELLAADAEDQVALRGGARYVARLVRAPARPL-----RPDATYLIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1191 GTAAVRAPHLLRRLAEHGAPHLLLAG---PDAPA--------DLGVEVTVLD----DPAALPAALDRLAAAGTPVRTVVH 1255
Cdd:cd08955 156 GGLGGLGLLVAEWLVERGARHLVLTGrraPSAAArqaiaaleEAGAEVVVLAadvsDRDALAAALAQIRASLPPLRGVIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1256 VA---DSGgagdPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAGLAALAAHR 1332
Cdd:cd08955 236 AAgvlDDG----VLANQDWERFRKVLAPKVQGAWNLHQLTQDLPLDFFVLFSSVASLLGSPGQANYAAANAFLDALAHYR 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215099124 1333 RAAGRPATVLAWVPWAD-----EVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVDW 1392
Cdd:cd08955 312 RARGLPALSINWGPWAEvgmaaSLARQARLEARGVGAISPAAGLQALGQLLRTGSTQVGVAPVDW 376
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
196-416 |
7.95e-25 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 109.31 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 196 GLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVeF-----SRQRGLATDGRCKSFAAAADGTG 270
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAV-FdtlfaTSTRNDAPELTPRPFDANRDGLV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 271 WSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASsgLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLG 350
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRG 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215099124 351 DPIEAQALLATYGRQRPadrpllLGSVKSNIGHTQAAAGV---AGVIKMvlaMRHGVLPPTLHVDAPTP 416
Cdd:PRK09116 309 DIAESQATAAVFGARMP------ISSLKSYFGHTLGACGAleaWMSIEM---MNEGWFAPTLNLTQVDP 368
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
183-414 |
2.03e-24 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 107.45 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 183 AAAVASGRIsyaLGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGrCKSF 262
Cdd:PRK05952 124 QAAIAAARQ---IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPF 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 263 AAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEA 342
Cdd:PRK05952 200 DRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHA 279
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215099124 343 HGTGTTLGDPIEAQALLATYGrQRPAdrpllLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAP 414
Cdd:PRK05952 280 HGTATRLNDQREANLIQALFP-HRVA-----VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP 345
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
105-419 |
1.55e-23 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 105.20 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 105 DFDPAFFgISPREALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAAtssqgdyaallAGVGG------------ 172
Cdd:PRK08439 54 DFDPTEV-MDPKEVKKADRFIQLGLKAAREAMKDAGFLPEELDAERFGVSSA-----------SGIGGlpnieknsiicf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 173 -----GVEGYLGTGSAAAVASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEF 247
Cdd:PRK08439 122 ekgprKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 248 SRQRGLAT--DGRCKS---FAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGsaVNQDGASSGLTAPNGPSQRRV 322
Cdd:PRK08439 202 AAMKALSTrnDDPKKAsrpFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 323 ITQALANAGlsADEIDVVEAHGTGTTLGDPIEAQALLATYGRQRPADrplLLGSVKSNIGHTQAAAGVAGVIKMVLAMRH 402
Cdd:PRK08439 280 MKAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKELFGSKEKVP---PVSSTKGQIGHCLGAAGAIEAVISIMAMRD 354
|
330
....*....|....*..
gi 1215099124 403 GVLPPTLHVDAPTPHVD 419
Cdd:PRK08439 355 GILPPTINQETPDPECD 371
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
186-461 |
2.40e-23 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 103.66 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 186 VASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLAT------DGRC 259
Cdd:PRK14691 69 LAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfnstpEKAS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 260 KSFAAAADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDV 339
Cdd:PRK14691 149 RPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQH 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 340 VEAHGTGTTLGDPIEAQALLATYGRQrpadRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPhvd 419
Cdd:PRK14691 229 LNAHATSTPVGDLGEINAIKHLFGES----NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDP--- 301
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1215099124 420 wSAGAVTLLTGTT-PWPATgrprRAGVSAFGVSGTNAHTIVEQ 461
Cdd:PRK14691 302 -AAKGLNIIAGNAqPHDMT----YALSNGFGFAGVNASILLKR 339
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1611-1811 |
2.52e-23 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 100.16 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1611 GPHEYARVAAGFRGRRDVWALPNPGFGVGEELPADLPALLRVHADTVRRTVGDGPFVLAGHSGGAMVANVLARELERQGR 1690
Cdd:pfam00975 12 SASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVARRLERQGE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1691 PPAAVVLMDTYPADSEVLGGWTSQLLDGMVERdsaytpMDDYRTTA---------WAGYLPLFLD-------WQPAPMDA 1754
Cdd:pfam00975 92 AVRSLFLSDASAPHTVRYEASRAPDDDEVVAE------FTDEGGTPeelledeelLSMLLPALRAdyralesYSCPPLDA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1215099124 1755 ATLLVRASR--PLGEWTGEPDGWRSRWPYPHEAVDAAGDHFTMVgERGPELAATVDEWL 1811
Cdd:pfam00975 166 QSATLFYGSddPLHDADDLAEWVRDHTPGEFDVHVFDGDHFYLI-EHLEAVLEIIEAKL 223
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
122-459 |
4.58e-23 |
|
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: 103.98 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 122 DPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSS------QGDYAALLAGVGGGVEGYLGTGSAAAVASGRISYAL 195
Cdd:cd00832 69 DRMTRLALAAADWALADAGVDPAALPPYDMGVVTASAAggfefgQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 196 GLEGPAVTVDTACSSSLVALHLACQALRLGECtLALAGGVSVMATPTVFVEFSRQRGLATDGRCKS----FAAAADGTGW 271
Cdd:cd00832 149 GMRGPSGVVVAEQAGGLDALAQARRLVRRGTP-LVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARaylpFDAAAAGYVP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 272 SEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSgltAPNGPSQRRVITQALANAGLSADEIDVVEAHGTGTTLGD 351
Cdd:cd00832 228 GEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG---SGRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 352 PIEAQALLATYGRQR-PADRPlllgsvKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPhvdwsAGAVTLLTG 430
Cdd:cd00832 305 RAEAAALAAVFGPRGvPVTAP------KTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPP-----AYGLDLVTG 373
|
330 340
....*....|....*....|....*....
gi 1215099124 431 TtpwPATGRPRRAGVSAFGVSGTNAHTIV 459
Cdd:cd00832 374 R---PRPAALRTALVLARGRGGFNSALVV 399
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
194-463 |
1.03e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 102.61 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 194 ALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQrgLATDGRCKSFAAAADGTGWSE 273
Cdd:PRK09185 146 YLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLE--SLSPQPCRPFSANRDGINIGE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 274 GVGMLLVERLSDArrnghPVLavVRGSavnqdGASSG---LTAPN--GPSQRRVITQALANAGLSADEIDVVEAHGTGTT 348
Cdd:PRK09185 224 AAAFFLLEREDDA-----AVA--LLGV-----GESSDahhMSAPHpeGLGAILAMQQALADAGLAPADIGYINLHGTATP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 349 LGDPIEAQALLATYGRQRPAdrplllGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVdwsaGAVTLL 428
Cdd:PRK09185 292 LNDAMESRAVAAVFGDGVPC------SSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPAL----PPLYLV 361
|
250 260 270
....*....|....*....|....*....|....*
gi 1215099124 429 TGttpwPATGRPRRAGVSAFGVSGTNAHTIVEQAD 463
Cdd:PRK09185 362 EN----AQALAIRYVLSNSFAFGGNNCSLIFGRAD 392
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
37-461 |
1.02e-21 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 100.08 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 37 VAIIGMSCRFPGGvRSPEQLWDLVAAGGDAMAPFPddrgwHLDAlydTDPASRGTSYVReggflpdagDFDPAFFgISPR 116
Cdd:PRK08722 6 VVVTGMGMLSPVG-NTVESSWKALLAGQSGIVNIE-----HFDT---TNFSTRFAGLVK---------DFNCEEY-MSKK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 117 EALAMDPQQRLLLETAWEAFERAGIDPTTLRGAPTGVYAATSSQG------DYAALLAGVGGGVEGYLGTGSAAAVASGR 190
Cdd:PRK08722 67 DARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGSGIGGlglieaGHQALVEKGPRKVSPFFVPSTIVNMIAGN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 191 ISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGR-----CKSFAAA 265
Cdd:PRK08722 147 LSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDepqkaSRPWDKD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 266 ADGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVVEAHGT 345
Cdd:PRK08722 227 RDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 346 GTTLGDPIEAQALLATYGRQrpADRPLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVDwsagaV 425
Cdd:PRK08722 307 STPAGDVAEIKGIKRALGEA--GSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLD-----I 379
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1215099124 426 TLLtgttpwPATGRP----RRAGVSAFGVSGTNAHTIVEQ 461
Cdd:PRK08722 380 DLV------PHTARKvesmEYAICNSFGFGGTNGSLIFKK 413
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
186-419 |
2.82e-19 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 93.89 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 186 VASGRISYALGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFVEFSRQRGLATDGRCKSFAAA 265
Cdd:PLN02787 269 MGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 266 A-----DGTGWSEGVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASSGLTAPNGPSQRRVITQALANAGLSADEIDVV 340
Cdd:PLN02787 349 PwdmnrDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYI 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1215099124 341 EAHGTGTTLGDPIEAQALLATYGrQRPAdrpLLLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAPTPHVD 419
Cdd:PLN02787 429 NAHATSTKAGDLKEYQALMRCFG-QNPE---LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD 503
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1005-1814 |
5.86e-18 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 90.53 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1005 LVVADPDAATGTLLAALAAAGLSPVRVSPDDLPAAVAGATPALVLSLLAVDTTSRDGGVAGPLAGTATLVRVLADAGCTA 1084
Cdd:COG3319 15 AAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1085 PVWCVTRGAVAVDADDAAPDVAGACLWGLGRVLALEAPRLWGGLVDLPADPDAAAYAALARAVTGDGGEDQLAVRAGGLH 1164
Cdd:COG3319 95 LLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1165 ARRLERAPTGPASDEDWRPRGAVLVHGTAAVRAPHLLRRLAEHGAPHLLLAGPDAPADLGVEVTVLDDPAALPAALDRLA 1244
Cdd:COG3319 175 LLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1245 AAGTPVRTVVHVADSGGAGDPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAG 1324
Cdd:COG3319 255 LLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1325 LAALAAHRRAAGRPATVLAWVPWADEVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVDwptftpAFTAVRP 1404
Cdd:COG3319 335 LPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL------RLQRLRR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1405 SALLRGVPEAVVEPSGRDGAEPADPARVLRDRLAGSAAVDRHRILLDLVRAHVATVLGHASPGAIEADRDFLELGFDSLT 1484
Cdd:COG3319 409 GLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLL 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1485 ALELRDALRQDTGAELSATLLFDHPTPSALARHLLDRILGADAAGDPAGGPAEGAPEGAGGILGGLFRQPKAREDAAGYA 1564
Cdd:COG3319 489 AALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALL 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1565 ELLVKLARFRPAFTEPAQLTRPAGVLRLAEGPGVPVVCCCTMSllSGPHEYARVAAGFRGRRDVWALPNPGFGVGEELPA 1644
Cdd:COG3319 569 LAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAG--GNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPA 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1645 DLPALLRVHADTVRRTVGDGPFVLAGHSGGAMVANVLARELERQGRPPAAVVLMDTYP-------ADSEVLGGWTSQLLD 1717
Cdd:COG3319 647 SVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYApgalarlDEAELLAALLRDLAR 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1718 GMVERDSA----------------------------YTPMDDYRTTAWAGYLPLFLDWQPAPMDAATLLVRASRPLGEWT 1769
Cdd:COG3319 727 GVDLPLDAeelraldpeerlarllerlreaglpaglDAERLRRLLRVFRANLRALRRYRPRPYDGPVLLFRAEEDPPGRA 806
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1215099124 1770 GEPD-GWRSRWPYPHEAVDAAGDHFTMVGERG-PELAATVDEWLTGR 1814
Cdd:COG3319 807 DDPAlGWRPLVAGGLEVHDVPGDHFSMLREPHvAELAAALRAALAAA 853
|
|
| KR_3_FAS_SDR_x |
cd08956 |
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); ... |
1008-1410 |
2.21e-17 |
|
beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 3, complex (x); Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta- ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes KR domains found in many multidomain PKSs, including six of seven Sorangium cellulosum PKSs (encoded by spiDEFGHIJ) which participate in the synthesis of the polyketide scaffold of the cytotoxic spiroketal polyketide spirangien. These seven PKSs have either a single PKS module (SpiF), two PKR modules (SpiD,-E,-I,-J), or three PKS modules (SpiG,-H). This subfamily includes the second KR domains of SpiE,-G, I, and -J, both KR domains of SpiD, and the third KR domain of SpiH. The single KR domain of SpiF, the first and second KR domains of SpiH, the first KR domains of SpiE,-G,- I, and -J, and the third KR domain of SpiG, belong to a different KR_FAS_SDR subfamily. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187659 [Multi-domain] Cd Length: 448 Bit Score: 86.94 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1008 ADPDAATGTLLAALAAAGLSPVRVSPDDLPAAVAGATPA---LVLSLLAVDTTSRDGGVAGPLAGTATLVRV-LADAGCT 1083
Cdd:cd08956 14 PAAAPPDWALLGLAAAGAAGAAHADLDALAAALAAGAAVpdvVVVPCPAAAGGDLAAAAHAAAARALALLQAwLADPRLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1084 -APVWCVTRGAVAVDADDAAPDVAGACLWGLGRVLALEAP-RLWggLVDLPADPDAAAYAALARavtgDGGEDQLAVRAG 1161
Cdd:cd08956 94 dSRLVVVTRGAVAAGPDEDVPDLAAAAVWGLVRSAQAEHPgRFV--LVDLDDDAASAAALPAAL----ASGEPQLALRDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1162 GLHARRLERAPTGPA---SDEDWRPRGAVLVHGTAAVRAPHLLRRL-AEHGAPHLLLA---GPDAP---------ADLGV 1225
Cdd:cd08956 168 RLLVPRLARVAPAATlppVPRPLDPDGTVLITGGTGTLGALLARHLvTEHGVRHLLLVsrrGPDAPgaaelvaelAALGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1226 EVTV----LDDPAALPAALDRLAAAGtPVRTVVHVADSGGAGdPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFV 1301
Cdd:cd08956 248 EVTVaacdVADRAALAALLAAVPADH-PLTAVVHAAGVLDDG-VLTSLTPERLDAVLRPKVDAAWHLHELTRDLDLAAFV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1302 VFTSTAATWGSGGAAVTAATGAGLAALAAHRRAAGRPATVLAWVPWAD--------EVADSAPLRRRGIRPLAADLAVAA 1373
Cdd:cd08956 326 LFSSAAGVLGSPGQANYAAANAFLDALAQHRRARGLPATSLAWGLWAQasgmtahlSDADLARLARGGLRPLSAEEGLAL 405
|
410 420 430
....*....|....*....|....*....|....*..
gi 1215099124 1374 VRQALGRGDDEVAVADVDWPTFTPAFTAVRPsALLRG 1410
Cdd:cd08956 406 FDAALAADEPVLVPARLDLAALRAAAAGALP-PLLRG 441
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
414-531 |
1.93e-15 |
|
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: 74.12 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 414 PTPHVD-WSAGAVTLLTGTTPWPATgrprRAGVSAFGVSGTNAHTIVEQADpadagTARPAGTPAPAGPWIV--SARSAP 490
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPWPGG----IVGVNSFGFGGANAHVILKSNP-----KPKIPPESPDNLPRLVllSGRTEE 71
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1215099124 491 ALAGQARRLLAHLAAHPELRPADVAYSLVTTRaaLPHRAVV 531
Cdd:pfam16197 72 AVKALLEKLENHLDDAEFLSLLNDIHSLPISG--HPYRGYA 110
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1449-1522 |
1.95e-14 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 69.88 E-value: 1.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215099124 1449 LLDLVRAHVATVLGHaSPGAIEADRDFL-ELGFDSLTALELRDALRQDTGAELSATLLFDHPTPSALARHLLDRI 1522
Cdd:COG0236 6 LEERLAEIIAEVLGV-DPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
536-795 |
1.11e-13 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 74.41 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 536 ADALRAGLRAVAEDAAHPHVVRGVARPA-----GKLAVLFTGQGAQRPGMGAELHRrFPVFAAAFDEvAAELdrhLTHPL 610
Cdd:PLN02752 5 AFAARRASASRVSMSVSVGSQATAADALfadykPTTAFLFPGQGAQAVGMGKEAAE-VPAAKALFDK-ASEI---LGYDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 611 REVvfaAAGTPQAALlDRTEFTQPALFAYEVAAYRLVTAWGLRPQQL------LGHSVGELAAAHVAGVLSLADAAALVA 684
Cdd:PLN02752 80 LDV---CVNGPKEKL-DSTVVSQPAIYVASLAAVEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 685 ARGRLMQALPEGG--AMLAVRATEAE-VTPLLGAgvALAAVNG-----------PTSVVLSGDADAVLAAGDRLTAQG-R 749
Cdd:PLN02752 156 LRGEAMQAAADAGpsGMVSVIGLDSDkVQELCAA--ANEEVGEddvvqianylcPGNYAVSGGKKGIDAVEAKAKSFKaR 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1215099124 750 QVRRLRVSHAFHSARMDAVLADFRVVAEKVTWHPPTLPLVSDRTGA 795
Cdd:PLN02752 234 MTVRLAVAGAFHTSFMEPAVDALEAALAAVEIRTPRIPVISNVDAQ 279
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
274-459 |
1.15e-13 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 75.09 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 274 GVGMLLVERLSDARRNGHPVLAVVRGSAVNQDGASsgLTAPNGPSQRRVITQALANAGLSADEIDVveaHGTGTTLGDPI 353
Cdd:PRK07967 233 GGGVVVVEELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMALATVDTPIDYINT---HGTSTPVGDVK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 354 EAQALLATYGRQRPAdrpllLGSVKSNIGHTQAAAGVAGVIKMVLAMRHGVLPPTLHVDAptphVDWSAGAVTLLTGTTp 433
Cdd:PRK07967 308 ELGAIREVFGDKSPA-----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEE----LDPQAAGMPIVTETT- 377
|
170 180 190
....*....|....*....|....*....|.
gi 1215099124 434 wpatgrpRRAGV-----SAFGVSGTNAhTIV 459
Cdd:PRK07967 378 -------DNAELttvmsNSFGFGGTNA-TLV 400
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1451-1513 |
7.75e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 64.89 E-value: 7.75e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215099124 1451 DLVRAHVATVLGHAsPGAIEADRDFLELGFDSLTALELRDALRQDTGAELSATLLFDHPTPSA 1513
Cdd:pfam00550 1 ERLRELLAEVLGVP-AEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1611-1697 |
8.69e-10 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 61.02 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1611 GPHEYARVAAGFRGRRDVWALPNPGFG--VGEELPADLPALLRVHADTVRRTVgDGPFVLAGHSGGAMVANVLARELERQ 1688
Cdd:COG3208 18 SASAYRPWAAALPPDIEVLAVQLPGRGdrLGEPPLTSLEELADDLAEELAPLL-DRPFALFGHSMGALLAFELARRLERR 96
|
90
....*....|
gi 1215099124 1689 GRP-PAAVVL 1697
Cdd:COG3208 97 GRPlPAHLFV 106
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1433-1526 |
7.71e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 60.82 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1433 LRDRLAgSAAVDRHRILLDLVRAHVATVLGHASPGAIEADRDFLELGFDSLTALELRDALRQDTGAELSATLLFDHPTPS 1512
Cdd:PRK06060 531 LRERLV-ALRQERQRLVVDAVCAEAAKMLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSIS 609
|
90
....*....|....
gi 1215099124 1513 ALARHLLDRILGAD 1526
Cdd:PRK06060 610 GLAQYLEAELAGGH 623
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1471-1706 |
3.23e-08 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 58.90 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1471 ADRDFLELGFDSLTALELRDALRQDTGAELSATLLFDHPTPSALARHLldrilgadaagdpAGGPAEGAPEGAGGILGgl 1550
Cdd:PRK10252 998 ADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL-------------DAEEDESRRLGFGTILP-- 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1551 frqpkaredaagyaellvklarfrpaftepaqltrpagvlrLAEGPGVPVVCCCTMSLLSgpHEYARVAAGFRGRRDVWA 1630
Cdd:PRK10252 1063 -----------------------------------------LREGDGPTLFCFHPASGFA--WQFSVLSRYLDPQWSIYG 1099
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215099124 1631 LPNPGFGVGEELPADLPALLRVHADTVRRTVGDGPFVLAGHSGGAMVANVLARELERQGRPPAAVVLMDTYPADSE 1706
Cdd:PRK10252 1100 IQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPETQ 1175
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1164-1697 |
4.39e-08 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 58.73 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1164 HARRLERAPTGPasdedWRPRGAVLVHGTAAvrAPHLLRRLAEHGAPHLLLAGPDAPADLGVEVTVLDDPAALPAALDRL 1243
Cdd:COG3321 856 RGRRRVPLPTYP-----FQREDAAAALLAAA--LAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1244 AAAGTPVRTVVHVADSGGAGDPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGA 1323
Cdd:COG3321 929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1324 GLAALAAHRRAAGRPATVLAWVPWADEVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVDWPTFTPAFTAVR 1403
Cdd:COG3321 1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA 1088
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1404 PSALLRGVPEAVVEPSGRDGAEPADPARVLRDRLAGSAAVDRHRILLDLVRAHVATVLGHASPGAIEADRDFLELGFDSL 1483
Cdd:COG3321 1089 ALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALL 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1484 TALELRDALRQDTGAELSATLLFDHPTPSALARHLLDRILGADAAGDPAGGPAEGAPEGAGGILGGLFRQPKAREDAAGY 1563
Cdd:COG3321 1169 AAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAAL 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1564 AELLVKLARFRPAFTEPAQLTRPAGVLRLAEGPGVPVVccctmsLLSGPHEYARVAAGFRGRRDVWALPNPGFGVGEELP 1643
Cdd:COG3321 1249 AAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALA------LAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1215099124 1644 ADLPALLRVHADTVRRTVGDGPFVLAGHSGGAMVANVLARELERQGRPPAAVVL 1697
Cdd:COG3321 1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAAL 1376
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
111-238 |
4.69e-07 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 53.08 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 111 FGISPREALAMDpqqrLLLETAWEAFERAGIDPTTLrgapTGVYAATSSQGDYAALLAgvgggvegylgtgSAAAVASGr 190
Cdd:pfam00108 14 FGGSLKDVSAVE----LGAEAIKAALERAGVDPEDV----DEVIVGNVLQAGEGQNPA-------------RQAALKAG- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1215099124 191 isyaLGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVM 238
Cdd:pfam00108 72 ----IPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| KR |
pfam08659 |
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ... |
1185-1349 |
4.90e-07 |
|
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 430138 [Multi-domain] Cd Length: 180 Bit Score: 51.79 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1185 GAVLVHGTAAVRAPHLLRRLAEHGAPHLLLAGPDAPAD------------LGVEVTVLD----DPAALPAALDRLAAAGT 1248
Cdd:pfam08659 1 GTYLITGGLGGLGRELARWLAERGARHLVLLSRSAAPRpdaqaliaeleaRGVEVVVVAcdvsDPDAVAALLAEIKAEGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1249 PVRTVVHVAdsGGAGD-PVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAGLAA 1327
Cdd:pfam08659 81 PIRGVIHAA--GVLRDaLLENMTDEDWRRVLAPKVTGTWNLHEATPDEPLDFFVLFSSIAGLLGSPGQANYAAANAFLDA 158
|
170 180
....*....|....*....|..
gi 1215099124 1328 LAAHRRAAGRPATVLAWVPWAD 1349
Cdd:pfam08659 159 LAEYRRSQGLPATSINWGPWAE 180
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
134-238 |
6.11e-07 |
|
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: 54.02 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 134 EAFERAGIDPTTLrgaptgvyaatssqgDYAALLAGVGGGVEGYLGTgsAAAVASGrisyaLGLEGPAVTVDTACSSSLV 213
Cdd:cd00751 32 ALLERAGLDPEEV---------------DDVIMGNVLQAGEGQNPAR--QAALLAG-----LPESVPATTVNRVCGSGLQ 89
|
90 100
....*....|....*....|....*
gi 1215099124 214 ALHLACQALRLGECTLALAGGVSVM 238
Cdd:cd00751 90 AVALAAQSIAAGEADVVVAGGVESM 114
|
|
| PKS_KR |
smart00822 |
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ... |
1199-1349 |
1.05e-06 |
|
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.
Pssm-ID: 214833 [Multi-domain] Cd Length: 180 Bit Score: 50.94 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1199 HLLRRLAEHGAPHLLLAGPDAPAD------------LGVEVTV----LDDPAALPAALDRLAAAGTPVRTVVHVADSGGA 1262
Cdd:smart00822 15 ALARWLAERGARRLVLLSRSGPDApgaaallaeleaAGARVTVvacdVADRDALAAVLAAIPAVEGPLTGVIHAAGVLDD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1263 GdPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSGGAAVTAATGAGLAALAAHRRAAGRPATVL 1342
Cdd:smart00822 95 G-VLASLTPERFAAVLAPKAAGAWNLHELTADLPLDFFVLFSSIAGVLGSPGQANYAAANAFLDALAEYRRARGLPALSI 173
|
....*..
gi 1215099124 1343 AWVPWAD 1349
Cdd:smart00822 174 AWGAWAE 180
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
134-238 |
2.49e-06 |
|
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: 51.99 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 134 EAFERAGIDPTTLrgaptgvyaatssqgDYAALLAGVGGGVEGYLGtgSAAAVASGrisyaLGLEGPAVTVDTACSSSLV 213
Cdd:COG0183 36 ALLERAGLDPEAV---------------DDVILGCVLQAGQGQNPA--RQAALLAG-----LPESVPAVTVNRVCGSGLQ 93
|
90 100
....*....|....*....|....*
gi 1215099124 214 ALHLACQALRLGECTLALAGGVSVM 238
Cdd:COG0183 94 AVALAAQAIAAGDADVVIAGGVESM 118
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
134-238 |
6.53e-06 |
|
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: 50.69 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 134 EAFERAGIDPTTLRGAPTGVYAATSSQ---GDYAALLAGVGGGVegylgtgsaaavasgrisyalglegPAVTVDTACSS 210
Cdd:TIGR01930 31 ELLERNPLDPELIDDVIFGNVLQAGEQqniARQAALLAGLPESV-------------------------PAYTVNRQCAS 85
|
90 100
....*....|....*....|....*...
gi 1215099124 211 SLVALHLACQALRLGECTLALAGGVSVM 238
Cdd:TIGR01930 86 GLQAVILAAQLIRAGEADVVVAGGVESM 113
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
134-238 |
1.01e-04 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 46.88 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 134 EAFERAGIDPTTLRGAPTGVYAATSSQGDYAALLAGVGGGVegylgtgsaaavasgrisyalGLEGPAVTVDTACSSSLV 213
Cdd:PRK09051 37 EALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGV---------------------PQETPAFNVNRLCGSGLQ 95
|
90 100
....*....|....*....|....*
gi 1215099124 214 ALHLACQALRLGECTLALAGGVSVM 238
Cdd:PRK09051 96 AIVSAAQAILLGDADVAIGGGAESM 120
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1420-1518 |
1.66e-04 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 45.51 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1420 GRDGAEPADPARVLRDRLAGSAAVDRHRILLDLVRAHVATVLGhASPGAIEADRDFLELGFDSLTALELRDALRQDtGAE 1499
Cdd:COG3433 191 VVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLG-VDPEEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLD 268
|
90
....*....|....*....
gi 1215099124 1500 LSATLLFDHPTPSALARHL 1518
Cdd:COG3433 269 VSFADLAEHPTLAAWWALL 287
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
184-238 |
4.32e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 44.76 E-value: 4.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1215099124 184 AAVASGrisyaLGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVM 238
Cdd:PRK05790 69 AALKAG-----LPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESM 118
|
|
| KR_2_SDR_x |
cd08953 |
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ... |
1112-1312 |
6.00e-04 |
|
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
Pssm-ID: 187656 [Multi-domain] Cd Length: 436 Bit Score: 44.28 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1112 GLGRVLALEAPRLWGGLVDLPADPDAAAYAALARAV-TGDGGEDQLAVRAGGLHARRLERAP--TGPASDEDWRPRGAVL 1188
Cdd:cd08953 130 GLLRTLAQEYPGLTCRLIDLDAGEASAEALARELAAeLAAPGAAEVRYRDGLRYVQTLEPLPlpAGAAASAPLKPGGVYL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1189 VHGTAAVRAPHLLRRLAEHGAPHLLLAG----PDAP----------ADLGVEVTV----LDDPAALPAALDRLAAAGTPV 1250
Cdd:cd08953 210 VTGGAGGIGRALARALARRYGARLVLLGrsplPPEEewkaqtlaalEALGARVLYisadVTDAAAVRRLLEKVRERYGAI 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215099124 1251 RTVVHVADSGgAGDPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGS 1312
Cdd:cd08953 290 DGVIHAAGVL-RDALLAQKTAEDFEAVLAPKVDGLLNLAQALADEPLDFFVLFSSVSAFFGG 350
|
|
| Docking |
pfam08990 |
Erythronolide synthase docking domain; Polyketide synthase (PKS) catalyzes the biosynthesis of ... |
6-31 |
6.04e-04 |
|
Erythronolide synthase docking domain; Polyketide synthase (PKS) catalyzes the biosynthesis of polyketides, which are structurally and functionally diverse natural products in microorganizms and plants. Type I modular PKSs are the large, multifunctional enzymes responsible for the production of a diverse family of structurally rich and often biologically active natural products. The efficiency of acyl transfer at the interfaces of the individual PKS proteins is thought to be governed by helical regions, termed docking domains (dd). Two such N-terminal domains dimerize to form amphipathic parallel alpha-helical coiled coils: dimerization is essential for protein function.
Pssm-ID: 462650 Cd Length: 29 Bit Score: 38.84 E-value: 6.04e-04
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1597-1814 |
7.46e-04 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 43.07 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1597 GVPVVCCctMSLLSGPHEYARVAAGFRGRRDVWALPNPGFG--VGEELPADLPALLRvHADTVRRTVGDGPFVLAGHSGG 1674
Cdd:COG0596 23 GPPVVLL--HGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGrsDKPAGGYTLDDLAD-DLAALLDALGLERVVLVGHSMG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1675 AMVANVLAReleRQGRPPAAVVLMDtypadsEVLGGWTSQLLDGMVERDSAYTPMDDYRTTAWAGYLplfldwqpAPMDA 1754
Cdd:COG0596 100 GMVALELAA---RHPERVAGLVLVD------EVLAALAEPLRRPGLAPEALAALLRALARTDLRERL--------ARITV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215099124 1755 ATLLVRASRPLGEWTGEPDGWRSRWP-YPHEAVDAAGdHFTMVgERGPELAATVDEWLTGR 1814
Cdd:COG0596 163 PTLVIWGEKDPIVPPALARRLAELLPnAELVVLPGAG-HFPPL-EQPEAFAAALRDFLARL 221
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1158-1573 |
1.66e-03 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 43.31 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1158 VRAGGLHARRL----ERAPTGPASDEDWRPRGAVLVHGTAAVRAPHLLRRLAEHGAPHLLLAGPDAPADLGVEVTVLDDP 1233
Cdd:COG1020 905 AREDAPGDKRLvayvVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPA 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1234 AALPAALDRLAAAGTPVRTVVHVADSGGAGDPVTATDPAVLAAAVDAQVTAVAALDAAVADRPVDEFVVFTSTAATWGSG 1313
Cdd:COG1020 985 EEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLA 1064
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1314 GAAVTAATGAGLAALAAHRRAAGRPATVLAWVPWADEVADSAPLRRRGIRPLAADLAVAAVRQALGRGDDEVAVADVDWP 1393
Cdd:COG1020 1065 AAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVAL 1144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1394 TFTPAFTAVRPSALLRGVPEAVVEpsgRDGAEPADPARVLRDRLAGSAAVDRHRILLDLVRAHVATVLGHASPGAIEADR 1473
Cdd:COG1020 1145 AAALALAALLALLLAAAAAAAELL---AAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1474 DFLELGFDSLTALELRDALRQDTGAELSATLLFDHPTPSALARHLLDRILGADAAGDPAGGPAEGAPEGAGGILGGLFRQ 1553
Cdd:COG1020 1222 LLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLL 1301
|
410 420
....*....|....*....|
gi 1215099124 1554 PKAREDAAGYAELLVKLARF 1573
Cdd:COG1020 1302 ALLLLLALALALLLLLLLLL 1321
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
175-253 |
2.86e-03 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 42.19 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 175 EGYLGTGSAAAVASGRISYALgLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMATPTVFV--------- 245
Cdd:PTZ00455 88 QGHLGPAAVGSLGQSGASNAL-LYKPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVggdylaraa 166
|
....*...
gi 1215099124 246 EFSRQRGL 253
Cdd:PTZ00455 167 DYRRQRKL 174
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
1611-1758 |
5.38e-03 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 40.15 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1611 GPHEYARVAAGFRGRRDVWALPNPGFGVGEELPADLPALLRVhADTVRRTVGDGPFVLAGHSGGAMVAnvlareLERQGR 1690
Cdd:pfam12697 7 AGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADL-AALLDELGAARPVVLVGHSLGGAVA------LAAAAA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215099124 1691 PPAAVVLMDTYPADSEVLGGWTSQLLDGMVERDSAYTPMDDYRTTAWAGYLPLFLDWQPAPMDAATLL 1758
Cdd:pfam12697 80 ALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALL 147
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1615-1725 |
8.37e-03 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 39.60 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215099124 1615 YARVAAGFRGRR-DVWALPNPGFGVGEELPADLPALLRVHADTVR-----RTVGDGPFVLAGHSGGAMVAnvlARELERQ 1688
Cdd:COG2267 44 YAELAEALAAAGyAVLAFDLRGHGRSDGPRGHVDSFDDYVDDLRAaldalRARPGLPVVLLGHSMGGLIA---LLYAARY 120
|
90 100 110
....*....|....*....|....*....|....*..
gi 1215099124 1689 GRPPAAVVLMDTYPADSEVLGGWTSQLLDGMVERDSA 1725
Cdd:COG2267 121 PDRVAGLVLLAPAYRADPLLGPSARWLRALRLAEALA 157
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
200-239 |
9.70e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 40.26 E-value: 9.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1215099124 200 PAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMA 239
Cdd:PRK05656 80 PAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMS 119
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
195-239 |
9.82e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 40.46 E-value: 9.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1215099124 195 LGLEGPAVTVDTACSSSLVALHLACQALRLGECTLALAGGVSVMA 239
Cdd:PRK07801 76 LPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMS 120
|
|
| |
