|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
30-1020 |
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: 1105.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 30 RTTEPIAIVGMACRLPGgVSSPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGFLQDAGEFDAGFF 109
Cdd:COG3321 1 AADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADR-WDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 110 GISAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVS 189
Cdd:COG3321 79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 190 YLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWA 269
Cdd:COG3321 159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 270 EGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDP 349
Cdd:COG3321 239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 350 IEAQALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEA 429
Cdd:COG3321 319 IEAAALTAAFGQGR-PADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 430 RPWPQLDRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPViPWVLSAKSPEALRAQADRLAAAVADGGGTDLSA 509
Cdd:COG3321 398 RPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQ-LLVLSAKTEEALRALAARLAAFLEAHPDLDLAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 510 VAHTLATGRAVFDHRAVVLGTEAADLLAGARRIAEGRTGAFAFTG-SRVRGRLALLFTGQGSQRLGMGRELHAAYPAFAA 588
Cdd:COG3321 477 VAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGaAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 589 ALDEALEQFGP----GLREVMWSsvEDGGAALDRTEHAQPALFAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVW 664
Cdd:COG3321 557 ALDECDALLRPhlgwSLREVLFP--DEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 665 SLPDAARLVAARGRLMQELPPGGAMVAVEAAEAEVLPLLG--PGVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVK 742
Cdd:COG3321 635 SLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 743 RLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVlTDPAYWVRQVRGTVRFHDAVTVLGARGATT 822
Cdd:COG3321 715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEA-LDADYWVRHLRQPVRFADAVEALLADGVRV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 823 ALEVGPLGVLTGMGERIRAAAGDeapgTVFVPALRGPGAETRDVLSAAGRLFTRGVAVNWRALLPATG--HADLPTYPFQ 900
Cdd:COG3321 794 FLEVGPGPVLTGLVRQCLAAAGD----AVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGrrRVPLPTYPFQ 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 901 RRRyWLERAAVSHTVTEEPMDQATPAGPEQQPEQQDQPQDEGPRPVLAAKLRELSEADGDRLLLDLVLAESAVVFEQQSL 980
Cdd:COG3321 870 RED-AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 2733316673 981 EAELGGDSPFFEMGLTSVGAVELRNRLVEATGLPLGPMLL 1020
Cdd:COG3321 949 AAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAA 988
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
33-457 |
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: 609.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 33 EPIAIVGMACRLPGGVSsPEELWRLVADGGDAISGFPADRgWDLETVYdPEPDRPGRSYVREGGFLQDAGEFDAGFFGIS 112
Cdd:cd00833 1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDR-WDADGYY-PDPGKPGKTYTRRGGFLDDVDAFDAAFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 113 AREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLF 192
Cdd:cd00833 78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 193 GFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWAEGV 272
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 273 GVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEA 352
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 353 QALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPW 432
Cdd:cd00833 318 EALAKVFGGSR-SADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPW 396
|
410 420
....*....|....*....|....*
gi 2733316673 433 PQLDRPRRAAVSSFGVSGTNAHVIV 457
Cdd:cd00833 397 PAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
35-907 |
0e+00 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 587.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 35 IAIVGMACRLPGGVSSPEELWRLVADGGDAISGFPADRgWDlETVYDPEPDRPGRSYVREGGFLQDAGEFDAGFFGISAR 114
Cdd:NF040607 102 IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGR-WS-EFAADPRIAERVAKANTRGGYLDDIKGFDAEFFALSPL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 115 EALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLFGF 194
Cdd:NF040607 180 EAENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQMLAVADPAEAHPYALTGTSSSIIANRVSYFFDF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 195 TGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSR-QRALAPDGRIKAFGSGADGTAWAEGVG 273
Cdd:NF040607 260 RGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 274 VLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQ 353
Cdd:NF040607 340 VVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEAD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 354 ALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPWP 433
Cdd:NF040607 420 ALGRVVGRGR-DADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWP 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 434 QLDRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPVIPWVLSAKSPEALRAQAD-------------------- 493
Cdd:NF040607 499 RYSGHAVAGVSGFGFGGTNAHVVVREVLPADLVEPEAQPDEDTEAELAGLTAEAKRLLAEaelaaefapaapegpvvplp 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 494 ----------RLAAAVAD------GGGTDLSAVAHTLAT---GRAvfdhRAVVLGTEAADLLAGARRIAEGRTGAFAFTG 554
Cdd:NF040607 579 vsgflpsrrrAAAADLADwleseeGRATPLADVARALARrnhGRS----RAVVLAHTHEEAIKGLRAVAEGKPGPGVFSA 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 555 -SRVRGRLALLFTGQGSQRLGMGRELHAAYPAFAAALDE--ALEQFgpglrEVMWSSVEdggAALD-----RTEHAQPAL 626
Cdd:NF040607 655 dAPAANGPVWVLSGFGSQHRKMAKQLYLENPVFAARIDEvdELVQD-----ESGYSIVE---LILDdeqtyDIETAQVGI 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 627 FAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQE---LPPG---GAMVAVEAAEAEVL 700
Cdd:NF040607 727 FAIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMGEgeaMLPGddiRLMALVEYSAEEIE 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 701 PLLG--PGVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPV 778
Cdd:NF040607 807 TVLAdfPDLEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTSQMDPLLGELAAELAGIEPQPLTVGL 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 779 VSTV-SGRLAEAG--VLTDPAYWVRQVRGTVRFHDAVTVLGARGATTALEVGPLGV-LTGMGErIRAAAGdeAPGTVFVP 854
Cdd:NF040607 887 YSSVdRGTFYRPGhePIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVaLMSVAA-TTFAAG--LHDAQLIP 963
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 2733316673 855 ALRGPGAETRDVLSAAGRLFTRGVAVNWRALLPATGHADLPTYPFQRRRYWLE 907
Cdd:NF040607 964 TLKRKEDESESVLNALAQLYVHGHDVDLRSLFGAGDYADIPRTRFKRKPYWLD 1016
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
35-459 |
6.17e-166 |
|
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: 489.15 E-value: 6.17e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 35 IAIVGMACRLPGgVSSPEELWRLVADGgdaisgfpadrgwdletvydpepdrpgrsyvreggfLQDAGEFDAGFFGISAR 114
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------------------LDDVDLFDAAFFGISPR 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 115 EALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYAtgvrklpegvdafvgmgtsgsvlsgrvsylfgf 194
Cdd:smart00825 44 EAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS--------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 195 tgpcMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWAEGVGV 274
Cdd:smart00825 91 ----VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 275 LVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQervirqalanaglstadvdaveahgtgttlgdpieaqa 354
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 355 llatygqgrgpddapLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPWPQ 434
Cdd:smart00825 209 ---------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPP 273
|
410 420
....*....|....*....|....*
gi 2733316673 435 LDRPRRAAVSSFGVSGTNAHVIVEQ 459
Cdd:smart00825 274 PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
34-846 |
2.90e-101 |
|
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: 351.62 E-value: 2.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 34 PIAIVGMAcRLPGGVSSPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGFLQDAgEFDAGFFGISA 113
Cdd:TIGR02813 8 PIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDH-WAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 114 REALAMDPQQRLFLETSWEALERAGIDPVSLR---GSDTGVFTGQMYHDYATGVRKLP--------EGV----------- 171
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGLPDGYDRdkiGITLGVGGGQKQSSSLNARLQYPvlkkvfkaSGVededsemlikk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 172 --DAFVGM------GTSGSVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYID 243
Cdd:TIGR02813 165 fqDQYIHWeensfpGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 244 FSRQRALAPDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQA 323
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 324 LANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRGpDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVL 403
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDND-QKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 404 PRTLHVDEPTDKVDWSSGSVELLTEARPWPQL--DRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPVIPWVL- 480
Cdd:TIGR02813 404 PPTINVDQPNPKLDIENSPFYLNTETRPWMQRedGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQTLLf 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 481 SAKSPEA----LRAQADRLAAAVADGGGTDLS-AVAHTL-----ATGRAVFdhrAVVLGTEAADLLAGARRIAEGRTGAF 550
Cdd:TIGR02813 484 TAANEKAlvssLKDWKNKLSAKADDQPYAFNAlAVENTLrtiavALARLGF---VAKNADELITMLEQAITQLEAKSCEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 551 --AFTGSRVR--------GRLALLFTGQGSQRLGMGRELHAAYPAFAAALDEALEQFG----PGLREVMW-------SSV 609
Cdd:TIGR02813 561 wqLPSGISYRksalvvesGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTqagkGALSPVLYpipvfndESR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 610 EDGGAALDRTEHAQPALFAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQElPPG--- 686
Cdd:TIGR02813 641 KAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAA-PTGead 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 687 -GAMVAVEAAEAEVLPLLGP------GVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPML 759
Cdd:TIGR02813 720 iGFMYAVILAVVGSPTVIANcikdfeGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 760 TAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVLTDPAYWVRQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGMGERI 839
Cdd:TIGR02813 800 KPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENT 879
|
....*..
gi 2733316673 840 RAAAGDE 846
Cdd:TIGR02813 880 LKDKENE 886
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
33-283 |
9.77e-100 |
|
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: 314.19 E-value: 9.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 33 EPIAIVGMACRLPGGVSsPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGfLQDAGEFDAGFFGIS 112
Cdd:pfam00109 1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADR-WDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 113 AREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFV---GMGTSGSVLSGRVS 189
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGspfAVGTMPSVIAGRIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 190 YLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWA 269
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
|
250
....*....|....
gi 2733316673 270 EGVGVLVLERLSDA 283
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
101-460 |
1.87e-31 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 128.37 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 101 AGE---FDAGFFgISAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGqmyhdyaTGVRKLPEGVDAFVGM 177
Cdd:PRK07314 49 AGEvkdFNPDDY-MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIG-------SGIGGLETIEEQHITL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 178 GTSG--------------SVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYID 243
Cdd:PRK07314 121 LEKGprrvspffvpmaiiNMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 244 FSRQRALA-----PDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASngLTAP--NGPSQ 316
Cdd:PRK07314 201 FAAARALStrnddPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH--MTAPapDGEGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 317 ERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGqgrgpDDAP-LWLGSLKSNIGHAQAAAGVAGVIKMV 395
Cdd:PRK07314 279 ARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFG-----EHAYkVAVSSTKSMTGHLLGAAGAVEAIFSV 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733316673 396 QAMREGVLPRTLHVDEPTDKVDwssgsVELLT-EARPwpqldRPRRAAVS-SFGVSGTNAHVIVEQY 460
Cdd:PRK07314 354 LAIRDQVIPPTINLDNPDEECD-----LDYVPnEARE-----RKIDYALSnSFGFGGTNASLVFKRY 410
|
|
| Docking |
pfam08990 |
Erythronolide synthase docking domain; Polyketide synthase (PKS) catalyzes the biosynthesis of ... |
1-29 |
2.58e-06 |
|
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: 44.62 E-value: 2.58e-06
10 20
....*....|....*....|....*....
gi 2733316673 1 MTDDKLVEALRAALTENEQLRQRHDRLLA 29
Cdd:pfam08990 1 ASEEKLVEYLRRSLAELERLRRRLRELEA 29
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
30-1020 |
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: 1105.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 30 RTTEPIAIVGMACRLPGgVSSPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGFLQDAGEFDAGFF 109
Cdd:COG3321 1 AADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADR-WDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 110 GISAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVS 189
Cdd:COG3321 79 GISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 190 YLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWA 269
Cdd:COG3321 159 YKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 270 EGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDP 349
Cdd:COG3321 239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 350 IEAQALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEA 429
Cdd:COG3321 319 IEAAALTAAFGQGR-PADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 430 RPWPQLDRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPViPWVLSAKSPEALRAQADRLAAAVADGGGTDLSA 509
Cdd:COG3321 398 RPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPPQ-LLVLSAKTEEALRALAARLAAFLEAHPDLDLAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 510 VAHTLATGRAVFDHRAVVLGTEAADLLAGARRIAEGRTGAFAFTG-SRVRGRLALLFTGQGSQRLGMGRELHAAYPAFAA 588
Cdd:COG3321 477 VAYTLATGRAHFEHRLAVVASSREELAAKLRALAAGEAAPGVVTGaAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 589 ALDEALEQFGP----GLREVMWSsvEDGGAALDRTEHAQPALFAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVW 664
Cdd:COG3321 557 ALDECDALLRPhlgwSLREVLFP--DEEESRLDRTEVAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 665 SLPDAARLVAARGRLMQELPPGGAMVAVEAAEAEVLPLLG--PGVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVK 742
Cdd:COG3321 635 SLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVEALLAgyDGVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRAR 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 743 RLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVlTDPAYWVRQVRGTVRFHDAVTVLGARGATT 822
Cdd:COG3321 715 RLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIPLISNVTGTWLTGEA-LDADYWVRHLRQPVRFADAVEALLADGVRV 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 823 ALEVGPLGVLTGMGERIRAAAGDeapgTVFVPALRGPGAETRDVLSAAGRLFTRGVAVNWRALLPATG--HADLPTYPFQ 900
Cdd:COG3321 794 FLEVGPGPVLTGLVRQCLAAAGD----AVVLPSLRRGEDELAQLLTALAQLWVAGVPVDWSALYPGRGrrRVPLPTYPFQ 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 901 RRRyWLERAAVSHTVTEEPMDQATPAGPEQQPEQQDQPQDEGPRPVLAAKLRELSEADGDRLLLDLVLAESAVVFEQQSL 980
Cdd:COG3321 870 RED-AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAA 948
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 2733316673 981 EAELGGDSPFFEMGLTSVGAVELRNRLVEATGLPLGPMLL 1020
Cdd:COG3321 949 AAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAA 988
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
33-457 |
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: 609.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 33 EPIAIVGMACRLPGGVSsPEELWRLVADGGDAISGFPADRgWDLETVYdPEPDRPGRSYVREGGFLQDAGEFDAGFFGIS 112
Cdd:cd00833 1 EPIAIVGMACRFPGAAD-PDEFWENLLEGRDAISEIPEDR-WDADGYY-PDPGKPGKTYTRRGGFLDDVDAFDAAFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 113 AREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLF 192
Cdd:cd00833 78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 193 GFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWAEGV 272
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 273 GVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEA 352
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 353 QALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPW 432
Cdd:cd00833 318 EALAKVFGGSR-SADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPW 396
|
410 420
....*....|....*....|....*
gi 2733316673 433 PQLDRPRRAAVSSFGVSGTNAHVIV 457
Cdd:cd00833 397 PAPAGPRRAGVSSFGFGGTNAHVIL 421
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
35-907 |
0e+00 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 587.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 35 IAIVGMACRLPGGVSSPEELWRLVADGGDAISGFPADRgWDlETVYDPEPDRPGRSYVREGGFLQDAGEFDAGFFGISAR 114
Cdd:NF040607 102 IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGR-WS-EFAADPRIAERVAKANTRGGYLDDIKGFDAEFFALSPL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 115 EALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLFGF 194
Cdd:NF040607 180 EAENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQMLAVADPAEAHPYALTGTSSSIIANRVSYFFDF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 195 TGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSR-QRALAPDGRIKAFGSGADGTAWAEGVG 273
Cdd:NF040607 260 RGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTPAVTLGFDElGGVLAPDGRIKAFSSDADGMVRSEGGG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 274 VLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQ 353
Cdd:NF040607 340 VVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQVDVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEAD 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 354 ALLATYGQGRgPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPWP 433
Cdd:NF040607 420 ALGRVVGRGR-DADKPALLGSAKTNFGHLESAAGAAGLAKVVLAMQHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWP 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 434 QLDRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPVIPWVLSAKSPEALRAQAD-------------------- 493
Cdd:NF040607 499 RYSGHAVAGVSGFGFGGTNAHVVVREVLPADLVEPEAQPDEDTEAELAGLTAEAKRLLAEaelaaefapaapegpvvplp 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 494 ----------RLAAAVAD------GGGTDLSAVAHTLAT---GRAvfdhRAVVLGTEAADLLAGARRIAEGRTGAFAFTG 554
Cdd:NF040607 579 vsgflpsrrrAAAADLADwleseeGRATPLADVARALARrnhGRS----RAVVLAHTHEEAIKGLRAVAEGKPGPGVFSA 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 555 -SRVRGRLALLFTGQGSQRLGMGRELHAAYPAFAAALDE--ALEQFgpglrEVMWSSVEdggAALD-----RTEHAQPAL 626
Cdd:NF040607 655 dAPAANGPVWVLSGFGSQHRKMAKQLYLENPVFAARIDEvdELVQD-----ESGYSIVE---LILDdeqtyDIETAQVGI 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 627 FAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQE---LPPG---GAMVAVEAAEAEVL 700
Cdd:NF040607 727 FAIQIALADLLRHHGAKPAAVVGHSMGEAAAAYAAGGLSLEDAVRVICHRSRLMGEgeaMLPGddiRLMALVEYSAEEIE 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 701 PLLG--PGVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPV 778
Cdd:NF040607 807 TVLAdfPDLEVCVYAAPTHTVIGGPREQVDAIVARAEAEGKFARKLQTKGASHTSQMDPLLGELAAELAGIEPQPLTVGL 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 779 VSTV-SGRLAEAG--VLTDPAYWVRQVRGTVRFHDAVTVLGARGATTALEVGPLGV-LTGMGErIRAAAGdeAPGTVFVP 854
Cdd:NF040607 887 YSSVdRGTFYRPGhePIHDVDYWVKGLRHSVWFTQAVRKAVDAGHTTFLELAPNPVaLMSVAA-TTFAAG--LHDAQLIP 963
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 2733316673 855 ALRGPGAETRDVLSAAGRLFTRGVAVNWRALLPATGHADLPTYPFQRRRYWLE 907
Cdd:NF040607 964 TLKRKEDESESVLNALAQLYVHGHDVDLRSLFGAGDYADIPRTRFKRKPYWLD 1016
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
35-459 |
6.17e-166 |
|
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: 489.15 E-value: 6.17e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 35 IAIVGMACRLPGgVSSPEELWRLVADGgdaisgfpadrgwdletvydpepdrpgrsyvreggfLQDAGEFDAGFFGISAR 114
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------------------LDDVDLFDAAFFGISPR 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 115 EALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYAtgvrklpegvdafvgmgtsgsvlsgrvsylfgf 194
Cdd:smart00825 44 EAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDYS--------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 195 tgpcMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWAEGVGV 274
Cdd:smart00825 91 ----VTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 275 LVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQervirqalanaglstadvdaveahgtgttlgdpieaqa 354
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 355 llatygqgrgpddapLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVELLTEARPWPQ 434
Cdd:smart00825 209 ---------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPWPP 273
|
410 420
....*....|....*....|....*
gi 2733316673 435 LDRPRRAAVSSFGVSGTNAHVIVEQ 459
Cdd:smart00825 274 PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
564-857 |
2.98e-113 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 351.70 E-value: 2.98e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 564 LFTGQGSQRLGMGRELHAAYPAFAAALDEALEQF----GPGLREVMWSsvEDGGAALDRTEHAQPALFAVEVALFRLLES 639
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALqpllGWSLLDVLLG--EDGAASLLDTEVAQPALFAVQVALARLLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 640 WDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQELPPGGAMVAVEAAEAEVLPLLGP---GVDLAAVNGPT 716
Cdd:smart00827 79 WGVRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGvpdRVSVAAVNSPS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 717 SVVLSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVLTDPA 796
Cdd:smart00827 159 SVVLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELDDAD 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2733316673 797 YWVRQVRGTVRFHDAV-TVLGARGATTALEVGPLGVLTGMGERIRAAAGdeapGTVFVPALR 857
Cdd:smart00827 239 YWVRNLREPVRFADAVrALLAEGGVTVFLEVGPHPVLTGPIKQTLAAAG----SAVVLPSLR 296
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
34-846 |
2.90e-101 |
|
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: 351.62 E-value: 2.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 34 PIAIVGMAcRLPGGVSSPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGFLQDAgEFDAGFFGISA 113
Cdd:TIGR02813 8 PIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDH-WAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 114 REALAMDPQQRLFLETSWEALERAGIDPVSLR---GSDTGVFTGQMYHDYATGVRKLP--------EGV----------- 171
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGLPDGYDRdkiGITLGVGGGQKQSSSLNARLQYPvlkkvfkaSGVededsemlikk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 172 --DAFVGM------GTSGSVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYID 243
Cdd:TIGR02813 165 fqDQYIHWeensfpGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 244 FSRQRALAPDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQA 323
Cdd:TIGR02813 245 FSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 324 LANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRGpDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVL 403
Cdd:TIGR02813 325 YDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDND-QKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 404 PRTLHVDEPTDKVDWSSGSVELLTEARPWPQL--DRPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPVIPWVL- 480
Cdd:TIGR02813 404 PPTINVDQPNPKLDIENSPFYLNTETRPWMQRedGTPRRAGISSFGFGGTNFHMVLEEYSPKHQRDDQYRQRAVAQTLLf 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 481 SAKSPEA----LRAQADRLAAAVADGGGTDLS-AVAHTL-----ATGRAVFdhrAVVLGTEAADLLAGARRIAEGRTGAF 550
Cdd:TIGR02813 484 TAANEKAlvssLKDWKNKLSAKADDQPYAFNAlAVENTLrtiavALARLGF---VAKNADELITMLEQAITQLEAKSCEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 551 --AFTGSRVR--------GRLALLFTGQGSQRLGMGRELHAAYPAFAAALDEALEQFG----PGLREVMW-------SSV 609
Cdd:TIGR02813 561 wqLPSGISYRksalvvesGKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMDSVFTqagkGALSPVLYpipvfndESR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 610 EDGGAALDRTEHAQPALFAVEVALFRLLESWDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQElPPG--- 686
Cdd:TIGR02813 641 KAQEEALTNTQHAQSAIGTLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAA-PTGead 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 687 -GAMVAVEAAEAEVLPLLGP------GVDLAAVNGPTSVVLSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPML 759
Cdd:TIGR02813 720 iGFMYAVILAVVGSPTVIANcikdfeGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPLVAHAQ 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 760 TAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVLTDPAYWVRQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGMGERI 839
Cdd:TIGR02813 800 KPFSAAIDKAKFNTPLVPLYSNGTGKLHSNDAAAIKKALKNHMLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENT 879
|
....*..
gi 2733316673 840 RAAAGDE 846
Cdd:TIGR02813 880 LKDKENE 886
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
33-283 |
9.77e-100 |
|
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: 314.19 E-value: 9.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 33 EPIAIVGMACRLPGGVSsPEELWRLVADGGDAISGFPADRgWDLETVYDPEPDRPGRSYVREGGfLQDAGEFDAGFFGIS 112
Cdd:pfam00109 1 EPVAIVGMGCRFPGGND-PEEFWENLLEGRDGISEIPADR-WDPDKLYDPPSRIAGKIYTKWGG-LDDIFDFDPLFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 113 AREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLPEGVDAFV---GMGTSGSVLSGRVS 189
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRGspfAVGTMPSVIAGRIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 190 YLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWA 269
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
|
250
....*....|....
gi 2733316673 270 EGVGVLVLERLSDA 283
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
559-839 |
3.37e-73 |
|
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: 244.65 E-value: 3.37e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 559 GRLALLFTGQGSQRLGMGRELHAAYPAFAAALDEALEQFGPGLREVMWSSVEDggaALDRTEHAQPALFAVEVALFRLLE 638
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEALGYDLSALCFEGPEE---ELNLTENTQPAILAASVAAYRALE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 639 SWDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQELPPG--GAMVAVEAAEAEVLPLL------GPGVDLA 710
Cdd:COG0331 78 EEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAVPAgpGGMAAVLGLDDEEVEALcaeaaqGEVVEIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 711 AVNGPTSVVLSGEEATVTAAADELAGQG-RRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRlaea 789
Cdd:COG0331 158 NYNSPGQIVISGEKEAVEAAAELAKEAGaKRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAA---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2733316673 790 gVLTDPAYW----VRQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGMGERI 839
Cdd:COG0331 234 -PVTDPEEIrellVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLSGLVKRI 286
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
122-457 |
9.33e-55 |
|
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: 194.01 E-value: 9.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 122 QQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKLP--EGVDAFVGMGTSGSVLSGRVSYLFGFTGPCM 199
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADamRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 200 TLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKAFGSGADGTAWAEGVGVLVLER 279
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 280 LSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATY 359
Cdd:cd00825 171 LEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 360 GqgrgpdDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDwssgsvELLTEARPwpqlDRPR 439
Cdd:cd00825 251 G------DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGL------NIVTETTP----RELR 314
|
330
....*....|....*...
gi 2733316673 440 RAAVSSFGVSGTNAHVIV 457
Cdd:cd00825 315 TALLNGFGLGGTNATLVL 332
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
564-880 |
1.65e-51 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 184.21 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 564 LFTGQGSQRLGMGRELHAAYPAFAAALDEALE----QFGPGLREVMWSSVEDGgaaLDRTEHAQPALFAVEVALFRLLES 639
Cdd:pfam00698 3 VFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEafkpQYGFSVSDVLRNNPEGT---LDGTQFVQPALFAMQIALAALLQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 640 WDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQELPPGGAMVAVEAAEAEVLPLLGPGVDLAAVNGPTSVV 719
Cdd:pfam00698 80 YGVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPDDVVGAVVNSPRSVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 720 LSGEEATVTAAADELAGQGRRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRLAEAGVLtDPAYWV 799
Cdd:pfam00698 160 ISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTL-SAEYWV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 800 RQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGMGERIRAAAGDEAPGTVFVPALRGPGAETRDVLSAAGRLFTRGVA 879
Cdd:pfam00698 239 RNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTLKSASDGKVATLVGTLIRDQTDFLVTFLYILAVAHLTGSA 318
|
.
gi 2733316673 880 V 880
Cdd:pfam00698 319 P 319
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
562-839 |
4.03e-51 |
|
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: 181.90 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 562 ALLFTGQGSQRLGMGRELHAAYPAFAAALDEALEQFGPGlrevMWSSVEDGGAA-LDRTEHAQPALFAVEVALFRLL-ES 639
Cdd:TIGR00128 4 AYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEALGYD----LKKLCQEGPAEeLNKTQYTQPALYVVSAILYLKLkEQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 640 WDVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQELPP--GGAMVAVEAAEAEVLPLL-----GPGVDLAAV 712
Cdd:TIGR00128 80 GGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAVPegGGAMAAVIGLDEEQLAQAceeatENDVDLANF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 713 NGPTSVVLSGEEATVTAAADELAGQG-RRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSgrlaeAGV 791
Cdd:TIGR00128 160 NSPGQVVISGTKDGVEAAAALFKEMGaKRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVD-----AKP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2733316673 792 LTDPAY----WVRQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGMGERI 839
Cdd:TIGR00128 235 YTNGDRikekLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVLTGLIKRI 286
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
34-457 |
5.92e-51 |
|
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: 185.43 E-value: 5.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 34 PIAIVGMACRLPGGVSsPEELWRLVADGGDAISGFPADRGWDLETVYDPEPDrpgrsyvreggflqdagEFDAGFFgISA 113
Cdd:cd00834 2 RVVITGLGAVTPLGNG-VEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVP-----------------DFDPEDY-LDR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 114 REALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTG-------QMYHDYATGVRKLPEGVDAFVGMGTSGSVLSG 186
Cdd:cd00834 63 KELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGsgigglaTIEEAYRALLEKGPRRVSPFFVPMALPNMAAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 187 RVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGRIKA-----FGS 261
Cdd:cd00834 143 QVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEkasrpFDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 262 GADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHG 341
Cdd:cd00834 223 DRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 342 TGTTLGDPIEAQALLATYgqgrGPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEP--TDKVDWs 419
Cdd:cd00834 303 TSTPLNDAAESKAIKRVF----GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPdpECDLDY- 377
|
410 420 430
....*....|....*....|....*....|....*....
gi 2733316673 420 sgsveLLTEARPWPQldrprRAAVS-SFGVSGTNAHVIV 457
Cdd:cd00834 378 -----VPNEAREAPI-----RYALSnSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
111-460 |
2.02e-50 |
|
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: 183.76 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 111 ISAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTG-------QMYHDYATGVRKLPEGVDAFVGMGTSGSV 183
Cdd:COG0304 60 LDRKELRRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGsgiggldTLEEAYRALLEKGPRRVSPFFVPMMMPNM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 184 LSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALA-----PDGRIKA 258
Cdd:COG0304 140 AAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddPEKASRP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 259 FGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVE 338
Cdd:COG0304 220 FDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYIN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 339 AHGTGTTLGDPIEAQALLATYGqgrgpDDAP-LWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPtD--- 414
Cdd:COG0304 300 AHGTSTPLGDAAETKAIKRVFG-----DHAYkVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENP-Dpec 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2733316673 415 KVDWssgsveLLTEARPwpqldRPRRAAVS-SFGVSGTNAHVIVEQY 460
Cdd:COG0304 374 DLDY------VPNEARE-----AKIDYALSnSFGFGGHNASLVFKRY 409
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
291-410 |
9.79e-44 |
|
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: 154.26 E-value: 9.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 291 LAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRgpDDAPL 370
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGA--RKQPL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2733316673 371 WLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVD 410
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
33-457 |
1.46e-42 |
|
"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: 160.68 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 33 EPIAIVGMACRLPGGVSSP--EELWRLVADGGDAISgfpadrgwdletvydPEPDRPGRSYVREGGFLQDAGefdagFFG 110
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDevEEFWEALREGRSGIA---------------PVARLKSRFDRGVAGQIPTGD-----IPG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 111 ISAREALAMDPQQRLFLETSWEALERAGI-DPVSLRGSDTGVFTGQ-----MYHDYATGVRKLPEGVDAFVGMGTSGSVL 184
Cdd:cd00828 61 WDAKRTGIVDRTTLLALVATEEALADAGItDPYEVHPSEVGVVVGSgmgglRFLRRGGKLDARAVNPYVSPKWMLSPNTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 185 SGRVSYLFGF-TGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMaTPEPYIDFSRQRALA-----PDGRIKA 258
Cdd:cd00828 141 AGWVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALStaeeePEEMSRP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 259 FGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPnGPSQERVIRQALANAGLSTADVDAVE 338
Cdd:cd00828 220 FDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVIS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 339 AHGTGTTLGDPIEAQALLATYgqgrGPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDW 418
Cdd:cd00828 299 AHGTSTPANDVAESRAIAEVA----GALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEH 374
|
410 420 430
....*....|....*....|....*....|....*....
gi 2733316673 419 SSgsveLLTEARPWPqlDRPRRAAVSSFGVSGTNAHVIV 457
Cdd:cd00828 375 LS----VVGLSRDLN--LKVRAALVNAFGFGGSNAALVL 407
|
|
| malonate_mdcH |
TIGR03131 |
malonate decarboxylase, epsilon subunit; Members of this protein family are the epsilon ... |
561-835 |
6.30e-38 |
|
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: 143.99 E-value: 6.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 561 LALLFTGQGSQRLGMGRELhAAYPAFAAALDEALEQFGPGLREVmwssveDGGAALDRTEHAQPALFAVEVALFRLLESW 640
Cdd:TIGR03131 1 IALLFPGQGSQRAGMLAEL-PDHPAVAAVLAEASDVLGIDPREL------DDAEALASTRSAQLCILAAGVAAWRALLAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 641 DVRPDFLAGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQELPPGGA--MVAVEAAEAEVLPLL-GPGVDLAAVNGPTS 717
Cdd:TIGR03131 74 LPRPSAVAGYSVGEYAAAVVAGVLTFDDALRLVALRAALMDQAVPGGYgmLAVLGLDLAAVEALIaKHGVYLAIINAPDQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 718 VVLSGEEATVTAAADELAGQG-RRVKRLRVSHAFHSALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRLAE--AGVLTD 794
Cdd:TIGR03131 154 VVIAGSRAALRAVAELARAAGaSRAKRLAVRVPSHTPLLAKAAEQFAEALAEIPLAAPRLPYLSGIDARLVRdaAQIRDD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2733316673 795 PAywvRQVRGTVRFHDAVTVLGARGATTALEVGPLGVLTGM 835
Cdd:TIGR03131 234 LA---RQIATPVDWHDCMQAAYERGARLVIELGPGDVLTKL 271
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
101-460 |
1.87e-31 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 128.37 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 101 AGE---FDAGFFgISAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGqmyhdyaTGVRKLPEGVDAFVGM 177
Cdd:PRK07314 49 AGEvkdFNPDDY-MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIG-------SGIGGLETIEEQHITL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 178 GTSG--------------SVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYID 243
Cdd:PRK07314 121 LEKGprrvspffvpmaiiNMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 244 FSRQRALA-----PDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASngLTAP--NGPSQ 316
Cdd:PRK07314 201 FAAARALStrnddPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH--MTAPapDGEGA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 317 ERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGqgrgpDDAP-LWLGSLKSNIGHAQAAAGVAGVIKMV 395
Cdd:PRK07314 279 ARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFG-----EHAYkVAVSSTKSMTGHLLGAAGAVEAIFSV 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2733316673 396 QAMREGVLPRTLHVDEPTDKVDwssgsVELLT-EARPwpqldRPRRAAVS-SFGVSGTNAHVIVEQY 460
Cdd:PRK07314 354 LAIRDQVIPPTINLDNPDEECD-----LDYVPnEARE-----RKIDYALSnSFGFGGTNASLVFKRY 410
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
35-460 |
3.65e-30 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 124.73 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 35 IAIVGMacrlpgGVSSP-----EELWRLVADGGDAISGFPADRGWDLETVYDPEPdrPGRSYVREGGFlqDAGEFdagff 109
Cdd:PRK06333 6 IVVTGM------GAVSPlgcgvETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQV--PDLAEDAEAGF--DPDRY----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 110 gISAREALAMDPQQRLFLETSWEALERAGIDPVSLR---------GSDTG---VFTGQMYHDYATGVRKL-PEGVDAF-V 175
Cdd:PRK06333 71 -LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEdrertatiiGSGVGgfpAIAEAVRTLDSRGPRRLsPFTIPSFlT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 176 GMGtsgsvlSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRAL----- 250
Cdd:PRK06333 150 NMA------AGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALstrfn 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 251 -APDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASngLTAP--NGPSQERVIRQALANA 327
Cdd:PRK06333 224 dAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYH--MTAGpeDGEGARRAMLIALRQA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 328 GLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRGpddapLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTL 407
Cdd:PRK06333 302 GIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGHVSG-----LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTL 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2733316673 408 HVDEPtdkvDWSSGSVELL-TEARPWPQldrpRRAAVSSFGVSGTNAHVIVEQY 460
Cdd:PRK06333 377 NLENP----DPAAEGLDVVaNKARPMDM----DYALSNGFGFGGVNASILFRRW 422
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
122-457 |
1.92e-29 |
|
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: 118.32 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 122 QQRLFLETSWEALERAGIDpvslRGSDTGVFTGQmyhdyatgvrklpegvdafVGMGTSGSVLSGRVSYLFGFT-GPCMT 200
Cdd:cd00327 7 ASELGFEAAEQAIADAGLS----KGPIVGVIVGT-------------------TGGSGEFSGAAGQLAYHLGISgGPAYS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 201 LDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATpepyidfsrqralapdgrikafgsgadgtawAEGVGVLVLERL 280
Cdd:cd00327 64 VNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVF-------------------------------GDGAAAAVVESE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 281 SDAERLGHRVLAVVRGSAVNQDGASnGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYG 360
Cdd:cd00327 113 EHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 361 QGrgpddaPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPrtlhvdeptdkvdwssgsvelltearpwPQLDRPRR 440
Cdd:cd00327 192 VR------SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIP----------------------------PTPREPRT 237
|
330
....*....|....*..
gi 2733316673 441 AAVSSFGVSGTNAHVIV 457
Cdd:cd00327 238 VLLLGFGLGGTNAAVVL 254
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
132-460 |
1.99e-29 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 122.49 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 132 EALERAGIDPVSLRGSD-TGVFTGQMyhdyATGVRKLPEGVDAFVGMGTS-----------GSVLSGRVSYLFGFTGPCM 199
Cdd:PTZ00050 87 EALADAKLDILSEKDQErIGVNIGSG----IGSLADLTDEMKTLYEKGHSrvspyfipkilGNMAAGLVAIKHKLKGPSG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 200 TLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALA------PDGRIKAFGSGADGTAWAEGVG 273
Cdd:PTZ00050 163 SAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRPFDKDRAGFVMGEGAG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 274 VLVLERLSDAERLGHRVLAVVRGSAVNQDGasNGLTAP--NGPSQERVIRQALANAG-LSTADVDAVEAHGTGTTLGDPI 350
Cdd:PTZ00050 243 ILVLEELEHALRRGAKIYAEIRGYGSSSDA--HHITAPhpDGRGARRCMENALKDGAnININDVDYVNAHATSTPIGDKI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 351 EAQALLATYGqgrGPDDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDwssgsVELLTEAR 430
Cdd:PTZ00050 321 ELKAIKKVFG---DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD-----LNLVQGKT 392
|
330 340 350
....*....|....*....|....*....|.
gi 2733316673 431 PWPQldRPRRAAVS-SFGVSGTNAHVIVEQY 460
Cdd:PTZ00050 393 AHPL--QSIDAVLStSFGFGGVNTALLFTKY 421
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
537-843 |
1.04e-28 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 118.71 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 537 AGARRIAEGRTGAFAFTGSRV-----RGRLALLFTGQGSQRLGMGRELHAAYPAFAAaLDEALEQFGPGLREVmwsSVED 611
Cdd:PLN02752 11 ASASRVSMSVSVGSQATAADAlfadyKPTTAFLFPGQGAQAVGMGKEAAEVPAAKAL-FDKASEILGYDLLDV---CVNG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 612 GGAALDRTEHAQPALFAVEVALFRLLESWDVRPDFL------AGHSIGEIAAAHVAGVWSLPDAARLVAARGRLMQEL-- 683
Cdd:PLN02752 87 PKEKLDSTVVSQPAIYVASLAAVEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMQAAad 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 684 PPGGAMVAVEAAEAEVLPLL--------GPG--VDLAAVNGPTSVVLSGE-EATVTAAADELAGQGRRVKRLRVSHAFHS 752
Cdd:PLN02752 167 AGPSGMVSVIGLDSDKVQELcaaaneevGEDdvVQIANYLCPGNYAVSGGkKGIDAVEAKAKSFKARMTVRLAVAGAFHT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 753 ALMDPMLTAFAEVAHGLEYREPRIPVVSTVSGRlaeagVLTDPA----YWVRQVRGTVRFHDAVTVLGARGATTALEVGP 828
Cdd:PLN02752 247 SFMEPAVDALEAALAAVEIRTPRIPVISNVDAQ-----PHSDPAtikkILARQVTSPVQWETTVKTLLEKGLEKSYELGP 321
|
330
....*....|....*
gi 2733316673 829 LGVLTGMGERIRAAA 843
Cdd:PLN02752 322 GKVIAGIVKRVDKGA 336
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
101-412 |
4.40e-28 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 118.58 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 101 AGEFDagFFGISAREALAMdpQQRLFLETSWEALERAGID-------------PVSLR-------GSDTGVFTGQMYHDY 160
Cdd:PRK06501 58 AGTVD--FLPESPFGASAL--SEALARLAAEEALAQAGIGkgdfpgplflaapPVELEwparfalAAAVGDNDAPSYDRL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 161 --ATGVRKLPEGVDAFVgmgtSGSVlSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATP 238
Cdd:PRK06501 134 lrAARGGRFDALHERFQ----FGSI-ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 239 EPYIDFSRQRAL-----APDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNG 313
Cdd:PRK06501 209 EALIRFSLLSALstqndPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 314 PSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRgpddAPLWLGSLKSNIGHAQAAAGVAGVIK 393
Cdd:PRK06501 289 SPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERL----ASIPVSSNKSMIGHTLTAAGAVEAVF 364
|
330
....*....|....*....
gi 2733316673 394 MVQAMREGVLPRTLHVDEP 412
Cdd:PRK06501 365 SLLTIQTGRLPPTINYDNP 383
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
185-453 |
4.49e-27 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 115.66 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 185 SGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRAL------APDGRIKA 258
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALstkfnsCPTEASRP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 259 FGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVE 338
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 339 AHGTGTTLGDPIEAQALLATYGqgrgpDDAP---LWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPtDK 415
Cdd:PLN02836 324 AHATSTPLGDAVEARAIKTVFS-----EHATsggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERP-DP 397
|
250 260 270
....*....|....*....|....*....|....*....
gi 2733316673 416 VdWSSGSVELLTEARpwpqldRPRRAAVS-SFGVSGTNA 453
Cdd:PLN02836 398 I-FDDGFVPLTASKA------MLIRAALSnSFGFGGTNA 429
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
85-458 |
3.40e-26 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 112.43 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 85 DRPGRSYVREGGFLQDAGEFDAGFFGISAREALAMDPQQRLFLE------TSWEALERAGIDPV-SLR------GSD-TG 150
Cdd:PRK07103 37 RRPGRQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSaqaalaAAREAWRDAALGPVdPDRiglvvgGSNlQQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 151 VFTGQMYHDYatgvRKLPEGVDAFVGMGTSGSVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALA- 229
Cdd:PRK07103 117 REQALVHETY----RDRPAFLRPSYGLSFMDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAv 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 230 GGVT--------------VMATpEPYIDfsrqralAPDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVR 295
Cdd:PRK07103 193 GALMdlsywecqalrslgAMGS-DRFAD-------EPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 296 GSAVNQDGasNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALlatygqgRGPDDAPLWLGSL 375
Cdd:PRK07103 265 GWSMRLDA--NRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAAL-------FASGLAHAWINAT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 376 KSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTD-KVDWssgsvellteARPWPQLDRPRRAAVSSFGVSGTNAH 454
Cdd:PRK07103 336 KSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDeRFRW----------VGSTAESARIRYALSLSFGFGGINTA 405
|
....
gi 2733316673 455 VIVE 458
Cdd:PRK07103 406 LVLE 409
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
133-412 |
1.27e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 101.60 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 133 ALERAG-IDPVSLRGSDTGVFTGQmyhdyATGVrklPEGVDAFVGMGTSGSV--LSG-------------RVSYLFGFTG 196
Cdd:PRK09116 84 ALEDAGlLGDPILTDGRMGIAYGS-----STGS---TDPIGAFGTMLLEGSMsgITAttyvrmmphttavNVGLFFGLKG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 197 PCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIdF-----SRQRALAPDGRIKAFGSGADGTAWAEG 271
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAV-FdtlfaTSTRNDAPELTPRPFDANRDGLVIGEG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 272 VGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASngLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIE 351
Cdd:PRK09116 235 AGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAE 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2733316673 352 AQALLATYGqgrgpDDAPlwLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEP 412
Cdd:PRK09116 313 SQATAAVFG-----ARMP--ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQV 366
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
146-460 |
3.31e-22 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 99.42 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 146 GSDTGVFTGqMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECA 225
Cdd:PRK14691 33 GAGIGGFPA-IAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEAD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 226 MALAGGVTVMATPEPYIDFSRQRALA------PDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAV 299
Cdd:PRK14691 112 VALCGGAEAVIDTVSLAGFAAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 300 NQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRGpddapLWLGSLKSNI 379
Cdd:PRK14691 192 SADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNA-----LAITSTKSAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 380 GHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPtdkvDWSSGSVELLT-EARPWPQldrpRRAAVSSFGVSGTNAHVIVE 458
Cdd:PRK14691 267 GHLLGAAGGLETIFTVLALRDQIVPATLNLENP----DPAAKGLNIIAgNAQPHDM----TYALSNGFGFAGVNASILLK 338
|
..
gi 2733316673 459 QY 460
Cdd:PRK14691 339 RW 340
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
192-460 |
5.10e-22 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 101.59 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 192 FGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALA-----PDGRIKAFGSGADGT 266
Cdd:PLN02787 278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddPTKASRPWDMNRDGF 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 267 AWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTL 346
Cdd:PLN02787 358 VMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 347 GDPIEAQALLATYGQgrgpdDAPLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDwssgsVELL 426
Cdd:PLN02787 438 GDLKEYQALMRCFGQ-----NPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD-----TKVL 507
|
250 260 270
....*....|....*....|....*....|....*
gi 2733316673 427 TEARPwPQLDrpRRAAVS-SFGVSGTNAHVIVEQY 460
Cdd:PLN02787 508 VGPKK-ERLD--IKVALSnSFGFGGHNSSILFAPY 539
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
100-459 |
7.80e-21 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 96.23 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 100 DAGEFDAGFFGI----------SAREALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQ-------MYHDYAT 162
Cdd:PRK08722 42 DTTNFSTRFAGLvkdfnceeymSKKDARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGSgigglglIEAGHQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 163 GVRKLPEGVDAFVGMGTSGSVLSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYI 242
Cdd:PRK08722 122 LVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 243 DFSRQRALA-----PDGRIKAFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQE 317
Cdd:PRK08722 202 GFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 318 RVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEAQALLATYGQGRGPDdapLWLGSLKSNIGHAQAAAGVAGVIKMVQA 397
Cdd:PRK08722 282 LAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQ---VLVSSTKSMTGHLLGAAGSVEAIITVMS 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2733316673 398 MREGVLPRTLHVDEPTDKVDwssgsVELLT-EARpwpQLDRPRRAAVSSFGVSGTNAHVIVEQ 459
Cdd:PRK08722 359 LVDQIVPPTINLDDPEEGLD-----IDLVPhTAR---KVESMEYAICNSFGFGGTNGSLIFKK 413
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
34-457 |
1.68e-20 |
|
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: 95.12 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 34 PIAIVGMACRLPGGVSSpEELWRLVADGGDAIsgfpadrgwDLETVYDPEpDRPGRSYVREGGFlqDAGEfdagffGISA 113
Cdd:cd00832 2 RAVVTGIGVVAPNGLGV-EEYWKAVLDGRSGL---------GPITRFDPS-GYPARLAGEVPDF--DAAE------HLPG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 114 REALAMDPQQRLFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHDYATGVRKL-------PEGVDAFVGMGTSGSVLSG 186
Cdd:cd00832 63 RLLPQTDRMTRLALAAADWALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELqklwskgPRHVSAYQSFAWFYAVNTG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 187 RVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGG---------ECAMALAGGVTVMATPEPYIDFSRQRALAPdgrik 257
Cdd:cd00832 143 QISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGtplvvsggvDSALCPWGWVAQLSSGRLSTSDDPARAYLP----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 258 aFGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNgltAPNGPSQERVIRQALANAGLSTADVDAV 337
Cdd:cd00832 218 -FDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG---SGRPPGLARAIRLALADAGLTPEDVDVV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 338 EAHGTGTTLGDPIEAQALLATYGQGRGPDDAPlwlgslKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVD 417
Cdd:cd00832 294 FADAAGVPELDRAEAAALAAVFGPRGVPVTAP------KTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG 367
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2733316673 418 wssgsVELLTeARPWPQldRPRRAAVSSFGVSGTNAHVIV 457
Cdd:cd00832 368 -----LDLVT-GRPRPA--ALRTALVLARGRGGFNSALVV 399
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
199-452 |
2.67e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 94.80 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 199 MTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALA------PDGRIKAFGSGADGTAWAEGV 272
Cdd:PRK07910 165 ITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMstnnddPAGACRPFDKDRDGFVFGEGG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 273 GVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPIEA 352
Cdd:PRK07910 245 ALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 353 QALLATYGQGRGPDDAPlwlgslKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDWSSGSVElltearpw 432
Cdd:PRK07910 325 KAINNALGGHRPAVYAP------KSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGE-------- 390
|
250 260
....*....|....*....|
gi 2733316673 433 PQLDRPRRAAVSSFGVSGTN 452
Cdd:PRK07910 391 PRPGNYRYAINNSFGFGGHN 410
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
119-460 |
6.17e-20 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 93.64 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 119 MDPQQ--------RLFLETSWEALERAGIDPVSLRGSDTGVFTG-------QMYHDYATGVRKLPEGVDAFVGMGTSGSV 183
Cdd:PRK08439 61 MDPKEvkkadrfiQLGLKAAREAMKDAGFLPEELDAERFGVSSAsgigglpNIEKNSIICFEKGPRKISPFFIPSALVNM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 184 LSGRVSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALA-----PDGRIKA 258
Cdd:PRK08439 141 LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStrnddPKKASRP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 259 FGSGADGTAWAEGVGVLVLERLSDAERLGHRVLAVVRGsaVNQDGASNGLTAPNGPSQERVIRQALANAGlsTADVDAVE 338
Cdd:PRK08439 221 FDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMAG--NPKIDYIN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 339 AHGTGTTLGDPIEAQALLATYGqgrGPDDAPLwLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDw 418
Cdd:PRK08439 297 AHGTSTPYNDKNETAALKELFG---SKEKVPP-VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECD- 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2733316673 419 ssgsvelltearpwpqLD----RPRRAAV-----SSFGVSGTNAHVIVEQY 460
Cdd:PRK08439 372 ----------------LDyipnVARKAELnvvmsNSFGFGGTNGVVIFKKV 406
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
951-1036 |
8.53e-19 |
|
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: 81.91 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 951 LRELSEADGDRLLLDLVLAESAVVFEQQSlEAELGGDSPFFEMGLTSVGAVELRNRLVEATGLPLGPMLLFDYPTPDYVV 1030
Cdd:smart00823 1 LAALPPAERRRLLLDLVREQVAAVLGHAA-AEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALA 79
|
....*.
gi 2733316673 1031 EHLRAQ 1036
Cdd:smart00823 80 EHLAAE 85
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
191-457 |
8.95e-17 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 83.56 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 191 LFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATPEPYIDFSRQRALAPDGrIKAFGSGADGTAWAE 270
Cdd:PRK05952 132 QIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 271 GVGVLVLERLSDAERLGHRVLAVVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHGTGTTLGDPI 350
Cdd:PRK05952 211 GGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 351 EAQALLATYGQGRGpddaplwLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPTDKVDwssgsveLLTEAR 430
Cdd:PRK05952 291 EANLIQALFPHRVA-------VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLN-------FVRQAQ 356
|
250 260
....*....|....*....|....*..
gi 2733316673 431 PWPQldrpRRAAVSSFGVSGTNAHVIV 457
Cdd:PRK05952 357 QSPL----QNVLCLSFGFGGQNAAIAL 379
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
132-460 |
1.73e-15 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 79.71 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 132 EALERAGIDPVSLRGSDTGVFTG--------QMYHDYATGVRKLPEGVDAFVGMGTSGSVLSGRVSYLFGFTGPCMTLDT 203
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGsgggstrnQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 204 ACSTSLVTLHLAVQALRGGECAMALAGGVT----VMATpepyiDFSRQRALA------PDGRIKAFGSGADGTAWAEGVG 273
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldwEMSC-----LFDAMGALStkyndtPEKASRAYDANRDGFVIAGGGG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 274 VLVLERLSDAERLGHRVLAVVRGSAVNQDGASngLTAPNGPSQERVIRQALANAglsTADVDAVEAHGTGTTLGDPIEAQ 353
Cdd:PRK07967 236 VVVVEELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMALATV---DTPIDYINTHGTSTPVGDVKELG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 354 ALLATYGqgrgpDDAPLwLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEptdkVDWSSGSVELLTEARPWP 433
Cdd:PRK07967 311 AIREVFG-----DKSPA-ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEE----LDPQAAGMPIVTETTDNA 380
|
330 340
....*....|....*....|....*...
gi 2733316673 434 QLDrprrAAVS-SFGVSGTNAHVIVEQY 460
Cdd:PRK07967 381 ELT----TVMSnSFGFGGTNATLVFRRY 404
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
418-528 |
3.20e-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: 72.58 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 418 WSSGSVELLTEARPWPqldrPRRAAVSSFGVSGTNAHVIVEQYPEQPEPEAAPAAPPVIpWVLSAKSPEALRAQADRLAA 497
Cdd:pfam16197 8 LLDGRLKVVTEPTPWP----GGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLPRL-VLLSGRTEEAVKALLEKLEN 82
|
90 100 110
....*....|....*....|....*....|.
gi 2733316673 498 AVADGGGTDLSAVAHTLATGRavFDHRAVVL 528
Cdd:pfam16197 83 HLDDAEFLSLLNDIHSLPISG--HPYRGYAI 111
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
188-456 |
1.00e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 74.11 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 188 VSYLFGFTGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGV------TVMAtpepyidFSRQRALAPdGRIKAFGS 261
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVdslcrlTLNG-------FNSLESLSP-QPCRPFSA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 262 GADGTAWAEGVGVLVLERLSDAERLghrvlavVRGSAVNQDGASNGLTAPNGPSQERVIRQALANAGLSTADVDAVEAHG 341
Cdd:PRK09185 215 NRDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 342 TGTTLGDPIEAQALLATYGQGrgpddapLWLGSLKSNIGHAQAAAGVAGVIKMVQAMREGVLPRTLHVDEPtdkvDWSSG 421
Cdd:PRK09185 288 TATPLNDAMESRAVAAVFGDG-------VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQP----DPALP 356
|
250 260 270
....*....|....*....|....*....|....*.
gi 2733316673 422 SVELLTEARPwpqldRPRRAAVS-SFGVSGTNAHVI 456
Cdd:PRK09185 357 PLYLVENAQA-----LAIRYVLSnSFAFGGNNCSLI 387
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
981-1036 |
2.44e-07 |
|
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: 49.08 E-value: 2.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2733316673 981 EAELGGDSPFF-EMGLTSVGAVELRNRLVEATGLPLGPMLLFDYPTPDYVVEHLRAQ 1036
Cdd:COG0236 22 PEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
983-1026 |
2.52e-07 |
|
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: 48.33 E-value: 2.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2733316673 983 ELGGDSPFFEMGLTSVGAVELRNRLVEATGLPLGPMLLFDYPTP 1026
Cdd:pfam00550 17 EIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTL 60
|
|
| Docking |
pfam08990 |
Erythronolide synthase docking domain; Polyketide synthase (PKS) catalyzes the biosynthesis of ... |
1-29 |
2.58e-06 |
|
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: 44.62 E-value: 2.58e-06
10 20
....*....|....*....|....*....
gi 2733316673 1 MTDDKLVEALRAALTENEQLRQRHDRLLA 29
Cdd:pfam08990 1 ASEEKLVEYLRRSLAELERLRRRLRELEA 29
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
125-238 |
9.52e-05 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 46.10 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 125 LFLETSWEALERAGIDPVSLRGSDTGVFTGQMYHdyatgvrklpegvdafvgmgtsgSVLSGRVSYLFGFTG-PCMTLDT 203
Cdd:cd00829 19 LAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQ-----------------------SFPGALIAEYLGLLGkPATRVEA 75
|
90 100 110
....*....|....*....|....*....|....*
gi 2733316673 204 ACSTSLVTLHLAVQALRGGECAMALAGGVTVMATP 238
Cdd:cd00829 76 AGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDV 110
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
102-235 |
1.19e-04 |
|
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: 44.99 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2733316673 102 GEFDAGFFGISAREALAmdpqqrlflETSWEALERAGIDPVSLrgsdTGVFTGQMyhdyatgvrkLPEGvdafvgmgtSG 181
Cdd:pfam00108 12 GSFGGSLKDVSAVELGA---------EAIKAALERAGVDPEDV----DEVIVGNV----------LQAG---------EG 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2733316673 182 SVLSGRVSYLFGF--TGPCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVM 235
Cdd:pfam00108 60 QNPARQAALKAGIpdSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
197-235 |
7.09e-04 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 43.24 E-value: 7.09e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2733316673 197 PCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVM 235
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESM 114
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
197-235 |
1.78e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 41.98 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2733316673 197 PCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVM 235
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESM 118
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
197-242 |
9.80e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 39.49 E-value: 9.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2733316673 197 PCMTLDTACSTSLVTLHLAVQALRGGECAMALAGGVTVMATpEPYI 242
Cdd:PRK05656 80 PAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSL-APYV 124
|
|
| |
