|
Name |
Accession |
Description |
Interval |
E-value |
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
7-363 |
7.00e-156 |
|
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: 443.24 E-value: 7.00e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 7 IGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGG---MMAGQRILGRVGLTGIPIVNVENACSSS 83
Cdd:cd00829 1 VGVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGrfqSFPGALIAEYLGLLGKPATRVEAAGASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 84 SSALRQAVMAIRSGEYDVVLVIGVEKLT------KFGGGTLPLEKEDWEVSQGLVMPALYAMRAQRYMHEYDLTPAQLAL 157
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMSdvptgdEAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTTREDLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 158 VSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAASDLTSGKYT 237
Cdd:cd00829 161 VAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGAASDTPS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 238 PGFR-DMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGASAIDGKIAVNPSG 316
Cdd:cd00829 241 LSERdDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGGDLPVNTSG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1817094313 317 GLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGG 363
Cdd:cd00829 321 GLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGT 367
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-379 |
5.90e-149 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 426.24 E-value: 5.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMAGQRILGRV-----GLTGIPIVN 75
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIAALiadyaGLAPIPATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFGGGTlPLE------KEDWEVSQGLVMPALYAMRAQRYMHEYD 149
Cdd:PRK06064 81 VEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPD-ATEaiaragDYEWEEFFGATFPGLYALIARRYMHKYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 150 LTPAQLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAAS 229
Cdd:PRK06064 160 TTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEYTDTPVWIKAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 230 DLTSGkyTPGF---RDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGASAI 306
Cdd:PRK06064 240 GQASD--TIALhdrKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQTYI 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817094313 307 DGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGE--CGARQVPDAKVGLSHATGGgiSGfdhGVCCIHIFTR 379
Cdd:PRK06064 318 GGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEaeKGRQQVIGAGYGLTHNVGG--TG---HTAVVHILSR 387
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
2-363 |
2.19e-115 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 341.11 E-value: 2.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 2 RDVAVIGTGLIPFGK------YPDktladLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMAGQRILGRVGLTGIPIVN 75
Cdd:PRK08256 1 NKVFVAGVGMTPFEKpgaswdYPD-----MAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYEVGMTGIPIVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT------KFGGGTLPLEKEDwEVSQGLVMPALYAMRAQ------- 142
Cdd:PRK08256 76 VNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQpgalgsVWDDRPSPLERFD-KALAELQGFDPAPPALRmfggagr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 143 RYMHEYDLTPAQLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSD 222
Cdd:PRK08256 155 EHMEKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 223 -PVRIAA----SDLTSGKYTPGFRDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGA 297
Cdd:PRK08256 235 rAVEIVAqamtTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817094313 298 FIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGG 363
Cdd:PRK08256 315 FIDDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLG 380
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
1-379 |
1.87e-97 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 295.40 E-value: 1.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGT---ALGGMMAGQRILGRVGLTGIPIVNVE 77
Cdd:PRK06157 6 KDKVAILGMGCTKFGERWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGThydEIGSGKSGTPLSRALRLPNIPVTRVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 78 NACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFGGGTLPL---EKEDWEVSQGLVMPALYAMRAQRYMHEYDLTPAQ 154
Cdd:PRK06157 86 NFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYGGLPVanpGTLADMTMPNVTAPGNFAQLASAYAAKYGVSRED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 155 L----ALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQY-RSDPVRIAAS 229
Cdd:PRK06157 166 LkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARALgKKDPVYVKAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 230 DLTSGKYT----PGFRDMTIPEiTVRGAKEAYEEAGL-GPQ-EIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGA 303
Cdd:PRK06157 246 QLAVSNGWelqyNGWDGSYFPT-TRIAARKAYREAGItDPReELSMAEVHDCFSITELVTMEDLGLSERGQAWRDVLDGF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817094313 304 SAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGGISgfdHGVCCIHIFTR 379
Cdd:PRK06157 325 FDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLGGAPG---QNVCSVSIVGR 397
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
2-362 |
2.89e-97 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 294.45 E-value: 2.89e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 2 RDVAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCG-TALGG--MMAGQRILGRVGLTGIPIVNVEN 78
Cdd:PRK12578 1 RRVAVIGVGNSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGsTAYRGieLYPAPIVAEYSGLTGKVPLRVEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 79 ACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKF-----------GGGTLplekedWEVSQ-GLVMPALYAMRAQRYMH 146
Cdd:PRK12578 81 MCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVdtstslaiggrGGNYQ------WEYHFyGTTFPTYYALYATRHMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 147 EYDLTPAQLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSD-PVR 225
Cdd:PRK12578 155 VYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKELKIDsPVW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 226 IA----ASDLTS----GKYTpGFRdmtipeITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGA 297
Cdd:PRK12578 235 ITgigyANDYAYvarrGEWV-GFK------ATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGKGGK 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817094313 298 FIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAK-VGLSHATGG 362
Cdd:PRK12578 308 FIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVGG 373
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
1-361 |
2.82e-87 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 269.33 E-value: 2.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYPdKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTAL----GGMMAGQRILGRVGLTGIPIVNV 76
Cdd:PRK06059 3 PEPVYILGAGMHPWGKWG-RDFVEYGVVAARAALADAGLDWRDVQLVVGADTIrngyPGFVAGATFAQALGWNGAPVSSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 77 ENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTK-F---GGGTLPlEKEDWEVSQ--GLVMPALYAMRAQRYMHEYDL 150
Cdd:PRK06059 82 YAACASGSQALQSARAQILAGLCDVALVVGADTTPKgFfapVGGERP-DDPDWLRFHliGATNPVYFALLARRRMDLYGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 151 TPAQLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYR---SDPVRIA 227
Cdd:PRK06059 161 TVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRHLgsvAGVPSVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 228 ASDLTSGKYTPGFRDM-----------TIPEITVRG--AKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGS 294
Cdd:PRK06059 241 AISTVTPRYPQHLPELpdiatdstaavPAPERVFKDqiLDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGLCPKGE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817094313 295 AGAFIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATG 361
Cdd:PRK06059 321 AEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQG 387
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-362 |
1.58e-79 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 249.09 E-value: 1.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM-----AGQRILGRVGLTGIPIVN 75
Cdd:PRK07516 1 MMTASIVGWAHTPFGKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSpqdfpASLVLQADPALRFKPATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFGG---GTLPL----EKEDWEVSQGlvMPALYAMRAQRYMHEY 148
Cdd:PRK07516 81 VENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTaevGDILLgasyLKEEGDTPGG--FAGVFGRIAQAYFQRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 149 DLTPAQLALVSVKNRRNGALNPDAQMRKPVTVE---EVLASRP-IADPFTLLQCCPTGDGAAALILCEAKLARQYRSdPV 224
Cdd:PRK07516 159 GDQSDALAMIAAKNHANGVANPYAQMRKDLGFEfcrTVSEKNPlVAGPLRRTDCSLVSDGAAALVLADAETARALQR-AV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 225 RIAASDLTSGKYTPGFRDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGAS 304
Cdd:PRK07516 238 RFRARAHVNDFLPLSRRDPLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPGQGARAIREGWT 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1817094313 305 AIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGG 362
Cdd:PRK07516 318 AKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMGG 375
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
4-365 |
1.66e-79 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 248.79 E-value: 1.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 4 VAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTAlGGMMAGQRILGRVGLTGIPIVNVENACSSS 83
Cdd:PRK06158 10 TAIVGAATAGLGEAPGLSAMELLAQAAHRALADAGLTMADVDGLFTASP-DDALWGLSVAEYLGIRPRFVDGTMIGGSSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 84 SSALRQAVMAIRSGEYDVVLVI-GVEKLTKFGGGTLPLEKEDWEVSQGLVMPA-LYAMRAQRYMHEYDLTPAQLALVSVK 161
Cdd:PRK06158 89 LAHLLPAALALEAGLCDVALICyGSNQRSAGGKLRSMLDPQPYEAPYKPVNPVsAYALAAARHMHQYGTTREQLAEVAVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 162 NRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIaasdLTSGKYTpGFR 241
Cdd:PRK06158 169 ARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRARDLPRPPVYV----LGAAAAT-WHR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 242 DMT-IPEITVRGAKE----AYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGASAIDGKIAVNPSG 316
Cdd:PRK06158 244 QISsMPDLTVTAAAEsgprAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1817094313 317 GLLAKGHPiGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGGIS 365
Cdd:PRK06158 324 GGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAHGNGGVLS 371
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
1-362 |
4.44e-71 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 228.64 E-value: 4.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGK-YPDKTLADLGWPAVKMAVKDADIAPAKIE---AAYCGTALGG-MMAGQRILGRVGLTGIPIVN 75
Cdd:PRK06365 15 SRDVYMVAAGVTKFDKaSPYMDFRERVKKAFDYAMNDAGLTLADIDgsvASYFSDHFQRqLLAGIMVQDYLGLVPKPSKR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKF----GGGTLPLEKE-DWEVSQGLVMPALYAMRAQRYMHEYDL 150
Cdd:PRK06365 95 IEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSHVntwkGNEFIALASDtNFDYPLGGFYTGYYAMMAVRHMYEFGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 151 TPAQLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAAsd 230
Cdd:PRK06365 175 TVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASEDKAFEITDKPVLIKA-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 231 LTSGKYT-------------------PGFRDMTIPEITV-----RGAKEAYEEAGLGP--QEIDVAEVHDAFSIAELLYY 284
Cdd:PRK06365 253 IGTGSDTlrladrpfgevpllpnespDDYKDLRYPGVHSfragrMAAKEAYEMAGITDplNDLDLIELHDAYTSSEIQTY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 285 EAFGFCERGSAGAFIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGAR------QVPDAKVGLSH 358
Cdd:PRK06365 333 EDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRIKKHfhddylQVKNAKRGLIH 412
|
....
gi 1817094313 359 ATGG 362
Cdd:PRK06365 413 SHAG 416
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
5-352 |
7.89e-61 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 200.59 E-value: 7.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 5 AVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGT-----------ALGgmMAGQRILGRVGLTGipi 73
Cdd:PRK07855 7 AIVGIGATEFSKNSGRSELRLACEAVLAALDDAGLAPSDVDGLVTFTmdtnpeiavarALG--IGELKFFSRIHYGG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 74 vnvenacSSSSSALRQAVMAIRSGEYDVVLVI-------GVekltKFGGGTLPLEKE--------DWEVSQGLVMPA-LY 137
Cdd:PRK07855 82 -------GAACATVQQAAMAVATGVADVVVCYrafnersGM----RFGQGQTGLAENptstgvdyGWSYPHGLLTPAaWV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 138 AMRAQRYMHEYDLTPAQLALVSVKNRRNGALNPDAQM-RKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLA 216
Cdd:PRK07855 151 AMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFyGRPITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 217 RQYRSDPVRIAASDLTSGK----YTPGFRD--MTIPEITVrGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFC 290
Cdd:PRK07855 231 RDLKQRPAVIKAAAQGSGAdqymMTSYYRDdiTGLPEMGL-VARQLWAQSGLGPADIDTAILYDHFTPFVLMQLEELGFC 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817094313 291 ERGSAGAFIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAveiVRQLRGEcGARQVPDA 352
Cdd:PRK07855 310 GRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGIAEA---VRQLRGT-SVNQVPGV 367
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
2-361 |
5.36e-58 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 193.50 E-value: 5.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 2 RDVAVIGTGLIPFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTAL----GGMMAGQRILGRVGLTGIPIVNVE 77
Cdd:PRK06065 9 KRVAVIGAGLTLFRRRLLETPQELAWEAASKALDEAGLELKDIDCVVIGSAPdafdGVHMKGEYLSHGSGGIRKPVSRVY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 78 NACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFGGGTLPLEKEDWE-VSQGLVMPAL---YAMRAQRYMHEYDLTPA 153
Cdd:PRK06065 89 VGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMSPARPHPQAVFRYIWDpILEKPLNPNLiwiFAMEMHRYMATYGIKKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 154 QLALVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAASDLTS 233
Cdd:PRK06065 169 EIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRYTDTPVWVEGVGWTL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 234 GKYTPGFRDMTIPEITVRGAKEAYEEAGL-GPQ-EIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGASAIDGKIA 311
Cdd:PRK06065 249 DNTEWPNRDLAYPRYVEFAARMAYKMAGIeRPRkEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIP 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1817094313 312 VNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVP-DAKVGLSHATG 361
Cdd:PRK06065 329 SSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVKkPVHTGVAQAWG 379
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-363 |
8.35e-57 |
|
nondecarboxylating condensing enzymes; In general, thiolases 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. 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: 238422 [Multi-domain] Cd Length: 393 Bit Score: 190.40 E-value: 8.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 7 IGTGLIPFGKYPDKTLAD-------LGWPAVKMAVKDADIAPAKIEAAYCGTALG---GMMAGQR-ILGRVGLTGIPIVN 75
Cdd:cd00826 1 AGAAMTAFGKFGGENGADandlaheAGAKAIAAALEPAGVAAGAVEEACLGQVLGageGQNCAQQaAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTkFGGGTLPLEKEDWEVSQGLVM------PALYAMRAQRYMHEYD 149
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-TSAENNAKEKHIDVLINKYGMracpdaFALAGQAGAEAAEKDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 150 LTPAQLALVSVKNRR---NGALNPDAQMRKPVTVEEVLASRPIADP---FTLLQCCPTGDGAAALILCEAKLARQYRSDP 223
Cdd:cd00826 160 RFKDEFAKFGVKGRKgdiHSDADEYIQFGDEASLDEIAKLRPAFDKedfLTAGNACGLNDGAAAAILMSEAEAQKHGLQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 224 VRIA------ASDLTSGKYTPGFRDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGA 297
Cdd:cd00826 240 KAREiqalemITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGQGGA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1817094313 298 FIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGG 363
Cdd:cd00826 320 LVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGG 385
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
1-363 |
6.42e-56 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 188.02 E-value: 6.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPF-GKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTA---LGGMMAGQRILG-RVGLTGIPIVN 75
Cdd:PRK08313 2 KRLAAVLGTGQTKYvAKRQDVSMAGLVREAIDRALADAGLTWDDIDAVVVGKApdfFEGVMMPELFLAdALGATGKPLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKfgggtlplEKEDWEVS------QGLVMPA--LYAMRAQRYMHE 147
Cdd:PRK08313 82 VHTAGSVGGSTAVVAASLVQSGVYRRVLAVAWEKQSE--------SNAMWALSipvpftKPVGAGAggYFAPHVRAYIRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 148 YDLTPAQLALVSVKNRRNGALNPDAQMRKP-VTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVR- 225
Cdd:PRK08313 154 SGAPEHIGAMVAVKDRLNGAKNPYAHLHQPdITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAGRPVAw 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 226 IAASDLTSGKYTPGFRDMTIPEITVRGAKEAYEEAGLGP--QEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGA 303
Cdd:PRK08313 234 IHGTAMRTEPLAFAGRDQVNPQAGRDAAAALWKAAGITDprDEIDVAEIYVPFSWFEPMWLENLGFAPEGEGWKLTEAGE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 304 SAIDGKIAVNPSGGLLAkGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGGG 363
Cdd:PRK08313 314 TAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYGGG 372
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
19-362 |
2.83e-53 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 181.42 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 19 DKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMAGQRILGRV------GLTGIPIVNVENACSSSSSALRQAVM 92
Cdd:PRK06289 23 GRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGHLGAMpatvhpALWGVPASRHEAACASGSVATLAAMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 93 AIRSGEYDVVLVIGVEKLTKFGG--GTLPLEKEDW---EVSQGLVM-PALYAMRAQRYMHEYDLTPAQLALVSVKNRRNG 166
Cdd:PRK06289 103 DLRAGRYDVALVVGVELMKTVPGdvAAEHLGAAAWtghEGQDARFPwPSMFARVADEYDRRYGLDEEHLRAIAEINFANA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 167 ALNPDAQMR-----KPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQY--------------RSDPV--- 224
Cdd:PRK06289 183 RRNPNAQTRgwafpDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLASDAYLRDYadarpiprikgwghRTAPLgle 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 225 -RIAASDltSGKYT-PGFRdmtipeitvRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESG 302
Cdd:PRK06289 263 qKLDRSA--GDPYVlPHVR---------QAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTGPGESWKAIENG 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 303 ASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGG 362
Cdd:PRK06289 332 EIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFGTLNIGG 391
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
13-370 |
4.77e-52 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 177.97 E-value: 4.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 13 PFGKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMmAGQRILGRVGLTGIPIVNVENACSSSSSALRQAVM 92
Cdd:PRK08142 16 PTRKAPDKSVAQLHAEVAKGALADAGLSLADVDGYFCAGDAPGL-GPASMVDYLGLKLRHVDSTETGGSSYLAHVGHAAQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 93 AIRSGEYDVVLVI----------GVEKLTKFGGGTLPLekeDWEVSQGLVMPALYAMRAQRYMHEYDLTPAQLALVSVKN 162
Cdd:PRK08142 95 AIAAGKCSVALITlagrprsegsSGTEPRNWGADAPDA---PFEAPYGPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 163 RRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIaasdLTSGKYTPGFRD 242
Cdd:PRK08142 172 SHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDGGGALVVVRPEIARSLKRPLVKV----LGAGEAIKGQMG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 243 MTIpEITVRGAK----EAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGA-SAIDGKIAVNPSGG 317
Cdd:PRK08142 248 GKV-DLTYSGAAwsgpAAFAEAGVTPADIKYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNlISGVGKLPFNTDGG 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1817094313 318 LLAKGHPIGATGAAQAVEIVRQLRGECG-ARQVPDAKVGLSHATGGGIsGFDHG 370
Cdd:PRK08142 327 GLCNNHPANRGGMTKVIEAVRQLRGEAHpAVQVPNCDLALAHGTGGLL-GSRHG 379
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
14-349 |
1.50e-47 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 167.38 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 14 FGKYPDKTLADLGWPAVKMAVKDA--DIAPAKIEAAYCGTALGGMMAGQRILG--RVGLTGI----------PIVNVENA 79
Cdd:PTZ00455 40 FGKKENKTLEELLATAIQGTLENTglDGKAALVDKVVVGNFLGELFSSQGHLGpaAVGSLGQsgasnallykPAMRVEGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 80 CSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFG---GGTLPLEKEDWEVSQGL---VMPALYAMRaQRYMHEYD-LTP 152
Cdd:PTZ00455 120 CASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarvGGDYLARAADYRRQRKLddfTFPCLFAKR-MKYIQEHGhFTM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 153 AQLALVSVKNRRNGALNPDAQMR-KPVTVEEVLASRP----------IADPFTLLQCCPTGDGAAALILCEAKLARQYRS 221
Cdd:PTZ00455 199 EDTARVAAKAYANGNKNPLAHMHtRKLSLEFCTGASDknpkflgnetYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 222 DP-----VRIAASDLTSGKYTPGFRDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAG 296
Cdd:PTZ00455 279 SPndsrlVEIKSLACASGNLYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAK 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1817094313 297 AFIESGASAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQV 349
Cdd:PTZ00455 359 DLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQM 411
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
87-359 |
3.26e-44 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 157.22 E-value: 3.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 87 LRQAVMAIRSGEYDVVLVIGVEK---------LTKFGggTLPLekedWEVSQGLVMP-ALYAMRAQRYMHEYDLTPAQLA 156
Cdd:PRK06066 92 LAHAVMHINSGLANVVVVEAHSKpsdiltfsdVVKFA--MDPI----YVRPIGPPNPhFIAGLDAVKFMSRKGITREDLA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 157 LVSVKNRRNGALNPDAQMRKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAASDLTSGKY 236
Cdd:PRK06066 166 LVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKLTDDPVWIKGIGWSTESS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 237 TPGFRDMTIPEITVRGAKEAYEEAGLG-PQ-EIDVAEVHDAFSIAELLYYEAFGFCERGSAGAFIESGASAIDGKIAVNP 314
Cdd:PRK06066 246 NLETAELGKANYMRIAADMAYKMAGIEsPRkEVDAAEVDDRYSYKELQHIEALRLSEEPEKDSLLREGNFDPQGELPVNP 325
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1817094313 315 SGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQvPDAKVGLSHA 359
Cdd:PRK06066 326 SGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVAS 369
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
12-365 |
5.59e-27 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 110.40 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 12 IPFGK----YPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGgmMAGQRILGRVG--LTGIPI----VNVENACS 81
Cdd:TIGR01930 7 TPIGKfggsLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQ--AGEQQNIARQAalLAGLPEsvpaYTVNRQCA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 82 SSSSALRQAVMAIRSGEYDVVLVIGVEKLT--------------KFGGGTLP--LEKEDWEVSQGLVMPALYAMRAQRY- 144
Cdd:TIGR01930 85 SGLQAVILAAQLIRAGEADVVVAGGVESMSrvpygvprslrwgvKPGNAELEdaRLKDLTDANTGLPMGVTAENLAKKYg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 145 -----MHEYDLTPAQLAL--------------VSVKNRRNG-ALNPDAQMRKPVTVeEVLAS-RPIADP---FTLLQCCP 200
Cdd:TIGR01930 165 isreeQDEYALRSHQRAAkaweeglfkdeivpVTVKGRKGPvTVSSDEGIRPNTTL-EKLAKlKPAFDPdgtVTAGNSSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 201 TGDGAAALILCEAKLARQYRSDPVRIAASDLTSGKYTPGFRDMTIPEItvrgaKEAYEEAGLGPQEIDVAEVHDAFSIAE 280
Cdd:TIGR01930 244 LNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAI-----PKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 281 LLYYEAFGFcergsagafiesgasaIDGKIAVNpsGGLLAKGHPIGATGAAQAVEIVRQLRgecgaRQvpDAKVGLS--- 357
Cdd:TIGR01930 319 LACIKELGL----------------DLEKVNVN--GGAIALGHPLGASGARIVTTLLHELK-----RR--GGRYGLAtmc 373
|
....*...
gi 1817094313 358 HATGGGIS 365
Cdd:TIGR01930 374 IGGGQGAA 381
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
6-365 |
6.06e-26 |
|
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: 107.18 E-value: 6.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 6 VIGTGL-IPFGKYP----DKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGgmmAGQ-RILGRVG--LTGIPI---- 73
Cdd:cd00751 1 VIVSAVrTPIGRFGgalkDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ---AGEgQNPARQAalLAGLPEsvpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 74 VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT--------KFGGGTLPLEKEDWEVSQGLVMP-ALYAM--RAQ 142
Cdd:cd00751 78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSrapyllpkARRGGRLGLNTLDGMLDDGLTDPfTGLSMgiTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 143 RYMHEYDLTPAQL---ALVS----VKNRRNGALNPD------AQMRKPVTVE-----------EVLAS-RPIADPF---T 194
Cdd:cd00751 158 NVAEKYGISREEQdefALRShqraAAAQEAGRFKDEivpvevPGRKGPVVVDrdegprpdttlEKLAKlKPAFKKDgtvT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 195 LLQCCPTGDGAAALILCEAKLARQYRSDP-VRIAASDLTSGKytpgFRDMTI-PeitVRGAKEAYEEAGLGPQEIDVAEV 272
Cdd:cd00751 238 AGNASGINDGAAAVLLMSEEKAKELGLKPlARIVGYAVAGVD----PAIMGIgP---VPAIPKALKRAGLTLDDIDLIEI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 273 HDAFSIAELLYYEAFGfcergsagafiesgasaIDGKIaVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVpda 352
Cdd:cd00751 311 NEAFAAQALACLKELG-----------------LDPEK-VNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGL--- 369
|
410
....*....|...
gi 1817094313 353 kVGLSHATGGGIS 365
Cdd:cd00751 370 -ATMCIGGGQGAA 381
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
86-362 |
5.61e-24 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 101.30 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 86 ALRQAVMAIRSGEYDVVLVIGVEKLTKfgG---GTLPLEKEDWevsqgLVMP------ALYAMRAQRYMHEYDLTPAQLA 156
Cdd:PRK07937 89 ALYEAWVKLLTGEVDTALVYGFGKSSA--GtlrRVLALQLDPY-----TVAPlwpdsvSMAGLQARAGLDAGKWTEEQMA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 157 LVSVKNRRNGALNPDAQmrKPVTVEEVLASRPIADPFTLLQCCPTGDGAAALILCEAKLARQYRSDPVRIAASDLTSGKY 236
Cdd:PRK07937 162 EVAARSRADARRNPSAE--PSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGDRARELRERPAWITGIEHRIESP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 237 TPGFRDMTIPEITVRGAKEAyeeAGLGPQEIDVAEVHDAFSIAELLYYEAFGfcergsagafiesgasaIDGKIAVNPSG 316
Cdd:PRK07937 240 SLGARDLTRSPSTALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALG-----------------LGDKTKVNPSG 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1817094313 317 GLLAkGHPIGATGAAQAVEIVRQ-LRGEcgARQVpdakvgLSHATGG 362
Cdd:PRK07937 300 GALA-ANPMFAAGLERIGEAARHiWDGS--ARRA------LAHATSG 337
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-341 |
4.55e-23 |
|
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: 99.37 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYpDKTLA-----DLGWPAVKMAVKDADIAPAKIEAAYCGTALGgmmAGQ-RILGRVG--LTGIP 72
Cdd:COG0183 1 MREVVIVDAVRTPFGRF-GGALAdvradDLGAAVIKALLERAGLDPEAVDDVILGCVLQ---AGQgQNPARQAalLAGLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 73 I----VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTK---FGGGTLPLEKEDWEVSQGLVMPALYAMRAQRYM 145
Cdd:COG0183 77 EsvpaVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRapmLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 146 --------HEYDLTPAQ---LAL---------------------VSVKNRR-NGALNPDAQMRKPVTVeEVLAS-RPIAD 191
Cdd:COG0183 157 getaenvaERYGISREEqdaFALrshqraaaaiaagrfddeivpVEVPDRKgEVVVDRDEGPRPDTTL-EKLAKlKPAFK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 192 PF---TLLQCCPTGDGAAALILCEAKLARQYRSDP-VRIAASDLTSGKYtpgfRDMTI-PeitVRGAKEAYEEAGLGPQE 266
Cdd:COG0183 236 KDgtvTAGNASGINDGAAALLLMSEEAAKELGLKPlARIVAYAVAGVDP----EIMGIgP---VPATRKALARAGLTLDD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1817094313 267 IDVAEVHDAFSIAELLYYEAFGfcergsagafiesgasaIDGKIaVNPSGGLLAKGHPIGATGAAQAVEIVRQLR 341
Cdd:COG0183 309 IDLIEINEAFAAQVLAVLRELG-----------------LDPDK-VNVNGGAIALGHPLGASGARILVTLLHELE 365
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-213 |
4.08e-21 |
|
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: 91.60 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 4 VAVIGTGLIPFGKYP----DKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMmAGQRILGRVGL-TGIPI----V 74
Cdd:pfam00108 1 VVIVSAARTPFGSFGgslkDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAG-EGQNPARQAALkAGIPDsapaV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 75 NVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTK---------FGGGTLPLEKE--------DWEVSQGLVMpaly 137
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHapyalptdaRSGLKHGDEKKhdllipdgLTDAFNGYHM---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 138 AMRAQRYMHEYDLTPAQLALVSVKNRRNGALNPDAQM------------RKP---VTVEEVLASRPIADPFTLLQ----- 197
Cdd:pfam00108 156 GLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKfkdeivpvtvkgRKGkptVDKDEGIRPPTTAEPLAKLKpafdk 235
|
250 260
....*....|....*....|....
gi 1817094313 198 --------CCPTGDGAAALILCEA 213
Cdd:pfam00108 236 egtvtagnASPINDGAAAVLLMSE 259
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
25-363 |
4.73e-19 |
|
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: 85.57 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 25 LGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM---AGQRILGRVGLTGIPIVNVENACSSSSSALRQAVMAIRSGEYDV 101
Cdd:cd00327 10 LGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEfsgAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 102 VLVIGVEKltkfgggtlplekedwevsqglvmpalyamraqrymheydltpaqlalvsvknrrngalnpdaqmrkpvtve 181
Cdd:cd00327 90 VLAGGSEE------------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 182 evlasrpiadpftllqcCPTGDGAAALILCEAKLARQYRSDPV-RIAASDLTSGKYTPGFrdMTIPEITVRGAKEAYEEA 260
Cdd:cd00327 98 -----------------FVFGDGAAAAVVESEEHALRRGAHPQaEIVSTAATFDGASMVP--AVSGEGLARAARKALEGA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 261 GLGPQEIDVAEVHDAFSIAELLYYEAFGFCErgsagafiesgasaiDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQL 340
Cdd:cd00327 159 GLTPSDIDYVEAHGTGTPIGDAVELALGLDP---------------DGVRSPAVSATLIMTGHPLGAAGLAILDELLLML 223
|
330 340
....*....|....*....|....*
gi 1817094313 341 RGECGA--RQVPDAKVGLSHATGGG 363
Cdd:cd00327 224 EHEFIPptPREPRTVLLLGFGLGGT 248
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
18-366 |
6.32e-19 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 87.47 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADLgwpaVKMAVKDADIAPAKIEAAYCGTAL--------GGMMAgqRILGRVGLTgIPIVNVENACSSSSSALRQ 89
Cdd:PRK06445 32 PEELAAML----INRLIEKTGIKPEEIDDIITGCALqvgenwlyGGRHP--IFLARLPYN-IPAMAVDRQCASSLTTVSI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 90 AVMAIRSGEYDVVLVIGVEKLTKFGGGTLPL-----------EKEDWEVSQGLVM----PALYAMR--AQRYMHEYDLTP 152
Cdd:PRK06445 105 GAMEIATGMADIVIAGGVEHMTRTPMGDNPHiepnpklltdpKYIEYDLTTGYVMgltaEKLAEEAgiKREEMDRWSLRS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 153 AQLA------------LVSVKNRRNGA---LNPDAQMRKPVTVEEVLASRPIADP---FTLLQCCPTGDGAAALILCEAK 214
Cdd:PRK06445 185 HQLAakaiqegyfkdeILPIEVEVEGKkkvVDVDQSVRPDTSLEKLAKLPPAFKPdgvITAGNSSPLNSGASYVLLMSKK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 215 LARQYRSDPV-RIAASdltsgkytpGFRDMTiPEIT----VRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGf 289
Cdd:PRK06445 265 AVKKYGLKPMaKIRSF---------GFAGVP-PAIMgkgpVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELG- 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817094313 290 cergsagafiesgasaIDGKIaVNPSGGLLAKGHPIGATGAAQAVEIVRQLrgecgarQVPDAKVGLSHATGGGISG 366
Cdd:PRK06445 334 ----------------LDPET-VNIKGGAIAIGHPLGATGARIVGTLARQL-------QIKGKDYGVATLCVGGGQG 386
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
24-330 |
2.02e-16 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 80.05 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 24 DLGWPAVKMAV-KDADIAPAKIEAAYCGTALGGMMAGQRIlGRV-----GLTGIPIVNVENACSSSSSALRQAVMAIRSG 97
Cdd:PRK07851 29 DLAAQMVRAALdKVPALDPTDIDDLMLGCGLPGGEQGFNM-ARVvavllGYDFLPGTTVNRYCSSSLQTTRMAFHAIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 98 EYDVVLVIGVEKLTKFGGGTL--------PLEKEDWEVS----------------QGLVMPALYAM-------------- 139
Cdd:PRK07851 108 EGDVFISAGVETVSRFAKGNSdslpdtknPLFAEAQARTaaraeggaeawhdpreDGLLPDVYIAMgqtaenvaqltgis 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 140 -------------RAQRYMH----EYDLTPAQLALVSVKNRRNGAlnpdaqmRKPVTVEEVLASRPIADP---FTLLQCC 199
Cdd:PRK07851 188 reeqdewgvrsqnRAEEAIAngffEREITPVTLPDGTVVSTDDGP-------RAGTTYEKVSQLKPVFRPdgtVTAGNAC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 200 PTGDGAAALILCEAKLARQYRSDPV-RIAASDLTSgkytpgfrdmTIPEIT----VRGAKEAYEEAGLGPQEIDVAEVHD 274
Cdd:PRK07851 261 PLNDGAAAVVIMSDTKARELGLTPLaRIVSTGVSG----------LSPEIMglgpVEASKQALARAGMSIDDIDLVEINE 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1817094313 275 AFSIAELLYYEAFGfcergsagafiesgasaIDGKiAVNPSGGLLAKGHPIGATGA 330
Cdd:PRK07851 331 AFAAQVLPSARELG-----------------IDED-KLNVSGGAIALGHPFGMTGA 368
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
23-330 |
6.60e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 69.35 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 23 ADLGWPAVKMAVKDADIAPAKIEAAY--CGTALGGMmAGQriLGRV-----GLT-GIPIVNVENACSSSSSALRQAVMAI 94
Cdd:PRK07801 27 ADLGAHVLKGLVDRTGIDPAAVDDVIfgCVDTIGPQ-AGN--IARTswlaaGLPeEVPGVTVDRQCGSSQQAIHFAAQAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 95 RSGEYDVVLVIGVEKLTK------------FGGGTLPLEKEDW-------EVSQ--GLVMPALYAMRAQRYMHEYDLTPA 153
Cdd:PRK07801 104 MSGTQDLVVAGGVQNMSQipissamtageqLGFTSPFAESKGWlhrygdqEVSQfrGAELIAEKWGISREEMERFALESH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 154 QLALVSVKN----RRNGALNPDAQMRKP--VTVEEVLASRPIADPFTLLQCCP--TGDGAAALILCEAKLARQYrsdpvr 225
Cdd:PRK07801 184 RRAFAAIRAgrfdNEIVPVGGVTVDEGPreTSLEKMAGLKPLVEGGRLTAAVAsqISDGASAVLLASERAVKRH------ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 226 iaasdltsgKYTPGFRdmtIPEITVRGA-------------KEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEafgfcer 292
Cdd:PRK07801 258 ---------GLTPRAR---IHHLSVRGDdpvfmltapipatRYALEKTGLSIDDIDVVEINEAFAPVVLAWLK------- 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 1817094313 293 gsagafiESGASAIDgkiaVNPSGGLLAKGHPIGATGA 330
Cdd:PRK07801 319 -------ETGADPAK----VNPNGGAIALGHPLGATGA 345
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-341 |
8.42e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 68.97 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKY----PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTAL-GGmmAGQ---RILGRvgLTGIP 72
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFggslKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLqGG--QGQipsRQAAR--AAGIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 73 ----IVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT-------------KFGGGTLplekEDWEVSQGL---- 131
Cdd:PRK08235 77 wevqTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSnapyilpgarwgyRMGDNEV----IDLMVADGLtcaf 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 132 --VMPALYAMRA-------QRYMHEYDLTPAQLAL--------------VSVKNRRNGAL--NPDAQMRKPVTVEEVLAS 186
Cdd:PRK08235 153 sgVHMGVYGGEVakelgisREAQDEWAYRSHQRAVsaheegrfeeeivpVTIPQRKGDPIvvAKDEAPRKDTTIEKLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 187 RPIADP---FTLLQCCPTGDGAAALILCEAKLARQYRSDP---------VRIAASDLTSgkyTPGFrdmtipeitvrGAK 254
Cdd:PRK08235 233 KPVFDKtgtITAGNAPGVNDGAAALVLMSEDRAKQEGRKPlatilahtaIAVEAKDFPR---TPGY-----------AIN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 255 EAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERgsagafiesgasaidgKIAVNpsGGLLAKGHPIGATGAAQAV 334
Cdd:PRK08235 299 ALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE----------------KVNVN--GGAVALGHPIGASGARIIV 360
|
....*..
gi 1817094313 335 EIVRQLR 341
Cdd:PRK08235 361 TLIHELK 367
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-363 |
3.06e-12 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 67.34 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKYP---DKTLA-DLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMaGQRILGRVGL-TGIP--- 72
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGrsfSKIKApQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGV-GQNPAGQAAYhAGLPfgv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 73 ---IVNVenACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT----------KFGGGTLpLEK----EDWEVSQGLVmPA 135
Cdd:PRK06366 80 tkyTVNV--VCASGMLAVESAAREIMLGERDLVIAGGMENMSnapfllpsdlRWGPKHL-LHKnykiDDAMLVDGLI-DA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 136 LY----AMRAQRYMHEYDLTPAQLALVSVKNRRNG-----------------ALNPDAQMRKpVTVEEVLASRPIADPFT 194
Cdd:PRK06366 156 FYfehmGVSAERTARKYGITREMADEYSVQSYERAiratesgefrneivpfnDLDRDEGIRK-TTMEDLAKLPPAFDKNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 195 LL---QCCPTGDGAAALILCEAKLARQYRSDPV-RIAASDltSGKYTP-GFRDMTIPeitvrGAKEAYEEAGLGPQEIDV 269
Cdd:PRK06366 235 ILtagNSAQLSDGGSALVMASEKAINEYGLKPIaRITGYE--SASLDPlDFVEAPIP-----ATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 270 AEVHDAFSIAELLYYEAFgfcergsagafiesgasAIDGKiAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRgecgARQV 349
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQL-----------------KIDNE-RFNVNGGAVAIGHPIGNSGSRIIVTLINALK----TRHM 365
|
410
....*....|....
gi 1817094313 350 PDAKVGLSHATGGG 363
Cdd:PRK06366 366 KTGLATLCHGGGGA 379
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
18-113 |
5.49e-12 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 65.90 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM---AGQRILGRVGLTGIPIVNVENACSSSSSALRQAVMAI 94
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLfpsTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALI 126
|
90
....*....|....*....
gi 1817094313 95 RSGEYDVVLVIGVEKLTKF 113
Cdd:COG0332 127 RSGQAKNVLVVGAETLSRI 145
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-363 |
3.98e-10 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 60.94 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKY----PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGgmmAGQ-RILGR-VGL-TGIPI 73
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFggalKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQ---AGAgQNPARqAALkAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 74 ----VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT-------------KFGGGTLplekED-------WEVSQ 129
Cdd:PRK05790 78 evpaLTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSqaphvlpgsrwgqKMGDVEL----VDtmihdglTDAFN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 130 GLVMPALYAMRAQRYM------HEYDLTPAQLAL--------------VSVKNRRNGAL--NPDAQMRkPVTVEEVLAS- 186
Cdd:PRK05790 154 GYHMGITAENLAEQYGitreeqDEFALASQQKAEaaikagrfkdeivpVTIKQRKGDPVvvDTDEHPR-PDTTAESLAKl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 187 RPIADP---FTLLQCCPTGDGAAALILCEAKLARQYRSDPV-RIAASDLTSGkytpgfrDMTIPEI-TVRGAKEAYEEAG 261
Cdd:PRK05790 233 RPAFDKdgtVTAGNASGINDGAAAVVVMSEAKAKELGLTPLaRIVSYAVAGV-------DPAIMGIgPVPAIRKALEKAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 262 LGPQEIDVAEVHDAF------SIAELlyyeafgfcergsagafiesgasAIDGKIaVNPSGGLLAKGHPIGATGAAQAVE 335
Cdd:PRK05790 306 WSLADLDLIEINEAFaaqalaVEKEL-----------------------GLDPEK-VNVNGGAIALGHPIGASGARILVT 361
|
410 420
....*....|....*....|....*...
gi 1817094313 336 IVRQLRgecgaRQvpDAKVGLSHATGGG 363
Cdd:PRK05790 362 LLHEMK-----RR--GAKKGLATLCIGG 382
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
15-364 |
1.11e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 59.52 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 15 GKYPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTAL----GGMMAGQRILGrvglTGIPI----VNVENACSSSSSA 86
Cdd:PRK06954 24 GEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLpagqGQAPARQAALG----AGLPLsvgcTTVNKMCGSGMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 87 LRQAVMAIRSGEYDVVLVIGVEKLTKfGGGTLPLEKEDWEVSQGLVMPALY------AMRAQRYM--------HEYDLT- 151
Cdd:PRK06954 100 AMFAHDMLVAGSVDVIVAGGMESMTN-APYLLPKARGGMRMGHGQVLDHMFldgledAYDKGRLMgtfaeecaGEYGFTr 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 152 PAQLALVSVKNRRNGALNPDAQMR---KPVTVE----EVLASR------------PIADP-------FTLLQCCPTGDGA 205
Cdd:PRK06954 179 EAQDAFAIESLARAKRANEDGSFAweiAPVTVAgkkgDTVIDRdeqpfkanpekiPTLKPafsktgtVTAANSSSISDGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 206 AALILCEAKLARQYRSDPVRIAASDLTSGKYTPGFrdMTIPeitVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELlyye 285
Cdd:PRK06954 259 AALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKF--TTAP---VGAIRKLFEKNGWRAAEVDLFEINEAFAVVTM---- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 286 afgfcergsagafiesgASAIDGKIA---VNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARQVPDAKVGLSHATGG 362
Cdd:PRK06954 330 -----------------AAMKEHGLPhekVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAM 392
|
..
gi 1817094313 363 GI 364
Cdd:PRK06954 393 GI 394
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
18-341 |
1.12e-09 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 59.63 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADlgwpAVKMAVKDA-DIAPAKIEAAYCGTAlggMMAGQRIL--GRVGL------TGIPIVNVENACSSSSSALR 88
Cdd:PRK09052 31 PDDLLAH----VLRSAVAQVpGLDPKLIEDAIVGCA---MPEAEQGLnvARIGAllaglpNSVGGVTVNRFCASGLQAVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 89 QAVMAIRSGEYDVVLVIGVEKLT------------------------KFGGGtLPLEK--EDWEVS---QGLV-----MP 134
Cdd:PRK09052 104 MAADRIRVGEADVMIAAGVESMSmvpmmgnkpsmspaifardenvgiAYGMG-LTAEKvaEQWKVSredQDAFaleshQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 135 ALYAMRAQRYMHE---YDLTPAQLAL----VSVKNRRngaLNPDAQMRKPVTVEEVLASRPIADP---FTLLQCCPTGDG 204
Cdd:PRK09052 183 AIAAQQAGEFKDEitpYEITERFPDLatgeVDVKTRT---VDLDEGPRADTSLEGLAKLKPVFANkgsVTAGNSSQTSDG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 205 AAALILCEAKLARQYRSDPVRIAASDLTSGkyTPgfrdmtiPEITVRGAKEA----YEEAGLGPQEIDVAEVHDAFSIAE 280
Cdd:PRK09052 260 AGAVILVSEKALKQFNLTPLARFVSFAVAG--VP-------PEIMGIGPIEAipaaLKQAGLKQDDLDWIELNEAFAAQS 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817094313 281 LlyyeafgfcergsagAFIESgaSAIDGKiAVNPSGGLLAKGHPIGATGAAQAVEIVRQLR 341
Cdd:PRK09052 331 L---------------AVIRD--LGLDPS-KVNPLGGAIALGHPLGATGAIRTATVVHGLR 373
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
18-113 |
2.37e-09 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 57.94 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM---AGQRILGRVGLTGIPIVNVENACSSSSSALRQAVMAI 94
Cdd:cd00830 46 PGETTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLfpaTACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLI 125
|
90
....*....|....*....
gi 1817094313 95 RSGEYDVVLVIGVEKLTKF 113
Cdd:cd00830 126 RSGGAKNVLVVGAETLSRI 144
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
254-363 |
6.99e-09 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 53.41 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 254 KEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERgsagafiesgasaidgkiAVNPSGGLLAKGHPIGATGAAQA 333
Cdd:pfam02803 29 PKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGARIL 90
|
90 100 110
....*....|....*....|....*....|
gi 1817094313 334 VEIVRQLRGEcgarqvpDAKVGLSHATGGG 363
Cdd:pfam02803 91 VTLLHELKRR-------GGKYGLASLCIGG 113
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
18-113 |
1.17e-08 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 55.85 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM---AGQRILGRVGLTGIPIVNVENACSSSSSALRQAVMAI 94
Cdd:PRK09352 48 PDETTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPDYAfpsTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFI 127
|
90
....*....|....*....
gi 1817094313 95 RSGEYDVVLVIGVEKLTKF 113
Cdd:PRK09352 128 RSGAYKNVLVIGAEKLSRI 146
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
29-341 |
1.47e-08 |
|
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: 55.87 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 29 AVKMAVKDADIAPAKIEAA----YCGTALGGM-----------------------------MAGQRILGRVGLTGIPIVN 75
Cdd:COG0304 78 AAREALADAGLDLDEVDPDrtgvIIGSGIGGLdtleeayrallekgprrvspffvpmmmpnMAAGHVSIRFGLKGPNYTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 76 VeNACSSSSSALRQAVMAIRSGEYDVVLVIGVEKltkfgggtlplekedwEVSQGLVMpALYAMRAqrymheydltpaql 155
Cdd:COG0304 158 S-TACASGAHAIGEAYRLIRRGRADVMIAGGAEA----------------AITPLGLA-GFDALGA-------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 156 alVSVKNRrngalNPDAqmrkpvtveevlASRPI---ADPFTLlqccptGDGAAALILCEAKLARQyRSDPV--RIAASD 230
Cdd:COG0304 206 --LSTRND-----DPEK------------ASRPFdkdRDGFVL------GEGAGVLVLEELEHAKA-RGAKIyaEVVGYG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 231 LTSGKYtpgfrDMTIPEITVRGA----KEAYEEAGLGPQEIDVAEVH----DAFSIAELL-YYEAFGfcERGSagafies 301
Cdd:COG0304 260 ASSDAY-----HITAPAPDGEGAaramRAALKDAGLSPEDIDYINAHgtstPLGDAAETKaIKRVFG--DHAY------- 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1817094313 302 gasaidgKIAVNPSGGLLakGHPIGATGAAQAVEIVRQLR 341
Cdd:COG0304 326 -------KVPVSSTKSMT--GHLLGAAGAIEAIASVLALR 356
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
23-341 |
1.55e-08 |
|
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: 56.01 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 23 ADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMAGQRILG---------------------------------RVGLT 69
Cdd:cd00834 72 AQFALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnmaagqvaiRLGLR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 70 GiPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEkltkfgggtlplekedwEVSQGLVMPALYAMRaqrymheyd 149
Cdd:cd00834 152 G-PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE-----------------ALITPLTLAGFAALR--------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 150 ltpaqlalvsvknrrngALNPDAQMRKpvtveevLASRPIA---DPFTLlqccptGDGAAALILCEAKLARQyRSDPV-- 224
Cdd:cd00834 205 -----------------ALSTRNDDPE-------KASRPFDkdrDGFVL------GEGAGVLVLESLEHAKA-RGAKIya 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 225 RIAASDLTSGKYtpgfrDMTIPEITVRGA----KEAYEEAGLGPQEIDVAEVH-------DafsIAELLYYEAFgFCERG 293
Cdd:cd00834 254 EILGYGASSDAY-----HITAPDPDGEGAaramRAALADAGLSPEDIDYINAHgtstplnD---AAESKAIKRV-FGEHA 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1817094313 294 SagafiesgasaidgKIAVNPSGGLLakGHPIGATGAAQAVEIVRQLR 341
Cdd:cd00834 325 K--------------KVPVSSTKSMT--GHLLGAAGAVEAIATLLALR 356
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
23-330 |
1.14e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 53.19 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 23 ADLGWPAVKMAVKDADIAPAKIEAAYCGTAlggMMAGQRI--LGRVGLTG------IPIVNVENACSSSSSALRQAVMAI 94
Cdd:PRK06504 27 ADLAAQVLDALVDRSGADPALIEDVIMGCV---SQVGEQAtnVARNAVLAsklpesVPGTSIDRQCGSSQQALHFAAQAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 95 RSGEYDVVLVIGVEKLTK---FGGGTLPlEKEDWEVSQGLVMPALYA-------MRAQRYMHEYDLTPAQL---ALVS-- 159
Cdd:PRK06504 104 MSGTMDIVIAAGVESMTRvpmGSPSTLP-AKNGLGHYKSPGMEERYPgiqfsqfTGAEMMAKKYGLSKDQLdefALQShq 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 160 --VKNRRNGALNP-------------------DAQMRKPVTVEEVLASRPIAD-----PFTLLQCCptgDGAAALILCEA 213
Cdd:PRK06504 183 raIAATQAGKFKAeivpleitradgsgemhtvDEGIRFDATLEGIAGVKLIAEggrltAATASQIC---DGASGVMVVNE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 214 KLARQYRSDPV-RIAASDLTSGkytpgfrDMTIP-EITVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGfce 291
Cdd:PRK06504 260 RGLKALGVKPLaRIHHMTVIGG-------DPVIMlEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATG--- 329
|
330 340 350
....*....|....*....|....*....|....*....
gi 1817094313 292 rgsagafiesgasAIDGKIAVNpsGGLLAKGHPIGATGA 330
Cdd:PRK06504 330 -------------ADPERLNVN--GGAIALGHPLGASGT 353
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
17-106 |
2.22e-07 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 52.05 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 17 YPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALG-GMMAGQ--RILGRVGLTGIPIVNVENACSSSSSALRQAVMA 93
Cdd:cd00827 43 GDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPiDKGKSAatYLAELLGLTNAEAFDLKQACYGGTAALQLAANL 122
|
90
....*....|...
gi 1817094313 94 IRSGEYDVVLVIG 106
Cdd:cd00827 123 VESGPWRYALVVA 135
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
17-330 |
2.55e-07 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 52.46 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 17 YPDKTLAdlgwPAVKMAVKDADIAPAKIEAAYCGTALGGmmAGQR-ILGRVG--LTGIP----IVNVENACSSSSSALRQ 89
Cdd:PLN02287 70 YPDDLLA----PVLKAVVEKTGLNPSEVGDIVVGTVLAP--GSQRaNECRMAafYAGFPetvpVRTVNRQCSSGLQAVAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 90 AVMAIRSGEYDVVLVIGVEKLTKF---GGGTLPLEKEDWEVSQGLVMPAlyAMRAQRYMHEYDLTPAQLALVSVKNRRNG 166
Cdd:PLN02287 144 VAAAIKAGFYDIGIGAGVESMTTNpmaWEGGVNPRVESFSQAQDCLLPM--GITSENVAERFGVTREEQDQAAVESHRKA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 167 A-------------------LNPDAQMRKPVTVEEVLASRPIADPFTLLQCCP---------------TGDGAAALILCE 212
Cdd:PLN02287 222 AaatasgkfkdeivpvhtkiVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPvfkkngtttagnssqVSDGAGAVLLMK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 213 AKLARQyRSDPVRIAASDLTSGKYTPGFrdMTI-PEITVRGAKEAyeeAGLGPQEIDVAEVHDAFSiaellyyEAFGFCe 291
Cdd:PLN02287 302 RSVAMQ-KGLPILGVFRSFAAVGVDPAV--MGIgPAVAIPAAVKA---AGLELDDIDLFEINEAFA-------SQFVYC- 367
|
330 340 350
....*....|....*....|....*....|....*....
gi 1817094313 292 RGSAGAFIESgasaidgkiaVNPSGGLLAKGHPIGATGA 330
Cdd:PLN02287 368 CKKLGLDPEK----------VNVNGGAIALGHPLGATGA 396
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
87-362 |
3.14e-07 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 52.22 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 87 LRQAVMAIRSGEYDVVLVIGVEKL---------------TKFGGGTLPLEKEDW-------EVSQGLVMPA-LYAMRAQR 143
Cdd:PRK08257 96 VNEAALRIAAGEADVALVAGAEAQstatklrkagekldwTPQDEGPLADRGGDPrpmaspaELRHGLDRPVyVYPLFENA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 144 YMHEYDLTPAQLAlvsvknRRNGAL----------NPDAQMRKPVTVEEVL----ASRPIADPFTLLQCC-PTGDGAAAL 208
Cdd:PRK08257 176 LRAALGRSPEEHR------AEMGELwapfsavaakNPHAWIPRERSAEEIVtptpDNRMIAWPYTKLMNAnDMVDQGAAV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 209 ILCEAKLARQYRSDPVRI-------AASDLtsgkYTPGFRDM--TIPEITVRGAKeAYEEAGLGPQEIDVAEVHDAFSIA 279
Cdd:PRK08257 250 LLTSVAKARRLGVPEDRWvylhggaDAHDP----YDILERPDlhRSPAIRAAGRR-ALALAGLGIDDIDAFDLYSCFPSA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 280 ELLYYEAFGFcergsagafiesgasAIDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRGECGARqvpdakvGLSHA 359
Cdd:PRK08257 325 VQVAARELGL---------------DLDDPRPLTVTGGLPFFGGPGNNYVTHAIAEMVERLRANPGRR-------GLVTA 382
|
...
gi 1817094313 360 TGG 362
Cdd:PRK08257 383 NGG 385
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
47-107 |
3.65e-07 |
|
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: 51.79 E-value: 3.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1817094313 47 AYCGTALGGMMAGQRILGRVGLTGiPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGV 107
Cdd:cd00833 138 AYAATGTSRAFLANRISYFFDLRG-PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGV 197
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
68-330 |
5.91e-07 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 51.12 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 68 LTGIPI----VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLtkfggGTLPLE-------KEDWEVSQGLVMPAL 136
Cdd:PRK08947 75 LAGIPHsvpaVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM-----GHVPMNhgvdfhpGLSKNVAKAAGMMGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 137 YA-MRAQryMH--------EYDLTPAQLALVSVKNRR-------------NGAL---NPDAQMRKPVTVEEVLASRPIAD 191
Cdd:PRK08947 150 TAeMLGK--MHgisreqqdAFAARSHQRAWAATQEGRfkneiipteghdaDGVLklfDYDEVIRPETTVEALAALRPAFD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 192 P----FTLLQCCPTGDGAAALILCEAKLARQYRSDP-VRIaasdltsgkytpgfRDMTI----PEIT----VRGAKEAYE 258
Cdd:PRK08947 228 PvngtVTAGTSSALSDGASAMLVMSESRAKELGLKPrARI--------------RSMAVagcdPSIMgygpVPATQKALK 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817094313 259 EAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERgsagafiesgasaIDGKiaVNPSGGLLAKGHPIGATGA 330
Cdd:PRK08947 294 RAGLSISDIDVFELNEAFAAQSLPCLKDLGLLDK-------------MDEK--VNLNGGAIALGHPLGCSGA 350
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
203-347 |
2.70e-06 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 48.80 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 203 DGAAALILCEAKLARQYRSDPV-RIAASdlTSGKYTPgfRDMTI-PeitVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAE 280
Cdd:PRK09050 258 DGAAALLLASEAAAKKHGLTPRaRILGM--ATAGVEP--RIMGIgP---APATRKLLARLGLTIDQFDVIELNEAFAAQG 330
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1817094313 281 LLYYEAFGFCergsagafiesgasaiDGKIAVNPSGGLLAKGHPIGATGAAQAVEIVRQLRgECGAR 347
Cdd:PRK09050 331 LAVLRQLGLA----------------DDDARVNPNGGAIALGHPLGMSGARLVLTALHQLE-RTGGR 380
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-341 |
3.23e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 48.83 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKY----PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMMAGQriLGRV-----GL-TG 70
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFggafKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA--IGRVaaldaGLpVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 71 IPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT---------KFGGGTLPLEKEDW-----EVSQGLVMPAL 136
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSnvefyttdmRWGVRGGGVQLHDRlargrETAGGRRFPVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 137 YAM--RAQRYMHEYDLTPAQ---LAL---------------------VSVKNRRNGAL--NPDAQMRKPVTVEEVLASRP 188
Cdd:PRK06205 159 GGMieTAENLRREYGISREEqdaLAVrshqravaaqeagrfddeivpVTVPQRKGDPTvvDRDEHPRADTTLESLAKLRP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 189 I---ADP---FTLLQCCPTGDGAAA-LILCEAKLARQYRSDPVRIAASDLTSgkYTPgfRDMTI-PeitVRGAKEAYEEA 260
Cdd:PRK06205 239 ImgkQDPeatVTAGNASGQNDAAAAcLVTTEDKAEELGLRPLARLVSWAVAG--VEP--SRMGIgP---VPATEKALARA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 261 GLGPQEIDVAEVHDAFSIAELLYYEAFGFCERGSAgafiesgasaidgKIAVNPSGGLLakGHPIGATGAAQAVEIVRQL 340
Cdd:PRK06205 312 GLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEE-------------RLNVNGSGISL--GHPVGATGGRILATLLREL 376
|
.
gi 1817094313 341 R 341
Cdd:PRK06205 377 Q 377
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-340 |
5.69e-06 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 48.03 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGKY----PDKTLADLGWPAVKMAVKDADIAPAKIeaaycgtalGGMMAGQRI--------LGRVGL 68
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFggslKDVAPTDLGATVVREALARAGVDPDQV---------GHVVFGHVIpteprdmyLSRVAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 69 --TGIPI----VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTK---------FGG------------GTL--P 119
Cdd:PRK09051 73 inAGVPQetpaFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRapyllpaarWGArmgdaklvdmmvGALhdP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 120 LEK-----------EDWEVSQglVMPALYAM----RAQRYMHEYDLTpAQLALVSVKNRR-NGALNPDAQMRKPVTVEEV 183
Cdd:PRK09051 153 FGTihmgvtaenvaAKYGISR--EAQDALALeshrRAAAAIAAGYFK-DQIVPVEIKTRKgEVVFDTDEHVRADTTLEDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 184 LASRPI--ADPFTLLQCCPTG--DGAAALILCEAKLARQYRSDPV-RIAAsdltsgkYT-PGFRDMTIPEITVRGAKEAY 257
Cdd:PRK09051 230 AKLKPVfkKENGTVTAGNASGinDGAAAVVLAEADAAEARGLKPLaRLVG-------YAhAGVDPEYMGIGPVPATQKAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 258 EEAGLGPQEIDVAEVHDAFSIAELLYYEAFGFCERgsagafiesgasaidgkiAVNPSGGLLAKGHPIGATGAAQAVEIV 337
Cdd:PRK09051 303 ERAGLTVADLDVIEANEAFAAQACAVTRELGLDPA------------------KVNPNGSGISLGHPVGATGAIITVKAL 364
|
...
gi 1817094313 338 RQL 340
Cdd:PRK09051 365 YEL 367
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
47-108 |
8.95e-06 |
|
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: 46.47 E-value: 8.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1817094313 47 AYCGTALGGMMAGqRILGRVGLTGiPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVE 108
Cdd:pfam00109 142 PFAVGTMPSVIAG-RISYFLGLRG-PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVN 201
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
18-113 |
1.00e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 46.78 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 18 PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGTALGGMM---AGQRILGRVGLTGIPIVNVENACSSSSSALRQAVMAI 94
Cdd:PRK12879 49 VEEYTSDLAIKAAERALARAGLDAEDIDLIIVATTTPDYLfpsTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLI 128
|
90
....*....|....*....
gi 1817094313 95 RSGEYDVVLVIGVEKLTKF 113
Cdd:PRK12879 129 TSGLYKKVLVIGAERLSKV 147
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-363 |
1.33e-05 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 46.62 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 2 RDVAVIGTGLIPFGKY----PDKTLADLGWPAVKMAVKDADIAPAKIEAAYCG----TALGGMMAGQRILGRVGLTGIPI 73
Cdd:PLN02644 1 RDVCIVGVARTPIGGFlgslSSLSATELGSIAIQAALERAGVDPALVQEVFFGnvlsANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 74 VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKL-------------TKFGGGTLP---LEKEDWEVSQGLVMPALY 137
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMsnapkylpearkgSRLGHDTVVdgmLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 138 AMRAQRY-----------MHEYD---------LTPAQLALVSVKNRRN------------GALNPdAQMRK--PV----- 178
Cdd:PLN02644 161 ELCADQYsisreeqdayaIQSYEraiaaqeagAFAWEIVPVEVPGGRGrpsvivdkdeglGKFDP-AKLRKlrPSfkedg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 179 -TVEEVLASrpiadpftllqccPTGDGAAALILCEAKLARQYRSDPV-RIAasdltsgkytpGFRD--------MTIPEI 248
Cdd:PLN02644 240 gSVTAGNAS-------------SISDGAAALVLVSGEKALELGLQVIaKIR-----------GYADaaqapelfTTAPAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 249 TVrgaKEAYEEAGLGPQEIDVAEVHDAFSIAELLYYEAFGF-CERgsagafiesgasaidgkiaVNPSGGLLAKGHPIGA 327
Cdd:PLN02644 296 AI---PKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLdPEK-------------------VNVHGGAVSLGHPIGC 353
|
410 420 430
....*....|....*....|....*....|....*.
gi 1817094313 328 TGAAQAVEIVRQLRGEcgarqvpDAKVGLSHATGGG 363
Cdd:PLN02644 354 SGARILVTLLGVLRSK-------NGKYGVAGICNGG 382
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
203-340 |
2.81e-05 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 45.92 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 203 DGAAALILCEAKLARQYRSDPVriaASDLTSGKYTPGFRDMTIPeiTVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELl 282
Cdd:PRK08131 257 DGAAALLIGSRAAGEKYGLKPM---ARILSSAAAGVEPRIMGIG--PVEAIKKALARAGLTLDDMDIIEINEAFASQVL- 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1817094313 283 yyeafgFCERGSAGAFIESgasaidgkiAVNPSGGLLAKGHPIGATGAAQAVEIVRQL 340
Cdd:PRK08131 331 ------GCLKGLGVDFDDP---------RVNPNGGAIAVGHPLGASGARLALTAAREL 373
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
203-330 |
3.51e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 45.64 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 203 DGAAALILCEAKLARQYRSDP-VRIAASDLTSgkytpgfrdmTIPEITVRG----AKEAYEEAGLGPQEIDVAEVHDAFS 277
Cdd:PRK08242 261 DGAAAVLIGSEEAGKALGLKPrARIVATATIG----------SDPTIMLTGpvpaTRKALAKAGLTVDDIDLFELNEAFA 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1817094313 278 IAELLYYEAFGFCergsagafiesgasaiDGKIAVNpsGGLLAKGHPIGATGA 330
Cdd:PRK08242 331 SVVLRFMQALDIP----------------HDKVNVN--GGAIAMGHPLGATGA 365
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
203-330 |
7.83e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 44.38 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 203 DGAAALILCEAKLARQYRSDP-VRIAA-----SDLTSGKYTPgfrdmtipeitVRGAKEAYEEAGLGPQEIDVAEVHDAF 276
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPrARIVAmanmgDDPTLMLNAP-----------VPAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1817094313 277 SIAellyyeafgfcergsAGAFIEsgasaiDGKI---AVNPSGGLLAKGHPIGATGA 330
Cdd:PRK06025 345 AVV---------------AEKFIR------DLDLdrdKVNVNGGAIALGHPIGATGS 380
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
23-366 |
1.32e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 43.72 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 23 ADLGWPAVKMAVKDADIAPAKIEAAYCG---TALGGMMAGQRILGRVGLT-GIPIVNVENACSSSSSALRQAVMAIRSGE 98
Cdd:PRK05656 27 VELGAAVIRRLLEQTGLDPAQVDEVILGqvlTAGAGQNPARQAAIKAGLPhSVPAMTLNKVCGSGLKALHLAAQAIRCGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 99 YDVVLVIGVEKLTkFGGGTLPLEKEDWEVSQGLVMPAL-----------YAM--RAQRYMHEYDLT-PAQLALVSVKNRR 164
Cdd:PRK05656 107 AEVIIAGGQENMS-LAPYVLPGARTGLRMGHAQLVDSMitdglwdafndYHMgiTAENLVEKYGISrEAQDAFAAASQQK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 165 NGA-------------------------LNPDAQMRKPVTVEEVLASRPIAD---PFTLLQCCPTGDGAAALILCEAKLA 216
Cdd:PRK05656 186 AVAaieagrfddeitpilipqrkgeplaFATDEQPRAGTTAESLAKLKPAFKkdgSVTAGNASSLNDGAAAVLLMSAAKA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 217 RQYrSDPV--RIAAsdltsgkYTPGFRDMTIPEI-TVRGAKEAYEEAGLGPQEIDVAEVHDAFSIAELlyyeafgfcerg 293
Cdd:PRK05656 266 KAL-GLPVlaKIAA-------YANAGVDPAIMGIgPVSATRRCLDKAGWSLAELDLIEANEAFAAQSL------------ 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817094313 294 SAGAFIESGASAidgkiaVNPSGGLLAKGHPIGATGAAQAVEIVRQLrgecgarQVPDAKVGLSHATGGGISG 366
Cdd:PRK05656 326 AVGKELGWDAAK------VNVNGGAIALGHPIGASGCRVLVTLLHEM-------IRRDAKKGLATLCIGGGQG 385
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
76-113 |
1.32e-04 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 40.19 E-value: 1.32e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1817094313 76 VENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKF 113
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKI 40
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
74-107 |
2.10e-04 |
|
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: 42.70 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|....
gi 1817094313 74 VNVENACSSSSSALRQAVMAIRSGEYDVVLVIGV 107
Cdd:smart00825 91 VTVDTACSSSLVALHLACQSLRSGECDMALAGGV 124
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
203-330 |
2.38e-04 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 42.79 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 203 DGAAALILCEAKLARQYRSDP-VRIAASDLTSGKytpgfrdmtiPEITVRGAKEA----YEEAGLGPQEIDVAEVHDAFS 277
Cdd:PRK07850 246 DGAAAVLWMDEDRARALGLRPrARIVAQALVGAE----------PYYHLDGPVQAtakvLEKAGMKIGDIDLVEINEAFA 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1817094313 278 IAELlyyeafgfcergsagafieSGASAIDGKIA-VNPSGGLLAKGHPIGATGA 330
Cdd:PRK07850 316 SVVL-------------------SWAQVHEPDMDkVNVNGGAIALGHPVGSTGA 350
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
64-107 |
2.78e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 43.32 E-value: 2.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1817094313 64 GRV----GLTGiPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGV 107
Cdd:COG3321 155 GRIsyklDLRG-PSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV 201
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
199-364 |
3.71e-04 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 42.06 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 199 CPTGDGAAALILCEAKLARQYRSDPV-RIAASDLTsgkytpGFRDMTIPEITVRGAKEAYEEAGLGPQEIDVAEVHDAFS 277
Cdd:PRK06690 215 CGVNDGACAVLVMEEGQARKLGYKPVlRFVRSAVV------GVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 278 IAELLYYEAFGFCErgsagafiesgasaidGKIAVNpsGGLLAKGHPIGATGAAQAVEIVRQLRGEcgarqvpDAKVGLS 357
Cdd:PRK06690 289 SKVVACAKELQIPY----------------EKLNVN--GGAIALGHPYGASGAMLVTRLFYQAKRE-------DMKYGIA 343
|
....*...
gi 1817094313 358 H-ATGGGI 364
Cdd:PRK06690 344 TlGIGGGI 351
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-111 |
8.04e-04 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 41.29 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 1 MRDVAVIGTGLIPFGK-----YPDKTLADLGWPAVKMAVKDADIAPAKIEAAYCGT-----ALGGMMAGQRILgRVGL-T 69
Cdd:PRK07108 1 MTEAVIVSTARTPLAKswrgaFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCanpegATGANIARQIAL-RAGLpV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1817094313 70 GIPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLT 111
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS 121
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
258-330 |
1.96e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 39.88 E-value: 1.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1817094313 258 EEAGLGPQEIDVAEVHDAFS---IAELLYYEAFGFC-ER-GSAGAFiesgaSAID-GKIAVNpsGGLLAKGHPIGATGA 330
Cdd:PRK09268 320 ARNGLTLQDFDFYEIHEAFAsqvLATLKAWEDEEYCrERlGLDAPL-----GSIDrSKLNVN--GSSLAAGHPFAATGG 391
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
29-113 |
2.08e-03 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 39.89 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 29 AVKMAVKDADIAPAKIEAAYCGTALGG-MMAGQ--RILGRVGLTGIPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVI 105
Cdd:PRK06816 70 AIRDLLDDAGFSLGDIELLACGTSQPDqLMPGHasMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVAT 149
|
....*...
gi 1817094313 106 GVEKLTKF 113
Cdd:PRK06816 150 ASELASRW 157
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-114 |
2.93e-03 |
|
"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: 39.34 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 3 DVAVIGTglIPFGKYPDKTLADLGWP---------AVKMAVKDADIAPAKIE-----AAYCGTALGGMMAGQRILG---- 64
Cdd:cd00828 46 DRGVAGQ--IPTGDIPGWDAKRTGIVdrttllalvATEEALADAGITDPYEVhpsevGVVVGSGMGGLRFLRRGGKldar 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1817094313 65 -----------------------RVGLTGIPIVNVENACSSSSSALRQAVMAIRSGEYDVVLVIGVEKLTKFG 114
Cdd:cd00828 124 avnpyvspkwmlspntvagwvniLLLSSHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEG 196
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
200-341 |
3.02e-03 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 39.58 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1817094313 200 PTGDGAAALILCEAKLARQYRSDP---VR---IAASDLtsgkytpgFRDMTI-PeitVRGAKEAYEEAGLGPQEIDVAEV 272
Cdd:PRK08963 266 PLTDGAAAVLLMSESRAKALGLTPlgyLRsyaFAAIDV--------WQDMLLgP---AYATPLALERAGLTLADLTLIDM 334
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1817094313 273 HDAFSIAELLYYEAFGfcergsAGAFIES--GASAIDGKI---AVNPSGGLLAKGHPIGATGAAQAVEIVRQLR 341
Cdd:PRK08963 335 HEAFAAQTLANLQMFA------SERFAREklGRSQAIGEVdmsKFNVLGGSIAYGHPFAATGARMITQTLHELR 402
|
|
| |
