|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
8-388 |
0e+00 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 693.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 8 FMKPGgeNSRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHsLGLTGIPIINVNNNCSTGSTALFM 87
Cdd:PRK08256 13 FEKPG--ASWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVNNNCSTGSTALFL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 88 AHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKYGTKVEHFAK 167
Cdd:PRK08256 90 ARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHMEKYGTTAETFAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 168 IGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqSKAVEIVAQEMMTDL 247
Cdd:PRK08256 170 IGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAVEIVAQAMTTDT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 248 PSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWV 327
Cdd:PRK08256 249 PSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFIDDGDNTYGGRWV 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507949 328 INPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLYR 388
Cdd:PRK08256 329 VNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
8-387 |
0e+00 |
|
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: 581.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 8 FMKPGGENSRDYPDMAKEAGQKALEDAQIPYS----AVEQACVGYVYGD---STSGQRAIYHSLGLTGIPIINVNNNCST 80
Cdd:cd00826 8 FGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLGAgegQNCAQQAAMHAGGLQEAPAIGMNNLCGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 81 GSTALFMAHQLIQGGLANCVLALGFEKMErgsigtkFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKYGT 160
Cdd:cd00826 88 GLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAEAAEKDGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 161 KVEHFAKIGWKN---HKHSVNNTYSQFQDEYSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSK 234
Cdd:cd00826 161 FKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQKHGLQSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 235 AVEIVAQEMMTDLPSTFEEKSIIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTL 314
Cdd:cd00826 241 AREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGQGGAL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507949 315 VDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLY 387
Cdd:cd00826 321 VDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
8-387 |
2.63e-158 |
|
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: 455.57 E-value: 2.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 8 FMKPGGensRDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGD---STSGQRAIYHsLGLTGIPIINVNNNCSTGSTA 84
Cdd:cd00829 8 FGRRSD---RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGrfqSFPGALIAEY-LGLLGKPATRVEAAGASGSAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 85 LFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIdkYGLSAhpitPQMFGYAGKEHMEKYGTKVEH 164
Cdd:cd00829 84 VRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHRYGTTRED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 165 FAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLqsKAVEIVAQEMM 244
Cdd:cd00829 158 LAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVWILGVGAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 245 TDLPSTFEEKSIikvVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGG 324
Cdd:cd00829 236 SDTPSLSERDDF---LSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREGDTAIGG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755507949 325 KWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTLY 387
Cdd:cd00829 313 DLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
17-388 |
7.12e-99 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 304.13 E-value: 7.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 17 RDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAI------YhsLGLTGIPIINVNNNCSTGSTALFMAHQ 90
Cdd:PRK06064 20 VSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIaaliadY--AGLAPIPATRVEAACASGGAALRQAYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 91 LIQGGLANCVLALGFEKMergsigtkfsdrttpTDKHIEVLIDKYGLSAHPITPQMFG------YA--GKEHMEKYGTKV 162
Cdd:PRK06064 98 AVASGEADVVLAAGVEKM---------------TDVPTPDATEAIARAGDYEWEEFFGatfpglYAliARRYMHKYGTTE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 163 EHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYglQSKAVEIVAQE 242
Cdd:PRK06064 163 EDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEY--TDTPVWIKASG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 243 MMTDLPSTFEEKSIikvVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTY 322
Cdd:PRK06064 241 QASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKGEGGKLAREGQTYI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507949 323 GGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEA--GKRQVPGAKVALQHNL-GLGGAVVVTLYR 388
Cdd:PRK06064 318 GGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVgGTGHTAVVHILS 386
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
21-388 |
1.63e-74 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 240.90 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRA--IYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGLAN 98
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApiVAEYSGLTGKVPLRVEAMCATGLAASLTAYTAVASGLVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 99 CVLALGFEKMergsigtkfSDRTTPTDKHIEVLIDKYGLSAH---PITPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKH 175
Cdd:PRK12578 103 MAIAVGVDKM---------TEVDTSTSLAIGGRGGNYQWEYHfygTTFPTYYALYATRHMAVYGTTEEQMALVSVKAHKY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 176 SVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLQSkAVEIVAQEMMTDLPSTFEEks 255
Cdd:PRK12578 174 GAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKELKIDS-PVWITGIGYANDYAYVARR-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 256 iIKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLI 335
Cdd:PRK12578 251 -GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLK 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755507949 336 SKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAK-VALQHNLGLGG--AVVVTLYR 388
Cdd:PRK12578 330 AKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVGGTGhfAYVMILRR 385
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
9-385 |
1.14e-70 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 231.58 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 9 MKPGGENSRDYPDMAKEAGQKALEDAQIPY---------SAVEQACVGYVYGdSTSGQraiyhSLGLTGIPIINVNNNCS 79
Cdd:PRK06059 13 MHPWGKWGRDFVEYGVVAARAALADAGLDWrdvqlvvgaDTIRNGYPGFVAG-ATFAQ-----ALGWNGAPVSSSYAACA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 80 TGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTKFSDRTTPTDkhievlidkyGLSAHPI---TPQMFGYAGKEHME 156
Cdd:PRK06059 87 SGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGERPDDPD----------WLRFHLIgatNPVYFALLARRRMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 157 KYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLQSK-A 235
Cdd:PRK06059 157 LYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRHLGSVAgV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 236 VEIVAQEMMT--------DLPsTFEEKSIIKVVGYDMS--KEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGL 305
Cdd:PRK06059 237 PSVRAISTVTprypqhlpELP-DIATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 306 CPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGL---GGAV 382
Cdd:PRK06059 316 CPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQGLfghGSSV 395
|
...
gi 755507949 383 VVT 385
Cdd:PRK06059 396 IVA 398
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
17-377 |
7.89e-62 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 207.96 E-value: 7.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 17 RDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHS--LGLTGIPIINVNNNCSTGSTALFMAHQLIQG 94
Cdd:PRK06157 25 AGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPLSraLRLPNIPVTRVENFCATGSEAFRGAVYAVAS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 95 GLANCVLALGFEK-MERGSIGTKFSDRTTPTDKHIEvlidkyGLSAhpitPQMFGYAGKEHMEKYGTKVEHF----AKIG 169
Cdd:PRK06157 105 GAYDIALALGVEKlKDTGYGGLPVANPGTLADMTMP------NVTA----PGNFAQLASAYAAKYGVSREDLkramAHVS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 170 WKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYG----LQSKAVEIVA---QE 242
Cdd:PRK06157 175 VKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARALGkkdpVYVKALQLAVsngWE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 243 MMTDlpstfeeksiikvvGYDMS-----KEAARRCYEKSGLT-P-NDVDVIELHDCFSVNELITYEALGLCPEGQGGTLV 315
Cdd:PRK06157 255 LQYN--------------GWDGSyfpttRIAARKAYREAGITdPrEELSMAEVHDCFSITELVTMEDLGLSERGQAWRDV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507949 316 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLG 377
Cdd:PRK06157 321 LDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLG 382
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
20-385 |
7.98e-62 |
|
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: 203.44 E-value: 7.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGD---STSGQRAIYHsLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSgefSGAAGQLAYH-LGISGGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKmergsigtkfsdrttptdkhievlidkyglsahpitpqmfgyagkehmekygtkvehfakigwknhkhs 176
Cdd:cd00327 87 ADIVLAGGSEE--------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 177 vnntysqfqdeysleevmkskpvfdfltilqcCPTSDGAAAAILSSEEFVQQYGlqskaveIVAQEMMTDLPSTFEEKSI 256
Cdd:cd00327 98 --------------------------------FVFGDGAAAAVVESEEHALRRG-------AHPQAEIVSTAATFDGASM 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 257 IKVVGYDMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGtlvdrgdntyggkwvINPSGGLIS 336
Cdd:cd00327 139 VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIM 203
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755507949 337 KGHPLGATGLAQCAELCWQLRGEAGK--RQVPGAKVALQHNLGLGGAVVVT 385
Cdd:cd00327 204 TGHPLGAAGLAILDELLLMLEHEFIPptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
21-382 |
3.14e-60 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 203.64 E-value: 3.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYG----DSTSGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:PRK07516 24 SLIVRVAREALAHAGIAAGDVDGIFLGHFNAgfspQDFPASLVLQADPALRFKPATRVENACATGSAAVYAALDAIEAGR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKMERgsigtkfsdrtTPTDKHIEVLID-KYGLSAHPIT---PQMFGYAGKEHMEKYGTKVEHFAKIGWKN 172
Cdd:PRK07516 104 ARIVLVVGAEKMTA-----------TPTAEVGDILLGaSYLKEEGDTPggfAGVFGRIAQAYFQRYGDQSDALAMIAAKN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 173 HKHSVNNTYSQFQDEYSLE---EVMKSKP-VFDFLTILQCCPTSDGAAAAILSSEEFVQQYglqSKAVEIVAQEMMTD-L 247
Cdd:PRK07516 173 HANGVANPYAQMRKDLGFEfcrTVSEKNPlVAGPLRRTDCSLVSDGAAALVLADAETARAL---QRAVRFRARAHVNDfL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 248 PstfeeksiikvvgydMSK------EAARRC----YEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDR 317
Cdd:PRK07516 250 P---------------LSRrdplafEGPRRAwqraLAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPGQGARAIRE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755507949 318 GDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGlGGAV 382
Cdd:PRK07516 315 GWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG-GAAV 378
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
17-386 |
6.67e-55 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 190.51 E-value: 6.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 17 RDYPDMAKEAGQKALEDAQIPYSAVEQACVGYV---YGDSTSGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQ 93
Cdd:PRK06365 35 MDFRERVKKAFDYAMNDAGLTLADIDGSVASYFsdhFQRQLLAGIMVQDYLGLVPKPSKRIEGGGATGGLAFQAGYEEIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 94 GGLANCVLALGFEKMERgsigtkfsdrtTPTDKHIEVLidkyGLSA-----HPITPQMFGY---AGKEHMEKYGTKVEHF 165
Cdd:PRK06365 115 SGRMDCVAVYGFETMSH-----------VNTWKGNEFI----ALASdtnfdYPLGGFYTGYyamMAVRHMYEFGTTVEQL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 166 AKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEfvQQYGLQSKAVEIVAQEMMT 245
Cdd:PRK06365 180 AKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASED--KAFEITDKPVLIKAIGTGS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 246 D--------------LPStfEEKSIIK------VVGYDMSKEAARRCYEKSGLTP--NDVDVIELHDCFSVNELITYEAL 303
Cdd:PRK06365 258 DtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGITDplNDLDLIELHDAYTSSEIQTYEDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 304 GLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKR------QVPGAKVALQH-NL 376
Cdd:PRK06365 336 GLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRIKKHfhddylQVKNAKRGLIHsHA 415
|
410
....*....|
gi 755507949 377 GLGGAVVVTL 386
Cdd:PRK06365 416 GTGTYVTVTI 425
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
17-386 |
1.63e-46 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 167.56 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 17 RDYPDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQR------AIYHSlGLTGIPIINVNNNCSTGSTALFMAHQ 90
Cdd:PRK06289 24 RDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGhlgampATVHP-ALWGVPASRHEAACASGSVATLAAMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 91 LIQGGLANCVLALGFEKMergsigtkfsdRTTPTDKHIEVL-----IDKYGLSAHPITPQMFGYAGKEHMEKYGTKVEHF 165
Cdd:PRK06289 103 DLRAGRYDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMFARVADEYDRRYGLDEEHL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 166 AKIGWKNHKHSVNNTYSQ-----FQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQY----------- 229
Cdd:PRK06289 172 RAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLASDAYLRDYadarpiprikg 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 230 --------GLQSKAVEIVAQEMMtdLPSTfeeksiikvvgydmsKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYE 301
Cdd:PRK06289 252 wghrtaplGLEQKLDRSAGDPYV--LPHV---------------RQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 302 ALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGA 381
Cdd:PRK06289 315 HIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFGTLNIGGSTT 394
|
....*
gi 755507949 382 VVVTL 386
Cdd:PRK06289 395 TTVSF 399
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
22-381 |
8.65e-45 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 162.21 E-value: 8.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 22 MAKEAGQKALEDAQIPYSAVEQACVGY---VYGDSTSGQRAIYHSLGLTGIPIINVNNNCSTG-STALFMAHqLIQGGLA 97
Cdd:PRK08313 27 LVREAIDRALADAGLTWDDIDAVVVGKapdFFEGVMMPELFLADALGATGKPLIRVHTAGSVGgSTAVVAAS-LVQSGVY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 98 NCVLALGFEKMERGSigtkfsdrttptdkhievliDKYGLSAH-PITPQMFGYAG-------KEHMEKYGTKVEHFAKIG 169
Cdd:PRK08313 106 RRVLAVAWEKQSESN--------------------AMWALSIPvPFTKPVGAGAGgyfaphvRAYIRRSGAPEHIGAMVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 170 WKNHKHSVNNTYSQF-QDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVeIVAQEMMTDlP 248
Cdd:PRK08313 166 VKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAGRPVAW-IHGTAMRTE-P 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 249 STFEEKSiikVVGYDMSKEAARRCYEKSGLT-P-NDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKW 326
Cdd:PRK08313 244 LAFAGRD---QVNPQAGRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPEGEGWKLTEAGETAIGGRL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755507949 327 VINPSGGLISkGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGlGGA 381
Cdd:PRK08313 321 PVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG-GGS 373
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
21-380 |
7.62e-40 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 148.64 E-value: 7.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYgDSTSGQRAIYHslglTGIPIINVNNNCSTGSTalFMAH-----QLIQGG 95
Cdd:PRK06158 30 ELLAQAAHRALADAGLTMADVDGLFTASPD-DALWGLSVAEY----LGIRPRFVDGTMIGGSS--FLAHllpaaLALEAG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVL-ALGfekMERGSIGTKFSDRTTPTdkhievlidkygLSAHPITPQM----FGYAGKEHMEKYGTKVEHFAKIGW 170
Cdd:PRK06158 103 LCDVALiCYG---SNQRSAGGKLRSMLDPQ------------PYEAPYKPVNpvsaYALAAARHMHQYGTTREQLAEVAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 171 KNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQqyGLQSKAVEIVAQEM------- 243
Cdd:PRK06158 168 AARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRAR--DLPRPPVYVLGAAAatwhrqi 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 244 --MTDLPSTfeeksiikvvgydMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNT 321
Cdd:PRK06158 246 ssMPDLTVT-------------AAAESGPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 755507949 322 YGGKWVINPSGGLISKGHPlGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHnlGLGG 380
Cdd:PRK06158 313 PGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH--GNGG 368
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
21-366 |
5.55e-34 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 132.64 E-value: 5.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVyGDSTSG--QRAIYHSLGLTGI--PIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:PRK06065 31 ELAWEAASKALDEAGLELKDIDCVVIGSA-PDAFDGvhMKGEYLSHGSGGIrkPVSRVYVGGATGVMTAIAGWYHVASGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKMErgsigtkfSDRTTPTD--KHI-EVLIDKyglsahPITPQM---FGYAGKEHMEKYGTKVEHFAKIGW 170
Cdd:PRK06065 110 CQKVLAVAEEKMS--------PARPHPQAvfRYIwDPILEK------PLNPNLiwiFAMEMHRYMATYGIKKEEIALVSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 171 KNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYglqskaveivaqemmTDLPST 250
Cdd:PRK06065 176 KNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY---------------TDTPVW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 251 feeksiIKVVGYDMS---------------KEAARRCYEKSGLT-PN-DVDVIELHDCFSVNELITYEALGLCPEGQGGT 313
Cdd:PRK06065 241 ------VEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPFDYKELHHLEGLQLAKRGEAPK 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 755507949 314 LVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 366
Cdd:PRK06065 315 LLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
20-384 |
8.75e-33 |
|
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: 129.14 E-value: 8.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGdSTSGQ---RAIYHSLGL-TGIPIINVNNNCSTGSTALFMAHQLIQGG 95
Cdd:cd00751 23 DDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ-AGEGQnpaRQAALLAGLpESVPATTVNRVCGSGLQAVALAAQSIAAG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAgkEHM-EKYG-TKVE---------- 163
Cdd:cd00751 102 EADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITA--ENVaEKYGiSREEqdefalrshq 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 164 ---------HFA------KIGWKNHKHSVNntysqfQDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAIL 220
Cdd:cd00751 180 raaaaqeagRFKdeivpvEVPGRKGPVVVD------RDEGprpdtTLEKLAKLKPAFKkdgTVTAGNASGINDGAAAVLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 221 SSEEFVQQYGLQSKAVeIVAQEmmtdlpstfeeksiikVVGYD---MSK---EAARRCYEKSGLTPNDVDVIELHDCFSV 294
Cdd:cd00751 254 MSEEKAKELGLKPLAR-IVGYA----------------VAGVDpaiMGIgpvPAIPKALKRAGLTLDDIDLIEINEAFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 295 NELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQH 374
Cdd:cd00751 317 QALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGL----ATMCI 374
|
410
....*....|
gi 755507949 375 NLGLGGAVVV 384
Cdd:cd00751 375 GGGQGAAMVI 384
|
|
| SCP2 |
pfam02036 |
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ... |
436-522 |
3.94e-32 |
|
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.
Pssm-ID: 460423 [Multi-domain] Cd Length: 100 Bit Score: 118.90 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 436 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMG 514
Cdd:pfam02036 15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90
|
....*...
gi 755507949 515 LAMKLQNL 522
Cdd:pfam02036 91 LAQKLEGL 98
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
88-384 |
3.40e-31 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 124.48 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 88 AHQLIQGGLANCVLALGFEKmergsigtkfsdrttPTDkhIEVLIDKYGLSAHPI------TPQMFGYAGKE---HMEKY 158
Cdd:PRK06066 95 AVMHINSGLANVVVVEAHSK---------------PSD--ILTFSDVVKFAMDPIyvrpigPPNPHFIAGLDavkFMSRK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 159 GTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEFVQQYglqskavei 238
Cdd:PRK06066 158 GITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 239 vaqemmTDLPStfeeksIIKVVGY--DMS-------------KEAARRCYEKSGLTP--NDVDVIELHDCFSVNELITYE 301
Cdd:PRK06066 229 ------TDDPV------WIKGIGWstESSnletaelgkanymRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 302 ALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQvPGAKVALQHNL----G 377
Cdd:PRK06066 297 ALRLSEEPEKDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVASWrgipT 375
|
....*..
gi 755507949 378 LGGAVVV 384
Cdd:PRK06066 376 LTGSVVV 382
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
70-380 |
1.25e-30 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 123.85 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 70 PIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGS--IGTKFSDRTTptDKHIEVLIDKYGLsahpitPQMF 147
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarVGGDYLARAA--DYRRQRKLDDFTF------PCLF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 148 GYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDEYSLEEVMK---SKPVF-------DFLTILQCCPTSDGAA 216
Cdd:PTZ00455 184 AKRMKYIQEHGHFTMEDTARVAAKAYANGNKNPLAHmHTRKLSLEFCTGasdKNPKFlgnetykPFLRMTDCSQVSDGGA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 217 AAILSSEEFVQQYGLQ---SKAVEIVAQE-----MMTDLPSTfeeksiikvvgYDM--SKEAARRCYEKSGLTPNDVDVI 286
Cdd:PTZ00455 264 GLVLASEEGLQKMGLSpndSRLVEIKSLAcasgnLYEDPPDA-----------TRMftSRAAAQKALSMAGVKPSDLQVA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 287 ELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 366
Cdd:PTZ00455 333 EVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMK 412
|
330
....*....|....
gi 755507949 367 GAkVALQHNLGLGG 380
Cdd:PTZ00455 413 NI-PALGATLNMGG 425
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
21-384 |
2.58e-29 |
|
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: 119.25 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVygDSTSGQR------AIYHSLGLTgIPIINVNNNCSTGSTALFMAHQLIQG 94
Cdd:TIGR01930 23 DLGAAVIKELLERNPLDPELIDDVIFGNV--LQAGEQQniarqaALLAGLPES-VPAYTVNRQCASGLQAVILAAQLIRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 95 GLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAGKEHMEKYG-TKVE--HFA----K 167
Cdd:TIGR01930 100 GEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLAKKYGiSREEqdEYAlrshQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 168 IGWKNHK-------------HSVNNTYSQFQDE-----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFV 226
Cdd:TIGR01930 180 RAAKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTLEKLAKLKPAFDpdgTVTAGNSSPLNDGAAALLLMSEEKA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 227 QQYGLQSKAvEIVAQEMMTDLPSTFeeksiikvvGYdMSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLC 306
Cdd:TIGR01930 260 KELGLTPLA-RIVSFAVAGVDPEIM---------GL-GPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLD 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507949 307 PEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 384
Cdd:TIGR01930 329 LE------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGL----ATMCIGGGQGAAVIL 384
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
140-381 |
1.87e-27 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 114.03 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 140 HPITPQMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAI 219
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDGGGALV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 220 LSSEEfvqqyglqskaveiVAQEMmtdlpstfeEKSIIKVVGY------------DMSKEAAR----RCYEKSGLTPNDV 283
Cdd:PRK08142 219 VVRPE--------------IARSL---------KRPLVKVLGAgeaikgqmggkvDLTYSGAAwsgpAAFAEAGVTPADI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 284 DVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG- 361
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHp 355
|
250 260
....*....|....*....|
gi 755507949 362 KRQVPGAKVALQHnlGLGGA 381
Cdd:PRK08142 356 AVQVPNCDLALAH--GTGGL 373
|
|
| SCP2 |
COG3255 |
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism]; |
437-522 |
1.72e-24 |
|
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
Pssm-ID: 442486 [Multi-domain] Cd Length: 104 Bit Score: 97.67 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 437 KKIGGIFAFKVKDGPGGkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLA 516
Cdd:COG3255 18 AGWDGVVQFVITGEGGG---AYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLA 94
|
....*.
gi 755507949 517 MKLQNL 522
Cdd:COG3255 95 MKLMSL 100
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
135-368 |
3.26e-24 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 104.29 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 135 YGLSahpiTP-QMFGYAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQFQDE-YSLEEVMKSKPVFDFLTILQCCPTS 212
Cdd:PRK07855 141 HGLL----TPaAWVAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQES 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 213 DGAAAAILSSEEFVQQygLQSKAVEIVA--------QEMMT----DLPSTFEEKSIikvvgydmskeAARRCYEKSGLTP 280
Cdd:PRK07855 217 DGAVALVVTSAERARD--LKQRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 281 NDVDVIELHDCFSVNELITYEALGLCPEGQGGTLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLRGEA 360
Cdd:PRK07855 284 ADIDTAILYDHFTPFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLRGTS 360
|
....*...
gi 755507949 361 gKRQVPGA 368
Cdd:PRK07855 361 -VNQVPGV 367
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
20-384 |
1.62e-22 |
|
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: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVygdSTSGQ-----RAIYHSLGL-TGIPIINVNNNCSTGSTALFMAHQLIQ 93
Cdd:COG0183 27 DDLGAAVIKALLERAGLDPEAVDDVILGCV---LQAGQgqnpaRQAALLAGLpESVPAVTVNRVCGSGLQAVALAAQAIA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 94 GGLANCVLALGFEKMERGSIGTKFSDRTTPTDKHIEVLIDKYGLSAHPITPQMFGYAgkEHM-EKYG-TKVE-------- 163
Cdd:COG0183 104 AGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSMGETA--ENVaERYGiSREEqdafalrs 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 164 -----------HFAK------IGWKNHKHSVNntysqfQDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAA 218
Cdd:COG0183 182 hqraaaaiaagRFDDeivpveVPDRKGEVVVD------RDEGprpdtTLEKLAKLKPAFKkdgTVTAGNASGINDGAAAL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 219 ILSSEEFVQQYGLQSKAvEIVAQ-------EMMTDLPStfeeksiikvvgydmskEAARRCYEKSGLTPNDVDVIELHDC 291
Cdd:COG0183 256 LLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLDDIDLIEINEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 292 FSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVA 371
Cdd:COG0183 318 FAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGL----AT 375
|
410
....*....|...
gi 755507949 372 LQHNLGLGGAVVV 384
Cdd:COG0183 376 MCIGGGQGIALII 388
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
69-384 |
2.44e-18 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 87.08 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 69 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGTkfsdrttptDKHIEV----LID-KY-------- 135
Cdd:PRK06445 86 IPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGD---------NPHIEPnpklLTDpKYieydlttg 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 136 ---GLSAHpitpQMFGYAG--KEHMEKYGTKVEHFA----KIGW-----------KNHKHSVNNTYSQFQDEYSLEEVMK 195
Cdd:PRK06445 157 yvmGLTAE----KLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 196 SKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQ--SKAVEI----VAQEMMTDLPSTfeeksiikvvgydmsk 266
Cdd:PRK06445 233 LPPAFKpdgVITAGNSSPLNSGASYVLLMSKKAVKKYGLKpmAKIRSFgfagVPPAIMGKGPVP---------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 267 eAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGL 346
Cdd:PRK06445 297 -ASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGA 357
|
330 340 350
....*....|....*....|....*....|....*...
gi 755507949 347 AQCAELCWQLRGEAGKRQVPGAKVAlqhnLGLGGAVVV 384
Cdd:PRK06445 358 RIVGTLARQLQIKGKDYGVATLCVG----GGQGGAVVL 391
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
21-362 |
4.48e-17 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 83.13 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALedAQIP---YSAVEQACVGYVYGDSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQ 93
Cdd:PRK09052 33 DLLAHVLRSAV--AQVPgldPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNsvggVTVNRFCASGLQAVAMAADRIR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 94 GGLANCVLALGFEKMERGSI-GTKFSDRTTPTDKHIEVLI----------------------DKYGLSAH--PITPQMFG 148
Cdd:PRK09052 111 VGEADVMIAAGVESMSMVPMmGNKPSMSPAIFARDENVGIaygmgltaekvaeqwkvsredqDAFALESHqkAIAAQQAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 149 YAGKEhMEKYgTKVEHFAKIgwkNHKHSVNNTYSQFQDE-----YSLEEVMKSKPVFDF---LTILQCCPTSDGAAAAIL 220
Cdd:PRK09052 191 EFKDE-ITPY-EITERFPDL---ATGEVDVKTRTVDLDEgpradTSLEGLAKLKPVFANkgsVTAGNSSQTSDGAGAVIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 221 SSEEFVQQYGLQ------SKAVEIVAQEMMTDLPstfeeksiikvvgydmsKEAARRCYEKSGLTPNDVDVIELHDCFSV 294
Cdd:PRK09052 266 VSEKALKQFNLTplarfvSFAVAGVPPEIMGIGP-----------------IEAIPAALKQAGLKQDDLDWIELNEAFAA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507949 295 NELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGK 362
Cdd:PRK09052 329 QSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLK 378
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
20-386 |
6.25e-16 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 79.67 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQrAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGG 95
Cdd:PRK06366 27 PQLGGAAIKAVIDDAKLDPALVQEVIMGNVIqagvGQNPAGQ-AAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKMERGSIGTKFSDRTTPtdKHIevLIDKYGLSAHPITPQMFGYAGKEHM--------EKYGTKVEHFAK 167
Cdd:PRK06366 106 ERDLVIAGGMENMSNAPFLLPSDLRWGP--KHL--LHKNYKIDDAMLVDGLIDAFYFEHMgvsaertaRKYGITREMADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 168 IGWKNHKHSVNNTYS-QFQDEY---------------SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQ 228
Cdd:PRK06366 182 YSVQSYERAIRATESgEFRNEIvpfndldrdegirktTMEDLAKLPPAFDkngILTAGNSAQLSDGGSALVMASEKAINE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 229 YGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLcpe 308
Cdd:PRK06366 262 YGLKPIA-RITGYESASLDPLDFVEAPI----------PATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKI--- 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507949 309 gqggtlvdrgDNTYggkwvINPSGGLISKGHPLGATGlaqcAELCWQLRGEAGKRQVPGAKVALQHnlGLGGAVVVTL 386
Cdd:PRK06366 328 ----------DNER-----FNVNGGAVAIGHPIGNSG----SRIIVTLINALKTRHMKTGLATLCH--GGGGAHTLTL 384
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
21-224 |
1.72e-15 |
|
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: 76.57 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVyGDSTSGQ---RAIYHSLGLT-GIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:pfam00108 25 ELGAEAIKAALERAGVDPEDVDEVIVGNV-LQAGEGQnpaRQAALKAGIPdSAPAVTINKVCGSGLKAVYLAAQSIASGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKMERGSIGTKFSDR---TTPTDKHIEVLIdKYGLSAHPITPQMfGYAGKEHMEKYGTKVEHFAKIGWKNH 173
Cdd:pfam00108 104 ADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLTAENVAKKYGISREEQDAFAVKSH 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507949 174 KHSVNNTYSQ-FQDE------------------------YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEE 224
Cdd:pfam00108 182 QKAAAAPKAGkFKDEivpvtvkgrkgkptvdkdegirppTTAEPLAKLKPAFDkegTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
20-345 |
2.30e-14 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 74.80 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGdSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQGG 95
Cdd:PRK05790 27 VELGAIVIKAALERAGVPPEQVDEVIMGQVLQ-AGAGQNPARQAALKAGLPVevpaLTINKVCGSGLKAVALAAQAIRAG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKMER------GS-IGTKFSDrTTPTDKHI-EVLIDKYglsahpiTPQMFGYAGKEHMEKYG-TKVE--H 164
Cdd:PRK05790 106 DADIVVAGGQESMSQaphvlpGSrWGQKMGD-VELVDTMIhDGLTDAF-------NGYHMGITAENLAEQYGiTREEqdE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 165 F-------AKIGWKNHKHS---VNNTYSQ--------FQDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAA 218
Cdd:PRK05790 178 FalasqqkAEAAIKAGRFKdeiVPVTIKQrkgdpvvvDTDEHprpdtTAESLAKLRPAFDkdgTVTAGNASGINDGAAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 219 ILSSEEFVQQYGLQSKAvEIVAQemmtdlpstfeeksiiKVVGYDMSK------EAARRCYEKSGLTPNDVDVIELHDCF 292
Cdd:PRK05790 258 VVMSEAKAKELGLTPLA-RIVSY----------------AVAGVDPAImgigpvPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 755507949 293 SVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 345
Cdd:PRK05790 321 AAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
26-345 |
3.31e-14 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 74.36 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 26 AGQKALEDAQIPYSAVEQACVGYVYgDSTSGQ---RAIYHSLGLT-GIPIINVNNNCSTGSTALFMAHQLIQGGLANCVL 101
Cdd:PRK08235 33 AIKEALERANVSAEDVEEVIMGTVL-QGGQGQipsRQAARAAGIPwEVQTETVNKVCASGLRAVTLADQIIRAGDASVIV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 102 ALGFEKM-------ERGSIGTKFSDRT------------TPTDKHIEV----LIDKYGLSAHpitpQMFGYAGKEHME-- 156
Cdd:PRK08235 112 AGGMESMsnapyilPGARWGYRMGDNEvidlmvadgltcAFSGVHMGVyggeVAKELGISRE----AQDEWAYRSHQRav 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 157 ---KYGTKVEHFAKIGWKNHKhsvNNTYSQFQDE-----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEF 225
Cdd:PRK08235 188 sahEEGRFEEEIVPVTIPQRK---GDPIVVAKDEaprkdTTIEKLAKLKPVFDktgTITAGNAPGVNDGAAALVLMSEDR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 226 VQQYGLQSKAVeIVAQEMMTDLPSTFEeksiiKVVGYdmskeAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGL 305
Cdd:PRK08235 265 AKQEGRKPLAT-ILAHTAIAVEAKDFP-----RTPGY-----AINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGI 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755507949 306 CPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 345
Cdd:PRK08235 334 DPE------------------KVNVNGGAVALGHPIGASG 355
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
26-389 |
3.02e-13 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 71.28 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 26 AGQKALEDAQIPYSAVEQACVGYVYgDSTSGQR-AIYHSLGlTGIP----IINVNNNCSTGSTALFMAHQLIQGGLANCV 100
Cdd:PLN02644 32 AIQAALERAGVDPALVQEVFFGNVL-SANLGQApARQAALG-AGLPpstiCTTVNKVCASGMKAVMLAAQSIQLGINDVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 101 LALGFEKME-------RGSIGTKFSDRTTP------------TDKHI----EVLIDKYGLS-----AHPITPQMFGYAGK 152
Cdd:PLN02644 110 VAGGMESMSnapkylpEARKGSRLGHDTVVdgmlkdglwdvyNDFGMgvcaELCADQYSISreeqdAYAIQSYERAIAAQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 153 E--HMEKYGTKVEHFAKIGwknhKHSVNNTYSQFQDEYSLEEVMKSKPVFD----FLTILQCCPTSDGAAAAILSSEEFV 226
Cdd:PLN02644 190 EagAFAWEIVPVEVPGGRG----RPSVIVDKDEGLGKFDPAKLRKLRPSFKedggSVTAGNASSISDGAAALVLVSGEKA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 227 QQYGLQSKAVEI----VAQ--EMMTDLPStfeeKSIIKVVgydmskeaarrcyEKSGLTPNDVDVIELHDCFSVNELITY 300
Cdd:PLN02644 266 LELGLQVIAKIRgyadAAQapELFTTAPA----LAIPKAL-------------KHAGLEASQVDYYEINEAFSVVALANQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 301 EALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAkvalqHNlGLGG 380
Cdd:PLN02644 329 KLLGLDPEK------------------VNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGI-----CN-GGGG 384
|
....*....
gi 755507949 381 AVVVTLYRM 389
Cdd:PLN02644 385 ASAIVVELM 393
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
29-345 |
3.32e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 71.28 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 29 KAL-EDAQIPYSAVEQACVGYVygDSTSGQ-----RAIYHSLGLT-GIPIINVNNNCSTGSTALFMAHQLIQGGLANCVL 101
Cdd:PRK07801 35 KGLvDRTGIDPAAVDDVIFGCV--DTIGPQagniaRTSWLAAGLPeEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 102 ALGFEKMERGSIGTK--------FSDRTTPTDKHIEvlidKYGlsAHPITPqmfgYAGKEHM-EKYGTKVEHFAKIGWKN 172
Cdd:PRK07801 113 AGGVQNMSQIPISSAmtageqlgFTSPFAESKGWLH----RYG--DQEVSQ----FRGAELIaEKWGISREEMERFALES 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 173 HKHSVNNTYS-QFQDEY---------------SLEEVMKSKPVFD--FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSK 234
Cdd:PRK07801 183 HRRAFAAIRAgRFDNEIvpvggvtvdegpretSLEKMAGLKPLVEggRLTAAVASQISDGASAVLLASERAVKRHGLTPR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 235 AvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGqggtl 314
Cdd:PRK07801 263 A-RIHHLSVRGDDPVFMLTAPI----------PATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAK----- 326
|
330 340 350
....*....|....*....|....*....|.
gi 755507949 315 vdrgdntyggkwvINPSGGLISKGHPLGATG 345
Cdd:PRK07801 327 -------------VNPNGGAIALGHPLGATG 344
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
189-345 |
1.07e-12 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 69.65 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 189 SLEEVMKSKPVF---DFLTILQCCPTSDGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTDLPStfeeksiikv 259
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 260 vgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLcPEgqggtlvDRgdntyggkwvINPSGGLISKGH 339
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
|
....*.
gi 755507949 340 PLGATG 345
Cdd:PRK07851 362 PFGMTG 367
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
185-363 |
2.06e-12 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 68.83 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 185 QDEY-----SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEI------VAQEMMTDLPST 250
Cdd:PRK09050 222 RDEHprpetTLEALAKLKPVFRpdgTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILgmatagVEPRIMGIGPAP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 251 feeksiikvvgydmskeAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLcpegqggtlVDRGDNtyggkwvINP 330
Cdd:PRK09050 302 -----------------ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNP 348
|
170 180 190
....*....|....*....|....*....|....*
gi 755507949 331 SGGLISKGHPLGATG--LAQCAELcwQLRGEAGKR 363
Cdd:PRK09050 349 NGGAIALGHPLGMSGarLVLTALH--QLERTGGRY 381
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
268-384 |
2.23e-11 |
|
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: 61.12 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 268 AARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 347
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGAR 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 755507949 348 QCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 384
Cdd:pfam02803 89 ILVTLLHELKRRGGKYGL----ASLCIGGGQGVAMII 121
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
21-122 |
2.73e-11 |
|
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: 64.75 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGD----STSGQraIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:COG0332 53 DLAVEAARKALEAAGIDPEDIDLIIVATVTPDylfpSTACL--VQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQ 130
|
90 100
....*....|....*....|....*.
gi 755507949 97 ANCVLALGFEKMERgsiGTKFSDRTT 122
Cdd:COG0332 131 AKNVLVVGAETLSR---IVDWTDRST 153
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
66-345 |
3.82e-11 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 64.99 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 66 LTGIPI----INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMerGSIG-TKFSDRTTPTDKHIEVLIDKYGLSA- 139
Cdd:PRK08947 75 LAGIPHsvpaVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM--GHVPmNHGVDFHPGLSKNVAKAAGMMGLTAe 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 140 -----HPITPQM---FGYagKEHMEKYGTKVE-HFAKIGWKNHKHSVNNTYSQFQD------EYSLEEVMKSKPVFD--- 201
Cdd:PRK08947 153 mlgkmHGISREQqdaFAA--RSHQRAWAATQEgRFKNEIIPTEGHDADGVLKLFDYdevirpETTVEALAALRPAFDpvn 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 202 -FLTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVeIVAqemMTdlpstfeeksiikVVGYDMS------KEAARRCYE 274
Cdd:PRK08947 231 gTVTAGTSSALSDGASAMLVMSESRAKELGLKPRAR-IRS---MA-------------VAGCDPSimgygpVPATQKALK 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507949 275 KSGLTPNDVDVIELHDCFSVNELITYEALGlcpegqggtLVDRGDNTyggkwvINPSGGLISKGHPLGATG 345
Cdd:PRK08947 294 RAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
213-345 |
5.65e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 64.41 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 213 DGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCF 292
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPTLMLNAPV----------PAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755507949 293 SVNELITYEALGLcpegqggtlvDRGDntyggkwvINPSGGLISKGHPLGATG 345
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
28-376 |
1.36e-10 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 62.78 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 28 QKALEDAQIPYSAVEQACVG---YVYGDSTSGQRAIyHSLGltGIPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALG 104
Cdd:PRK07937 33 AELYAELGITKSDIGFWCSGssdYLAGRAFSFISAI-DSIG--AVPPINESHVEMDAAWALYEAWVKLLTGEVDTALVYG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 105 FEKmerGSIGTkfSDRTTPTDkhievlIDKYGLSahPITPQMFGYAG---KEHMEKYGTKVEHFAKIGWKNHKHSVNNTY 181
Cdd:PRK07937 110 FGK---SSAGT--LRRVLALQ------LDPYTVA--PLWPDSVSMAGlqaRAGLDAGKWTEEQMAEVAARSRADARRNPS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 182 SQfqDEYSLEEVMKSKPVFDFLTILQCCPTSDGAAAAILSSEEfvqqyglqsKAVEIVAQEM------------------ 243
Cdd:PRK07937 177 AE--PSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGD---------RARELRERPAwitgiehriespslgard 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 244 MTDLPSTfeeksiikvvgydmsKEAARRCyekSGLTPNDVDVIELHDCFSVNELITYEALGLcpegqggtlvdrGDNTyg 323
Cdd:PRK07937 246 LTRSPST---------------ALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-- 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 755507949 324 gkwVINPSGGLISkGHPLGATGLAQCAELCWQ-LRGEAGkRQVPGAKV--ALQHNL 376
Cdd:PRK07937 294 ---KVNPSGGALA-ANPMFAAGLERIGEAARHiWDGSAR-RALAHATSgpALQQNL 344
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
68-345 |
1.50e-10 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 63.05 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 68 GIPI----INVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSI-------GTKFSDrTTPTDKHIEVLIDKYG 136
Cdd:PRK09051 76 GVPQetpaFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYllpaarwGARMGD-AKLVDMMVGALHDPFG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 137 lsahpitpqmfgyagKEHM--------EKYGTKVEH---FAKIGWKNHKHSVNNTYSQFQ-----------------DEY 188
Cdd:PRK09051 155 ---------------TIHMgvtaenvaAKYGISREAqdaLALESHRRAAAAIAAGYFKDQivpveiktrkgevvfdtDEH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 189 -----SLEEVMKSKPVF--DFLTIlqccpTS-------DGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEK 254
Cdd:PRK09051 220 vradtTLEDLAKLKPVFkkENGTV-----TAgnasginDGAAAVVLAEADAAEARGLKPLA-RLVGYAHAGVDPEYMGIG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 255 SIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGL 334
Cdd:PRK09051 294 PV----------PATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSG 345
|
330
....*....|.
gi 755507949 335 ISKGHPLGATG 345
Cdd:PRK09051 346 ISLGHPVGATG 356
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
20-384 |
4.11e-10 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 61.58 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYgDSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQGG 95
Cdd:PRK06633 28 PMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPKevpgYTINKVCGSGLKSVALAANSIMTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKMERG------SIGTKFSDRTTPTDKHIEVLIDKY-----GLSAHPITPQmFGYAGKEHMEKYGTKVEH 164
Cdd:PRK06633 107 DNEIVIAGGQENMSLGmhgsyiRAGAKFGDIKMVDLMQYDGLTDVFsgvfmGITAENISKQ-FNISRQEQDEFALSSHKK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 165 FAKIG----WKNH----KHSVNNTYSQF-QDE-----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEEFVQ 227
Cdd:PRK06633 186 AAKAQlagiFKDEilpiEVTIKKTTSLFdHDEtvrpdTSLEILSKLRPAFDkngVVTAGNASSINDGAACLMVVSEEALK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 228 QYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALglcp 307
Cdd:PRK06633 266 KHNLTPLA-RIVSYASAGVDPSIMGTAPV----------PASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 308 egqggtlvdrgdntyggKW---VINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGLGGAVVV 384
Cdd:PRK06633 331 -----------------KWdmeKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGL----VTLCIGGGMGMAMCV 389
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
69-345 |
5.85e-10 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 61.05 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 69 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMERGSIGtkfSD-RTTPTDKhiEVLIDKY----GLSAHPIT 143
Cdd:PRK08242 82 VPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMG---SDgGAWAMDP--STNFPTYfvpqGISADLIA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 144 pQMFGYaGKEHMEKYGTKVEHFAKIGWKNH--KHSVNNTYSQF------QDEY-----SLEEVMKSKPVFDFL------- 203
Cdd:PRK08242 157 -TKYGF-SREDVDAYAVESQQRAAAAWAEGyfAKSVVPVKDQNgltildHDEHmrpgtTMESLAKLKPSFAMMgemggfd 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 204 -TILQCCPT----------------SDGAAAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSK 266
Cdd:PRK08242 235 aVALQKYPEverinhvhhagnssgiVDGAAAVLIGSEEAGKALGLKPRA-RIVATATIGSDPT-------IMLTG---PV 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755507949 267 EAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 345
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
21-122 |
7.49e-10 |
|
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: 60.25 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIpySAVEQACVgyVYGDSTSGQRA------IYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQG 94
Cdd:cd00830 52 DLAVEAAKKALEDAGI--DADDIDLI--IVATSTPDYLFpataclVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRS 127
|
90 100
....*....|....*....|....*...
gi 755507949 95 GLANCVLALGFEKMERgsiGTKFSDRTT 122
Cdd:cd00830 128 GGAKNVLVVGAETLSR---ILDWTDRST 152
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
21-384 |
1.73e-09 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 59.79 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHSLGLTGIPI----INVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:PRK08131 28 DLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVtvpgQTVNRLCASGLAAVIDAARAITCGE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKMER-----GSIGTKFSDRTTPTDKHI------EVLIDKYGLSAHPITPQ----MFG--------YAGKE 153
Cdd:PRK08131 108 GDLYLAGGVESMSRapfvmGKAESAFSRDAKVFDTTIgarfpnPKIVAQYGNDSMPETGDnvaaEFGisredadrFAAQS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 154 HMEKYGTKVEHF---------AKIGWKNHKHSVNntysqfQDEY-----SLEEVMKSKPVFD--FLTILQCCPTSDGAAA 217
Cdd:PRK08131 188 QAKYQAAKEEGFfadeitpieVPQGRKLPPKLVA------EDEHprpssTVEALTKLKPLFEggVVTAGNASGINDGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 218 AILSSEEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSKEAARRCYEKSGLTPNDVDVIELHDCFSVNEL 297
Cdd:PRK08131 262 LLIGSRAAGEKYGLKPMA-RILSSAAAGVEPR-------IMGIG---PVEAIKKALARAGLTLDDMDIIEINEAFASQVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 298 ITYEALGlcpegqggtlVDRGDNTyggkwvINPSGGLISKGHPLGATGlaqcAELCWQLRGEAGKRQVPGAKVALQHNLG 377
Cdd:PRK08131 331 GCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG----ARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*..
gi 755507949 378 LGGAVVV 384
Cdd:PRK08131 391 QGLAMVI 397
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
21-363 |
2.89e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 58.97 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQA---CVGYVYGDSTS-GQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:PRK06504 28 DLAAQVLDALVDRSGADPALIEDVimgCVSQVGEQATNvARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 97 ANCVLALGFEKMERGSIGTKFSdrttptdkhievLIDKYGLsAHPITPQM--------FG-YAGKEHM-EKYGTKVEHFA 166
Cdd:PRK06504 108 MDIVIAAGVESMTRVPMGSPST------------LPAKNGL-GHYKSPGMeerypgiqFSqFTGAEMMaKKYGLSKDQLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 167 KIGWKNHKHSVNNTYSQ-FQDEY-------------------------SLEEVMKSKPVFD-----FLTILQCCptsDGA 215
Cdd:PRK06504 175 EFALQSHQRAIAATQAGkFKAEIvpleitradgsgemhtvdegirfdaTLEGIAGVKLIAEggrltAATASQIC---DGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 216 AAAILSSEEFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVN 295
Cdd:PRK06504 252 SGVMVVNERGLKALGVKPLA-RIHHMTVIGGDPVIMLEAPL----------PATERALKKAGMKIDDIDLYEVNEAFASV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755507949 296 ELITYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRgEAGKR 363
Cdd:PRK06504 321 PLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTKLMTTLVHALK-QRGKR 369
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
26-345 |
3.52e-09 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 58.58 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 26 AGQKA-LEDAQIPYSAVEQ---ACVGYVYGDSTSGQRAIYHSLGL---TGIPIINVNnnCSTGSTALFMAHQLIQGGLAN 98
Cdd:PRK07850 32 AVQRAvLDRAGIDPGDVEQvigGCVTQAGEQSNNITRTAWLHAGLpyhVGATTIDCQ--CGSAQQANHLVAGLIAAGAID 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 99 CVLALGFEKMERGSIGTKFSDRTT---PTDKHI---------EVLIDKYGLSahpitpqmfgyagKEHMEKYGTKVEHFA 166
Cdd:PRK07850 110 VGIACGVEAMSRVPLGANAGPGRGlprPDSWDIdmpnqfeaaERIAKRRGIT-------------REDVDAFGLRSQRRA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 167 KIGWKNHK---------------------HSVNNTYSQFQDEYSLEEVMKSKPVFD--FLTILQCCPTSDGAAAAILSSE 223
Cdd:PRK07850 177 AQAWAEGRfdreispvqapvldeegqptgETRLVTRDQGLRDTTMEGLAGLKPVLEggIHTAGTSSQISDGAAAVLWMDE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 224 EFVQQYGLQSKAvEIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSvnelityeAL 303
Cdd:PRK07850 257 DRARALGLRPRA-RIVAQALVGAEPYYHLDGPV----------QATAKVLEKAGMKIGDIDLVEINEAFA--------SV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 755507949 304 GLCPEGQGGTLVDRgdntyggkwvINPSGGLISKGHPLGATG 345
Cdd:PRK07850 318 VLSWAQVHEPDMDK----------VNVNGGAIALGHPVGSTG 349
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
20-366 |
7.17e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 57.98 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQRAIYHSLGLtGIPIINVNNNCSTGSTALFMAHQLIQGG 95
Cdd:PRK06954 32 PQLGAAAIAAAVERAGLKPEQIDEVVMGCVLpagqGQAPARQAALGAGLPL-SVGCTTVNKMCGSGMRAAMFAHDMLVAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKME-------RGSIGTKFSDRTTPTDKHIEVLIDKYGLSahpitpQMFGYAGKEHMEKYGTKVEH---F 165
Cdd:PRK06954 111 SVDVIVAGGMESMTnapyllpKARGGMRMGHGQVLDHMFLDGLEDAYDKG------RLMGTFAEECAGEYGFTREAqdaF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 166 AKIGWKNHKHSVNNTYSQFQ-----------------DE----YSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILS 221
Cdd:PRK06954 185 AIESLARAKRANEDGSFAWEiapvtvagkkgdtvidrDEqpfkANPEKIPTLKPAFSktgTVTAANSSSISDGAAALVMM 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 222 SEEFVQQYGLQSKAVeIVAQEMMTDLPSTFEEKSIikvvgydmskEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYE 301
Cdd:PRK06954 265 RASTAKRLGLAPLAR-VVGHSTFAQAPSKFTTAPV----------GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMK 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755507949 302 ALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 366
Cdd:PRK06954 334 EHGLPHEK------------------VNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVA 380
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
31-349 |
9.43e-09 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 57.47 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 31 LEDAQIPYSAVEQACVGYVYGDSTsgQRAIYHSLG--LTGIP----IINVNNNCSTGSTALFMAHQLIQGGLANCVLALG 104
Cdd:PLN02287 83 VEKTGLNPSEVGDIVVGTVLAPGS--QRANECRMAafYAGFPetvpVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 105 FEKM------ERGSIGTKFSDRTTPTDKHIEVlidkyGLSAHPITpqmfgyagkehmEKYGTKVEHFAKIGWKNHKHSVN 178
Cdd:PLN02287 161 VESMttnpmaWEGGVNPRVESFSQAQDCLLPM-----GITSENVA------------ERFGVTREEQDQAAVESHRKAAA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 179 NTYS-QFQDEY------------------------------SLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSSEE 224
Cdd:PLN02287 224 ATASgKFKDEIvpvhtkivdpktgeekpivisvddgirpntTLADLAKLKPVFKkngTTTAGNSSQVSDGAGAVLLMKRS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 225 FVQQYGL------QSKAVEIVAQEMMTDLPSTfeekSIIKVVgydmskeaarrcyEKSGLTPNDVDVIELHDCFSVNELI 298
Cdd:PLN02287 304 VAMQKGLpilgvfRSFAAVGVDPAVMGIGPAV----AIPAAV-------------KAAGLELDDIDLFEINEAFASQFVY 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755507949 299 TYEALGLCPEGqggtlvdrgdntyggkwvINPSGGLISKGHPLGATGlAQC 349
Cdd:PLN02287 367 CCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
189-352 |
1.23e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 57.22 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 189 SLEEVMKSKPVFDF-----LTILQCCPTSDGAAAAILSSEEFVQQYGLQSKAVEIVAQEMMTDLpstfeeksiikVVGYD 263
Cdd:PRK09268 237 SLEKLAKLKPVFGKggratMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDF-----------VHGKE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 264 ---MSKE-AARRCYEKSGLTPNDVDVIELHDCFSVNELIT---YEALGLCPE--GQGGTL--VDRGDntyggkwvINPSG 332
Cdd:PRK09268 306 gllMAPAyAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlkaWEDEEYCRErlGLDAPLgsIDRSK--------LNVNG 377
|
170 180
....*....|....*....|...
gi 755507949 333 GLISKGHPLGATG---LAQCAEL 352
Cdd:PRK09268 378 SSLAAGHPFAATGgriVATLAKL 400
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
20-345 |
3.94e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 55.67 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVY----GDSTSGQRAIYHSLGLTgIPIINVNNNCSTGSTALFMAHQLIQGG 95
Cdd:PRK05656 27 VELGAAVIRRLLEQTGLDPAQVDEVILGQVLtagaGQNPARQAAIKAGLPHS-VPAMTLNKVCGSGLKALHLAAQAIRCG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 96 LANCVLALGFEKMERGS-----------------IGTKFSDR--TTPTDKHI----EVLIDKYGLS-----AHPITPQMF 147
Cdd:PRK05656 106 DAEVIIAGGQENMSLAPyvlpgartglrmghaqlVDSMITDGlwDAFNDYHMgitaENLVEKYGISreaqdAFAAASQQK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 148 GYAGKEHmekyGTKVEHFAKIGWKNHKHS--VNNTYSQFQDEYSLEEVMKSKPVFD---FLTILQCCPTSDGAAAAILSS 222
Cdd:PRK05656 186 AVAAIEA----GRFDDEITPILIPQRKGEplAFATDEQPRAGTTAESLAKLKPAFKkdgSVTAGNASSLNDGAAAVLLMS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 223 EEFVQQYGLQSKAvEIVAQEMMTDLPStfeeksiIKVVGydmSKEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEA 302
Cdd:PRK05656 262 AAKAKALGLPVLA-KIAAYANAGVDPA-------IMGIG---PVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKE 330
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 755507949 303 LGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 345
Cdd:PRK05656 331 LGWDAA------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
69-386 |
2.45e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 52.83 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 69 IPIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergSIGTKFSDRTTPTDKHIEVLIDKYglsahpitpQMFG 148
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESM---SLVPMMGHVVRPNPRLVEAAPEYY---------MGMG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 149 YAGKEHMEKYGTKVEHFAKIGWKNHKHSVNNTYSQ-FQDEY---------------------------------SLEEVM 194
Cdd:PRK07661 149 HTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGkFADEIvpvdvtlrtvgennklqeetitfsqdegvradtTLEILG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 195 KSKPVFDF---LTILQCCPTSDGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTDLPStfeeksiikvvgydms 265
Cdd:PRK07661 229 KLRPAFNVkgsVTAGNSSQMSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI---------------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 266 kEAARRCYEKSGLTPNDVDVIELHDCFSVNELITYEALGLCPEgqggtlvdrgdntyggkwVINPSGGLISKGHPLGATG 345
Cdd:PRK07661 293 -AAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTG 353
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755507949 346 laqcAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAVVVTL 386
Cdd:PRK07661 354 ----AKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFEL 390
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
20-104 |
7.87e-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: 50.89 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 20 PDMAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIY--HSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGLA 97
Cdd:cd00827 49 PTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYlaELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPW 128
|
....*..
gi 755507949 98 NCVLALG 104
Cdd:cd00827 129 RYALVVA 135
|
|
| Alkyl_sulf_C |
pfam14864 |
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ... |
455-512 |
9.11e-07 |
|
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates.
Pssm-ID: 405542 [Multi-domain] Cd Length: 124 Bit Score: 47.96 E-value: 9.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755507949 455 EATWVVDVKNGkgsVL----PNSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGN 512
Cdd:pfam14864 43 DEQYRLTLSNG---VLtyrkGRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGD 101
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
213-345 |
2.37e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 49.99 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 213 DGAAAAILSSEEFVQQYGLQ------SKAVEIVAQEMMTdlpstfeeksiIKVVGydmskeAARRCYEKSGLTPNDVDVI 286
Cdd:PRK06205 259 DAAAACLVTTEDKAEELGLRplarlvSWAVAGVEPSRMG-----------IGPVP------ATEKALARAGLTLDDIDLI 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 755507949 287 ELHDCFSVNELITYEALGLCPEGqggtlVDRgdntyggkwvINPSGGLISKGHPLGATG 345
Cdd:PRK06205 322 ELNEAFAAQVLAVLKEWGFGADD-----EER----------LNVNGSGISLGHPVGATG 365
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
21-122 |
5.09e-06 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 48.53 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 21 DMAKEAGQKALEDAQIPYSAVEQACVGYVYGD----STSGQraIYHSLGLTGIPIINVNNNCSTGSTALFMAHQLIQGGL 96
Cdd:PRK09352 54 DLATEAAKKALEAAGIDPEDIDLIIVATTTPDyafpSTACL--VQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGA 131
|
90 100
....*....|....*....|....*.
gi 755507949 97 ANCVLALGFEKMERgsIgTKFSDRTT 122
Cdd:PRK09352 132 YKNVLVIGAEKLSR--I-VDWTDRST 154
|
|
| BDS1 |
COG2015 |
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
456-522 |
8.67e-06 |
|
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441618 [Multi-domain] Cd Length: 629 Bit Score: 48.30 E-value: 8.67e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755507949 456 ATWVVDVKNGkgsVLPN----SDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLAMKLQNL 522
Cdd:COG2015 551 EKYLLELRNG---VLTYrkgpQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGL 618
|
|
| UbiJ |
COG3165 |
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism]; ... |
469-522 |
1.37e-05 |
|
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism];
Pssm-ID: 442398 Cd Length: 204 Bit Score: 46.01 E-value: 1.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755507949 469 VLPNSDKKADCTITMADSDLLALMTGKmNPQSAFFQGKLKIAGNMGLAMKLQNL 522
Cdd:COG3165 58 VLGAWEGEADCTLTGSLSALLRLADAQ-DLTALIASGELRIEGDAQLAQQLSRL 110
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
74-122 |
2.36e-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: 39.81 E-value: 2.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755507949 74 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFEKMergSIGTKFSDRTT 122
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETL---SKILDWTDRST 48
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
22-106 |
4.25e-04 |
|
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: 42.91 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 22 MAKEAGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIY--------------------------------HSLGLTGi 69
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnmaagqvaIRLGLRG- 152
|
90 100 110
....*....|....*....|....*....|....*..
gi 755507949 70 PIINVNNNCSTGSTALFMAHQLIQGGLANCVLALGFE 106
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
26-106 |
6.66e-04 |
|
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: 42.00 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 26 AGQKALEDAQIPYSAVEQACVGYVYGDSTSGQRAIYHS--------------------------------LGLTGiPIIN 73
Cdd:COG0304 78 AAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAyrallekgprrvspffvpmmmpnmaaghvsirFGLKG-PNYT 156
|
90 100 110
....*....|....*....|....*....|...
gi 755507949 74 VNNNCSTGSTALFMAHQLIQGGLANCVLALGFE 106
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
7-154 |
1.03e-03 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 41.36 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 7 WFMKPGGENSRDYPD------MAKEAGQKALEDAQIPYSAVEQacvgyVYGDSTSGQRAI-------YHSLGL--TGIPI 71
Cdd:PRK07204 34 WVLKKSGVKTRHFVDgetssyMGAEAAKKAVEDAKLTLDDIDC-----IICASGTIQQAIpctasliQEQLGLqhSGIPC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755507949 72 INVNNNCSTGSTALFMAHQLIQGGLANCVLALgfeKMERGSIGTKFSDRTTPT---DKHIEVLIDKYGLSAHPITPQMFG 148
Cdd:PRK07204 109 FDINSTCLSFITALDTISYAIECGRYKRVLII---SSEISSVGLNWGQNESCIlfgDGAAAVVITKGDHSSRILASHMET 185
|
....*.
gi 755507949 149 YAGKEH 154
Cdd:PRK07204 186 YSSGAH 191
|
|
| |
