|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
12-404 |
0e+00 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 706.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHsLGMTGIPIINVN 91
Cdd:PRK08256 1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 92 NNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHM 171
Cdd:PRK08256 78 NNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 172 EKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKA 251
Cdd:PRK08256 158 EKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 252 VEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLV 331
Cdd:PRK08256 237 VEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFI 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530363124 332 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYK 404
Cdd:PRK08256 317 DDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
17-403 |
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: 573.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVFGD---STCGQRAIYHSLGMTGIPIIN 89
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLGAgegQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 90 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 169
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 170 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 243
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 244 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 323
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 324 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 403
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
17-403 |
5.15e-153 |
|
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: 439.39 E-value: 5.15e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 17 VGVGMTKFVKPGaenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGD---STCGQRAIYHsLGMTGIPIINVNNN 93
Cdd:cd00829 1 VGVGMTPFGRRS---DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGrfqSFPGALIAEY-LGLLGKPATRVEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 94 CATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEK 173
Cdd:cd00829 77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 174 YGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVE 253
Cdd:cd00829 151 YGTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 254 ILAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDR 333
Cdd:cd00829 229 ILGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVRE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 334 GDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 403
Cdd:cd00829 306 GDTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
11-403 |
3.73e-96 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 294.88 E-value: 3.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAI------YhsLGMTG 84
Cdd:PRK06064 1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIaaliadY--AGLAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 85 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAh 156
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 157 pvaPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAIL 236
Cdd:PRK06064 144 ---PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 237 ASEAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 316
Cdd:PRK06064 221 ASEEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 317 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEA--GKRQVPGAKVALQHNL-G 393
Cdd:PRK06064 296 EDLGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVgG 375
|
410
....*....|
gi 530363124 394 IGGAVVVTLY 403
Cdd:PRK06064 376 TGHTAVVHIL 385
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
12-393 |
8.89e-73 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 234.35 E-value: 8.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGyvfgdsTCGQRA--------IYHSLGMT 83
Cdd:PRK12578 1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVG------STAYRGielypapiVAEYSGLT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 84 GIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSAhpva 159
Cdd:PRK12578 72 GKVPLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTTF---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 160 PQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASE 239
Cdd:PRK12578 142 PTYYALYATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 240 AFVQKYGLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEAL 319
Cdd:PRK12578 222 EKVKELKIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530363124 320 GLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAK-VALQHNLG 393
Cdd:PRK12578 298 GFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVG 372
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
10-401 |
9.29e-71 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 229.65 E-value: 9.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 10 TLRRVFVVGVGMTKFVKPGaensRDYPDLAEEAGKKALADAQIPYSAVdQACV----------GYVFGdSTCGQraiyhS 79
Cdd:PRK06059 2 MPEPVYILGAGMHPWGKWG----RDFVEYGVVAARAALADAGLDWRDV-QLVVgadtirngypGFVAG-ATFAQ-----A 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 80 LGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVa 159
Cdd:PRK06059 71 LGWNGAPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 160 pqMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASE 239
Cdd:PRK06059 146 --YFALLARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 240 AFVQKYGLQSK-AVEILAQEMMT--------DLPSsFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCF 308
Cdd:PRK06059 224 SFARRHLGSVAgVPSVRAISTVTprypqhlpELPD-IATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 309 STNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVAL 388
Cdd:PRK06059 303 TALELDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGI 382
|
410
....*....|....*.
gi 530363124 389 QHNLGI---GGAVVVT 401
Cdd:PRK06059 383 TANQGLfghGSSVIVA 398
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
13-398 |
5.94e-63 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 209.03 E-value: 5.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 13 RVFVVGVGMTKFVKPGAEnsrDYPDLAEEAGKKALADAQIPYSAVDQACVGyVF-----GDSTCGQRAIYHSLGMTGIPI 87
Cdd:PRK07516 3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLG-HFnagfsPQDFPASLVLQADPALRFKPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 88 INVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQMF 163
Cdd:PRK07516 79 TRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 164 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILASE 239
Cdd:PRK07516 148 GRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLADA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 240 AFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 318
Cdd:PRK07516 228 ETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 319 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGiGGAV 398
Cdd:PRK07516 300 MGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG-GAAV 378
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
12-393 |
1.70e-61 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 205.26 E-value: 1.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHS--LGMTGIPIIN 89
Cdd:PRK06157 7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPLSraLRLPNIPVTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 90 VNNNCATGSTALFMARQLIQGGVAECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 168
Cdd:PRK06157 84 VENFCATGSEAFRGAVYAVASGAYDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 169 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 244
Cdd:PRK06157 154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 245 YG----LQSKAVEILA---QEMMTDL--PSSFEEKSIikmvgfdmskeAARKCYEKSGLT-P-NDIDVIELHDCFSTNEL 313
Cdd:PRK06157 234 LGkkdpVYVKALQLAVsngWELQYNGwdGSYFPTTRI-----------AARKAYREAGITdPrEELSMAEVHDCFSITEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 314 LTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLG 393
Cdd:PRK06157 303 VTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLG 382
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
8-404 |
4.71e-56 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 192.05 E-value: 4.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYV---FGDSTCGQRAIYHSLGMTG 84
Cdd:PRK06365 12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYFsdhFQRQLLAGIMVQDYLGLVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 85 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 158
Cdd:PRK06365 90 KPSKRIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 159 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 235
Cdd:PRK06365 154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 236 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 295
Cdd:PRK06365 234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 296 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLR 373
Cdd:PRK06365 310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQ 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 530363124 374 GEAGKR------QVPGAKVALQH-NLGIGGAVVVTLYK 404
Cdd:PRK06365 390 GRIKKHfhddylQVKNAKRGLIHsHAGTGTYVTVTILE 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
36-401 |
3.86e-54 |
|
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: 181.49 E-value: 3.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVGYVFGD---STCGQRAIYHsLGMTGIPIINVNNNCATGSTALFMARQLIQGGV 112
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSgefSGAAGQLAYH-LGISGGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 113 AECVLALGFEKmskgslgikfsdrtiptdkhvdllinkyglsahpvapqmfgyagkehmekygtkiehfakigwknhkhs 192
Cdd:cd00327 87 ADIVLAGGSEE--------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 193 vnnpysqfqdeysldevmaskevfdfltilqcCPTSDGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSI 272
Cdd:cd00327 98 --------------------------------FVFGDGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASM 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 273 IKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLIS 352
Cdd:cd00327 139 VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIM 203
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 530363124 353 KGHPLGATGLAQCAELCWQLRGEAGK--RQVPGAKVALQHNLGIGGAVVVT 401
Cdd:cd00327 204 TGHPLGAAGLAILDELLLMLEHEFIPptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
12-406 |
3.71e-47 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 167.21 E-value: 3.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFVKPGAENSrdYPDLAEEAGKKALADAQIPYSAVDQACVGY---VFGDSTCGQRAIYHSLGMTGIPII 88
Cdd:PRK08313 3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDAVVVGKapdFFEGVMMPELFLADALGATGKPLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 89 NVNNNCATG-STALfMARQLIQGGVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHPVApqmfgyag 167
Cdd:PRK08313 81 RVHTAGSVGgSTAV-VAASLVQSGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPHVR-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 168 kEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYG 246
Cdd:PRK08313 149 -AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 247 LQSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYEALGLCPE 324
Cdd:PRK08313 228 GRPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 325 GQGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGiGGAVVVTLYK 404
Cdd:PRK08313 303 GEGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG-GGSQFFSMWV 380
|
..
gi 530363124 405 MG 406
Cdd:PRK08313 381 VG 382
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
14-401 |
2.77e-46 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 165.25 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 14 VFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQR------AIYHSlGMTGIPI 87
Cdd:PRK06289 5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGhlgampATVHP-ALWGVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 88 INVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQM 162
Cdd:PRK06289 84 SRHEAACASGSVATLAAMADLRAGRYDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 163 FGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILA 237
Cdd:PRK06289 153 FARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 238 SEAFVQKYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNEL 313
Cdd:PRK06289 233 SDAYLRDYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 314 LTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALqhNLG 393
Cdd:PRK06289 311 LAIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFG--TLN 388
|
....*...
gi 530363124 394 IGGAVVVT 401
Cdd:PRK06289 389 IGGSTTTT 396
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
37-396 |
4.82e-37 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 139.78 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDqacvgyvfGDSTCgqrAIYHSL-GMT-----GIPIINVNNNCATGS---TALFMARQL 107
Cdd:PRK06158 30 ELLAQAAHRALADAGLTMADVD--------GLFTA---SPDDALwGLSvaeylGIRPRFVDGTMIGGSsflAHLLPAALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 108 IQGGVAECVL-ALGFEKMSKGSLGIKFSDrtiptdkhvdllINKYGLSAHPVAPqMFGYA--GKEHMEKYGTKIEHFAKI 184
Cdd:PRK06158 99 LEAGLCDVALiCYGSNQRSAGGKLRSMLD------------PQPYEAPYKPVNP-VSAYAlaAARHMHQYGTTREQLAEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 185 GWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQkyGLQSKAVEILAQEMMTDlp 264
Cdd:PRK06158 166 AVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMVRADRAR--DLPRPPVYVLGAAAATW-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 265 ssfeEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGG 340
Cdd:PRK06158 242 ----HRQISSMP--DLTVTAAaesgPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530363124 341 KWVINPSGGLISKGHPlGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHnlGIGG 396
Cdd:PRK06158 316 RLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH--GNGG 368
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
12-382 |
1.85e-33 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 129.94 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFVKPGAENSRDypdLAEEAGKKALADAQIPYSAVDqaCVgyVFG---DSTCG--QRAIYHSLGMTGI- 85
Cdd:PRK06065 9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDID--CV--VIGsapDAFDGvhMKGEYLSHGSGGIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 86 -PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM-- 162
Cdd:PRK06065 82 kPVSRVYVGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiw 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 163 -FGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAF 241
Cdd:PRK06065 151 iFAMEMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 242 VQKYglqskaveilaqemmTDLPSsfeeksIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIEL 304
Cdd:PRK06065 231 ARRY---------------TDTPV------WVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEP 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530363124 305 HDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 382
Cdd:PRK06065 290 YDPFDYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
10-396 |
9.01e-31 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 123.46 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 10 TLRRVFVVGVGMTKFVKPGAEN--SRDYPDLAEEAGK---KALADA----------QIPYSAVDQACVGYVFGDSTCGQ- 73
Cdd:PTZ00455 10 AAKRVFVVGGHITPFVGKGSPLfiDKKHPDFGKKENKtleELLATAiqgtlentglDGKAALVDKVVVGNFLGELFSSQg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 74 ---RAIYHSLGMTGI-------PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKH 143
Cdd:PTZ00455 90 hlgPAAVGSLGQSGAsnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 144 VDLLINKYGLsahpvaPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MAS 212
Cdd:PTZ00455 170 RQRKLDDFTF------PCLFAKRMKYIQEHGHFTMEDTARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 213 KEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKC 288
Cdd:PTZ00455 244 ETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 289 YEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAEL 368
Cdd:PTZ00455 319 LSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEV 398
|
410 420
....*....|....*....|....*...
gi 530363124 369 CWQLRGEAGKRQVPGAkVALQHNLGIGG 396
Cdd:PTZ00455 399 YRQMKGQCGEYQMKNI-PALGATLNMGG 425
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
171-400 |
1.29e-28 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 116.39 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 171 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 250
Cdd:PRK06066 154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 251 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 328
Cdd:PRK06066 232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530363124 329 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQvPGAKVALQHNL-GI---GGAVVV 400
Cdd:PRK06066 308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVASWrGIptlTGSVVV 382
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
156-397 |
1.53e-25 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 107.48 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 156 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 235
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 236 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 299
Cdd:PRK08142 214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 300 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG- 377
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHp 355
|
250 260
....*....|....*....|
gi 530363124 378 KRQVPGAKVALQHnlGIGGA 397
Cdd:PRK08142 356 AVQVPNCDLALAH--GTGGL 373
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
16-384 |
1.19e-24 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 105.06 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 16 VVGVGMTKFVKpgaENSRDYPDLAEEAGKKALADAQIPYSAVDqacvGYV-FGDSTCGQRAIYHSLGM---TGIPIINVN 91
Cdd:PRK07855 8 IVGIGATEFSK---NSGRSELRLACEAVLAALDDAGLAPSDVD----GLVtFTMDTNPEIAVARALGIgelKFFSRIHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 92 NNCATGSTA-LFMArqlIQGGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqM 162
Cdd:PRK07855 81 GGAACATVQqAAMA---VATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--M 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 163 FGyagKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAF 241
Cdd:PRK07855 153 LA---RRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 242 VQKygLQSKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFS 309
Cdd:PRK07855 230 ARD--LKQRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFT 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530363124 310 TNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLRGEAgKRQVPGA 384
Cdd:PRK07855 297 PFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLRGTS-VNQVPGV 367
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
36-400 |
5.54e-23 |
|
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: 100.25 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVGYVFGdSTCGQ---RAIYHSLGM-TGIPIINVNNNCATGSTALFMARQLIQGG 111
Cdd:cd00751 23 DDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ-AGEGQnpaRQAALLAGLpESVPATTVNRVCGSGLQAVALAAQSIAAG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 112 VAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAgkEHM-EKYG--------------- 175
Cdd:cd00751 102 EADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITA--ENVaEKYGisreeqdefalrshq 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 176 -----TKIEHFA------KIGWKNHKHSVNnpysqfQDEY-----SLdEVMAS-KEVFD---FLTILQCCPTSDGAAAAI 235
Cdd:cd00751 180 raaaaQEAGRFKdeivpvEVPGRKGPVVVD------RDEGprpdtTL-EKLAKlKPAFKkdgTVTAGNASGINDGAAAVL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 236 LASEAFVQKYGLQSKAVeILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDCF 308
Cdd:cd00751 253 LMSEEKAKELGLKPLAR-IVGYavagvdpAIMGIGPV-----------------PAIPKALKRAGLTLDDIDLIEINEAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 309 STNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVAL 388
Cdd:cd00751 315 AAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGL----ATM 372
|
410
....*....|..
gi 530363124 389 QHNLGIGGAVVV 400
Cdd:cd00751 373 CIGGGQGAAMVI 384
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
37-400 |
1.07e-20 |
|
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: 93.45 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQACVGYVF----GDSTCGQRAIYHSLGMTgIPIINVNNNCATGSTALFMARQLIQGGV 112
Cdd:TIGR01930 23 DLGAAVIKELLERNPLDPELIDDVIFGNVLqageQQNIARQAALLAGLPES-VPAYTVNRQCASGLQAVILAAQLIRAGE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 113 AECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIE---HFA----KIG 185
Cdd:TIGR01930 102 ADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLAKKYGISREeqdEYAlrshQRA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 186 WKNHK-------------HSVNNPYSQFQDE-----YSLdEVMAS-KEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 243
Cdd:TIGR01930 182 AKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTL-EKLAKlKPAFDpdgTVTAGNSSPLNDGAAALLLMSEEKAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 244 KYGLQSKAVEILAQEMMTDlPSSFeeksiikmvGFdMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 323
Cdd:TIGR01930 261 ELGLTPLARIVSFAVAGVD-PEIM---------GL-GPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530363124 324 EgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 400
Cdd:TIGR01930 330 E------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGL----ATMCIGGGQGAAVIL 384
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
14-203 |
8.70e-18 |
|
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: 82.74 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFGdSTCGQ---RAIYHSLGMT-GIPII 88
Cdd:pfam00108 1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQ-AGEGQnpaRQAALKAGIPdSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 89 NVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGY 165
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GL 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 530363124 166 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 203
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
12-400 |
6.70e-13 |
|
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: 70.10 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMTKFVKP-GAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF--GDSTCGQRAIyhSLgMTGIPI- 87
Cdd:COG0183 2 REVVIVDAVRTPFGRFgGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLqaGQGQNPARQA--AL-LAGLPEs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 88 ---INVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS-------KGSLGIKFSDRTiptdkhVDLLINKyGLSAHP 157
Cdd:COG0183 79 vpaVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSrapmllpKARWGYRMNAKL------VDPMINP-GLTDPY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 158 VAPQMFGYAgkEHM-EKYG-TKIEhfakigwknhkhsvnnpysqfQDEYSL----------------DEVM--------- 210
Cdd:COG0183 152 TGLSMGETA--ENVaERYGiSREE---------------------QDAFALrshqraaaaiaagrfdDEIVpvevpdrkg 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 211 -------------ASKE-------VFD---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMM 260
Cdd:COG0183 209 evvvdrdegprpdTTLEklaklkpAFKkdgTVTAGNASGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 261 TDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntygg 340
Cdd:COG0183 288 GIGPV-----------------PATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPD---------------- 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 341 kwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 400
Cdd:COG0183 335 --KVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGL----ATMCIGGGQGIALII 388
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
85-400 |
1.67e-12 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 68.60 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 85 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 156
Cdd:PRK06445 86 IPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 157 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 217
Cdd:PRK06445 161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 218 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 287
Cdd:PRK06445 241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 288 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAE 367
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVGT 362
|
330 340 350
....*....|....*....|....*....|...
gi 530363124 368 LCWQLRGEAGKRQVPGAKVAlqhnLGIGGAVVV 400
Cdd:PRK06445 363 LARQLQIKGKDYGVATLCVG----GGQGGAVVL 391
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
284-400 |
6.13e-12 |
|
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: 62.66 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 284 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 363
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGAR 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 530363124 364 QCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 400
Cdd:pfam02803 89 ILVTLLHELKRRGGKYGL----ASLCIGGGQGVAMII 121
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
11-361 |
1.49e-11 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 65.89 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 11 LRRVFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF--GDSTCGQRAIYHSLGMT-GIP 86
Cdd:PRK08235 1 MSKTVIVSAARTPFGKfGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLqgGQGQIPSRQAARAAGIPwEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 87 IINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS-------KGSLGIKFSDRTIptdkhVDLLINKyGLSAHPVA 159
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSnapyilpGARWGYRMGDNEV-----IDLMVAD-GLTCAFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 160 PQMfGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYS-QFQDEY-------------------------SLDEVMASK 213
Cdd:PRK08235 155 VHM-GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEgRFEEEIvpvtipqrkgdpivvakdeaprkdtTIEKLAKLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 214 EVFD---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeILAQEMMTDLPSSFEeksiiKMVGFdmskeAARKCYE 290
Cdd:PRK08235 234 PVFDktgTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLAT-ILAHTAIAVEAKDFP-----RTPGY-----AINALLE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530363124 291 KSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK08235 303 KTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
37-137 |
4.65e-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: 63.59 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQACVGYVFGD----ST-CgqrAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGG 111
Cdd:COG0332 53 DLAVEAARKALEAAGIDPEDIDLIIVATVTPDylfpSTaC---LVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSG 129
|
90 100
....*....|....*....|....*.
gi 530363124 112 VAECVLALGFEKMSKgslGIKFSDRT 137
Cdd:COG0332 130 QAKNVLVVGAETLSR---IVDWTDRS 152
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
11-402 |
1.34e-10 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 62.72 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 11 LRRVFVVGVGMTKFVKPGAENSR-DYPDLAEEAGKKALADAQIPYSAVDQACVGYVF----GDSTCGQrAIYHSLGMTGI 85
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKiKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIqagvGQNPAGQ-AAYHAGLPFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 86 PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPtdKHvdLLINKYGLSAHPVAPQMFGY 165
Cdd:PRK06366 80 TKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGP--KH--LLHKNYKIDDAMLVDGLIDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 166 AGKEHM--------EKYGTKIEHFAKIGWKNHKHSVNNPYS-QFQDEYSLDEVMASKE---------------VFD---F 218
Cdd:PRK06366 156 FYFEHMgvsaertaRKYGITREMADEYSVQSYERAIRATESgEFRNEIVPFNDLDRDEgirkttmedlaklppAFDkngI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 219 LTILQCCPTSDGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSSFEEKSIikmvgfdmskEAARKCYEKSGLTPND 298
Cdd:PRK06366 236 LTAGNSAQLSDGGSALVMASEKAINEYGLKPIA-RITGYESASLDPLDFVEAPI----------PATRKLLEKQNKSIDY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 299 IDVIELHDCFSTNELLTYEALGLcpegqgatlvdrgDNTYggkwvINPSGGLISKGHPLGATGlaqcAELCWQLRGEAGK 378
Cdd:PRK06366 305 YDLVEHNEAFSIASIIVRDQLKI-------------DNER-----FNVNGGAVAIGHPIGNSG----SRIIVTLINALKT 362
|
410 420
....*....|....*....|....
gi 530363124 379 RQVPGAKVALQHnlGIGGAVVVTL 402
Cdd:PRK06366 363 RHMKTGLATLCH--GGGGAHTLTL 384
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
37-361 |
1.22e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 59.72 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQACVGYVfgDSTCGQ-----RAIYHSLGMT-GIPIINVNNNCATGSTALFMARQLIQG 110
Cdd:PRK07801 28 DLGAHVLKGLVDRTGIDPAAVDDVIFGCV--DTIGPQagniaRTSWLAAGLPeEVPGVTVDRQCGSSQQAIHFAAQAVMS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 111 GVAECVLALGFEKMSK--------------------GSLG--IKFSDRTIPTDKHVDLLINKYGLSahpvapqmfgyagK 168
Cdd:PRK07801 106 GTQDLVVAGGVQNMSQipissamtageqlgftspfaESKGwlHRYGDQEVSQFRGAELIAEKWGIS-------------R 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 169 EHMEKYGTKIEHFAKIGWKN-HKHSVNNPYSQF-QDEYSLD---EVMASKEVFD---FLTILQCCPTSDGAAAAILASEA 240
Cdd:PRK07801 173 EEMERFALESHRRAFAAIRAgRFDNEIVPVGGVtVDEGPREtslEKMAGLKPLVeggRLTAAVASQISDGASAVLLASER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 241 FVQKYGLQSKAvEILAQEMMTDLPssfeeksiIKMVGFDMSkeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALG 320
Cdd:PRK07801 253 AVKRHGLTPRA-RIHHLSVRGDDP--------VFMLTAPIP--ATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETG 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530363124 321 LCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK07801 322 ADPAK------------------VNPNGGAIALGHPLGATG 344
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
83-378 |
2.18e-09 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 59.25 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 83 TGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLG---IKFSDRTIPTDKHVDLlinKYG--LSAHP 157
Cdd:PRK09052 84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgnkPSMSPAIFARDENVGI---AYGmgLTAEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 158 VAPQ---------MFGYAG-------------KEHMEKYgTKIEHFAKIGW---KNHKHSVNnpysqfQDE-----YSLD 207
Cdd:PRK09052 161 VAEQwkvsredqdAFALEShqkaiaaqqagefKDEITPY-EITERFPDLATgevDVKTRTVD------LDEgpradTSLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 208 EVMASKEVFDF---LTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPssfeeksiikmvgf 278
Cdd:PRK09052 234 GLAKLKPVFANkgsVTAGNSSQTSDGAGAVILVSEKALKQFNLTplarfvSFAVAGVPPEIMGIGP-------------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 279 dmsKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLG 358
Cdd:PRK09052 300 ---IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLG 358
|
330 340
....*....|....*....|
gi 530363124 359 ATGLAQCAELCWQLRGEAGK 378
Cdd:PRK09052 359 ATGAIRTATVVHGLRRTNLK 378
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
37-137 |
4.34e-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: 57.55 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDqaCVGYVfgdSTCGQRA-------IYHSLGMTGIPIINVNNNCATGSTALFMARQLIQ 109
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDID--LIIVA---TSTPDYLfpataclVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIR 126
|
90 100
....*....|....*....|....*...
gi 530363124 110 GGVAECVLALGFEKMSKgslGIKFSDRT 137
Cdd:cd00830 127 SGGAKNVLVVGAETLSR---ILDWTDRS 151
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
284-361 |
4.77e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 57.97 E-value: 4.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530363124 284 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
284-379 |
1.08e-08 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 56.89 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 284 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG-- 361
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSGar 365
|
90
....*....|....*...
gi 530363124 362 LAQCAELcwQLRGEAGKR 379
Cdd:PRK09050 366 LVLTALH--QLERTGGRY 381
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
281-392 |
4.29e-08 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 54.70 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 281 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 360
Cdd:PRK07937 252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310
|
90 100 110
....*....|....*....|....*....|....*
gi 530363124 361 GLAQCAELCWQ-LRGEAGkRQVPGAKV--ALQHNL 392
Cdd:PRK07937 311 GLERIGEAARHiWDGSAR-RALAHATSgpALQQNL 344
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
36-361 |
7.44e-08 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 54.39 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVGYVF----GDSTCGQRAIYHSLGMTgIPIINVNNNCATGSTALFMARQLIQGG 111
Cdd:PRK05790 27 VELGAIVIKAALERAGVPPEQVDEVIMGQVLqagaGQNPARQAALKAGLPVE-VPALTINKVCGSGLKAVALAAQAIRAG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 112 VAECVLALGFEKMS-------KGSLGIKFSDRTIptdkhVDLLI--------NKY--GLSAHPVAPQmfgYA-GKEHMEK 173
Cdd:PRK05790 106 DADIVVAGGQESMSqaphvlpGSRWGQKMGDVEL-----VDTMIhdgltdafNGYhmGITAENLAEQ---YGiTREEQDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 174 YGTKIEHFAKIGWKNHKhsvnnpysqFQDEYSLDEVMASKE---VFD--------------------F-----LTILQCC 225
Cdd:PRK05790 178 FALASQQKAEAAIKAGR---------FKDEIVPVTIKQRKGdpvVVDtdehprpdttaeslaklrpaFdkdgtVTAGNAS 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 226 PTSDGAAAAILASEAFVQKYGLQSKAvEILAQemmtdlpssfeeksiiKMVGFDMSK------EAARKCYEKSGLTPNDI 299
Cdd:PRK05790 249 GINDGAAAVVVMSEAKAKELGLTPLA-RIVSY----------------AVAGVDPAImgigpvPAIRKALEKAGWSLADL 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530363124 300 DVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK05790 312 DLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
36-400 |
1.23e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 53.50 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTcGQRAIYHSLGMTGIPI----INVNNNCATGSTALFMARQLIQGG 111
Cdd:PRK06633 28 PMLAAHLIKDILQNSKIDPALVNEVILGQVITGGS-GQNPARQTLIHAGIPKevpgYTINKVCGSGLKSVALAANSIMTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 112 VAECVLALGFEKMSKG------SLGIKFSDRTIPTDKHVDLLINKY-----GLSAHPVAPQmFGYAGKEHMEkygtkieh 180
Cdd:PRK06633 107 DNEIVIAGGQENMSLGmhgsyiRAGAKFGDIKMVDLMQYDGLTDVFsgvfmGITAENISKQ-FNISRQEQDE-------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 181 FAkigWKNHKHSVNNPYSQ-FQDEYSLDEVMASK--EVFDF---------LTIL-QCCPTSDGAAAAILASEAFVQKYG- 246
Cdd:PRK06633 178 FA---LSSHKKAAKAQLAGiFKDEILPIEVTIKKttSLFDHdetvrpdtsLEILsKLRPAFDKNGVVTAGNASSINDGAa 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 247 -LQSKAVEILAQEMMTDLPS--SFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcp 323
Cdd:PRK06633 255 cLMVVSEEALKKHNLTPLARivSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 324 egqgatlvdrgdntyggKW---VINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 400
Cdd:PRK06633 331 -----------------KWdmeKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGL----VTLCIGGGMGMAMCV 389
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
284-361 |
1.23e-07 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 53.42 E-value: 1.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530363124 284 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
290-365 |
9.97e-07 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 50.92 E-value: 9.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530363124 290 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGlAQC 365
Cdd:PLN02287 342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
37-137 |
1.05e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 50.25 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQACVG-----YVFGDSTCGqraIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGG 111
Cdd:PRK12879 55 DLAIKAAERALARAGLDAEDIDLIIVAtttpdYLFPSTASQ---VQARLGIPNAAAFDINAACAGFLYGLETANGLITSG 131
|
90 100
....*....|....*....|....*.
gi 530363124 112 VAECVLALGFEKMSKgslGIKFSDRT 137
Cdd:PRK12879 132 LYKKVLVIGAERLSK---VTDYTDRT 154
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
37-137 |
1.29e-06 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 50.07 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRA--IYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAE 114
Cdd:PRK09352 54 DLATEAAKKALEAAGIDPEDIDLIIVATTTPDYAFPSTAclVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAYK 133
|
90 100
....*....|....*....|...
gi 530363124 115 CVLALGFEKMSKgslGIKFSDRT 137
Cdd:PRK09352 134 NVLVIGAEKLSR---IVDWTDRS 153
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
229-361 |
1.47e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 50.16 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 229 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 308
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 530363124 309 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
283-400 |
2.15e-06 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 49.78 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 283 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATGl 362
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG- 362
|
90 100 110
....*....|....*....|....*....|....*...
gi 530363124 363 aqcAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVV 400
Cdd:PRK08131 363 ---ARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVI 397
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
284-361 |
4.28e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 48.83 E-value: 4.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530363124 284 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATG 365
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
205-361 |
6.16e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 48.46 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 205 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 275
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 276 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 355
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
|
....*.
gi 530363124 356 PLGATG 361
Cdd:PRK07851 362 PFGMTG 367
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
36-120 |
8.33e-06 |
|
"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: 47.43 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVG--YVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVA 113
Cdd:cd00827 49 PTMAVEAARRALERAGIDPDDIGLLIVAteSPIDKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPW 128
|
....*..
gi 530363124 114 ECVLALG 120
Cdd:cd00827 129 RYALVVA 135
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
12-383 |
9.57e-06 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 47.78 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 12 RRVFVVGVGMT---KFVkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF----GDSTCGQRAiyhsLGmTG 84
Cdd:PLN02644 1 RDVCIVGVARTpigGFL--GSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLsanlGQAPARQAA----LG-AG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 85 IP----IINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS-------KGSLGIKFSDRTIPTDKHVDLLINKY-- 151
Cdd:PLN02644 74 LPpstiCTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnapkylpEARKGSRLGHDTVVDGMLKDGLWDVYnd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 152 ---GLSAHPVAPQMF-------GYAgkehMEKYGTKIE-----HFA------KIGWKNHKHSVNNPYSQFQDEYSLDEVM 210
Cdd:PLN02644 154 fgmGVCAELCADQYSisreeqdAYA----IQSYERAIAaqeagAFAweivpvEVPGGRGRPSVIVDKDEGLGKFDPAKLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 211 ASKEVFD----FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVEI----LAQ--EMMTDLPSSfeeksiikmvgfdm 280
Cdd:PLN02644 230 KLRPSFKedggSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRgyadAAQapELFTTAPAL-------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 281 skeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGAT 360
Cdd:PLN02644 296 ---AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCS 354
|
410 420
....*....|....*....|...
gi 530363124 361 GLAQCAELCWQLRGEAGKRQVPG 383
Cdd:PLN02644 355 GARILVTLLGVLRSKNGKYGVAG 377
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
90-137 |
2.87e-05 |
|
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: 42.12 E-value: 2.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530363124 90 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslGIKFSDRT 137
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSK---ILDWTDRS 47
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
38-122 |
3.03e-05 |
|
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: 45.99 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 38 LAEEAGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIY--------------------------------HSLGMTGi 85
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPERIGVVIGSGIGGLATIEeayrallekgprrvspffvpmalpnmaagqvaIRLGLRG- 152
|
90 100 110
....*....|....*....|....*....|....*..
gi 530363124 86 PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFE 122
Cdd:cd00834 153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
284-361 |
4.10e-05 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 45.73 E-value: 4.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530363124 284 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 361
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
283-382 |
4.42e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 45.65 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 283 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGL 362
Cdd:PRK06954 299 GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEK------------------VNVNGGACALGHPIGASGA 360
|
90 100
....*....|....*....|
gi 530363124 363 AQCAELCWQLRGEAGKRQVP 382
Cdd:PRK06954 361 RILVTLIGALRARGGKRGVA 380
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
85-361 |
4.50e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 45.51 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 85 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHVdllinkygLSAHPV----AP 160
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSL-----------VPMMGHV--------VRPNPRlveaAP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 161 QMF---GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNN-PYSQFQDE-----------------------YSLDEVMASK 213
Cdd:PRK07661 142 EYYmgmGHTAEQVAVKYGISREDQDAFAVRSHQRAAKAlAEGKFADEivpvdvtlrtvgennklqeetitFSQDEGVRAD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 214 EVFDFLTILQ-------------CCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiik 274
Cdd:PRK07661 222 TTLEILGKLRpafnvkgsvtagnSSQMSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI--------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 275 mvgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKG 354
Cdd:PRK07661 293 --------AAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALG 346
|
....*..
gi 530363124 355 HPLGATG 361
Cdd:PRK07661 347 HPLGCTG 353
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
37-379 |
4.68e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 45.49 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 37 DLAEEAGKKALADAQIPYSAVDQA---CVGYVFGDST-CGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGV 112
Cdd:PRK06504 28 DLAAQVLDALVDRSGADPALIEDVimgCVSQVGEQATnVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 113 AECVLALGFEKMSKGSLGikfSDRTIPTdkhvdllinKYGLsAHPVAPQM--------FG-YAGKEHM-EKYGTKIEHFA 182
Cdd:PRK06504 108 MDIVIAAGVESMTRVPMG---SPSTLPA---------KNGL-GHYKSPGMeerypgiqFSqFTGAEMMaKKYGLSKDQLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 183 KIGWKNHKHSVNNPYSQ-FQDE---------------YSLDE---------------VMASKEVFDFLTILQCCptsDGA 231
Cdd:PRK06504 175 EFALQSHQRAIAATQAGkFKAEivpleitradgsgemHTVDEgirfdatlegiagvkLIAEGGRLTAATASQIC---DGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 232 AAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSSFEEKSIikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTN 311
Cdd:PRK06504 252 SGVMVVNERGLKALGVKPLA-RIHHMTVIGGDPVIMLEAPL----------PATERALKKAGMKIDDIDLYEVNEAFASV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530363124 312 ELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRgEAGKR 379
Cdd:PRK06504 321 PLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTKLMTTLVHALK-QRGKR 369
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
36-361 |
1.74e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 43.72 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 36 PDLAEEAGKKALADAQIPYSAVDQACVGYVF----GDSTCGQRAIYHSLGMTgIPIINVNNNCATGSTALFMARQLIQGG 111
Cdd:PRK05656 27 VELGAAVIRRLLEQTGLDPAQVDEVILGQVLtagaGQNPARQAAIKAGLPHS-VPAMTLNKVCGSGLKALHLAAQAIRCG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 112 VAECVLALGFEKMS-------KGSLGIKFSDRTIPTDKHVDLL---INKYGLsahpvapqmfGYAGKEHMEKYG-TKIEH 180
Cdd:PRK05656 106 DAEVIIAGGQENMSlapyvlpGARTGLRMGHAQLVDSMITDGLwdaFNDYHM----------GITAENLVEKYGiSREAQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 181 FAKIGWKNHKHSVNNPYSQFQDE---------------YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEafvqky 245
Cdd:PRK05656 176 DAFAAASQQKAVAAIEAGRFDDEitpilipqrkgeplaFATDEQPRAGTTAESLAKLKPAFKKDGSVTAGNASS------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 246 gLQSKAVEILAqeMMTDLPSSFEEKSIIKMVGFDMSK-----------EAARKCYEKSGLTPNDIDVIELHDCFSTNELL 314
Cdd:PRK05656 250 -LNDGAAAVLL--MSAAKAKALGLPVLAKIAAYANAGvdpaimgigpvSATRRCLDKAGWSLAELDLIEANEAFAAQSLA 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 530363124 315 TYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 361
Cdd:PRK05656 327 VGKELGWDAA------------------KVNVNGGAIALGHPIGASG 355
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
42-122 |
2.34e-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: 43.16 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530363124 42 AGKKALADAQIPYSAVDQACVGYVFGDSTCGQRAIYHS--------------------------------LGMTGiPIIN 89
Cdd:COG0304 78 AAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAyrallekgprrvspffvpmmmpnmaaghvsirFGLKG-PNYT 156
|
90 100 110
....*....|....*....|....*....|...
gi 530363124 90 VNNNCATGSTALFMARQLIQGGVAECVLALGFE 122
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
279-302 |
5.20e-03 |
|
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: 38.68 E-value: 5.20e-03
10 20
....*....|....*....|....
gi 530363124 279 DMSKEAARKCYEKSGLTPNDIDVI 302
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLI 75
|
|
| |
