|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
12-380 |
0e+00 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 652.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEA------------------------GDSTCGQRAIYHsLGMTGIPIINVN 67
Cdd:PRK08256 1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAgraaladagidydavqqayvgyvyGDSTSGQRALYE-VGMTGIPIVNVN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 68 NNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHM 147
Cdd:PRK08256 78 NNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 148 EKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKA 227
Cdd:PRK08256 158 EKYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 228 VEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLV 307
Cdd:PRK08256 237 VEIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFI 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302344760 308 DRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYK 380
Cdd:PRK08256 317 DDGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
17-379 |
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: 527.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 17 VGVGMTKFVKPGAENSRDYPDLAEEAG-------------------------------DSTCGQRAIYHSLGMTGIPIIN 65
Cdd:cd00826 1 AGAAMTAFGKFGGENGADANDLAHEAGakaiaaalepagvaagaveeaclgqvlgageGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 145
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 146 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 219
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 220 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 299
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 300 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 379
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
17-379 |
2.52e-137 |
|
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: 401.64 E-value: 2.52e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 17 VGVGMTKFVKPGaenSRDYPDLAEEAGD---------------------------STCGQRAIYHsLGMTGIPIINVNNN 69
Cdd:cd00829 1 VGVGMTPFGRRS---DRSPLELAAEAARaalddaglepadidavvvgnaaggrfqSFPGALIAEY-LGLLGKPATRVEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 70 CATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEK 149
Cdd:cd00829 77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 150 YGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVE 229
Cdd:cd00829 151 YGTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 230 ILAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDR 309
Cdd:cd00829 229 ILGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVRE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 310 GDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLY 379
Cdd:cd00829 306 GDTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
11-379 |
4.81e-87 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 273.31 E-value: 4.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAG-----DSTCGQRAI----------------YHS-------LGMTGIP 62
Cdd:PRK06064 1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGlealeDAGIDGKDIdamyvgnmsaglfvsqEHIaaliadyAGLAPIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 63 IINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAhpv 134
Cdd:PRK06064 78 ATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 135 aPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 214
Cdd:PRK06064 144 -PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 215 EAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 294
Cdd:PRK06064 223 EEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 295 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEA--GKRQVPGAKVALQHNL-GIG 371
Cdd:PRK06064 298 LGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAekGRQQVIGAGYGLTHNVgGTG 377
|
....*...
gi 302344760 372 GAVVVTLY 379
Cdd:PRK06064 378 HTAVVHIL 385
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
12-369 |
9.40e-66 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 217.79 E-value: 9.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEA-----GDSTCGQRAIYHSL---------------------GMTGIPIIN 65
Cdd:PRK12578 1 RRVAVIGVGNSKF---GRRDDVSVQELAWESikealNDAGVSQTDIELVVvgstayrgielypapivaeysGLTGKVPLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSahpvAPQMFGY 141
Cdd:PRK12578 78 VEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTT----FPTYYAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 142 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 221
Cdd:PRK12578 148 YATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 222 GLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEG 301
Cdd:PRK12578 228 KIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKG 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302344760 302 QGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAK-VALQHNLG 369
Cdd:PRK12578 304 KGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVG 372
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
10-377 |
1.81e-65 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 217.71 E-value: 1.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 10 TLRRVFVVGVGM-------TKFVKPG--------AENSRDYPDLAEEAGDST--CGQRAIYH------SLGMTGIPIINV 66
Cdd:PRK06059 2 MPEPVYILGAGMhpwgkwgRDFVEYGvvaaraalADAGLDWRDVQLVVGADTirNGYPGFVAgatfaqALGWNGAPVSSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 67 NNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVapqMFGYAGKEH 146
Cdd:PRK06059 82 YAACASGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV---YFALLARRR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 147 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQSK 226
Cdd:PRK06059 155 MDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRHLGSVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 227 -AVEILAQEMMT--------DLPSsFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEAL 295
Cdd:PRK06059 235 gVPSVRAISTVTprypqhlpELPD-IATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 296 GLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGI---GG 372
Cdd:PRK06059 314 GLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQGLfghGS 393
|
....*
gi 302344760 373 AVVVT 377
Cdd:PRK06059 394 SVIVA 398
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
62-374 |
1.99e-56 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 193.24 E-value: 1.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 62 PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQ 137
Cdd:PRK07516 77 PATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 138 MFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILA 213
Cdd:PRK07516 146 VFGRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 214 SEAFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 292
Cdd:PRK07516 226 DAETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEY 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 293 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGiGG 372
Cdd:PRK07516 298 EAMGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG-GA 376
|
..
gi 302344760 373 AV 374
Cdd:PRK07516 377 AV 378
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
12-369 |
1.81e-51 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 180.22 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGD------------------STC------GQRAIYHS--LGMTGIPIIN 65
Cdd:PRK06157 7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLealadagiepkdidaawfGTHydeigsGKSGTPLSraLRLPNIPVTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 144
Cdd:PRK06157 84 VENFCATGSEAFRGAVYAVASGAYDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 145 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 220
Cdd:PRK06157 154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 221 YG----LQSKAVEILA---QEMMTDL--PSSFEEKSIikmvgfdmskeAARKCYEKSGLT-P-NDIDVIELHDCFSTNEL 289
Cdd:PRK06157 234 LGkkdpVYVKALQLAVsngWELQYNGwdGSYFPTTRI-----------AARKAYREAGITdPrEELSMAEVHDCFSITEL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 290 LTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLG 369
Cdd:PRK06157 303 VTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHNLG 382
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
8-380 |
2.22e-49 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 175.87 E-value: 2.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEA---------------------------GDSTCGQRAIYHSLGMTG 60
Cdd:PRK06365 12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAfdyamndagltladidgsvasyfsdhfQRQLLAGIMVQDYLGLVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 134
Cdd:PRK06365 90 KPSKRIEGGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 135 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 211
Cdd:PRK06365 154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 212 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 271
Cdd:PRK06365 234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 272 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLR 349
Cdd:PRK06365 310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQ 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 302344760 350 GEAGKR------QVPGAKVALQH-NLGIGGAVVVTLYK 380
Cdd:PRK06365 390 GRIKKHfhddylQVKNAKRGLIHsHAGTGTYVTVTILE 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
45-377 |
2.32e-45 |
|
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: 159.92 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 45 STCGQRAIYHsLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKmskgslgikfsdrtiptdkhvdlli 124
Cdd:cd00327 44 SGAAGQLAYH-LGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 125 nkyglsahpvapqmfgyagkehmekygtkiehfakigwknhkhsvnnpysqfqdeysldevmaskevfdfltilqcCPTS 204
Cdd:cd00327 98 ----------------------------------------------------------------------------FVFG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 205 DGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 284
Cdd:cd00327 102 DGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTG 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 285 STNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGK--RQVPGAKV 362
Cdd:cd00327 175 TPIGDAVELALGLDPDGVRS---------------PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptPREPRTVL 239
|
330
....*....|....*
gi 302344760 363 ALQHNLGIGGAVVVT 377
Cdd:cd00327 240 LLGFGLGGTNAAVVL 254
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
55-382 |
1.40e-39 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 147.95 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 55 SLGMTGIPIINVNNNCATG-STALfMARQLIQGGVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHP 133
Cdd:PRK08313 71 ALGATGKPLIRVHTAGSVGgSTAV-VAASLVQSGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 134 VApqmfgyagkEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAIL 212
Cdd:PRK08313 147 VR---------AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 213 ASEAFVQKYGLQSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELL 290
Cdd:PRK08313 218 GDEEAADAAAGRPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 291 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGi 370
Cdd:PRK08313 293 WLENLGFAPEGEGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG- 370
|
330
....*....|..
gi 302344760 371 GGAVVVTLYKMG 382
Cdd:PRK08313 371 GGSQFFSMWVVG 382
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
70-377 |
1.73e-37 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 142.52 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 70 CATGSTALFMARQLIQGGVAECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQMFGYAGK 144
Cdd:PRK06289 90 CASGSVATLAAMADLRAGRYDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMFARVAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 145 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQ 219
Cdd:PRK06289 159 EYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLASDAYLR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 220 KYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEAL 295
Cdd:PRK06289 239 DYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 296 GLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALqhNLGIGGAVV 375
Cdd:PRK06289 317 GLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGAKTFG--TLNIGGSTT 394
|
..
gi 302344760 376 VT 377
Cdd:PRK06289 395 TT 396
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
133-372 |
2.90e-34 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 133.23 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 133 PVAPqMFGYA--GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAA 210
Cdd:PRK06158 137 PVNP-VSAYAlaAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 211 ILASEAFVQkyGLQSKAVEILAQEMMTDlpssfeEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDIDVIELHDCFST 286
Cdd:PRK06158 216 VMVRADRAR--DLPRPPVYVLGAAAATW------HRQISSMP--DLTVTAAaesgPRAFAMAGLTPADIDVVELYDAFTI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 287 NELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPlGATGLAQCAELCWQLRGEAGKRQVPGAKVALQH 366
Cdd:PRK06158 286 NTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH 364
|
....*.
gi 302344760 367 nlGIGG 372
Cdd:PRK06158 365 --GNGG 368
|
|
| SCP2 |
pfam02036 |
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ... |
428-514 |
2.48e-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: 119.28 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 428 VKKIGG-IFAFKVKDGPGgkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMG 506
Cdd:pfam02036 15 LKKLNGkVIRFDLTDLGL----SLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFMQGKLKIEGDME 90
|
....*...
gi 302344760 507 LAMKLQNL 514
Cdd:pfam02036 91 LAQKLEGL 98
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
12-358 |
3.58e-29 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 118.77 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 12 RRVFVVGVGMTKFVKPGAENSRDYPDLA-----EEAG----DSTC-------------GQRAIYHSLGMTGI--PIINVN 67
Cdd:PRK06065 9 KRVAVIGAGLTLFRRRLLETPQELAWEAaskalDEAGlelkDIDCvvigsapdafdgvHMKGEYLSHGSGGIrkPVSRVY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 68 NNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM---FGYAGK 144
Cdd:PRK06065 89 VGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiwiFAMEMH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 145 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglq 224
Cdd:PRK06065 158 RYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 225 skaveilaqemmTDLPSsfeeksIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIELHDCFSTN 287
Cdd:PRK06065 235 ------------TDTPV------WVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPFDYK 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302344760 288 ELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVP 358
Cdd:PRK06065 297 ELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
147-376 |
2.63e-28 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 116.39 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 147 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 226
Cdd:PRK06066 154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 227 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 304
Cdd:PRK06066 232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302344760 305 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQvPGAKVALQHNL-GI---GGAVVV 376
Cdd:PRK06066 308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVASWrGIptlTGSVVV 382
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
10-372 |
1.17e-27 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 115.38 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 10 TLRRVFVVGVGMTKFVKPGAEN--SRDYPDLAEEAGDS--TCGQRAIYHSLGMTGI------------------------ 61
Cdd:PTZ00455 10 AAKRVFVVGGHITPFVGKGSPLfiDKKHPDFGKKENKTleELLATAIQGTLENTGLdgkaalvdkvvvgnflgelfssqg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 62 ----------------------PIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKH 119
Cdd:PTZ00455 90 hlgpaavgslgqsgasnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 120 VDLLINKYGLsahpvaPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MAS 188
Cdd:PTZ00455 170 RQRKLDDFTF------PCLFAKRMKYIQEHGHFTMEDTARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 189 KEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKC 264
Cdd:PTZ00455 244 ETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 265 YEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAEL 344
Cdd:PTZ00455 319 LSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEV 398
|
410 420
....*....|....*....|....*...
gi 302344760 345 CWQLRGEAGKRQVPGAkVALQHNLGIGG 372
Cdd:PTZ00455 399 YRQMKGQCGEYQMKNI-PALGATLNMGG 425
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
132-373 |
3.67e-25 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 107.10 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 132 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 211
Cdd:PRK08142 139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 212 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 275
Cdd:PRK08142 214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 276 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAG- 353
Cdd:PRK08142 276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHp 355
|
250 260
....*....|....*....|
gi 302344760 354 KRQVPGAKVALQHnlGIGGA 373
Cdd:PRK08142 356 AVQVPNCDLALAH--GTGGL 373
|
|
| SCP2 |
COG3255 |
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism]; |
429-514 |
7.31e-25 |
|
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
Pssm-ID: 442486 [Multi-domain] Cd Length: 104 Bit Score: 98.83 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 429 KKIGGIFAFKVKDGPGGkeaTWVVDVKNGKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLA 508
Cdd:COG3255 18 AGWDGVVQFVITGEGGG---AYYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLA 94
|
....*.
gi 302344760 509 MKLQNL 514
Cdd:COG3255 95 MKLMSL 100
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
70-360 |
1.63e-20 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 93.50 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 70 CATGSTALfMArqlIQGGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqMFGy 141
Cdd:PRK07855 85 CATVQQAA-MA---VATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--MLA- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 142 agKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 220
Cdd:PRK07855 155 --RRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 221 ygLQSKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFSTNE 288
Cdd:PRK07855 233 --LKQRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFV 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302344760 289 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLRGEAgKRQVPGA 360
Cdd:PRK07855 300 LMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLRGTS-VNQVPGV 367
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
61-376 |
4.44e-17 |
|
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: 82.91 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFG 140
Cdd:cd00751 75 VPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 141 YAgkEHM-EKYG--------------------TKIEHFA------KIGWKNHKHSVNnpysqfQDEY-----SLdEVMAS 188
Cdd:cd00751 155 TA--ENVaEKYGisreeqdefalrshqraaaaQEAGRFKdeivpvEVPGRKGPVVVD------RDEGprpdtTL-EKLAK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 189 -KEVFD---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeILAQ-------EMMTDLPSsfeeksiikmvgfdms 257
Cdd:cd00751 226 lKPAFKkdgTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLAR-IVGYavagvdpAIMGIGPV---------------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 258 kEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 337
Cdd:cd00751 289 -PAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASG 349
|
330 340 350
....*....|....*....|....*....|....*....
gi 302344760 338 LAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 376
Cdd:cd00751 350 ARIVVTLLHELKRRGGRYGL----ATMCIGGGQGAAMVI 384
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
61-376 |
1.07e-15 |
|
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: 78.81 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFG 140
Cdd:TIGR01930 74 VPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 141 YAGKEHMEKYGTKIE---HFA----KIGWKNHK-------------HSVNNPYSQFQDE-----YSLdEVMAS-KEVFD- 193
Cdd:TIGR01930 154 VTAENLAKKYGISREeqdEYAlrshQRAAKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTL-EKLAKlKPAFDp 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 194 --FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVEILAQEMMTDlPSSFeeksiikmvGFdMSKEAARKCYEKSGLT 271
Cdd:TIGR01930 233 dgTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVD-PEIM---------GL-GPVPAIPKALKKAGLS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 272 PNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGE 351
Cdd:TIGR01930 302 ISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRR 363
|
330 340
....*....|....*....|....*
gi 302344760 352 AGKRQVpgakVALQHNLGIGGAVVV 376
Cdd:TIGR01930 364 GGRYGL----ATMCIGGGQGAAVIL 384
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
61-376 |
2.14e-12 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 68.60 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 132
Cdd:PRK06445 86 IPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 133 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 193
Cdd:PRK06445 161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 194 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 263
Cdd:PRK06445 241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 264 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLAQCAE 343
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVGT 362
|
330 340 350
....*....|....*....|....*....|...
gi 302344760 344 LCWQLRGEAGKRQVPGAKVAlqhnLGIGGAVVV 376
Cdd:PRK06445 363 LARQLQIKGKDYGVATLCVG----GGQGGAVVL 391
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
260-376 |
1.41e-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: 61.50 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLA 339
Cdd:pfam02803 27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGAR 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 302344760 340 QCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 376
Cdd:pfam02803 89 ILVTLLHELKRRGGKYGL----ASLCIGGGQGVAMII 121
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
58-376 |
1.91e-09 |
|
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: 59.69 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 58 MTGIPI----INVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS-------KGSLGIKFSDRTiptdkhVDLLINK 126
Cdd:COG0183 72 LAGLPEsvpaVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSrapmllpKARWGYRMNAKL------VDPMINP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 127 yGLSAHPVAPQMFGYAgkEHM-EKYG-TKIEhfakigwknhkhsvnnpysqfQDEYSL----------------DEVM-- 186
Cdd:COG0183 146 -GLTDPYTGLSMGETA--ENVaERYGiSREE---------------------QDAFALrshqraaaaiaagrfdDEIVpv 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 187 --------------------ASKE-------VFD---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ--- 233
Cdd:COG0183 202 evpdrkgevvvdrdegprpdTTLEklaklkpAFKkdgTVTAGNASGINDGAAALLLMSEEAAKELGLKPLA-RIVAYava 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 234 ----EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdr 309
Cdd:COG0183 281 gvdpEIMGIGPV-----------------PATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPD--------- 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302344760 310 gdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 376
Cdd:COG0183 335 ---------KVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGL----ATMCIGGGQGIALII 388
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
59-354 |
4.88e-09 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 58.48 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 59 TGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLG---IKFSDRTIPTDKHVDLlinKYG--LSAHP 133
Cdd:PRK09052 84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgnkPSMSPAIFARDENVGI---AYGmgLTAEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 134 VAPQ---------MFGYAG-------------KEHMEKYgTKIEHFAKIGW---KNHKHSVNnpysqfQDE-----YSLD 183
Cdd:PRK09052 161 VAEQwkvsredqdAFALEShqkaiaaqqagefKDEITPY-EITERFPDLATgevDVKTRTVD------LDEgpradTSLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 184 EVMASKEVFDF---LTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPssfeeksiikmvgf 254
Cdd:PRK09052 234 GLAKLKPVFANkgsVTAGNSSQTSDGAGAVILVSEKALKQFNLTplarfvSFAVAGVPPEIMGIGP-------------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 255 dmsKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLG 334
Cdd:PRK09052 300 ---IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLG 358
|
330 340
....*....|....*....|
gi 302344760 335 ATGLAQCAELCWQLRGEAGK 354
Cdd:PRK09052 359 ATGAIRTATVVHGLRRTNLK 378
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
14-179 |
7.99e-09 |
|
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: 56.54 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAG---------------DSTCGQ-----------RAIYHSLGMT-GIPIIN 65
Cdd:pfam00108 1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIkaaleragvdpedvdEVIVGNvlqagegqnpaRQAALKAGIPdSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGYA 142
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLT 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 302344760 143 GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 179
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
260-337 |
8.25e-09 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 57.59 E-value: 8.25e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 337
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
260-355 |
1.33e-08 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 56.89 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG-- 337
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSGar 365
|
90
....*....|....*...
gi 302344760 338 LAQCAELcwQLRGEAGKR 355
Cdd:PRK09050 366 LVLTALH--QLERTGGRY 381
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
61-337 |
1.62e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 56.64 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSK--------------------GSLG--IKFSDRTIPTDK 118
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipissamtageqlgftspfaESKGwlHRYGDQEVSQFR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 119 HVDLLINKYGLSahpvapqmfgyagKEHMEKYGTKIEHFAKIGWKN-HKHSVNNPYSQF-QDEYSLD---EVMASKEVFD 193
Cdd:PRK07801 160 GAELIAEKWGIS-------------REEMERFALESHRRAFAAIRAgRFDNEIVPVGGVtVDEGPREtslEKMAGLKPLV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 194 ---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPssfeeksiIKMVGFDMSkeAARKCYEKSGL 270
Cdd:PRK07801 227 eggRLTAAVASQISDGASAVLLASERAVKRHGLTPRA-RIHHLSVRGDDP--------VFMLTAPIP--ATRYALEKTGL 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302344760 271 TPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 337
Cdd:PRK07801 296 SIDDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATG 344
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
66-337 |
2.22e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 56.26 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS-------KGSLGIKFSDRTIptdkhVDLLINKyGLSAHPVAPQM 138
Cdd:PRK08235 84 VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSnapyilpGARWGYRMGDNEV-----IDLMVAD-GLTCAFSGVHM 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 139 fGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYS-QFQDEY-------------------------SLDEVMASKEVF 192
Cdd:PRK08235 158 -GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEgRFEEEIvpvtipqrkgdpivvakdeaprkdtTIEKLAKLKPVF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 193 D---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeILAQEMMTDLPSSFEeksiiKMVGFdmskeAARKCYEKSG 269
Cdd:PRK08235 237 DktgTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLAT-ILAHTAIAVEAKDFP-----RTPGY-----AINALLEKTG 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 270 LTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 337
Cdd:PRK08235 306 KTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
257-368 |
5.23e-08 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 54.70 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 257 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 336
Cdd:PRK07937 252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310
|
90 100 110
....*....|....*....|....*....|....*
gi 302344760 337 GLAQCAELCWQ-LRGEAGkRQVPGAKV--ALQHNL 368
Cdd:PRK07937 311 GLERIGEAARHiWDGSAR-RALAHATSgpALQQNL 344
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
260-337 |
1.96e-07 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 53.42 E-value: 1.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 337
Cdd:PRK09051 297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
|
|
| Alkyl_sulf_C |
pfam14864 |
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ... |
447-504 |
5.74e-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: 48.34 E-value: 5.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302344760 447 EATWVVDVKNGkgsVL----PNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGN 504
Cdd:pfam14864 43 DEQYRLTLSNG---VLtyrkGRQADDADATLTLTRADLLALLLGKATLGKLIAAGKIKVEGD 101
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
266-341 |
1.38e-06 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 50.92 E-value: 1.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302344760 266 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGlAQC 341
Cdd:PLN02287 342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
22-376 |
2.44e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 49.64 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 22 TKFVKPGAENSRDYPDLAEE-------AGDStcGQRAIYHSLGMTGIPI----INVNNNCATGSTALFMARQLIQGGVAE 90
Cdd:PRK06633 32 AHLIKDILQNSKIDPALVNEvilgqviTGGS--GQNPARQTLIHAGIPKevpgYTINKVCGSGLKSVALAANSIMTGDNE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 91 CVLALGFEKMSKG------SLGIKFSDRTIPTDKHVDLLINKY-----GLSAHPVAPQmFGYAGKEHMEkygtkiehFAk 159
Cdd:PRK06633 110 IVIAGGQENMSLGmhgsyiRAGAKFGDIKMVDLMQYDGLTDVFsgvfmGITAENISKQ-FNISRQEQDE--------FA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 160 igWKNHKHSVNNPYSQ-FQDEYSLDEVMASK--EVFDF---------LTIL-QCCPTSDGAAAAILASEAFVQKYG--LQ 224
Cdd:PRK06633 180 --LSSHKKAAKAQLAGiFKDEILPIEVTIKKttSLFDHdetvrpdtsLEILsKLRPAFDKNGVVTAGNASSINDGAacLM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 225 SKAVEILAQEMMTDLPS--SFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcpegq 302
Cdd:PRK06633 258 VVSEEALKKHNLTPLARivSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM------- 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302344760 303 gatlvdrgdntyggKW---VINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVpgakVALQHNLGIGGAVVV 376
Cdd:PRK06633 331 --------------KWdmeKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGL----VTLCIGGGMGMAMCV 389
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
205-337 |
2.64e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 49.77 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 205 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 284
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 302344760 285 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG 337
Cdd:PRK06025 345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
|
|
| BDS1 |
COG2015 |
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
448-514 |
2.78e-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: 49.84 E-value: 2.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302344760 448 ATWVVDVKNGkgsVLPN----SDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNL 514
Cdd:COG2015 551 EKYLLELRNG---VLTYrkgpQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGDAAALARLLGL 618
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
259-376 |
2.97e-06 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 49.39 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 259 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATGl 338
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG- 362
|
90 100 110
....*....|....*....|....*....|....*...
gi 302344760 339 aqcAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVV 376
Cdd:PRK08131 363 ---ARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVI 397
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
260-337 |
5.18e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 48.83 E-value: 5.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302344760 260 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATG 337
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATG 365
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
43-378 |
7.55e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 48.08 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 43 GDSTCGQrAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGIKFSDRTIPtdKHvdL 122
Cdd:PRK06366 62 GQNPAGQ-AAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGP--KH--L 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 123 LINKYGLSAHPVAPQMFGYAGKEHM--------EKYGTKIEHFAKIGWKNHKHSVNNPYS-QFQDEYSLDEVMASKE--- 190
Cdd:PRK06366 137 LHKNYKIDDAMLVDGLIDAFYFEHMgvsaertaRKYGITREMADEYSVQSYERAIRATESgEFRNEIVPFNDLDRDEgir 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 191 ------------VFD---FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSSFEEKSIikmvgfd 255
Cdd:PRK06366 217 kttmedlaklppAFDkngILTAGNSAQLSDGGSALVMASEKAINEYGLKPIA-RITGYESASLDPLDFVEAPI------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 256 mskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrgDNTYggkwvINPSGGLISKGHPLGA 335
Cdd:PRK06366 289 ---PATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKI-------------DNER-----FNVNGGAVAIGHPIGN 347
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 302344760 336 TGlaqcAELCWQLRGEAGKRQVPGAKVALQHnlGIGGAVVVTL 378
Cdd:PRK06366 348 SG----SRIIVTLINALKTRHMKTGLATLCH--GGGGAHTLTL 384
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
181-337 |
7.70e-06 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 48.08 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 181 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 251
Cdd:PRK07851 237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 252 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 331
Cdd:PRK07851 307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
|
....*.
gi 302344760 332 PLGATG 337
Cdd:PRK07851 362 PFGMTG 367
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
260-337 |
9.55e-06 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 47.84 E-value: 9.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 337
Cdd:PRK05790 296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
54-113 |
1.21e-05 |
|
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: 47.41 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 54 HSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslGIKFSDRT 113
Cdd:COG0332 96 HKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQAKNVLVVGAETLSR---IVDWTDRS 152
|
|
| UbiJ |
COG3165 |
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism]; ... |
461-514 |
2.43e-05 |
|
Ubiquinone biosynthesis protein UbiJ, contains SCP2 domain [Coenzyme transport and metabolism];
Pssm-ID: 442398 Cd Length: 204 Bit Score: 45.23 E-value: 2.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 302344760 461 VLPNSDKKADCTITMADSDFLALMTGKmNPQSAFFQGKLKITGNMGLAMKLQNL 514
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- ... |
66-113 |
4.43e-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: 41.73 E-value: 4.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslGIKFSDRT 113
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSK---ILDWTDRS 47
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
260-337 |
6.68e-05 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 45.34 E-value: 6.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 337
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
259-358 |
6.89e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 45.27 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 259 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGL 338
Cdd:PRK06954 299 GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEK------------------VNVNGGACALGHPIGASGA 360
|
90 100
....*....|....*....|
gi 302344760 339 AQCAELCWQLRGEAGKRQVP 358
Cdd:PRK06954 361 RILVTLIGALRARGGKRGVA 380
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
61-337 |
1.18e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 44.36 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKgslgikfsdrtIPTDKHVdllinkygLSAHPV----AP 136
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSL-----------VPMMGHV--------VRPNPRlveaAP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 137 QMF---GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE-----------------------YSLDEVMASK 189
Cdd:PRK07661 142 EYYmgmGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGkFADEivpvdvtlrtvgennklqeetitFSQDEGVRAD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 190 EVFDFLTILQ-------------CCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiik 250
Cdd:PRK07661 222 TTLEILGKLRpafnvkgsvtagnSSQMSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI--------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 251 mvgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKG 330
Cdd:PRK07661 293 --------AAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALG 346
|
....*..
gi 302344760 331 HPLGATG 337
Cdd:PRK07661 347 HPLGCTG 353
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
61-355 |
1.76e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 43.95 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 61 IPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFEKMSKGSLGikfSDRTIPTdkhvdllinKYGLsAHPVAPQM-- 138
Cdd:PRK06504 80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMG---SPSTLPA---------KNGL-GHYKSPGMee 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 139 ------FG-YAGKEHM-EKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE---------------YSLDE---------- 184
Cdd:PRK06504 147 rypgiqFSqFTGAEMMaKKYGLSKDQLDEFALQSHQRAIAATQAGkFKAEivpleitradgsgemHTVDEgirfdatleg 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 185 -----VMASKEVFDFLTILQCCptsDGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSSFEEKSIikmvgfdmskE 259
Cdd:PRK06504 227 iagvkLIAEGGRLTAATASQIC---DGASGVMVVNERGLKALGVKPLA-RIHHMTVIGGDPVIMLEAPL----------P 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLA 339
Cdd:PRK06504 293 ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTK 354
|
330
....*....|....*.
gi 302344760 340 QCAELCWQLRgEAGKR 355
Cdd:PRK06504 355 LMTTLVHALK-QRGKR 369
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
260-337 |
3.25e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 42.95 E-value: 3.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 337
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAA------------------KVNVNGGAIALGHPIGASG 355
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
260-359 |
2.68e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 40.08 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302344760 260 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLA 339
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSGAR 357
|
90 100
....*....|....*....|
gi 302344760 340 QCAELCWQLRGEAGKRQVPG 359
Cdd:PLN02644 358 ILVTLLGVLRSKNGKYGVAG 377
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
66-101 |
3.60e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 39.69 E-value: 3.60e-03
10 20 30
....*....|....*....|....*....|....*.
gi 302344760 66 VNNNCATGSTALFMARQLIQGGVAECVLALGFEKMS 101
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMS 118
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
44-98 |
4.62e-03 |
|
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: 39.44 E-value: 4.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 302344760 44 DSTCGQRAIYhsLGMTGiPIINVNNNCATGSTALFMARQLIQGGVAECVLALGFE 98
Cdd:cd00834 138 NMAAGQVAIR--LGLRG-PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
255-278 |
6.46e-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: 6.46e-03
10 20
....*....|....*....|....
gi 302344760 255 DMSKEAARKCYEKSGLTPNDIDVI 278
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLI 75
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
54-96 |
7.58e-03 |
|
"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: 38.57 E-value: 7.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 302344760 54 HSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALG 96
Cdd:cd00827 93 ELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVA 135
|
|
| |
