|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
6-397 |
0e+00 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 727.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 6 NRVFVIGVGMTKFEKPGARDiDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTCGQRAIYHsLGLSGIPIINVNN 85
Cdd:PRK08256 1 NKVFVAGVGMTPFEKPGASW-DYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDSTSGQRALYE-VGMTGIPIVNVNN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 86 NCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSLSSKYMDRTNPMDKHMEVMINRYGLAAVPAAPQMFGNAGREHME 165
Cdd:PRK08256 79 NCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 166 KYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVRRNGLEKkAV 245
Cdd:PRK08256 159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGLDR-AV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 246 EIVAQEMVTDLSTTFEENSCMKMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCPEGKAGELID 325
Cdd:PRK08256 238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053664 326 RGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNIGLGGAVVVTLYK 397
Cdd:PRK08256 318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGLAQCAELTWQLRGTAGARQVEGARLALQHNLGLGGACVVTLYQ 389
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
11-396 |
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: 522.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 11 IGVGMTKFEKPGARD-IDYPDMAKEAGQRALADAGIKYS----AIQQACVGYVYGD---STCGQRAIYHSLGLSGIPIIN 82
Cdd:cd00826 1 AGAAMTAFGKFGGENgADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLGAgegQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 83 VNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMErgslsskYMDRTNPMDKHMEVMINRYGLAAVPAAPQMFGNAGRE 162
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 163 HMEKYGTKPEHFAKVAWKN---HKHSTNNPYSQFQDEYSLEQVIDSRKVFE---FLTLLQCCPTSDGAGAAVLASESFVR 236
Cdd:cd00826 154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 237 RNGLEKKAVEIVAQEMVTDLSTTFEENSCMKMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCP 316
Cdd:cd00826 234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 317 EGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNIGLGGAVVVTLY 396
Cdd:cd00826 314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQGAGAGLALLCIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
11-396 |
8.26e-167 |
|
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: 477.53 E-value: 8.26e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 11 IGVGMTKFEKPgaRDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGD---STCGQRAIYHsLGLSGIPIINVNNNC 87
Cdd:cd00829 1 VGVGMTPFGRR--SDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGrfqSFPGALIAEY-LGLLGKPATRVEAAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 88 STGSTALFMGRQLIQGGLADCVLALGFEKMERGSLSSKYMDRTNPMDKHMEVMINryglaaVPAAPQMFGNAGREHMEKY 167
Cdd:cd00829 78 ASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPG------GLTPPALYALAARRYMHRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 168 GTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVRRngLEKKAVEI 247
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARE--LTDRPVWI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 248 VAQEMVTDLSTTFEENScmkMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCPEGKAGELIDRG 327
Cdd:cd00829 230 LGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053664 328 DNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNIGLGGAVVVTLY 396
Cdd:cd00829 307 DTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
6-396 |
1.88e-98 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 303.36 E-value: 1.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 6 NRVFVIGVGMTKFekpGAR-DIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTCGQRAI------YhsLGLSGI 78
Cdd:PRK06064 2 RDVAIIGVGQTKF---GELwDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFVSQEHIaaliadY--AGLAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 79 PIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMER--GSLSSKYMDRTNpmDKHMEVMinrYGLAAvpaaPQMF 156
Cdd:PRK06064 77 PATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDvpTPDATEAIARAG--DYEWEEF---FGATF----PGLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 157 GNAGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVR 236
Cdd:PRK06064 148 ALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILASEEKAK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 237 RngLEKKAVEIVAQEMVTDlstTFEENSCMKMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCP 316
Cdd:PRK06064 228 E--YTDTPVWIKASGQASD---TIALHDRKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 317 EGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLR--AEAGPRQVPGAKLALQHNI-GLGGAVVV 393
Cdd:PRK06064 303 KGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRgeAEKGRQQVIGAGYGLTHNVgGTGHTAVV 382
|
...
gi 41053664 394 TLY 396
Cdd:PRK06064 383 HIL 385
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
7-386 |
1.51e-78 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 251.69 E-value: 1.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 7 RVFVIGVGMTKFekpGARD-IDYPDMAKEAGQRALADAGIKYSAIQQACVGyvygdsTCGQRA--------IYHSLGLSG 77
Cdd:PRK12578 2 RVAVIGVGNSKF---GRRDdVSVQELAWESIKEALNDAGVSQTDIELVVVG------STAYRGielypapiVAEYSGLTG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 78 IPIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMER---------GSLSSKYMdrtnpMDKHMevminrYGlAA 148
Cdd:PRK12578 73 KVPLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEvdtstslaiGGRGGNYQ-----WEYHF------YG-TT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 149 VPAAPQMFGNAgreHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAV 228
Cdd:PRK12578 141 FPTYYALYATR---HMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 229 LASESFVRRNGLEKkAVEIVAQEMVTDLSTTFEENScmkMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELIT 308
Cdd:PRK12578 218 FASEEKVKELKIDS-PVWITGIGYANDYAYVARRGE---WVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMG 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053664 309 YEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAK-LALQHNIG 386
Cdd:PRK12578 294 YEDLGFTEKGKGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKLQQPLKKyIGLVHNVG 372
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
8-394 |
3.91e-72 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 235.43 E-value: 3.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 8 VFVIGVGMTKFEKPGARDIDYPDMAKEAgqrALADAGIKYSAIQ---------QACVGYVYGdSTCGQraiyhSLGLSGI 78
Cdd:PRK06059 6 VYILGAGMHPWGKWGRDFVEYGVVAARA---ALADAGLDWRDVQlvvgadtirNGYPGFVAG-ATFAQ-----ALGWNGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 79 PIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSLSSKYMDRTNPMDkhmevmINRYGLAAVpAAPQMFGN 158
Cdd:PRK06059 77 PVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKGFFAPVGGERPDDPD------WLRFHLIGA-TNPVYFAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 159 AGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVRRN 238
Cdd:PRK06059 150 LARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 239 GLEKK-AVEIVAQEMVTdlsTTFEENSC-MKMVGYDMTRL--AAER---------CYDTAGVKPSDVDVIELHDCFSANE 305
Cdd:PRK06059 230 LGSVAgVPSVRAISTVT---PRYPQHLPeLPDIATDSTAAvpAPERvfkdqildaAYAEAGIGPEDLSLAEVYDLSTALE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 306 LITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNI 385
Cdd:PRK06059 307 LDWYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCELTWQLRGQAGGRQVEGARVGITANQ 386
|
410
....*....|..
gi 41053664 386 GL---GGAVVVT 394
Cdd:PRK06059 387 GLfghGSSVIVA 398
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
1-413 |
2.05e-67 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 222.98 E-value: 2.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 1 MAA-LRNRVFVIGVGMTKFekpGAR-DIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTCGQRAIYHS--LGLS 76
Cdd:PRK06157 1 MATgIKDKVAILGMGCTKF---GERwDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPLSraLRLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 77 GIPIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEK-MERGSLSSKYMDRTNPMDkhmevMINRYGlaavpAAPQM 155
Cdd:PRK06157 78 NIPVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKlKDTGYGGLPVANPGTLAD-----MTMPNV-----TAPGN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 156 FGNAGREHMEKYGTKPEHF----AKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLAS 231
Cdd:PRK06157 148 FAQLASAYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 232 ESFVRRNGlEKKAVEIVAQEMVTdlSTTFEenscMKMVGYD-----MTRLAAERCYDTAGVK-P-SDVDVIELHDCFSAN 304
Cdd:PRK06157 228 PEIARALG-KKDPVYVKALQLAV--SNGWE----LQYNGWDgsyfpTTRIAARKAYREAGITdPrEELSMAEVHDCFSIT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 305 ELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHN 384
Cdd:PRK06157 301 ELVTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGERQLKNPRLALTHN 380
|
410 420
....*....|....*....|....*....
gi 41053664 385 IGlggavvvtlykmGFPQETSSRIAAVST 413
Cdd:PRK06157 381 LG------------GAPGQNVCSVSIVGR 397
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
6-391 |
3.33e-61 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 206.34 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 6 NRVFVIGVGMTKFEKPGARDIDypDMAKEAGQRALADAGIKYSAIQQACVGYVYG----DSTCGQRAIYHSLGLSGIPII 81
Cdd:PRK07516 2 MTASIVGWAHTPFGKLDAETLE--SLIVRVAREALAHAGIAAGDVDGIFLGHFNAgfspQDFPASLVLQADPALRFKPAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 82 NVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERgslsskymdrtNPMDKHMEVMIN---RYGLAAVPAA-PQMFG 157
Cdd:PRK07516 80 RVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTA-----------TPTAEVGDILLGasyLKEEGDTPGGfAGVFG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 158 NAGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLE---QVIDSRK-VFEFLTLLQCCPTSDGAGAAVLASES 233
Cdd:PRK07516 149 RIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEfcrTVSEKNPlVAGPLRRTDCSLVSDGAAALVLADAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 234 FVRRnglEKKAVEIVAQEMVTDlsttFEENSCMKMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALG 313
Cdd:PRK07516 229 TARA---LQRAVRFRARAHVND----FLPLSRRDPLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEAMG 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 314 LCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNIGlGGAV 391
Cdd:PRK07516 302 LAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGVSMHVLAAMQLTGEAGGMQIPGAKLAGVFNMG-GAAV 378
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
11-394 |
1.12e-55 |
|
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: 187.65 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 11 IGVGMTkfekpgardidYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGD---STCGQRAIYHsLGLSGIPIINVNNNC 87
Cdd:cd00327 1 TGLGIT-----------ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSgefSGAAGQLAYH-LGISGGPAYSVNQAC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 88 STGSTALFMGRQLIQGGLADCVLALGFEKmergslsskymdrtnpmdkhmevminryglaavpaapqmfgnagrehmeky 167
Cdd:cd00327 69 ATGLTALALAVQQVQNGKADIVLAGGSEE--------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 168 gtkpehfakvawknhkhstnnpysqfqdeysleqvidsrkvfefltllqcCPTSDGAGAAVLASESFVRRNGlekkaveI 247
Cdd:cd00327 98 --------------------------------------------------FVFGDGAAAAVVESEEHALRRG-------A 120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 248 VAQEMVTDLSTTFEENSCMKMVGYDMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCPEGKAGelidrg 327
Cdd:cd00327 121 HPQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRS------ 194
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053664 328 dntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGP--RQVPGAKLALQHNIGLGGAVVVT 394
Cdd:cd00327 195 ---------PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
8-397 |
1.30e-53 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 187.42 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 8 VFVIGVGMTKFEKpGARDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYV---YGDSTCGQRAIYHSLGLSGIPIINVN 84
Cdd:PRK06365 18 VYMVAAGVTKFDK-ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYFsdhFQRQLLAGIMVQDYLGLVPKPSKRIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 85 NNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSlsskyMDRTNPM-----DKHMEVMINRY--GLAAVPAApqmfg 157
Cdd:PRK06365 97 GGGATGGLAFQAGYEEIASGRMDCVAVYGFETMSHVN-----TWKGNEFialasDTNFDYPLGGFytGYYAMMAV----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 158 nagrEHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASEsfvrr 237
Cdd:PRK06365 167 ----RHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAILASE----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 238 ngleKKAVEI----VAQEMVTDLSTTF---------------EENSCMK------MVGYDMTRLAAERCYDTAGVK-PS- 290
Cdd:PRK06365 238 ----DKAFEItdkpVLIKAIGTGSDTLrladrpfgevpllpnESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGITdPLn 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 291 DVDVIELHDCFSANELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAG 370
Cdd:PRK06365 314 DLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGIMQAVFMFWQLQGRIK 393
|
410 420 430
....*....|....*....|....*....|....
gi 41053664 371 PR------QVPGAKLALQH-NIGLGGAVVVTLYK 397
Cdd:PRK06365 394 KHfhddylQVKNAKRGLIHsHAGTGTYVTVTILE 427
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
8-395 |
1.01e-48 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 173.34 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 8 VFVIGVGMTKFEKPGARD-IDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTCGQR------AIYHSlGLSGIPI 80
Cdd:PRK06289 5 VWVLGGYQSDFARNWTKEgRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGELFAGQGhlgampATVHP-ALWGVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 81 INVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMergslsskymdRTNPMDKHMEVM-----INRYGLAAVPAAPQM 155
Cdd:PRK06289 84 SRHEAACASGSVATLAAMADLRAGRYDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 156 FGNAGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQ----------FQDEYSLEQVIDSRkvfefLTLLQCCPTSDGAG 225
Cdd:PRK06289 153 FARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwafpdeaTNDDDATNPVVEGR-----LRRQDCSQVTDGGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 226 AAVLASESFVRRN-------------------GLEKKAVEIVAQEMVtdlsttfeenscmkmvgYDMTRLAAERCYDTAG 286
Cdd:PRK06289 228 GVVLASDAYLRDYadarpiprikgwghrtaplGLEQKLDRSAGDPYV-----------------LPHVRQAVLDAYRRAG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 287 VKPSDVDVIELHDCFSANELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLR 366
Cdd:PRK06289 291 VGLDDLDGFEVHDCFTPSEYLAIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKQVT 370
|
410 420
....*....|....*....|....*....
gi 41053664 367 AEAGPRQVPGAKLALQHNIGLGGAVVVTL 395
Cdd:PRK06289 371 GTAGDYQVEGAKTFGTLNIGGSTTTTVSF 399
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
5-399 |
1.53e-46 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 167.21 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 5 RNRVFVIGVGMTKFEkpGAR-DIDYPDMAKEAGQRALADAGIKYSAIQQACVGY---VYGDSTCGQRAIYHSLGLSGIPI 80
Cdd:PRK08313 2 KRLAAVLGTGQTKYV--AKRqDVSMAGLVREAIDRALADAGLTWDDIDAVVVGKapdFFEGVMMPELFLADALGATGKPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 81 INVNNNCSTG-STALfMGRQLIQGGLADCVLALGFEKMERGslsskymdrtNPMdkhmevminrYGLAA-VPAAPQMFGN 158
Cdd:PRK08313 80 IRVHTAGSVGgSTAV-VAASLVQSGVYRRVLAVAWEKQSES----------NAM----------WALSIpVPFTKPVGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 159 AG-------REHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQF-QDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLA 230
Cdd:PRK08313 139 AGgyfaphvRAYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 231 SESFVRRNGlEKKAVEIVAQEMVTDLSTTFEENSCMKMVGydmtRLAAERCYDTAGVK-PSD-VDVIELHDCFSANELIT 308
Cdd:PRK08313 219 DEEAADAAA-GRPVAWIHGTAMRTEPLAFAGRDQVNPQAG----RDAAAALWKAAGITdPRDeIDVAEIYVPFSWFEPMW 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 309 YEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISkGHPLGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHNIGlG 388
Cdd:PRK08313 294 LENLGFAPEGEGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAEAALQVMGKAGEHQVDGARKALGHAYG-G 371
|
410
....*....|.
gi 41053664 389 GAVVVTLYKMG 399
Cdd:PRK08313 372 GSQFFSMWVVG 382
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
2-389 |
1.92e-44 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 161.35 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 2 AALRNRVFVIGVGMTKF-EKPGARDIDypdMAKEAGQRALADAGIKYSAIQQACVGYVYgDSTCGQRAIYHsLGLSgiPI 80
Cdd:PRK06158 4 RFLRGRTAIVGAATAGLgEAPGLSAME---LLAQAAHRALADAGLTMADVDGLFTASPD-DALWGLSVAEY-LGIR--PR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 81 InVNNNCSTGSTalFMGR-----QLIQGGLADCVLaLGFEKMER---GSLSSkyMDRTNPMDKHMEVM--INRYGLAAVp 150
Cdd:PRK06158 77 F-VDGTMIGGSS--FLAHllpaaLALEAGLCDVAL-ICYGSNQRsagGKLRS--MLDPQPYEAPYKPVnpVSAYALAAA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 151 aapqmfgnagrEHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLA 230
Cdd:PRK06158 150 -----------RHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDGAGAVVMV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 231 SESfvRRNGLEKKAVEIVAQEMvtdlSTTFEENSCMKmvgyDMTRLAA----ERCYDTAGVKPSDVDVIELHDCFSANEL 306
Cdd:PRK06158 219 RAD--RARDLPRPPVYVLGAAA----ATWHRQISSMP----DLTVTAAaesgPRAFAMAGLTPADIDVVELYDAFTINTI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 307 ITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPlGATGLAQCAELCWQLRAEAGPRQVPGAKLALQHniG 386
Cdd:PRK06158 289 LFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGLFLLIEAVRQLRGEAGERQVAGAEVALAH--G 365
|
...
gi 41053664 387 LGG 389
Cdd:PRK06158 366 NGG 368
|
|
| PRK06065 |
PRK06065 |
thiolase domain-containing protein; |
4-375 |
2.90e-38 |
|
thiolase domain-containing protein;
Pssm-ID: 180379 [Multi-domain] Cd Length: 392 Bit Score: 144.58 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 4 LRNRVFVIGVGMTKFEKpgaRDIDYP-DMAKEAGQRALADAGIKYSAIQQACVGYVyGDSTCG--QRAIYHSLGLSGI-- 78
Cdd:PRK06065 7 LNKRVAVIGAGLTLFRR---RLLETPqELAWEAASKALDEAGLELKDIDCVVIGSA-PDAFDGvhMKGEYLSHGSGGIrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 79 PIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSLSSKYMDRTnPMDKHMEVMINryglaavPAAPQMFGN 158
Cdd:PRK06065 83 PVSRVYVGGATGVMTAIAGWYHVASGLCQKVLAVAEEKMSPARPHPQAVFRY-IWDPILEKPLN-------PNLIWIFAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 159 AGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVRRN 238
Cdd:PRK06065 155 EMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 239 GLEKKAVEIVAQEmvtdLSTTFEENSCMKMVGYdmTRLAAERCYDTAGV-KP-SDVDVIELHDCFSANELITYEALGLCP 316
Cdd:PRK06065 235 TDTPVWVEGVGWT----LDNTEWPNRDLAYPRY--VEFAARMAYKMAGIeRPrKEIDVAEPYDPFDYKELHHLEGLQLAK 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 41053664 317 EGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVP 375
Cdd:PRK06065 309 RGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGLMKVISIYWQLKGTAGKMQVK 367
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
7-389 |
1.32e-36 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 141.18 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 7 RVFVIGVGMTKFEKPGARD-ID--YPDMAK-----------EAGQRALADAGI--KYSAIQQACVGYVYGDSTCGQ---- 66
Cdd:PTZ00455 13 RVFVVGGHITPFVGKGSPLfIDkkHPDFGKkenktleellaTAIQGTLENTGLdgKAALVDKVVVGNFLGELFSSQghlg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 67 RAIYHSLGLSGI-------PIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGS--LSSKYMDRTnpMDKHM 137
Cdd:PTZ00455 93 PAAVGSLGQSGAsnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarVGGDYLARA--ADYRR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 138 EVMINRYGLaavpaaPQMFgnAGREH-MEKYGT-KPEHFAKVAWKNHKHSTNNPYSQ-FQDEYSLEQVID---------- 204
Cdd:PTZ00455 171 QRKLDDFTF------PCLF--AKRMKyIQEHGHfTMEDTARVAAKAYANGNKNPLAHmHTRKLSLEFCTGasdknpkflg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 205 SRKVFEFLTLLQCCPTSDGAGAAVLASESFVRRNGL---EKKAVEIVAQEM-VTDLSTTFEENSCMKMvgydmTRLAAER 280
Cdd:PTZ00455 243 NETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLspnDSRLVEIKSLACaSGNLYEDPPDATRMFT-----SRAAAQK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 281 CYDTAGVKPSDVDVIELHDCFSANELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAE 360
Cdd:PTZ00455 318 ALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIME 397
|
410 420
....*....|....*....|....*....
gi 41053664 361 LCWQLRAEAGPRQVPGAkLALQHNIGLGG 389
Cdd:PTZ00455 398 VYRQMKGQCGEYQMKNI-PALGATLNMGG 425
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
6-393 |
2.77e-34 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 133.34 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 6 NRVFVIGVGMTKFeKPGARDIDYPDMAKEAGQRALADAG-IKYSAIQQACVgyvygdsTCgQRAIYHSLGLS-------- 76
Cdd:PRK06066 4 NRVAIVGIGWYGF-RPTTPEVSFREMMFEAASRAYKDAGnINPRRDVDSFI-------SC-QEDFWEGIAIAdefapdqi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 77 -GI--PIINVNNNCSTGSTALFMgrqLIQGGLADCVLalgfekMERGSLSSKYMDRTNPMDKHMEVMINR-------YGL 146
Cdd:PRK06066 75 gGAmrPTMTVAGDGLQGLAHAVM---HINSGLANVVV------VEAHSKPSDILTFSDVVKFAMDPIYVRpigppnpHFI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 147 AAVPAapqmfgnagREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGA 226
Cdd:PRK06066 146 AGLDA---------VKFMSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 227 AVLASESFVRRngLEKKAVEIVAQEMVTDlSTTFEENSCMKMVgydMTRLAAERCYDTAGV-KPS-DVDVIELHDCFSAN 304
Cdd:PRK06066 217 VVLASEEVAKK--LTDDPVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIeSPRkEVDAAEVDDRYSYK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 305 ELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQvPGAKLALQHN 384
Cdd:PRK06066 291 ELQHIEALRLSEEPEKDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQ-GKAERAVVAS 369
|
410
....*....|...
gi 41053664 385 I----GLGGAVVV 393
Cdd:PRK06066 370 WrgipTLTGSVVV 382
|
|
| SCP2 |
pfam02036 |
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ... |
428-529 |
1.97e-31 |
|
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: 116.97 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 428 FKEIEKKLqEEGEAYVKKIGG-VFAFKVKDGPGGsdalWVVDVKNGKGSVSSDAGKKADCTIAMADADLLDMMTGQLNPQ 506
Cdd:pfam02036 1 LNQLLARD-PAARELLKKLNGkVIRFDLTDLGLS----LTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQ 75
|
90 100
....*....|....*....|...
gi 41053664 507 TAFFQGKLKITGNMGMAMKLQNL 529
Cdd:pfam02036 76 KAFMQGKLKIEGDMELAQKLEGL 98
|
|
| PRK08142 |
PRK08142 |
thiolase domain-containing protein; |
150-386 |
1.04e-28 |
|
thiolase domain-containing protein;
Pssm-ID: 236164 [Multi-domain] Cd Length: 388 Bit Score: 117.50 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 150 PAAPQMFGNAGREHMEKYGTKPEHFA--KVAwKNHkHSTNNPYSQFQDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAA 227
Cdd:PRK08142 140 PTTHNLYAMCAMRHMHEYGTTSEQLAwiKVA-ASH-HAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDGGGAL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 228 VLASESFVRRngLEKKAVEIV-AQEMVTDLsttfeenscmkMVGY-DMT----RLAAERCYDTAGVKPSDVDVIELHDCF 301
Cdd:PRK08142 218 VVVRPEIARS--LKRPLVKVLgAGEAIKGQ-----------MGGKvDLTysgaAWSGPAAFAEAGVTPADIKYASIYDSF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 302 SANELITYEALGLCPEGKAGELIDRGDNTYG-GKWVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPR-QVPGAKL 379
Cdd:PRK08142 285 TITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHPANRGGMTKVIEAVRQLRGEAHPAvQVPNCDL 364
|
....*..
gi 41053664 380 ALQHNIG 386
Cdd:PRK08142 365 ALAHGTG 371
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
29-393 |
9.63e-27 |
|
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: 111.80 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 29 PDMAKEAGQRALADAGIKYSAIQQACVGYVYGdSTCGQ---RAIYHSLGLS-GIPIINVNNNCSTGSTALFMGRQLIQGG 104
Cdd:cd00751 23 DDLGAAVIKALLERAGLDPEEVDDVIMGNVLQ-AGEGQnpaRQAALLAGLPeSVPATTVNRVCGSGLQAVALAAQSIAAG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 105 LADCVLALGFEKMERGSLSSKYMDRTNPMDKHMEVMINRYGLAAVPAAPQMFGNAG---------REHMEKYGTKPEHFA 175
Cdd:cd00751 102 EADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAEnvaekygisREEQDEFALRSHQRA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 176 KVAWKNHKhstnnpysqFQDEysLEQV-IDSRKVFEFLTLLQC----------------------------CPTSDGAGA 226
Cdd:cd00751 182 AAAQEAGR---------FKDE--IVPVeVPGRKGPVVVDRDEGprpdttleklaklkpafkkdgtvtagnaSGINDGAAA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 227 AVLASESFVRRNGLEKKAVeIVAqemvtdlsttfeenscMKMVGYD---MTR---LAAERCYDTAGVKPSDVDVIELHDC 300
Cdd:cd00751 251 VLLMSEEKAKELGLKPLAR-IVG----------------YAVAGVDpaiMGIgpvPAIPKALKRAGLTLDDIDLIEINEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 301 FSANELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRAEagprqvpGAKLA 380
Cdd:cd00751 314 FAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASGARIVVTLLHELKRR-------GGRYG 368
|
410
....*....|....*.
gi 41053664 381 LQ---HNIGLGGAVVV 393
Cdd:cd00751 369 LAtmcIGGGQGAAMVI 384
|
|
| SCP2 |
COG3255 |
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism]; |
427-529 |
7.68e-26 |
|
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
Pssm-ID: 442486 [Multi-domain] Cd Length: 104 Bit Score: 101.52 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 427 VFKEIEKKLQEEGEAyvKKIGGVFAFKVKDGPGGSdalWVVDVKNGKGSVSSDAGKKADCTIAMADADLLDMMTGQLNPQ 506
Cdd:COG3255 3 WAEALCEKLNAADAA--AGWDGVVQFVITGEGGGA---YYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPM 77
|
90 100
....*....|....*....|...
gi 41053664 507 TAFFQGKLKITGNMGMAMKLQNL 529
Cdd:COG3255 78 TAFMTGKLKVEGDMGLAMKLMSL 100
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
144-377 |
1.72e-25 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 108.14 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 144 YGLAAvPAApqMFGNAGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQFQDE-YSLEQVIDSRKVFEFLTLLQCCPTSD 222
Cdd:PRK07855 141 HGLLT-PAA--WVAMLARRYMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 223 GAGAAVLASESfvRRNGLEKKAVEIVA--------QEMvtdlsttfeenscmkMVGY---DMTRL-----AAERCYDTAG 286
Cdd:PRK07855 218 GAVALVVTSAE--RARDLKQRPAVIKAaaqgsgadQYM---------------MTSYyrdDITGLpemglVARQLWAQSG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 287 VKPSDVDVIELHDCFSANELITYEALGLCPEGKAGELIDRGDNTYGGKWVINPSGGLISKGHPLGATGLaqcAELCWQLR 366
Cdd:PRK07855 281 LGPADIDTAILYDHFTPFVLMQLEELGFCGRGEAKDFIADGALELGGRLPINTHGGQLGEAYIHGMNGI---AEAVRQLR 357
|
250
....*....|.
gi 41053664 367 AEAgPRQVPGA 377
Cdd:PRK07855 358 GTS-VNQVPGV 367
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
24-393 |
1.73e-23 |
|
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: 102.31 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 24 RDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVY----GDSTCGQRAIYHSLGLSgIPIINVNNNCSTGSTALFMGRQ 99
Cdd:TIGR01930 17 KDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLqageQQNIARQAALLAGLPES-VPAYTVNRQCASGLQAVILAAQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 100 LIQGGLADCVLALGFEKMERG--SLSSKYMDRTNPMDKHMEVMInRYGLAAVPAAPQMfGNAGREHMEKYGTKPE---HF 174
Cdd:TIGR01930 96 LIRAGEADVVVAGGVESMSRVpyGVPRSLRWGVKPGNAELEDAR-LKDLTDANTGLPM-GVTAENLAKKYGISREeqdEY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 175 A----KVAWKNHK-------------HSTNNPYSQFQDE-----YSLEQVIDSRKVFE---FLTLLQCCPTSDGAGAAVL 229
Cdd:TIGR01930 174 AlrshQRAAKAWEeglfkdeivpvtvKGRKGPVTVSSDEgirpnTTLEKLAKLKPAFDpdgTVTAGNSSPLNDGAAALLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 230 ASESFVRRNGLEKKAvEIVAQEMVtdlsttfeenscmkmvGYDMTRL------AAERCYDTAGVKPSDVDVIELHDCFSA 303
Cdd:TIGR01930 254 MSEEKAKELGLTPLA-RIVSFAVA----------------GVDPEIMglgpvpAIPKALKKAGLSISDIDLFEINEAFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 304 NELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRAEagprqvpGAKLALQ- 382
Cdd:TIGR01930 317 QVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASGARIVTTLLHELKRR-------GGRYGLAt 371
|
410
....*....|...
gi 41053664 383 --HNIGLGGAVVV 393
Cdd:TIGR01930 372 mcIGGGQGAAVIL 384
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
8-233 |
3.37e-21 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 93.14 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 8 VFVIGVGMTKFEKPGA--RDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVyGDSTCGQ---RAIYHSLGLS-GIPII 81
Cdd:pfam00108 1 VVIVSAARTPFGSFGGslKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNV-LQAGEGQnpaRQAALKAGIPdSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 82 NVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSlsskYMDRTNPM------DKHMEVMINRYGLAAVPAAPQM 155
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAP----YALPTDARsglkhgDEKKHDLLIPDGLTDAFNGYHM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 156 fGNAGREHMEKYGTKPEHFAKVAWKNHKHSTNNPYSQ-FQDE--------------YSLEQVIDSRKVFEFLTLLQ---- 216
Cdd:pfam00108 156 -GLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDEivpvtvkgrkgkptVDKDEGIRPPTTAEPLAKLKpafd 234
|
250 260
....*....|....*....|....*.
gi 41053664 217 ---------CCPTSDGAGAAVLASES 233
Cdd:pfam00108 235 kegtvtagnASPINDGAAAVLLMSES 260
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
29-393 |
1.26e-17 |
|
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: 84.73 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 29 PDMAKEAGQRALADAGIKYSAIQQACVGYVY--GDSTCGQRAIYHSLGLS-GIPIINVNNNCSTGSTALFMGRQLIQGGL 105
Cdd:COG0183 27 DDLGAAVIKALLERAGLDPEAVDDVILGCVLqaGQGQNPARQAALLAGLPeSVPAVTVNRVCGSGLQAVALAAQAIAAGD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 106 ADCVLALGFEKMERGSLSSKYMDRTNPMDKHMEVMINRYGLAAVPAAPQMFGNAgrEHM-EKYG-TKPE---------HF 174
Cdd:COG0183 107 ADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMINPGLTDPYTGLSMGETA--ENVaERYGiSREEqdafalrshQR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 175 AKVAWKNHKhstnnpysqFQDE--------YSLEQVIDS----------------RKVFE---FLTLLQCCPTSDGAGAA 227
Cdd:COG0183 185 AAAAIAAGR---------FDDEivpvevpdRKGEVVVDRdegprpdttleklaklKPAFKkdgTVTAGNASGINDGAAAL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 228 VLASESFVRRNGLEKKAvEIVAqemvtdlsttfeenscMKMVGYDMTRL------AAERCYDTAGVKPSDVDVIELHDCF 301
Cdd:COG0183 256 LLMSEEAAKELGLKPLA-RIVA----------------YAVAGVDPEIMgigpvpATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 302 SANELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRAEagprqvpGAKLAL 381
Cdd:COG0183 319 AAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGARILVTLLHELERR-------GGRYGL 373
|
410
....*....|....*
gi 41053664 382 Q---HNIGLGGAVVV 393
Cdd:COG0183 374 AtmcIGGGQGIALII 388
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
37-385 |
7.69e-15 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 75.88 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 37 QRALADAGIKYSAIQQACVG---YVYGdstcgqRAIYHSLGLSGI---PIINVNNNCSTGSTALFMGRQLIQGGLADCVL 110
Cdd:PRK07937 33 AELYAELGITKSDIGFWCSGssdYLAG------RAFSFISAIDSIgavPPINESHVEMDAAWALYEAWVKLLTGEVDTAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 111 ALGFEKMERGSLsskymdrtnpmDKHMEVMINRYGLAAV-PAAPQMFGNAGREHMEKYGTKPEHFAKVAWKNHKHSTNNP 189
Cdd:PRK07937 107 VYGFGKSSAGTL-----------RRVLALQLDPYTVAPLwPDSVSMAGLQARAGLDAGKWTEEQMAEVAARSRADARRNP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 190 YSQfqDEYSLEQVIDSRKVFEFLTLLQCCPTSDGAGAAVLASESFVRR--------NGLEKKaveIVAQEM-VTDLSTTf 260
Cdd:PRK07937 176 SAE--PSISVDELLARPYFADPLRRHDIAPITDGAAAVVLAAGDRARElrerpawiTGIEHR---IESPSLgARDLTRS- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 261 eenscmkmvgyDMTRLAAERcydTAGVKPSDVDVIELHDCFSANELITYEALGLcpegkagelidrGDNTyggkwVINPS 340
Cdd:PRK07937 250 -----------PSTALAAEA---ATGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPS 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 41053664 341 GGLISkGHPLGATGLAQ---CAELCWQLRAE-------AGPrqvpgaklALQHNI 385
Cdd:PRK07937 299 GGALA-ANPMFAAGLERigeAARHIWDGSARralahatSGP--------ALQQNL 344
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
25-393 |
2.61e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 71.68 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 25 DIDYPDMAKEAGQRALADAGIKYSAIQQACVG--------YVYGdstcGQRAIYHSLGLSGIPIINVNNNCSTGSTALFM 96
Cdd:PRK06445 29 NIRPEELAAMLINRLIEKTGIKPEEIDDIITGcalqvgenWLYG----GRHPIFLARLPYNIPAMAVDRQCASSLTTVSI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 97 GRQLIQGGLADCVLALGFEKMERGSLSS--------KYMDRTNPMDKHMEVMINrYGLAAvpaaPQMFGNAG--REHMEK 166
Cdd:PRK06445 105 GAMEIATGMADIVIAGGVEHMTRTPMGDnphiepnpKLLTDPKYIEYDLTTGYV-MGLTA----EKLAEEAGikREEMDR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 167 YGTKPEHFAKVAWK---------------NHKHSTNNPYSQFQDEYSLEQVIDSRKVFE---FLTLLQCCPTSDGAGAAV 228
Cdd:PRK06445 180 WSLRSHQLAAKAIQegyfkdeilpievevEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpdgVITAGNSSPLNSGASYVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 229 LASESFVRRNGLEKKAvEIVAqemvtdLSTTFEENSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHDCFSANELIT 308
Cdd:PRK06445 260 LMSKKAVKKYGLKPMA-KIRS------FGFAGVPPAIMGKGPVPASKKALEK----AGLSVKDIDLWEINEAFAVVVLYA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 309 YEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLRAEAGPRQVpgAKLALQHniGLG 388
Cdd:PRK06445 329 IKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGV--ATLCVGG--GQG 386
|
....*
gi 41053664 389 GAVVV 393
Cdd:PRK06445 387 GAVVL 391
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
78-354 |
4.74e-13 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 70.89 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 78 IPIINVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMERGSLSS-----KYMDRTNPMDKHmEVMINRYGLAAVP-- 150
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSamtagEQLGFTSPFAES-KGWLHRYGDQEVSqf 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 151 AAPQMFG---NAGREHMEKYGTKPEHFAKVAWKN-HKHSTNNPYSQF-QDE----YSLEQVIDSRKVFE--FLTLLQCCP 219
Cdd:PRK07801 159 RGAELIAekwGISREEMERFALESHRRAFAAIRAgRFDNEIVPVGGVtVDEgpreTSLEKMAGLKPLVEggRLTAAVASQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 220 TSDGAGAAVLASESFVRRNGLEKKAveivaqeMVTDLSTTFEENSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHD 299
Cdd:PRK07801 239 ISDGASAVLLASERAVKRHGLTPRA-------RIHHLSVRGDDPVFMLTAPIPATRYALEK----TGLSIDDIDVVEINE 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41053664 300 CFSANELITYEALGLCPEGkagelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK07801 308 AFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATG 344
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
24-354 |
1.73e-10 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 62.86 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 24 RDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGdSTCGQRAIYHSLGLSGIPI----INVNNNCSTGSTALFMGRQ 99
Cdd:PRK05790 22 KDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQ-AGAGQNPARQAALKAGLPVevpaLTINKVCGSGLKAVALAAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 100 LIQGGLADCVLALGFEKMER------GSLSSKYMDRTNPMDkHMEV-----MINRY--GLAAVPAAPQMfgNAGREHMEK 166
Cdd:PRK05790 101 AIRAGDADIVVAGGQESMSQaphvlpGSRWGQKMGDVELVD-TMIHdgltdAFNGYhmGITAENLAEQY--GITREEQDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 167 YGTKPEHFAKVAWKNH-----------KHSTNNPYSQFQDEY-----SLEQVIDSRKVFE---FLTLLQCCPTSDGAGAA 227
Cdd:PRK05790 178 FALASQQKAEAAIKAGrfkdeivpvtiKQRKGDPVVVDTDEHprpdtTAESLAKLRPAFDkdgTVTAGNASGINDGAAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 228 VLASESFVRRNGLEKKAvEIV--AQEMVTDlsttfeenSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHDCFSANE 305
Cdd:PRK05790 258 VVMSEAKAKELGLTPLA-RIVsyAVAGVDP--------AIMGIGPVPAIRKALEK----AGWSLADLDLIEINEAFAAQA 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41053664 306 LITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATG 354
Cdd:PRK05790 325 LAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
220-366 |
2.13e-10 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 62.71 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 220 TSDGAGAAVLASESFVRRNGLEKKAveivaqemvtdlsttfeenscmKMVGYDMTRLAAE-----------RCYDTAGVK 288
Cdd:PRK09052 256 TSDGAGAVILVSEKALKQFNLTPLA----------------------RFVSFAVAGVPPEimgigpieaipAALKQAGLK 313
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 289 PSDVDVIELHDCFSANELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGLAQCAELCWQLR 366
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATGAIRTATVVHGLR 373
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
217-354 |
3.88e-10 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 61.94 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 217 CCPTSDGAGAAVLASESFVRRNGLEKKAvEIVAQEmVTDLSTTFeenscMKMVGYDMTRLAAERcydtAGVKPSDVDVIE 296
Cdd:PRK07851 259 ACPLNDGAAAVVIMSDTKARELGLTPLA-RIVSTG-VSGLSPEI-----MGLGPVEASKQALAR----AGMSIDDIDLVE 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 297 LHDCFSANELITYEALGLcPEGKagelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK07851 328 INEAFAAQVLPSARELGI-DEDK-----------------LNVSGGAIALGHPFGMTG 367
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
222-354 |
1.86e-09 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 59.58 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 222 DGAGAAVLASESFVRRNGLEKKAvEIVAqemvtdLSTTFEENSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHDCF 301
Cdd:PRK09050 258 DGAAALLLASEAAAKKHGLTPRA-RILG------MATAGVEPRIMGIGPAPATRKLLAR----LGLTIDQFDVIELNEAF 326
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 41053664 302 SANELITYEALGLCPEGKAgelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK09050 327 AAQGLAVLRQLGLADDDAR----------------VNPNGGAIALGHPLGMSG 363
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
35-354 |
5.59e-09 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 58.18 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 35 AGQRALADAGIKYSAIQQACVGYVY----GDSTCGQRAiyhsLGlSGIP----IINVNNNCSTGSTALFMGRQLIQGGLA 106
Cdd:PLN02644 32 AIQAALERAGVDPALVQEVFFGNVLsanlGQAPARQAA----LG-AGLPpstiCTTVNKVCASGMKAVMLAAQSIQLGIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 107 DCVLALGFEKMergSLSSKYMDRTNPMDK--HMEV---MI----------NRYGLAAVPAAPQMfgNAGREHMEKYGTKP 171
Cdd:PLN02644 107 DVVVAGGMESM---SNAPKYLPEARKGSRlgHDTVvdgMLkdglwdvyndFGMGVCAELCADQY--SISREEQDAYAIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 172 E----------HFA------KVAWKNHKHSTNNPYSQFQDEYSLEQVIDSRKVFE----FLTLLQCCPTSDGAGAAVLAS 231
Cdd:PLN02644 182 YeraiaaqeagAFAweivpvEVPGGRGRPSVIVDKDEGLGKFDPAKLRKLRPSFKedggSVTAGNASSISDGAAALVLVS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 232 ESFVRRNGLEKKAVEI----VAQEmvTDLSTTfeenscmkmvgydMTRLAAERCYDTAGVKPSDVDVIELHDCFSANELI 307
Cdd:PLN02644 262 GEKALELGLQVIAKIRgyadAAQA--PELFTT-------------APALAIPKALKHAGLEASQVDYYEINEAFSVVALA 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 41053664 308 TYEALGLCPEGkagelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PLN02644 327 NQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSG 355
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
30-132 |
1.20e-08 |
|
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: 56.66 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 30 DMAKEAGQRALADAGIKYSAIQQACVGYVYGD----ST-CgqrAIYHSLGLSGIPIINVNNNCSTGSTALFMGRQLIQGG 104
Cdd:COG0332 53 DLAVEAARKALEAAGIDPEDIDLIIVATVTPDylfpSTaC---LVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSG 129
|
90 100
....*....|....*....|....*...
gi 41053664 105 LADCVLALGFEKMergslsSKYMDRTNP 132
Cdd:COG0332 130 QAKNVLVVGAETL------SRIVDWTDR 151
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
222-354 |
1.28e-08 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 56.89 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 222 DGAGAAVLASESFVRRNGLEKKAvEIV--AQEMVtdlsttfeENSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHD 299
Cdd:PRK09051 253 DGAAAVVLAEADAAEARGLKPLA-RLVgyAHAGV--------DPEYMGIGPVPATQKALER----AGLTVADLDVIEANE 319
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41053664 300 CFSANELITYEALGLCPEGkagelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
276-370 |
1.82e-08 |
|
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: 52.64 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 276 LAAERCYDTAGVKPSDVDVIELHDCFSANELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATGL 355
Cdd:pfam02803 26 YAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASGA 87
|
90
....*....|....*
gi 41053664 356 AQCAELCWQLRAEAG 370
Cdd:pfam02803 88 RILVTLLHELKRRGG 102
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
222-354 |
3.36e-08 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 55.66 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 222 DGAGAAVLASESFVRRNGLEKKAvEIVAqemvtdLSTTFEENSCMkmvgydMT--RLAAERCYDTAGVKPSDVDVIELHD 299
Cdd:PRK08242 261 DGAAAVLIGSEEAGKALGLKPRA-RIVA------TATIGSDPTIM------LTgpVPATRKALAKAGLTVDDIDLFELNE 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41053664 300 CFSANELITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATG 354
Cdd:PRK08242 328 AFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
30-131 |
1.42e-07 |
|
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: 53.31 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 30 DMAKEAGQRALADAGIKYSAIqqACVGYVygdSTCGQRA-------IYHSLGLSGIPIINVNNNCSTGSTALFMGRQLIQ 102
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDI--DLIIVA---TSTPDYLfpataclVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIR 126
|
90 100
....*....|....*....|....*....
gi 41053664 103 GGLADCVLALGFEKMergslsSKYMDRTN 131
Cdd:cd00830 127 SGGAKNVLVVGAETL------SRILDWTD 149
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
75-354 |
2.98e-07 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 52.66 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 75 LSGIPI----INVNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMerGSLSSKYMDRTNP-MDKHMEVMINRYGLAAv 149
Cdd:PRK08947 75 LAGIPHsvpaVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM--GHVPMNHGVDFHPgLSKNVAKAAGMMGLTA- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 150 paapQMFG---NAGREHMEKYGTKPEHFAKVA-----WKN-----HKHSTNNPYSQFQD------EYSLEQVIDSRKVFE 210
Cdd:PRK08947 152 ----EMLGkmhGISREQQDAFAARSHQRAWAAtqegrFKNeiiptEGHDADGVLKLFDYdevirpETTVEALAALRPAFD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 211 ----FLTLLQCCPTSDGAGAAVLASESFVRRNGLEKKAVeIVAqemvtdlsttfeenscMKMVGYD---M-------TRL 276
Cdd:PRK08947 228 pvngTVTAGTSSALSDGASAMLVMSESRAKELGLKPRAR-IRS----------------MAVAGCDpsiMgygpvpaTQK 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 277 AAERcydtAGVKPSDVDVIELHDCFSANELITYEALGlcpegkageLIDRGDNTyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK08947 291 ALKR----AGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
222-354 |
9.57e-07 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 51.31 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 222 DGAGAAVLASESFVRRNGLEKKAvEIVAQEMVTDlSTTFEENSCMKmvgydmtrlAAERCYDTAGVKPSDVDVIELHDCF 301
Cdd:PRK06025 276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGD-DPTLMLNAPVP---------AAKKVLAKAGLTKDDIDLWEINEAF 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41053664 302 S--ANELItyEALGLcpegkageliDRGDntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK06025 345 AvvAEKFI--RDLDL----------DRDK--------VNVNGGAIALGHPIGATG 379
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
15-358 |
2.81e-06 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 49.76 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 15 MTKFEKPGARDIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTcgQRAIYHSLG--LSGIP----IINVNNNCS 88
Cdd:PLN02287 58 ICKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGS--QRANECRMAafYAGFPetvpVRTVNRQCS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 89 TGSTALFMGRQLIQGGLADCVLALGFEKME------------RGSLSSKYMDRTNPMDKHMEVMINRYGL-------AAV 149
Cdd:PLN02287 136 SGLQAVADVAAAIKAGFYDIGIGAGVESMTtnpmaweggvnpRVESFSQAQDCLLPMGITSENVAERFGVtreeqdqAAV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 150 -----PAAPQMFGNAgREHMEKYGTKpehfakvaWKNHKHSTNNPYSQFQDE-----YSLEQVIDSRKVFE---FLTLLQ 216
Cdd:PLN02287 216 eshrkAAAATASGKF-KDEIVPVHTK--------IVDPKTGEEKPIVISVDDgirpnTTLADLAKLKPVFKkngTTTAGN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 217 CCPTSDGAGAAVLASESFVRRNGLEKKAVeivaqemvtdlSTTFeenscmKMVGYD---M---TRLAAERCYDTAGVKPS 290
Cdd:PLN02287 287 SSQVSDGAGAVLLMKRSVAMQKGLPILGV-----------FRSF------AAVGVDpavMgigPAVAIPAAVKAAGLELD 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 291 DVDVIELHDCFSANELITYEALGLCPEGkagelidrgdntyggkwvINPSGGLISKGHPLGATGlAQC 358
Cdd:PLN02287 350 DIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG-ARC 398
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
5-146 |
3.83e-06 |
|
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: 49.46 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 5 RNRV-FVIGVGMtkfekPGARDIdypdmakEAGQRALADAGIKYsaIQQACVGYVYGDSTCGQRAIYhsLGLSGiPIINV 83
Cdd:cd00834 95 PERIgVVIGSGI-----GGLATI-------EEAYRALLEKGPRR--VSPFFVPMALPNMAAGQVAIR--LGLRG-PNYTV 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053664 84 NNNCSTGSTALFMGRQLIQGGLADCVLA------------LGFEKMerGSLSSKYMDRTN---PMDKhmevmiNRYGL 146
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAggaealitpltlAGFAAL--RALSTRNDDPEKasrPFDK------DRDGF 227
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
30-131 |
7.47e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 47.94 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 30 DMAKEAGQRALADAGIKYSAIQQACVGYVYGD----STCGQraIYHSLGLSGIPIINVNNNCSTGSTALFMGRQLIQGGL 105
Cdd:PRK12879 55 DLAIKAAERALARAGLDAEDIDLIIVATTTPDylfpSTASQ--VQARLGIPNAAAFDINAACAGFLYGLETANGLITSGL 132
|
90 100
....*....|....*....|....*.
gi 41053664 106 ADCVLALGFEKMergslsSKYMDRTN 131
Cdd:PRK12879 133 YKKVLVIGAERL------SKVTDYTD 152
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
25-113 |
8.78e-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: 47.81 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 25 DIDYPDMAKEAGQRALADAGIKYSAIQQACVGYVYGDSTCGQRAIY--HSLGLSGIPIINVNNNCSTGSTALFMGRQLIQ 102
Cdd:cd00827 45 DEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYlaELLGLTNAEAFDLKQACYGGTAALQLAANLVE 124
|
90
....*....|.
gi 41053664 103 GGLADCVLALG 113
Cdd:cd00827 125 SGPWRYALVVA 135
|
|
| BDS1 |
COG2015 |
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
449-529 |
4.97e-05 |
|
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: 45.99 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 449 VFAFKVKDgpggSDALWVVDVKNG-----KGsvssDAGKKADCTIAMADADLLDMMTGQLNPQTAFFQGKLKITGNmgmA 523
Cdd:COG2015 541 TINLIFTD----TGEKYLLELRNGvltyrKG----PQADDADATLTLTRADLLALLLGKTTLDDLVASGGAKVEGD---A 609
|
....*.
gi 41053664 524 MKLQNL 529
Cdd:COG2015 610 AALARL 615
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
26-354 |
7.46e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 45.26 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 26 IDYPDMAKEAGQRALADAGIKYSAIQQACVGYVY----GDSTCGQRAIYHSLGLSgIPIINVNNNCSTGSTALFMGRQLI 101
Cdd:PRK05656 24 IPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLtagaGQNPARQAAIKAGLPHS-VPAMTLNKVCGSGLKALHLAAQAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 102 QGGLADCVLALGFEKME---------RGSLSSKYMDRTNPM----------DKHM----EVMINRYGLA-----AVPAAP 153
Cdd:PRK05656 103 RCGDAEVIIAGGQENMSlapyvlpgaRTGLRMGHAQLVDSMitdglwdafnDYHMgitaENLVEKYGISreaqdAFAAAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 154 QMFGNAGREHmekyGTKPEHFAKVAWKNHKhstNNPYSQFQDEY-----SLEQVIDSRKVFE---FLTLLQCCPTSDGAG 225
Cdd:PRK05656 183 QQKAVAAIEA----GRFDDEITPILIPQRK---GEPLAFATDEQpragtTAESLAKLKPAFKkdgSVTAGNASSLNDGAA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 226 AAVLASESFVRRNGLEKKAveivaqeMVTDLSTTFEENSCMKMVGYDMTRlaaeRCYDTAGVKPSDVDVIELHDCFSANE 305
Cdd:PRK05656 256 AVLLMSAAKAKALGLPVLA-------KIAAYANAGVDPAIMGIGPVSATR----RCLDKAGWSLAELDLIEANEAFAAQS 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41053664 306 LITYEALGLCPEgkagelidrgdntyggkwVINPSGGLISKGHPLGATG 354
Cdd:PRK05656 325 LAVGKELGWDAA------------------KVNVNGGAIALGHPIGASG 355
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
277-354 |
1.24e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 44.59 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41053664 277 AAERCYDTAGVKPSDVDVIELHDCFSAnelityEALGLCPEGKAGEL-IDRgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK06205 303 ATEKALARAGLTLDDIDLIELNEAFAA------QVLAVLKEWGFGADdEER----------LNVNGSGISLGHPVGATG 365
|
|
| Alkyl_sulf_C |
pfam14864 |
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ... |
461-519 |
5.96e-04 |
|
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: 39.87 E-value: 5.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41053664 461 SDALWVVDVKNG-----KGSVSSDAgkkaDCTIAMADADLLDMMTGQLNPQTAFFQGKLKITGN 519
Cdd:pfam14864 42 VDEQYRLTLSNGvltyrKGRQADDA----DATLTLTRADLLALLLGKATLGKLIAAGKIKVEGD 101
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
19-161 |
6.62e-04 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 41.91 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 19 EKPGARDIDYP-DMAKEAGQRALADAGIKYSAIQqaCVGYV---YGDSTCGQRAIY--HSLGLSGIPIINVNNNCSTGST 92
Cdd:PRK06840 43 EKPVPGPEDHTsDMAIAAAKPALKQAGVDPAAID--VVIYIgseHKDYPVWSSAPKiqHEIGAKNAWAFDIMAVCASFPI 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 93 ALFMGR-QLIQGGLADCVLALGfekmerGSLSSKYMDRTNPmdkHMEVMINrygLAAVPAAPQMFGNAGR 161
Cdd:PRK06840 121 ALKVAKdLLYSDPSIENVLLVG------GYRNSDLVDYDNP---RTRFMFN---FAAGGSAALLKKDAGK 178
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
35-115 |
6.66e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 42.00 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 35 AGQRALADAGIKYSAIQQACVGYVYGDSTCGQRAIYHS--------------------------------LGLSGiPIIN 82
Cdd:COG0304 78 AAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAyrallekgprrvspffvpmmmpnmaaghvsirFGLKG-PNYT 156
|
90 100 110
....*....|....*....|....*....|...
gi 41053664 83 VNNNCSTGSTALFMGRQLIQGGLADCVLALGFE 115
Cdd:COG0304 157 VSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
222-354 |
1.11e-03 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 41.30 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 222 DGAGAAVLASESFVRRNGLEKKAvEIVAQEMVTdlsttfEENSCMKMVGYDMTRLAAERcydtAGVKPSDVDVIELHDCF 301
Cdd:PRK08131 257 DGAAALLIGSRAAGEKYGLKPMA-RILSSAAAG------VEPRIMGIGPVEAIKKALAR----AGLTLDDMDIIEINEAF 325
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 41053664 302 SANELITYEALGLCPEGKAgelidrgdntyggkwvINPSGGLISKGHPLGATG 354
Cdd:PRK08131 326 ASQVLGCLKGLGVDFDDPR----------------VNPNGGAIAVGHPLGASG 362
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
83-131 |
2.03e-03 |
|
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: 37.11 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 41053664 83 VNNNCSTGSTALFMGRQLIQGGLADCVLALGFEKMergslsSKYMDRTN 131
Cdd:pfam08545 3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETL------SKILDWTD 45
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
30-395 |
2.63e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 40.10 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 30 DMAKEAGQRALADAGIKYSAIQQA---CVGYVYGDST-CGQRAIYHSLGLSGIPIINVNNNCSTGSTALFMGRQLIQGGL 105
Cdd:PRK06504 28 DLAAQVLDALVDRSGADPALIEDVimgCVSQVGEQATnVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 106 ADCVLALGFEKMER---------------GSLSSKYMDRTNPMDKH-----MEVMINRYGLAavpaapqmfgnagREHME 165
Cdd:PRK06504 108 MDIVIAAGVESMTRvpmgspstlpaknglGHYKSPGMEERYPGIQFsqftgAEMMAKKYGLS-------------KDQLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 166 KYGTKPEHFAKVAWKNHKHSTN-----------NPYSQFQDE-----YSLEQV-----IDSRKVFEFLTLLQCCptsDGA 224
Cdd:PRK06504 175 EFALQSHQRAIAATQAGKFKAEivpleitradgSGEMHTVDEgirfdATLEGIagvklIAEGGRLTAATASQIC---DGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 225 GAAVLASESFVRRNGLEKKAveivaqemvtdlsttfeENSCMKMVGYDMTRL------AAERCYDTAGVKPSDVDVIELH 298
Cdd:PRK06504 252 SGVMVVNERGLKALGVKPLA-----------------RIHHMTVIGGDPVIMleaplpATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053664 299 DCFSANELITYEALGLCPEGkagelidrgdntyggkwvINPSGGLISKGHPLGATGLAQCAELCWQLRAEagprqvpGAK 378
Cdd:PRK06504 315 EAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTKLMTTLVHALKQR-------GKR 369
|
410
....*....|....*..
gi 41053664 379 LALQHNIGLGGAVVVTL 395
Cdd:PRK06504 370 YGLQTMCEGGGMANVTI 386
|
|
| |
