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Conserved domains on  [gi|2462512374|ref|XP_054194115|]
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sterol carrier protein 2 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08256 super family cl32282
lipid-transfer protein; Provisional
12-318 2.72e-178

lipid-transfer protein; Provisional


The actual alignment was detected with superfamily member PRK08256:

Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 499.81  E-value: 2.72e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256    1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256   79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256  159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256  238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462512374 289 RGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK08256  318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGL 347
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
12-318 2.72e-178

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 499.81  E-value: 2.72e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256    1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256   79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256  159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256  238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462512374 289 RGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK08256  318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGL 347
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
17-336 1.51e-149

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: 426.91  E-value: 1.51e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826     1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826    81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826   154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826   234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE--NDVRRSGILTKGP 336
Cdd:cd00826   314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAElcFELKGEAGKRQGA 372
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
240-317 2.31e-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: 60.35  E-value: 2.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:pfam02803  27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASG 86
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
239-317 4.63e-10

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: 60.32  E-value: 4.63e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASG 349
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
181-333 1.16e-06

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: 50.06  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183   246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG-------LKNLGENDV 326
Cdd:COG0183   308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGarilvtlLHELERRGG 369

                  ....*..
gi 2462512374 327 RRsGILT 333
Cdd:COG0183   370 RY-GLAT 375
 
Name Accession Description Interval E-value
PRK08256 PRK08256
lipid-transfer protein; Provisional
12-318 2.72e-178

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 499.81  E-value: 2.72e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFVKPGAenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------- 66
Cdd:PRK08256    1 NKVFVAGVGMTPFEKPGA--SWDYPDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdstsgqralyevgmtgipivnvnn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ------------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHME 128
Cdd:PRK08256   79 ncstgstalflarqavrsGAADCALALGFEQMQPGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRMFGGAGREHME 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqSKAV 208
Cdd:PRK08256  159 KYGTTAETFAKIGVKARRHAANNPYAQFRDEYTLEDVLASPMIWGPLTRLQCCPPTCGAAAAIVCSEEFARKHGL-DRAV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 209 EILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVD 288
Cdd:PRK08256  238 EIVAQAMTTDTPSTFDGRSMIDLVGYDMTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGEAEKFID 317
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462512374 289 RGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK08256  318 DGDNTYGGRWVVNPSGGLLSKGHPLGATGL 347
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
17-336 1.51e-149

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: 426.91  E-value: 1.51e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  17 VGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYS----AVDQACVGYVF-------------------------- 66
Cdd:cd00826     1 AGAAMTAFGKFGGENGADANDLAHEAGAKAIAAALEPAGvaagAVEEACLGQVLgagegqncaqqaamhagglqeapaig 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ---------------------GVAECVLALGFEKMSkgslgikFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKE 125
Cdd:cd00826    81 mnnlcgsglralalamqliagGDANCILAGGFEKME-------TSAENNAKEKHIDVLINKYGMRACPDAFALAGQAGAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 126 HMEKYGTKIEHFAKIGWKN---HKHSVNNPYSQFQDEYSLDEVMASKEVFD---FLTILQCCPTSDGAAAAILASEAFVQ 199
Cdd:cd00826   154 AAEKDGRFKDEFAKFGVKGrkgDIHSDADEYIQFGDEASLDEIAKLRPAFDkedFLTAGNACGLNDGAAAAILMSEAEAQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 200 KYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCP 279
Cdd:cd00826   234 KHGLQSKAREIQALEMITDMASTFEDKKVIKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCP 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 280 EGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE--NDVRRSGILTKGP 336
Cdd:cd00826   314 EGQGGALVDRGDNTYGGKSIINPNGGAIAIGHPIGASGAAICAElcFELKGEAGKRQGA 372
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
17-323 8.42e-105

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: 312.66  E-value: 8.42e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  17 VGVGMTKFVKPGaenSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF------------------------------ 66
Cdd:cd00829     1 VGVGMTPFGRRS---DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAggrfqsfpgaliaeylgllgkpatrveaag 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ----------------GVAECVLALGFEKMSKGSLGIKFSDRTIPTDKHVDLLInkYGLSAhpvaPQMFGYAGKEHMEKY 130
Cdd:cd00829    78 asgsaavraaaaaiasGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPP--GGLTP----PALYALAARRYMHRY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 131 GTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGLqsKAVEI 210
Cdd:cd00829   152 GTTREDLAKVAVKNHRNAARNPYAQFRKPITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELTD--RPVWI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 211 LAQEMMTDLPSSFEEKSiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRG 290
Cdd:cd00829   230 LGVGAASDTPSLSERDD---FLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKGEGGKLVREG 306
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2462512374 291 DNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:cd00829   307 DTAIGGDLPVNTSGGLLSKGHPLGATGLAQAVE 339
PRK06064 PRK06064
thiolase domain-containing protein;
11-323 1.77e-68

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 219.77  E-value: 1.77e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  11 LRRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQ-------------------------------------IP 53
Cdd:PRK06064    1 MRDVAIIGVGQTKF---GELWDVSLRDLAVEAGLEALEDAGidgkdidamyvgnmsaglfvsqehiaaliadyaglapIP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  54 YSAVDQAC--------VGYVF---GVAECVLALGFEKMSKgslgikfsdrtIPTDKHVDLLI--------NKYGLSAhpv 114
Cdd:PRK06064   78 ATRVEAACasggaalrQAYLAvasGEADVVLAAGVEKMTD-----------VPTPDATEAIAragdyeweEFFGATF--- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 115 aPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06064  144 -PGLYALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQFQKEITVEQVLNSPPVADPLKLLDCSPITDGAAAVILAS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 195 EAFVQKYglQSKAVEILAQEMMTDLPSSFEEKSIikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK06064  223 EEKAKEY--TDTPVWIKASGQASDTIALHDRKDF---TTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462512374 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06064  298 LGFAKKGEGGKLAREGQTYIGGDIPVNPSGGLKAKGHPVGATGVSQAVE 346
PRK12578 PRK12578
thiolase domain-containing protein;
12-318 2.73e-50

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 172.34  E-value: 2.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYV-------------------------- 65
Cdd:PRK12578    1 RRVAVIGVGNSKF---GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTayrgielypapivaeysgltgkvplr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  66 --------------------FGVAECVLALGFEKMSK----GSLGIKFSDRTIPTDKHvdllinKYGLSAhpvaPQMFGY 121
Cdd:PRK12578   78 veamcatglaasltaytavaSGLVDMAIAVGVDKMTEvdtsTSLAIGGRGGNYQWEYH------FYGTTF----PTYYAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK12578  148 YATRHMAVYGTTEEQMALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWPIKLLDSCPISDGSATAIFASEEKVKEL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 GLQSkAVEILAQEMMTDLpSSFEEKsiIKMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK12578  228 KIDS-PVWITGIGYANDY-AYVARR--GEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFTEKG 303
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2462512374 282 QGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK12578  304 KGGKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATGL 340
PRK07516 PRK07516
thiolase domain-containing protein;
13-317 2.61e-40

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 146.25  E-value: 2.61e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  13 RVFVVGVGMTKFVKPGAEnsrDYPDLAEEAGKKALADAQIPYSAVDQACVGyVF-------------------------- 66
Cdd:PRK07516    3 TASIVGWAHTPFGKLDAE---TLESLIVRVAREALAHAGIAAGDVDGIFLG-HFnagfspqdfpaslvlqadpalrfkpa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 -----------------------GVAECVLALGFEKMSkgslgikfsdrTIPTDKHVDLLIN-KYGLSAHPVA---PQMF 119
Cdd:PRK07516   79 trvenacatgsaavyaaldaieaGRARIVLVVGAEKMT-----------ATPTAEVGDILLGaSYLKEEGDTPggfAGVF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKE----VFDFLTILQCCPTSDGAAAAILASE 195
Cdd:PRK07516  148 GRIAQAYFQRYGDQSDALAMIAAKNHANGVANPYAQMRKDLGFEFCRTVSEknplVAGPLRRTDCSLVSDGAAALVLADA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 196 AFVQKYglqSKAVEILAQEMMTD-LPSSFEEksiikMVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEA 274
Cdd:PRK07516  228 ETARAL---QRAVRFRARAHVNDfLPLSRRD-----PLAFEGPRRAWQRALAQAGVTLDDLSFVETHDCFTIAELIEYEA 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2462512374 275 LGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATG 317
Cdd:PRK07516  300 MGLAPPGQGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
12-324 5.22e-37

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 137.47  E-value: 5.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFvkpGAENSRDYPDLAEEAGKKALADAQI-----------------------------------PYSA 56
Cdd:PRK06157    7 DKVAILGMGCTKF---GERWDAGAEDLMVEAFLEALADAGIepkdidaawfgthydeigsgksgtplsralrlpniPVTR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  57 VDQACV-------GYVFGVA----ECVLALGFEK-MSKGSLGIKFSDRTIPTDkhvdllinkyGLSAHPVAPQMFGYAGK 124
Cdd:PRK06157   84 VENFCAtgseafrGAVYAVAsgayDIALALGVEKlKDTGYGGLPVANPGTLAD----------MTMPNVTAPGNFAQLAS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 125 EHMEKYGTKIEHF----AKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQK 200
Cdd:PRK06157  154 AYAAKYGVSREDLkramAHVSVKSHANGARNPKAHLRKAVTEEQVLKAPMIAGPLGLFDCCGVSDGAAAAIVTTPEIARA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 201 YG----LQSKAVEILA---QEMMT---DLpSSFEEKSIikmvgfdmskeAARKCYEKSGLT-P-NDIDVIELHDCFSTNE 268
Cdd:PRK06157  234 LGkkdpVYVKALQLAVsngWELQYngwDG-SYFPTTRI-----------AARKAYREAGITdPrEELSMAEVHDCFSITE 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512374 269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGEN 324
Cdd:PRK06157  302 LVTMEDLGLSERGQAWRDVLDGFFDADGGLPCQIDGGLKCFGHPIGASGLRMLYEM 357
PRK06365 PRK06365
thiolase domain-containing protein;
8-318 5.70e-36

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 135.42  E-value: 5.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374   8 PATLRRVFVVGVGMTKFVKpgAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGY----------------------- 64
Cdd:PRK06365   12 KKKSRDVYMVAAGVTKFDK--ASPYMDFRERVKKAFDYAMNDAGLTLADIDGSVASYfsdhfqrqllagimvqdylglvp 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  65 ------------------------VFGVAECVLALGFEKMSKgslgikfsdrtIPTDKHvdlliNKY-GLSA-----HPV 114
Cdd:PRK06365   90 kpskriegggatgglafqagyeeiASGRMDCVAVYGFETMSH-----------VNTWKG-----NEFiALASdtnfdYPL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 115 APQMFGY---AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAI 191
Cdd:PRK06365  154 GGFYTGYyamMAVRHMYEFGTTVEQLAKVSVKNHGNAIHNPFAQSPMKITVEDVRKSPMVSYPLTRLDVCAMSDGAACAI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 192 LASEAfvQKYGLQSKAVEILAQEMMTD--------------LPSsfEEKSIIK------MVGFDMSKEAARKCYEKSGLT 251
Cdd:PRK06365  234 LASED--KAFEITDKPVLIKAIGTGSDtlrladrpfgevplLPN--ESPDDYKdlrypgVHSFRAGRMAAKEAYEMAGIT 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 252 P--NDIDVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK06365  310 DplNDLDLIELHDAYTSSEIQTYEDLGLCKYGEGGQFIESGKPELPGKLPVNPSGGLLAAGHAVGATGI 378
PRK06059 PRK06059
lipid-transfer protein; Provisional
10-323 5.78e-35

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 131.81  E-value: 5.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  10 TLRRVFVVGVGMTKFVKPGaensRDYPDLAEEAGKKALADAQIPYSAVdQACV----------GYVF------------- 66
Cdd:PRK06059    2 MPEPVYILGAGMHPWGKWG----RDFVEYGVVAARAALADAGLDWRDV-QLVVgadtirngypGFVAgatfaqalgwnga 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 -------------------------GVAECVLALGFEKMSKGSLGIKFSDRtiPTDKhvDLLINKYGLSAHPVapqMFGY 121
Cdd:PRK06059   77 pvsssyaacasgsqalqsaraqilaGLCDVALVVGADTTPKGFFAPVGGER--PDDP--DWLRFHLIGATNPV---YFAL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06059  150 LARRRMDLYGATVEDFAQVKVKNARHGLLNPNARYRKEVTVEDVLASPVVSDPLRLLDICATSDGAAALIVASKSFARRH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 GLQSK-AVEILAQEMMT--------DLPsSFEEKSIIKMVGFDMS--KEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06059  230 LGSVAgVPSVRAISTVTprypqhlpELP-DIATDSTAAVPAPERVfkDQILDAAYAEAGIGPEDLSLAEVYDLSTALELD 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06059  309 WYEHLGLCPKGEAEALLRSGATTLGGRIPVNPSGGLACFGEAIPAQAIAQVCE 361
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
14-321 1.39e-29

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 117.48  E-value: 1.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  14 VFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVFG-------------------------- 67
Cdd:PRK06289    5 VWVLGGYQSDFARNWTKEGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFFGelfagqghlgampatvhpalwgvpas 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  68 ----------VA-------------ECVLALGFEKMskgslgikfsdRTIPTDKHVDLL-----INKYGLSAHPVAPQMF 119
Cdd:PRK06289   85 rheaacasgsVAtlaamadlragryDVALVVGVELM-----------KTVPGDVAAEHLgaaawTGHEGQDARFPWPSMF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 120 GYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-----FQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILAS 194
Cdd:PRK06289  154 ARVADEYDRRYGLDEEHLRAIAEINFANARRNPNAQtrgwaFPDEATNDDDATNPVVEGRLRRQDCSQVTDGGAGVVLAS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 195 EAFVQKYGLQSKAVEILAQEMMTdLPSSFEEKsIIKMVG----FDMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNELL 270
Cdd:PRK06289  234 DAYLRDYADARPIPRIKGWGHRT-APLGLEQK-LDRSAGdpyvLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYL 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462512374 271 TYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNL 321
Cdd:PRK06289  312 AIDHIGLTGPGESWKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRML 362
PRK08313 PRK08313
thiolase domain-containing protein;
12-323 2.64e-26

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 107.89  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFVKPGAENSrdYPDLAEEAGKKALADAQIPYSAVD--------------------------------- 58
Cdd:PRK08313    3 RLAAVLGTGQTKYVAKRQDVS--MAGLVREAIDRALADAGLTWDDIDavvvgkapdffegvmmpelfladalgatgkpli 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  59 -----------QACVGYVF---GVAECVLALGFEKMSKGSLGIKFSdrtIPTDKHVDLLINKYGLSAHPVApqmfgyagk 124
Cdd:PRK08313   81 rvhtagsvggsTAVVAASLvqsGVYRRVLAVAWEKQSESNAMWALS---IPVPFTKPVGAGAGGYFAPHVR--------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 125 EHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQF-QDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYGL 203
Cdd:PRK08313  149 AYIRRSGAPEHIGAMVAVKDRLNGAKNPYAHLhQPDITLEKVMASQMLWDPIRFDETCPSSDGACAVVIGDEEAADAAAG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 204 QSKAVeILAQEMMTDlPSSFEEKSIIKMVGfdmSKEAARKCYEKSGLT-P-NDIDVIELHDCFSTNELLTYEALGLCPEG 281
Cdd:PRK08313  229 RPVAW-IHGTAMRTE-PLAFAGRDQVNPQA---GRDAAAALWKAAGITdPrDEIDVAEIYVPFSWFEPMWLENLGFAPEG 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2462512374 282 QGATLVDRGDNTYGGKWVINPSGGLISkGHPLGATGLKNLGE 323
Cdd:PRK08313  304 EGWKLTEAGETAIGGRLPVNPSGGVLS-SNPIGASGMIRFAE 344
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
181-323 7.78e-26

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: 104.06  E-value: 7.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 181 CPTSDGAAAAILASEAFVQKYGLQskaveilAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDIDVIEL 260
Cdd:cd00327    98 FVFGDGAAAAVVESEEHALRRGAH-------PQAEIVSTAATFDGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 261 HDCFSTNELLTYEALGLCPEGQGAtlvdrgdntyggkwvINPSGGLISKGHPLGATGLKNLGE 323
Cdd:cd00327   171 HGTGTPIGDAVELALGLDPDGVRS---------------PAVSATLIMTGHPLGAAGLAILDE 218
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
129-323 6.29e-24

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 101.89  E-value: 6.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 129 KYGTKIEHF-----AKIGWKNHKHSVNNPYSQ-FQDEYSLDEV----------MASKEVFDFLTILQCCPTSDGAAAAIL 192
Cdd:PTZ00455  188 KYIQEHGHFtmedtARVAAKAYANGNKNPLAHmHTRKLSLEFCtgasdknpkfLGNETYKPFLRMTDCSQVSDGGAGLVL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 193 ASEAFVQKYGLQ---SKAVEILAQEM-MTDLPSSFEEKSiiKMVgfdMSKEAARKCYEKSGLTPNDIDVIELHDCFSTNE 268
Cdd:PTZ00455  268 ASEEGLQKMGLSpndSRLVEIKSLACaSGNLYEDPPDAT--RMF---TSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462512374 269 LLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PTZ00455  343 LLMYEALGIAEYGHAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIME 397
PRK06158 PRK06158
thiolase; Provisional
113-318 4.37e-23

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 98.95  E-value: 4.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 113 PVAPqMFGYA--GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaa 190
Cdd:PRK06158  137 PVNP-VSAYAlaAARHMHQYGTTREQLAEVAVAARQWAQLNPEAFMRDPLTIDDVLAARMVSDPLSVRDCCLVTDG---- 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 191 ilaseafvqkyglqSKAVEILAQEMMTDLP----------SSFEEKSIIKMVgfDMSKEAA----RKCYEKSGLTPNDID 256
Cdd:PRK06158  212 --------------AGAVVMVRADRARDLPrppvyvlgaaAATWHRQISSMP--DLTVTAAaesgPRAFAMAGLTPADID 275
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512374 257 VIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPlGATGL 318
Cdd:PRK06158  276 VVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPGGRLPVNTNGGGLSCVHP-GMYGL 336
PRK06066 PRK06066
thiolase domain-containing protein;
127-323 9.45e-22

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 95.20  E-value: 9.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 127 MEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKYglQSK 206
Cdd:PRK06066  154 MSRKGITREDLALVVEKNKKAGLSNPRASYASNISLEDVLSSEYVVYPLTELDIAPFVDGAIVVVLASEEVAKKL--TDD 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 207 AVEILAQEMMTDlPSSFEEKSIIKMVgfdMSKEAARKCYEKSGLTP--NDIDVIELHDCFSTNELLTYEALGLCPEGQGA 284
Cdd:PRK06066  232 PVWIKGIGWSTE-SSNLETAELGKAN---YMRIAADMAYKMAGIESprKEVDAAEVDDRYSYKELQHIEALRLSEEPEKD 307
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462512374 285 TLVDRGDNTYGGKWVINPSGGLISKGHPLGATGLKNLGE 323
Cdd:PRK06066  308 SLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLD 346
PRK07855 PRK07855
lipid-transfer protein; Provisional
16-308 1.30e-20

lipid-transfer protein; Provisional


Pssm-ID: 181147 [Multi-domain]  Cd Length: 386  Bit Score: 91.96  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  16 VVGVGMTKFVKpgaENSRDYPDLAEEAGKKALADA------------------------------------QIPY----- 54
Cdd:PRK07855    8 IVGIGATEFSK---NSGRSELRLACEAVLAALDDAglapsdvdglvtftmdtnpeiavaralgigelkffsRIHYgggaa 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  55 -SAVDQACVGYVFGVAECVLAlgFEKMSKGSlGIKFS--DRTIPTDKHVDLLINK----YGLS--AHPVApqMFGyagKE 125
Cdd:PRK07855   85 cATVQQAAMAVATGVADVVVC--YRAFNERS-GMRFGqgQTGLAENPTSTGVDYGwsypHGLLtpAAWVA--MLA---RR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 126 HMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDE-YSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKygLQ 204
Cdd:PRK07855  157 YMHEYGATSEDFGRVAVADRKHAATNPKAWFYGRpITLEDHQNSRWIAEPLRLLDCCQESDGAVALVVTSAERARD--LK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 205 SKAVEILA--------QEMMT----DLPSSFEEKSIikmvgfdmskeAARKCYEKSGLTPNDIDVIELHDCFSTNELLTY 272
Cdd:PRK07855  235 QRPAVIKAaaqgsgadQYMMTsyyrDDITGLPEMGL-----------VARQLWAQSGLGPADIDTAILYDHFTPFVLMQL 303
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2462512374 273 EALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLIS 308
Cdd:PRK07855  304 EELGFCGRGEAKDFIADGALELGGRLPINTHGGQLG 339
PRK06065 PRK06065
thiolase domain-containing protein;
12-318 1.71e-18

thiolase domain-containing protein;


Pssm-ID: 180379 [Multi-domain]  Cd Length: 392  Bit Score: 85.65  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  12 RRVFVVGVGMTKFVKPGAENSRDypdLAEEAGKKALADAQIPYSAVDQACVGY--------------------------- 64
Cdd:PRK06065    9 KRVAVIGAGLTLFRRRLLETPQE---LAWEAASKALDEAGLELKDIDCVVIGSapdafdgvhmkgeylshgsggirkpvs 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  65 -VF-------------------GVAECVLALGFEKMSKGSLGIKFSDRTIptdkhVDLLINKyglsahPVAPQM---FGY 121
Cdd:PRK06065   86 rVYvggatgvmtaiagwyhvasGLCQKVLAVAEEKMSPARPHPQAVFRYI-----WDPILEK------PLNPNLiwiFAM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 122 AGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEAFVQKY 201
Cdd:PRK06065  155 EMHRYMATYGIKKEEIALVSVKNKRNALNNPYAQLGSKITVEDVLKSEVLVWPVQLLDVSPVSDGAAAIVLASEDLARRY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 202 glqskaveilaqemmTDLPssfeekSIIKMVGFDMS---------------KEAARKCYEKSGLT-PN-DIDVIELHDCF 264
Cdd:PRK06065  235 ---------------TDTP------VWVEGVGWTLDntewpnrdlaypryvEFAARMAYKMAGIErPRkEIDVAEPYDPF 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462512374 265 STNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGATGL 318
Cdd:PRK06065  294 DYKELHHLEGLQLAKRGEAPKLLKEGVFDIDGDIPSSPSGGLLGVGNPIAAAGL 347
PRK08142 PRK08142
thiolase domain-containing protein;
112-312 3.97e-18

thiolase domain-containing protein;


Pssm-ID: 236164 [Multi-domain]  Cd Length: 388  Bit Score: 84.75  E-value: 3.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 112 HPVAPQMFGYAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGaaaai 191
Cdd:PRK08142  139 GPTTHNLYAMCAMRHMHEYGTTSEQLAWIKVAASHHAQHNPHAMLRDVVTVEDVLNSPMIADPLHRLDCCVVTDG----- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 192 laseafvqkyglqSKAVEILAQEMMTDLpssfeEKSIIKMVG------------FDMSKEAAR----KCYEKSGLTPNDI 255
Cdd:PRK08142  214 -------------GGALVVVRPEIARSL-----KRPLVKVLGageaikgqmggkVDLTYSGAAwsgpAAFAEAGVTPADI 275
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 256 DVIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYG-GKWVINPSGGLISKGHP 312
Cdd:PRK08142  276 KYASIYDSFTITVLMQLEDLGFCKKGEGGKFVADGNLISGvGKLPFNTDGGGLCNNHP 333
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
240-317 3.36e-12

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: 66.73  E-value: 3.36e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:cd00751   290 AIPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPE------------------KVNVNGGAIALGHPLGASG 349
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
52-322 1.10e-11

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 65.51  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  52 IPYSAVDQAC------VGYVF-----GVAECVLALGFEKMSKGSLG--------IKFSDRtiPTDKHVDLLInkyGLSAH 112
Cdd:PRK06445   86 IPAMAVDRQCasslttVSIGAmeiatGMADIVIAGGVEHMTRTPMGdnphiepnPKLLTD--PKYIEYDLTT---GYVMG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 113 PVAPQMFGYAG--KEHMEKYGTKIEHFA----KIGW-----------KNHKHSVNNPYSQFQDEYSLDEVMASKEVFD-- 173
Cdd:PRK06445  161 LTAEKLAEEAGikREEMDRWSLRSHQLAakaiQEGYfkdeilpieveVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKpd 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 174 -FLTILQCCPTSDGAAAAILASEAFVQKYGLQSKAVeilaqemmtdlpssfeeksiIKMVGFD------MSK---EAARK 243
Cdd:PRK06445  241 gVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAK--------------------IRSFGFAgvppaiMGKgpvPASKK 300
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 244 CYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLKNLG 322
Cdd:PRK06445  301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPE------------------TVNIKGGAIAIGHPLGATGARIVG 361
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
240-317 2.31e-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: 60.35  E-value: 2.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:pfam02803  27 AIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPE------------------KVNVNGGAIALGHPLGASG 86
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
239-317 4.63e-10

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: 60.32  E-value: 4.63e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLE------------------KVNVNGGAIALGHPLGASG 349
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
240-317 1.86e-09

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 58.74  E-value: 1.86e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08242  305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHD------------------KVNVNGGAIAMGHPLGATG 364
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
240-317 8.35e-09

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 56.50  E-value: 8.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlVDRGDNtyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09050  302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGL---------ADDDAR-------VNPNGGAIALGHPLGMSG 363
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
240-319 3.84e-08

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 54.33  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PRK07801  285 ATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAK------------------VNPNGGAIALGHPLGATGAK 346
PRK09051 PRK09051
beta-ketothiolase BktB;
240-317 4.78e-08

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 54.20  E-value: 4.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK09051  297 ATQKALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAK------------------VNPNGSGISLGHPVGATG 356
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
238-317 9.02e-08

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 53.47  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 238 KEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK09052  300 IEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPS------------------KVNPLGGAIALGHPLGATG 361
PRK07937 PRK07937
lipid-transfer protein; Provisional
237-323 7.90e-07

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 50.46  E-value: 7.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 237 SKEAARKCyekSGLTPNDIDVIELHDCFSTNELLTYEALGLcpegqgatlvdrGDNTyggkwVINPSGGLISkGHPLGAT 316
Cdd:PRK07937  252 TALAAEAA---TGGDAGGVDVAELHAPFTHQELILREALGL------------GDKT-----KVNPSGGALA-ANPMFAA 310

                  ....*..
gi 2462512374 317 GLKNLGE 323
Cdd:PRK07937  311 GLERIGE 317
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
185-333 9.21e-07

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 50.16  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 185 DGAAAAILASEAFVQKYGLQSKAvEILAQEMMTDLPSsfeeksiikmVGFDMSKEAARKCYEKSGLTPNDIDVIELHDCF 264
Cdd:PRK06025  276 DGAAALLLASKAYAEKHGLKPRA-RIVAMANMGDDPT----------LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAF 344
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512374 265 STNELLTYEALGLcpegqgatlvDRGDntyggkwvINPSGGLISKGHPLGATG-------LKNLGENDVRRsGILT 333
Cdd:PRK06025  345 AVVAEKFIRDLDL----------DRDK--------VNVNGGAIALGHPIGATGsiligtvLDELERRGLKR-GLVT 401
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
14-159 1.00e-06

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: 49.61  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  14 VFVVGVGMTKFVK-PGAENSRDYPDLAEEAGKKALADAQIPYSAVDQACVGYVF-------------------------- 66
Cdd:pfam00108   1 VVIVSAARTPFGSfGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLqagegqnparqaalkagipdsapavt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374  67 ---------------------GVAECVLALGFEKMSKGSLGIKFSDR---TIPTDKHVDLLInKYGLSAHPVAPQMfGYA 122
Cdd:pfam00108  81 inkvcgsglkavylaaqsiasGDADVVLAGGVESMSHAPYALPTDARsglKHGDEKKHDLLI-PDGLTDAFNGYHM-GLT 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462512374 123 GKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQ-FQDE 159
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGkFKDE 196
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
181-333 1.16e-06

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: 50.06  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 181 CPTSDGAAAAILASEAFVQKYGLQSKAvEILAQ-------EMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPN 253
Cdd:COG0183   246 SGINDGAAALLLMSEEAAKELGLKPLA-RIVAYavagvdpEIMGIGPV-----------------PATRKALARAGLTLD 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 254 DIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG-------LKNLGENDV 326
Cdd:COG0183   308 DIDLIEINEAFAAQVLAVLRELGLDPD------------------KVNVNGGAIALGHPLGASGarilvtlLHELERRGG 369

                  ....*..
gi 2462512374 327 RRsGILT 333
Cdd:COG0183   370 RY-GLAT 375
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
246-317 1.91e-06

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 49.38  E-value: 1.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512374 246 EKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PLN02287  342 KAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEK------------------VNVNGGAIALGHPLGATG 395
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
240-330 2.01e-06

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 49.22  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELhdcfstNELLTYEALGLCPE-GQGATLVDRgdntyggkwvINPSGGLISKGHPLGATG- 317
Cdd:PRK06205  303 ATEKALARAGLTLDDIDLIEL------NEAFAAQVLAVLKEwGFGADDEER----------LNVNGSGISLGHPVGATGg 366
                          90
                  ....*....|....*
gi 2462512374 318 --LKNLGENDVRRSG 330
Cdd:PRK06205  367 riLATLLRELQRRQA 381
PRK05790 PRK05790
putative acyltransferase; Provisional
240-317 2.20e-06

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 49.00  E-value: 2.20e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK05790  296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPE------------------KVNVNGGAIALGHPIGASG 355
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
239-317 2.51e-06

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 49.01  E-value: 2.51e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512374 239 EAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatlVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08131  300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLG----------VDFDDPR------VNPNGGAIAVGHPLGASG 362
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
161-325 3.96e-06

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 48.46  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 161 SLDEVMASKEVF---DFLTILQCCPTSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikm 231
Cdd:PRK07851  237 TYEKVSQLKPVFrpdGTVTAGNACPLNDGAAAVVIMSDTKARELGLTplarivSTGVSGLSPEIMGLGPV---------- 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 232 vgfdmskEAARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLcPEgqgatlvDRgdntyggkwvINPSGGLISKGH 311
Cdd:PRK07851  307 -------EASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE-------DK----------LNVSGGAIALGH 361
                         170       180
                  ....*....|....*....|.
gi 2462512374 312 PLGATG-------LKNLGEND 325
Cdd:PRK07851  362 PFGMTGaritttlLNNLQTHD 382
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
240-317 2.18e-05

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 45.73  E-value: 2.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGlcpegqgatLVDRGDNTyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK08947  287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDLG---------LLDKMDEK------VNLNGGAIALGHPLGCSG 349
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
240-317 3.06e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 45.47  E-value: 3.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATG 317
Cdd:PRK08235  296 AINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPE------------------KVNVNGGAVALGHPIGASG 355
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
240-321 4.90e-05

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 44.88  E-value: 4.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLK 319
Cdd:PRK05656  296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAA------------------KVNVNGGAIALGHPIGASGCR 357

                  ..
gi 2462512374 320 NL 321
Cdd:PRK05656  358 VL 359
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
240-319 1.34e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 43.56  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PRK06504  293 ATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPER------------------LNVNGGAIALGHPLGASGTK 354
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
240-317 6.64e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 41.17  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALglcpegqgatlvdrgdntyggKW---VINPSGGLISKGHPLGAT 316
Cdd:PRK06633  295 ASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM---------------------KWdmeKVNINGGAIAIGHPIGAS 353

                  .
gi 2462512374 317 G 317
Cdd:PRK06633  354 G 354
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
183-319 7.50e-04

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 41.27  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 183 TSDGAAAAILASEAFVQKYGLQ------SKAVEILAQEMMTDLPSsfeeksiikmvgfdmskEAARKCYEKSGLTPNDID 256
Cdd:PRK07661  248 MSDGAAAVLLMDREKAESDGLKplakfrSFAVAGVPPEVMGIGPI-----------------AAIPKALKLAGLELSDIG 310
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462512374 257 VIELHDCFSTNELLTYEALGLCPEgqgatlvdrgdntyggkwVINPSGGLISKGHPLGATGLK 319
Cdd:PRK07661  311 LFELNEAFASQSIQVIRELGLDEE------------------KVNVNGGAIALGHPLGCTGAK 355
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
240-322 1.38e-03

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 40.46  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 240 AARKCYEKSGLTPNDIDVIELHDCFSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATGLK 319
Cdd:PLN02644  296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEK------------------VNVHGGAVSLGHPIGCSGAR 357

                  ...
gi 2462512374 320 NLG 322
Cdd:PLN02644  358 ILV 360
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
235-258 3.24e-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: 39.06  E-value: 3.24e-03
                          10        20
                  ....*....|....*....|....
gi 2462512374 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:cd00830    52 DLAVEAAKKALEDAGIDADDIDLI 75
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
235-258 7.30e-03

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: 37.78  E-value: 7.30e-03
                          10        20
                  ....*....|....*....|....
gi 2462512374 235 DMSKEAARKCYEKSGLTPNDIDVI 258
Cdd:COG0332    53 DLAVEAARKALEAAGIDPEDIDLI 76
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
184-317 9.32e-03

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 37.56  E-value: 9.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512374 184 SDGAAAAILASEAFVQKYGLQSKAVeILAQEMMTDLPSSFEEKSIikmvgfdmskEAARKCYEKSGLTPNDIDVIELHDC 263
Cdd:PRK06954  255 SDGAAALVMMRASTAKRLGLAPLAR-VVGHSTFAQAPSKFTTAPV----------GAIRKLFEKNGWRAAEVDLFEINEA 323
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462512374 264 FSTNELLTYEALGLCPEGqgatlvdrgdntyggkwvINPSGGLISKGHPLGATG 317
Cdd:PRK06954  324 FAVVTMAAMKEHGLPHEK------------------VNVNGGACALGHPIGASG 359
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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