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Conserved domains on  [gi|446588638|ref|WP_000665984|]
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MULTISPECIES: acetyl-CoA C-acetyltransferase [Salmonella]

Protein Classification

acetyl-CoA C-acetyltransferase( domain architecture ID 11481662)

acetyl-CoA C-acetyltransferase catalyzes the condensation of two acetyl-CoA molecules to form acetoacetyl-CoA, essentially joining two two-carbon units together to create a four-carbon unit, with the release of a CoA molecule; this reaction is a key step in the synthesis of ketone bodies and fatty acid metabolism

CATH:  3.40.47.10
EC:  2.3.1.9
Gene Ontology:  GO:0003985
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05790 PRK05790
putative acyltransferase; Provisional
1-392 0e+00

putative acyltransferase; Provisional


:

Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 676.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
 
Name Accession Description Interval E-value
PRK05790 PRK05790
putative acyltransferase; Provisional
1-392 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 676.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-391 0e+00

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: 594.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA-KLVDPMINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGS 240
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 241 VTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFA 320
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588638 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-391 0e+00

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: 580.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   5 VIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITI 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  85 NDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVTAENL 164
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL-NTLDGMLDDGLTDPFTGLSMGITAENV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 245 NASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQAL 324
Cdd:cd00751  240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588638 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:cd00751  320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-390 8.39e-176

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: 494.82  E-value: 8.39e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    6 IVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITIN 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   86 DVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGAL-PDADNLVDSLVHDgLWDAFNDYHIGVTAENL 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  245 NASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQAL 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588638  325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-261 1.20e-119

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: 347.37  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    4 VVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAIT 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLN-DSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTAE 162
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  163 NLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTaIVDTDEQPRADASAEGLALLHPAFDSLGSV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|
gi 446588638  242 TAGNASSINDGAAAVMMMSE 261
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSE 259
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
81-114 2.80e-04

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 42.32  E-value: 2.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 446588638    81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:smart00825  90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
 
Name Accession Description Interval E-value
PRK05790 PRK05790
putative acyltransferase; Provisional
1-392 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 676.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-391 0e+00

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: 594.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA-KLVDPMINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGS 240
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 241 VTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFA 320
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588638 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-392 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 586.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-391 0e+00

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: 580.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   5 VIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITI 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  85 NDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLVHDGLWDAFNDYHIGVTAENL 164
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL-NTLDGMLDDGLTDPFTGLSMGITAENV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:cd00751  160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 245 NASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQAL 324
Cdd:cd00751  240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588638 325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:cd00751  320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-390 8.39e-176

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: 494.82  E-value: 8.39e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    6 IVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAITIN 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   86 DVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGAL-PDADNLVDSLVHDgLWDAFNDYHIGVTAENL 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVkPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  165 AREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGSVTAG 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  245 NASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQAL 324
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588638  325 SVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-390 7.92e-151

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 431.83  E-value: 7.92e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK08235  81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLG 239
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
PRK09051 PRK09051
beta-ketothiolase BktB;
1-391 2.11e-148

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 425.53  E-value: 2.11e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPTTV 79
Cdd:PRK09051   2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVhDGLWDAFNDYHIGV 159
Cdd:PRK09051  82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAF-DSL 238
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFkKEN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 239 GSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEA 318
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
2-391 1.31e-144

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 416.03  E-value: 1.31e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSA 81
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTA 161
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 162 ENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVP--IVTQRNGQTAIVDTDEQPrADASAEGLALLHPAFDS-L 238
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPveVPGGRGRPSVIVDKDEGL-GKFDPAKLRKLRPSFKEdG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 239 GSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446588638 319 FAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-390 3.28e-141

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 407.49  E-value: 3.28e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVlNDSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVT 160
Cdd:PRK06633  82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 161 AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGLALLHPAFDSLGS 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 241 VTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFA 320
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 321 AQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-391 9.93e-141

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 406.68  E-value: 9.93e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQvlTAGAGQNPA--RQSAIKGGLPTT 78
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDadnlvDSLVHDGLWDA---FNDY 155
Cdd:PRK06205  79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGG-----GVQLHDRLARGretAGGR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 156 HIGV------TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGL 228
Cdd:PRK06205 154 RFPVpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtVPQRKGDPTVVDRDEHPRADTTLESL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 229 ALLHP---AFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGW 305
Cdd:PRK06205 234 AKLRPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 306 QLTEVDLIEANEAFAAQALSVGKMLEW---DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGG 382
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393

                 ....*....
gi 446588638 383 QGVALTIER 391
Cdd:PRK06205 394 QGLAAVFER 402
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-391 2.55e-134

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 390.08  E-value: 2.55e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTT 78
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLND-----SRTGALPDAD---NLVDSLVHDglwd 150
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKadsafSRQAEIFDTTigwRFVNPLMKA---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 151 afndyHIGV-----TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADAS 224
Cdd:PRK09050 157 -----QYGVdsmpeTAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtIPQKKGDPVVVDRDEHPRPETT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 225 AEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAG 304
Cdd:PRK09050 232 LEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLG 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 305 WQLTEVDLIEANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGG 382
Cdd:PRK09050 312 LTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVG 391

                 ....*....
gi 446588638 383 QGVALTIER 391
Cdd:PRK09050 392 QGIALAIER 400
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-391 1.34e-122

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 359.66  E-value: 1.34e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHS-AVELGSMVVKALIERT-GVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPT 77
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKGGAFRNVrAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSrapHVlndsrtgalpDADNLVDSLVHDGLWDAFNDYHI 157
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG---HV----------PMNHGVDFHPGLSKNVAKAAGMM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 158 GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQ-RNGQTAIVDTDEQPRADASAEGLALLHPAFD 236
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHdADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 237 SL-GSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEA 315
Cdd:PRK08947 228 PVnGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588638 316 NEAFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK08947 308 NEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
2-391 1.97e-122

3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.


Pssm-ID: 131483  Cd Length: 400  Bit Score: 359.87  E-value: 1.97e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    2 KEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:TIGR02430   1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTgALPDADNLVDS-----LVHDGLWDAFND 154
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADS-AFSRSAKIEDTtigwrFINPLMKALYGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  155 YHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHP 233
Cdd:TIGR02430 160 DSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvIPQKKGEPTVVDQDEHPRPETTLEGLAKLKP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  234 AFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLI 313
Cdd:TIGR02430 240 VVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  314 EANEAFAAQALSVGKMLEW--DERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02430 320 ELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-261 1.20e-119

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: 347.37  E-value: 1.20e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    4 VVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAIT 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLN-DSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTAE 162
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  163 NLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTaIVDTDEQPRADASAEGLALLHPAFDSLGSV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|
gi 446588638  242 TAGNASSINDGAAAVMMMSE 261
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSE 259
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-391 3.26e-118

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 348.66  E-value: 3.26e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPTT 78
Cdd:PRK07661   1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP---HVLNDSRTgalpdadnlvdslvhdgLWDAFNDY 155
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVVRPNPR-----------------LVEAAPEY 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 156 HIGV--TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQR----NGQ----TAIVDTDEQPRADAS 224
Cdd:PRK07661 144 YMGMghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdVTLRtvgeNNKlqeeTITFSQDEGVRADTT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 225 AEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAG 304
Cdd:PRK07661 224 LEILGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 305 WQLTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQG 384
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383

                 ....*..
gi 446588638 385 VALTIER 391
Cdd:PRK07661 384 AAGVFEL 390
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-391 4.99e-115

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 340.55  E-value: 4.99e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCF------QGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLtaGAGQN---PARQSAI 71
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  72 KGGLPTTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLN---DSRTGALPDADnlvdsLVHdgl 148
Cdd:PRK06445  79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiEPNPKLLTDPK-----YIE--- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 149 WDAFNDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRADASAEGL 228
Cdd:PRK06445 151 YDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 229 ALLHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLT 308
Cdd:PRK06445 231 AKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 309 EVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALT 388
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390

                 ...
gi 446588638 389 IER 391
Cdd:PRK06445 391 LER 393
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-390 2.12e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 334.17  E-value: 2.12e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06954   6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHDGLWDAFNDYH-IGV 159
Cdd:PRK06954  86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDEQPRAdASAEGLALLHPAFDSLG 239
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 240 SVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAF 319
Cdd:PRK06954 245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446588638 320 AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06954 325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-390 9.69e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 332.36  E-value: 9.69e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVL-NDSRTGA---LPDADNLVDSLVHDGLWDAFNDYH 156
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPkhlLHKNYKIDDAMLVDGLIDAFYFEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTqrngqtaiVDTDEQPRaDASAEGLALLHPAFD 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIR-KTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 237 SLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEAN 316
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588638 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
3-392 2.25e-110

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 330.96  E-value: 2.25e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   3 EVVIVGALRTPI-----GCFQGTLArhsaVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQ-NPARQSAIKGGLP 76
Cdd:PLN02287  47 DVVIVAAYRTPIckakrGGFKDTYP----DDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFP 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  77 TTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADNLVDSLVHdglwdafndyh 156
Cdd:PLN02287 123 ETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP----------- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQR------NGQTAIVDTDEQPRADASAEGLAL 230
Cdd:PLN02287 192 MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpktgEEKPIVISVDDGIRPNTTLADLAK 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 231 LHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEV 310
Cdd:PLN02287 272 LKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDI 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 311 DLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKR--DARKGLATLCIGGGQGVALT 388
Cdd:PLN02287 352 DLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAV 431

                 ....
gi 446588638 389 IERD 392
Cdd:PLN02287 432 FERG 435
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-391 2.72e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 328.77  E-value: 2.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQ--GTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPT 77
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlnDSRTGALPdadnlVDSLVhdglwdAFNDYHI 157
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM---GSDGGAWA-----MDPST------NFPTYFV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 158 --GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPiVTQRNGQTaIVDTDEQPRADASAEGLALLHPAF 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP-VKDQNGLT-ILDHDEHMRPGTTMESLAKLKPSF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 236 DSLGSV---------------------TAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVY 294
Cdd:PRK08242 225 AMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 295 ATRRCLERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGL 374
Cdd:PRK08242 305 ATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTAL 384
                        410
                 ....*....|....*..
gi 446588638 375 ATLCIGGGQGVALTIER 391
Cdd:PRK08242 385 ITLCVGGGMGIATIIER 401
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-391 7.24e-108

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 322.72  E-value: 7.24e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAV-ELGSMVVKALIERT-GVDANAIDEVILGQVL-TAGAGQNPARQSAIKGGLPT 77
Cdd:PRK09052   5 LQDAYIVAATRTPVGKAPRGMFKNTRPdDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  78 TVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLND-SRTGALPDADNLVDSLvhdglwdafndYH 156
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKpSMSPAIFARDENVGIA-----------YG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 157 IGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQR-----NGQTAI----VDTDEQPRADASAE 226
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeITERfpdlaTGEVDVktrtVDLDEGPRADTSLE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 227 GLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQ 306
Cdd:PRK09052 234 GLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 307 LTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVA 386
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393

                 ....*
gi 446588638 387 LTIER 391
Cdd:PRK09052 394 GIFER 398
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-391 3.43e-107

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 321.18  E-value: 3.43e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERT-GVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPT 77
Cdd:PRK07851   1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  78 tVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSrtgaLPDADNLV---------------DS 142
Cdd:PRK07851  81 -LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDS----LPDTKNPLfaeaqartaaraeggAE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 143 LVHDGLWD-AFNDYHI--GVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPiVTQRNGqtAIVDTDEQP 219
Cdd:PRK07851 156 AWHDPREDgLLPDVYIamGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP-VTLPDG--TVVSTDDGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 220 RADASAEGLALLHPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRC 299
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 300 LERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCI 379
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
                        410
                 ....*....|..
gi 446588638 380 GGGQGVALTIER 391
Cdd:PRK07851 393 GGGQGMAMVLER 404
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
3-391 1.37e-104

fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 131498  Cd Length: 385  Bit Score: 313.80  E-value: 1.37e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638    3 EVVIVGALRTPIGCFQGTLARHSAVE-LGSMVVKALIER-TGVDANAIDEVILGQV-LTAGAGQNPARQSAIKGGLPTTV 79
Cdd:TIGR02445   1 DVVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlndsrtgalpdADNLVDSLVHDGLWDAFNDYHIGV 159
Cdd:TIGR02445  81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-------------MMHGVDFHPGMSLHVAKAAGMMGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQ-RNGQTAIVDTDEQPRADASAEGLALLHPAFDSL 238
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHdADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  239 -GSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANE 317
Cdd:TIGR02445 228 nGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588638  318 AFAAQALSVGK---MLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-391 4.26e-103

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 310.56  E-value: 4.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:PRK08131   1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDAdNLVDSLV-----HDGLWDAFND 154
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDA-KVFDTTIgarfpNPKIVAQYGN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 155 YHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIV--TQRNGQTAIVDTDEQPRADASAEGLALLH 232
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEvpQGRKLPPKLVAEDEHPRPSSTVEALTKLK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 233 PAFDSlGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDL 312
Cdd:PRK08131 240 PLFEG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 313 IEANEAFAAQALSVGKML--EWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK08131 319 IEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398

                 .
gi 446588638 391 R 391
Cdd:PRK08131 399 R 399
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-391 5.53e-102

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 307.02  E-value: 5.53e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG--AGqNPARQSAIKGGLPTT 78
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvLNDSRTGALPDAdnLVDSLVHDGLWDA-FNDYHI 157
Cdd:PRK07801  80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTAGEQLG--FTSPFAESKGWLHrYGDQEV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 158 G--VTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvtqrngqtAIVDTDEQPRaDASAEGLALLHPAF 235
Cdd:PRK07801 156 SqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GGVTVDEGPR-ETSLEKMAGLKPLV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 236 DSlGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEA 315
Cdd:PRK07801 227 EG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEI 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446588638 316 NEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07801 306 NEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-391 4.56e-101

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 304.72  E-value: 4.56e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTTV 79
Cdd:PRK07850   1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPDADnlvdslvhDGLWDAFNDYhigV 159
Cdd:PRK07850  81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPD--------SWDIDMPNQF---E 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVT-------QRNGQTAIVDTDEQPRaDASAEGLALLH 232
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQApvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 233 PAFDSlGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDL 312
Cdd:PRK07850 229 PVLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588638 313 IEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-391 2.04e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 296.93  E-value: 2.04e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08170   2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPD---ADNLVDSLVH------------ 145
Cdd:PRK08170  82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGwyaAKSIGQKLAAlgklrpsylapv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 146 ----DGLWDAFNDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKdEIVPIVTqRNGQtaIVDTDEQPRA 221
Cdd:PRK08170 162 igllRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFD-RDGK--FYDHDDGVRP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 222 DASAEGLALLHPAFDS-LGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCL 300
Cdd:PRK08170 238 DSSMEKLAKLKPFFDRpYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 301 ERAGWQLTEVDLIEANEAFAAQALSV-----------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVH 363
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
                        410       420
                 ....*....|....*....|....*...
gi 446588638 364 EMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-391 3.48e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 295.10  E-value: 3.48e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAG-AGQNPARQSAIKGGLPTTV 79
Cdd:PRK06504   1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNdsrtGALPdADNLVDSLVHDGLWDAFNDYHIG- 158
Cdd:PRK06504  81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP----STLP-AKNGLGHYKSPGMEERYPGIQFSq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 159 -VTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPI-VTQRNGQTAIVDTDEQPRADASAEGLALLHPAFD 236
Cdd:PRK06504 156 fTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLeITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 237 SlGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEAN 316
Cdd:PRK06504 236 G-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446588638 317 EAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK06504 315 EAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
4-392 1.87e-91

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 281.49  E-value: 1.87e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   4 VVIVGALRTPigcF--QGTLARH-SAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK08963   7 IAIVSGLRTP---FakQATAFHGiPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAP--------HVLND-SRTGALPDADNLVDSLvhdGLWD- 150
Cdd:PRK08963  84 AYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVDlNKARTLGQRLKLFSRL---RLRDl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 151 -----AFNDYHIGV----TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTaiVDTDEQPRA 221
Cdd:PRK08963 161 lpvppAVAEYSTGLrmgdTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP--LEEDNNIRG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 222 DASAEGLALLHPAFD-SLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDP---ALMGiaPVYATR 297
Cdd:PRK08963 239 DSTLEDYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 298 RCLERAGWQLTEVDLIEANEAFAAQALSVGKML-----------------EWDERRVNVNGGAIALGHPIGASGCRILVS 360
Cdd:PRK08963 317 LALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQ 396
                        410       420       430
                 ....*....|....*....|....*....|..
gi 446588638 361 LVHEMVKRDARKGLATLCIGGGQGVALTIERD 392
Cdd:PRK08963 397 TLHELRRRGGGLGLTTACAAGGLGAAMVLEVE 428
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-386 3.36e-91

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 279.73  E-value: 3.36e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIG-CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLPTT 78
Cdd:PRK07108   1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTgalpdADNLVDSLVHDGLWDAFNdyhig 158
Cdd:PRK07108  81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHML-----REGWLVEHKPEIYWSMLQ----- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 159 vTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvTQRNG-----------QTAIVDTDEQPRADASAEG 227
Cdd:PRK07108 151 -TAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPI-TVTAGvadkatgrlftKEVTVSADEGIRPDTTLEG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 228 LALLHPAFDSlGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQL 307
Cdd:PRK07108 229 VSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKV 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446588638 308 TEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVA 386
Cdd:PRK07108 308 DDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
7-390 3.88e-87

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: 269.36  E-value: 3.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   7 VGALRTPIGCFQGTLARHS---AVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVSAIT 83
Cdd:cd00826    1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  84 INDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAphvlndSRTGALpdadnlvdslvhdglwdafnDYHIGVtaen 163
Cdd:cd00826   81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAK--------------------EKHIDV---- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 164 LAREYGiSRELQDAYALSSQQKARAAIDTGRFKDEIVPIVTQRNGQTAIVDTDE--QPRADASAEGLALLHPAFDSLGSV 241
Cdd:cd00826  131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiQFGDEASLDEIAKLRPAFDKEDFL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 242 TAGNASSINDGAAAVMMMSETKA-------RALGLPVLARIRAFASVGVDPA----LMGIAPVYATRRCLERAGWQLTEV 310
Cdd:cd00826  210 TAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 311 DLIEANEAFAAQALSVGKMLEWDERR------------------VNVNGGAIALGHPIGASGCRILVSLVHEMVKRD--- 369
Cdd:cd00826  290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkr 369
                        410       420
                 ....*....|....*....|...
gi 446588638 370 --ARKGLATLCIGGGQGVALTIE 390
Cdd:cd00826  370 qgAGAGLALLCIGGGGGAAMCIE 392
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-390 3.91e-83

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 258.16  E-value: 3.91e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   3 EVVIVGALRTPIGCFQGTLARHSAVELGSMVVKAL---IERtgvdanAIDEVILGQVLtaGAGQNPARQSAIKGGLPTTV 79
Cdd:PRK06690   2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLskgMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  80 SAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlnDSRTGALPDAdnlvdslvhdglwdaFNDYHIGV 159
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRARFSPET---------------IGDPDMGV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 160 TAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVP--------IVTQRNGQTAIvdtdeqPRADasaeglall 231
Cdd:PRK06690 136 AAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSfnglldesIKKEMNYERII------KRTK--------- 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 232 hPAFDSLGSVTAGNASSINDGAAAVMMMSETKARALGL-PVLARIRAfASVGVDPALMGIAPVYATRRCLERAGWQLTEV 310
Cdd:PRK06690 201 -PAFLHNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDI 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 311 DLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIE 390
Cdd:PRK06690 279 DYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-391 7.72e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 256.63  E-value: 7.72e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIG---CFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGA-GQNPARQSAIKGGLP 76
Cdd:PRK06025   1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  77 TTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS-RAPHVLNDSRTGALP---DADNLVDSLVHDglwdaf 152
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPPlgmGSGNLRLRALHP------ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 153 nDYHIGVTAENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIVtqRNGQTAIVDTDEQPRADASAEGLALLH 232
Cdd:PRK06025 155 -QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 233 PAFDSLGSVT--------------------------AGNASSINDGAAAVMMMSETKARALGLPVLARIRAFASVGVDPA 286
Cdd:PRK06025 232 PAFTAIADYPlddkgttyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 287 LMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEMV 366
Cdd:PRK06025 312 LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
                        410       420
                 ....*....|....*....|....*
gi 446588638 367 KRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK06025 392 RRGLKRGLVTMCAAGGMAPAIIIER 416
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
269-391 7.50e-67

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: 207.88  E-value: 7.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  269 LPVLARIRAFASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDERRVNVNGGAIALGH 348
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446588638  349 PIGASGCRILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-391 1.48e-59

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 198.97  E-value: 1.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTTVS 80
Cdd:PRK09268   6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHVLNDSRTGALPD---ADNLVDSLvhdGLWDAFNDYHI 157
Cdd:PRK09268  86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLElnrAKTTGDRL---KALGKLRPKHL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 158 GVT----------------AENLAREYGISRELQDAYALSSQQKARAAIDTGRFKDEIVPIvtqrNGqtaiVDTDEQPRA 221
Cdd:PRK09268 163 APEiprngeprtglsmgehAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF----LG----LTRDNNLRP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 222 DASAEGLALLHPAFD--SLGSVTAGNASSINDGAAAVMMMSETKARALGLPVLARIRAF--ASV----GVDPALMgiAPV 293
Cdd:PRK09268 235 DSSLEKLAKLKPVFGkgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEGLLM--APA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 294 YATRRCLERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDE-----------------RRVNVNGGAIALGHPIGASGCR 356
Cdd:PRK09268 313 YAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEycrerlgldaplgsidrSKLNVNGSSLAAGHPFAATGGR 392
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 446588638 357 ILVSLVHEMVKRDARKGLATLCIGGGQGVALTIER 391
Cdd:PRK09268 393 IVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
26-389 1.07e-23

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: 98.67  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  26 AVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLPTtVSAITINDVCGSGLKALHLATQAIQCG 105
Cdd:cd00327    7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 106 EADIVIAGGqenmsraphvlndsrtgalpdadnlvdslvhdglwdafndyhigvtaenlareygisrelqdayalssqqk 185
Cdd:cd00327   86 KADIVLAGG----------------------------------------------------------------------- 94
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 186 araaidtgrfkdeivpivtqrngqtaivdtdeqpradasaeglallhpafdslgsvtaGNASSINDGAAAVMMMSETKAR 265
Cdd:cd00327   95 ----------------------------------------------------------SEEFVFGDGAAAAVVESEEHAL 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 266 ALGLPVLARIRAFASVGVD----PALMGIAPVYATRRCLERAGWQLTEVDLIEANEAFAAQALSVGKMLEWDE---RRVN 338
Cdd:cd00327  117 RRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPA 196
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446588638 339 VNGGAIALGHPIGASGCRILVSLVHEM-------VKRDARKGLATLCIGGGQGVALTI 389
Cdd:cd00327  197 VSATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
PRK06064 PRK06064
thiolase domain-containing protein;
1-373 5.41e-17

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 81.87  E-value: 5.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGCFQGTLARHSAVELGsmvVKAlIERTGVDANAIDEVILGQVLTAG-AGQ-NPARQSAIKGGLpTT 78
Cdd:PRK06064   1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAG---LEA-LEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGL-AP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  79 VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPHvlndsrtgalPDADNLVDSLVhDGLWDAFNdyhiG 158
Cdd:PRK06064  76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPT----------PDATEAIARAG-DYEWEEFF----G 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 159 VTAENL----AR----EYGISRE------LQDAYALSSQQKARaaidtgrFKDEIvpivtqrngqtaivDTDEQPRADAS 224
Cdd:PRK06064 141 ATFPGLyaliARrymhKYGTTEEdlalvaVKNHYNGSKNPYAQ-------FQKEI--------------TVEQVLNSPPV 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 225 AEGLALLHpafdslgsvtagnASSINDGAAAVMMMSETKARALGL-PVlaRIRAFASVGVDPAL------MGI-APVYAT 296
Cdd:PRK06064 200 ADPLKLLD-------------CSPITDGAAAVILASEEKAKEYTDtPV--WIKASGQASDTIALhdrkdfTTLdAAVVAA 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 297 RRCLERAGWQLTEVDLIEANEAFA-AQALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGASGCRIL 358
Cdd:PRK06064 265 EKAYKMAGIEPKDIDVAEVHDCFTiAEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVSQA 344
                        410
                 ....*....|....*
gi 446588638 359 VSLVHEMvKRDARKG 373
Cdd:PRK06064 345 VEIVWQL-RGEAEKG 358
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
25-389 2.60e-15

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: 76.53  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  25 SAVELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPARQSAIKGGLpTTVSAITINDVCGSGLKALHLATQAIQC 104
Cdd:cd00829   15 SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGL-LGKPATRVEAAGASGSAAVRAAAAAIAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 105 GEADIVIAGGQENMSRAPhvlndSRTGALPDADNLVDSLVHDGLWDAFNDYHIGVTAENLAReYGISRElqdAYALSSQQ 184
Cdd:cd00829   94 GLADVVLVVGAEKMSDVP-----TGDEAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHR-YGTTRE---DLAKVAVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 185 KARAAIDTGR--FKDEIvpivtqrngqtaivDTDEQPRADASAEGLALLHpafdslgsvtagnASSINDGAAAVMMMSET 262
Cdd:cd00829  165 NHRNAARNPYaqFRKPI--------------TVEDVLNSRMIADPLRLLD-------------CCPVSDGAAAVVLASEE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 263 KARALGLPvLARIRAFAsVGVDPALMG--------IAPVYATRRCLERAGWQLTEVDLIE------ANEAFAAQAL---- 324
Cdd:cd00829  218 RARELTDR-PVWILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAElydcftIAELLALEDLgfce 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 325 --SVGKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVK-----------RDARKGLATLCIGGGQGV 385
Cdd:cd00829  296 kgEGGKLVREGDTAiggdlpVNTSGGLLSKGHPLGATG----LAQAVEAVRqlrgeagarqvPGARVGLAHNIGGTGSAA 371

                 ....
gi 446588638 386 ALTI 389
Cdd:cd00829  372 VVTI 375
PRK07516 PRK07516
thiolase domain-containing protein;
1-386 5.98e-10

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 60.35  E-value: 5.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638   1 MKEVVIVGALRTPIGcfqgtlaRHSAVELGSMVVKAL---IERTGVDANAIDEVILGQvLTAGAGQNPARQSAIKGGLPT 77
Cdd:PRK07516   1 MMTASIVGWAHTPFG-------KLDAETLESLIVRVAreaLAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  78 T--VSAITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMSRAPhvlNDSRTGALPDADNLV-DSLVHDGLWDAFnd 154
Cdd:PRK07516  73 LrfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP---TAEVGDILLGASYLKeEGDTPGGFAGVF-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 155 yhiGVTAENLAREYGisrelqdayalsSQQKARAAIdtgrfkdeivpivTQRNGQTAIVDTDEQPRADASaeglallhpa 234
Cdd:PRK07516 148 ---GRIAQAYFQRYG------------DQSDALAMI-------------AAKNHANGVANPYAQMRKDLG---------- 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 235 FDSLGSVTAGN-----------ASSINDGAAAVMMMSETKARALGLPVlaRIRAFASVG-------VDPALMGiAPVYAT 296
Cdd:PRK07516 190 FEFCRTVSEKNplvagplrrtdCSLVSDGAAALVLADAETARALQRAV--RFRARAHVNdflplsrRDPLAFE-GPRRAW 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 297 RRCLERAGWQLTEVDLIEANEAF------------------AAQALSVGKMLEWDERRVNVNGGAIALGHPIGASG---- 354
Cdd:PRK07516 267 QRALAQAGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIREGWTAKDGKLPVNPSGGLKAKGHPIGATGvsmh 346
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 446588638 355 ---CRILVSLVHEMVKRDARkgLATLCIGGGQGVA 386
Cdd:PRK07516 347 vlaAMQLTGEAGGMQIPGAK--LAGVFNMGGAAVA 379
PRK12578 PRK12578
thiolase domain-containing protein;
28-368 1.53e-09

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 59.09  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  28 ELGSMVVKALIERTGVDANAIDEVILGQVLTAGAGQNPA----RQSAIKGGLPTTVSAitindVCGSGLKALHLATQAIQ 103
Cdd:PRK12578  23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPApivaEYSGLTGKVPLRVEA-----MCATGLAASLTAYTAVA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 104 CGEADIVIAGGQENMSRAphvlnDSRTgalpdadnlvdSLVHDG-----LWD------AFNDYHIGVTAENLAReYGISR 172
Cdd:PRK12578  98 SGLVDMAIAVGVDKMTEV-----DTST-----------SLAIGGrggnyQWEyhfygtTFPTYYALYATRHMAV-YGTTE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 173 ElQDAYALSSQQKARAAIDTGRFKDEIVpivtqrngqtaivdTDEQPRADASAEGLALLhpafdslgsvtagNASSINDG 252
Cdd:PRK12578 161 E-QMALVSVKAHKYGAMNPKAHFQKPVT--------------VEEVLKSRAISWPIKLL-------------DSCPISDG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 253 AAAVMMMSETKARALGL--PVLARIRAFASvgvDPALMGI--------APVYATRRCLERAGWQLTEVDLIEANEAFA-A 321
Cdd:PRK12578 213 SATAIFASEEKVKELKIdsPVWITGIGYAN---DYAYVARrgewvgfkATQLAARQAYNMAKVTPNDIEVATVHDAFTiA 289
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446588638 322 QALSV-----------GKMLEWDERR------VNVNGGAIALGHPIGASGcrilVSLVHEMVKR 368
Cdd:PRK12578 290 EIMGYedlgftekgkgGKFIEEGQSEkggkvgVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
PRK08256 PRK08256
lipid-transfer protein; Provisional
34-354 1.78e-05

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 46.43  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638  34 VKALIERTGVDANAIDEVILGQVltagAGQNPARQSAIKGGLPTTVSAITINDVCGSGLKALHLATQAIQCGEADIVIAG 113
Cdd:PRK08256  30 GRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALYEVGMTGIPIVNVNNNCSTGSTALFLARQAVRSGAADCALAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 114 GQENMSraPHVLN---DSRTGALPDADNLVDSLVhdglwdafndyhiGVTAENLAREY--GISRELQDAYALSSQQKARA 188
Cdd:PRK08256 106 GFEQMQ--PGALGsvwDDRPSPLERFDKALAELQ-------------GFDPAPPALRMfgGAGREHMEKYGTTAETFAKI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 189 AIDTGR---------FKDEIvpivtqrngqtaivdTDEQPRADAsaeglallhPAFDSLgsvTAGNASSINDGAAAVMMM 259
Cdd:PRK08256 171 GVKARRhaannpyaqFRDEY---------------TLEDVLASP---------MIWGPL---TRLQCCPPTCGAAAAIVC 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 260 SETKARALGLPVLARIRA------FAS----------VGVDPALMGIAPVYatrrclERAGWQLTEVDLIEANEAFAAQA 323
Cdd:PRK08256 224 SEEFARKHGLDRAVEIVAqamttdTPStfdgrsmidlVGYDMTRAAAQQVY------EQAGIGPEDIDVVELHDCFSANE 297
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446588638 324 L------------SVGKMLEWDER----RVNVN--GGAIALGHPIGASG 354
Cdd:PRK08256 298 LltyealglcpegEAEKFIDDGDNtyggRWVVNpsGGLLSKGHPLGATG 346
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
81-114 3.29e-05

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 44.93  E-value: 3.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 446588638   81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGG 199
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
81-114 4.67e-05

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 45.24  E-value: 4.67e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446588638  81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:cd00833  163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
PRK07937 PRK07937
lipid-transfer protein; Provisional
176-354 2.04e-04

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 43.14  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 176 DAYALSSQQkARAAIDTGRFKDEIVPIVTQRNgqtaivdtdeqpRADASAEGLALLHPAFDSLGS-------VTAGNASS 248
Cdd:PRK07937 137 DSVSMAGLQ-ARAGLDAGKWTEEQMAEVAARS------------RADARRNPSAEPSISVDELLArpyfadpLRRHDIAP 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 249 INDGAAAVMMMSETKARALgLPVLARIRAFASvGVDPALMG---IAPVYATRRCLERA-GWQLTEVDLIEANEAFAAQAL 324
Cdd:PRK07937 204 ITDGAAAVVLAAGDRAREL-RERPAWITGIEH-RIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQEL 281
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446588638 325 SVGKMLEWDER-RVNVNGGAIAlGHPIGASG 354
Cdd:PRK07937 282 ILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
81-114 2.80e-04

Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 214836 [Multi-domain]  Cd Length: 298  Bit Score: 42.32  E-value: 2.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 446588638    81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:smart00825  90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
223-381 7.00e-04

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 41.60  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 223 ASAEGLALLHPAF---DSLGSVTAG-----NASSINDGAAAVMMMSETKARAL-GLPVLARIRAFasvGVDPALMGIAPV 293
Cdd:PRK06289 188 AQTRGWAFPDEATnddDATNPVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQK 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 294 YA-----------TRRCLE----RAGWQLTEVDLIEANEAFAA------------------QALSVGKMLEWDERRVNVN 340
Cdd:PRK06289 265 LDrsagdpyvlphVRQAVLdayrRAGVGLDDLDGFEVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPS 344
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446588638 341 GGAIALGHPIGASGCRILVSLVHEMVKR-------DARKGLaTLCIGG 381
Cdd:PRK06289 345 GGLIGGGHPVGASGVRMLLDAAKQVTGTagdyqveGAKTFG-TLNIGG 391
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
82-119 7.65e-04

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 41.27  E-value: 7.65e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446588638  82 ITINDVCGSGLKALHLATQAIQCGEADIVIAGGQENMS 119
Cdd:cd00828  156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
71-116 1.28e-03

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: 40.46  E-value: 1.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446588638  71 IKGGLPTTVSAitindvCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:COG0304  150 LKGPNYTVSTA------CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
81-114 1.43e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.01  E-value: 1.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 446588638   81 AITINDVCGSGLKALHLATQAIQCGEADIVIAGG 114
Cdd:COG3321   167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
252-354 2.15e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 40.10  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 252 GAAAVMMMSETK--ARALGLPVLARIRA-------FASVGVDPAlmGIAPVYATRRCLERAGWQLTEVDLIEANeafaAQ 322
Cdd:PRK07910 241 GEGGALMVIETEehAKARGANILARIMGasitsdgFHMVAPDPN--GERAGHAMTRAIELAGLTPGDIDHVNAH----AT 314
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446588638 323 ALSVGKMLE-------WDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK07910 315 GTSVGDVAEgkainnaLGGHRPAVYAPKSALGHSVGAVG 353
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
229-354 3.57e-03

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 39.06  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 229 ALLHP----AFDSLGSVTAGN-----AS----------SINDGAAAVMMMSETKARALGLPVLARIRAFASVG-----VD 284
Cdd:cd00834  190 ALITPltlaGFAALRALSTRNddpekASrpfdkdrdgfVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTA 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 285 PALMGIAPVYATRRCLERAGWQLTEVDLIEA----------NEAFAAQALsvgkMLEWDER-RVNVNGGAIalGHPIGAS 353
Cdd:cd00834  270 PDPDGEGAARAMRAALADAGLSPEDIDYINAhgtstplndaAESKAIKRV----FGEHAKKvPVSSTKSMT--GHLLGAA 343

                 .
gi 446588638 354 G 354
Cdd:cd00834  344 G 344
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
71-116 3.93e-03

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 39.06  E-value: 3.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446588638  71 IKGGLPTTVSAitindvCGSGLKALHLATQAIQCGEADIVIAGGQE 116
Cdd:cd00834  150 LRGPNYTVSTA------CASGAHAIGDAARLIRLGRADVVIAGGAE 189
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
247-365 4.93e-03

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 38.72  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 247 SSINDGAAAVMMMSETKARALGLP--------VLARIRAFASVGVDP--ALMGIAPVYATRRCLERAGWQLTEVDLIEAN 316
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSpndsrlveIKSLACASGNLYEDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446588638 317 EAFAA------QALSV------------GKMLEWDERRVNVNGGAIALGHPIGASGCRILVSLVHEM 365
Cdd:PTZ00455 336 DCFTIaellmyEALGIaeyghakdlirnGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
251-354 9.05e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 37.72  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446588638 251 DGAAAVMMMSETKARALGLPVLARIRAF-----ASVGVDPALMGIAPVYATRRCLERAGWQLTEVDLIEA-------NEA 318
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446588638 319 FAAQALSvgkmlEWDERRVNVNGGAIALGHPIGASG 354
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
 
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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