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Conserved domains on  [gi|872564445|ref|WP_048530803|]
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MULTISPECIES: acetyl-CoA C-acetyltransferase [Bacillus]

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
1-391 0e+00

putative acyltransferase; Provisional


:

Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 631.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDT-VWEVLEDPIHHIMMGET 159
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTmIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAGLKPAFRKGG 238
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
 
Name Accession Description Interval E-value
PRK05790 PRK05790
putative acyltransferase; Provisional
1-391 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 631.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDT-VWEVLEDPIHHIMMGET 159
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTmIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAGLKPAFRKGG 238
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
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: 608.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLqHGEIRDT-VWEVLEDPIHHIMMGET 159
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPmINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGS 239
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 240 VTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFA 319
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564445 320 AQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-390 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: 605.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   5 VITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYTI 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  85 QRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVWEVLEDPIHHIMMGETAENLV 164
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 165 EQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVTAGN 244
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 245 ASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLA 324
Cdd:cd00751  241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564445 325 VEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEA 390
Cdd:cd00751  321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-389 0e+00

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: 522.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445    6 ITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYTIQ 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   86 RQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQ-HRWGQRLQHGEIRDTVWEVLEDPIHHIMMGETAENLV 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRsLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  165 EQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVTAGN 244
Cdd:TIGR01930 161 KKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  245 ASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLA 324
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564445  325 VEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:TIGR01930 321 CIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-261 5.87e-102

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: 302.30  E-value: 5.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445    4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQH-RWGQRLQHGEIRD-TVWEVLEDPIHHIMMGETAE 161
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDlLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  162 NLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVT 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
                         250       260
                  ....*....|....*....|
gi 872564445  242 AGNASGLNDGSAVLVLMSEE 261
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PRK05790 PRK05790
putative acyltransferase; Provisional
1-391 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 631.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDT-VWEVLEDPIHHIMMGET 159
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTmIHDGLTDAFNGYHMGIT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAGLKPAFRKGG 238
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
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: 608.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLqHGEIRDT-VWEVLEDPIHHIMMGET 159
Cdd:COG0183   81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPmINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGS 239
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 240 VTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFA 319
Cdd:COG0183  240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564445 320 AQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:COG0183  320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-390 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: 605.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   5 VITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYTI 84
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  85 QRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVWEVLEDPIHHIMMGETAENLV 164
Cdd:cd00751   81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 165 EQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVTAGN 244
Cdd:cd00751  161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 245 ASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLA 324
Cdd:cd00751  241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564445 325 VEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEA 390
Cdd:cd00751  321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-389 0e+00

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: 522.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445    6 ITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYTIQ 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   86 RQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQ-HRWGQRLQHGEIRDTVWEVLEDPIHHIMMGETAENLV 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRsLRWGVKPGNAELEDARLKDLTDANTGLPMGVTAENLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  165 EQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVTAGN 244
Cdd:TIGR01930 161 KKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  245 ASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLA 324
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564445  325 VEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:TIGR01930 321 CIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK09051 PRK09051
beta-ketothiolase BktB;
1-391 3.27e-179

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 503.72  E-value: 3.27e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQrTD--EANTARTAALAAGFPDT 78
Cdd:PRK09051   2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIP-TEprDMYLSRVAAINAGVPQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVWEVLEDPIHHIMMGE 158
Cdd:PRK09051  81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVGALHDPFGTIHMGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 159 TAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRK-G 237
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKeN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 238 GSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEA 317
Cdd:PRK09051 241 GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEA 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564445 318 FAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK09051 321 FAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-390 8.99e-159

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 452.13  E-value: 8.99e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVWE--VLEDPIHHIM--- 155
Cdd:PRK06205  81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLARgrETAGGRRFPVpgg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 156 MGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAGLKPAF 234
Cdd:PRK06205 161 MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPRADTTLESLAKLRPIM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 235 RK---GGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADL 311
Cdd:PRK06205 241 GKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 312 LEINEAFAAQYLAVEKELGL---DREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFI 388
Cdd:PRK06205 321 IELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVF 400

                 ..
gi 872564445 389 EA 390
Cdd:PRK06205 401 ER 402
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-389 6.39e-144

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 414.29  E-value: 6.39e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDT-----VWEVLEDpiHHim 155
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSmitdgLWDAFND--YH-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 156 MGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAGLKPAF 234
Cdd:PRK05656 157 MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEpLAFATDEQPRAGTTAESLAKLKPAF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 235 RKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEI 314
Cdd:PRK05656 237 KKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEA 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872564445 315 NEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK05656 317 NEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-389 4.03e-140

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 404.72  E-value: 4.03e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVEL-AVPVLQEAVKRGGVEPHEVDEVILGHCIQR-TDEANTARTAALAAGFPDT 78
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLgAVPLKALMARNPGVDWEAVDDVIYGCANQAgEDNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYAL-KQHRWGQRlqHGEIRDTV--WEVLeDPIHHIM 155
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMgKADSAFSR--QAEIFDTTigWRFV-NPLMKAQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 156 -----MGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-VVFSKDEHPRADITAEKLAG 229
Cdd:PRK09050 158 ygvdsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPRPETTLEALAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 230 LKPAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDA 309
Cdd:PRK09050 238 LKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 310 DLLEINEAFAAQYLAVEKELGL--DREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALF 387
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397

                 ..
gi 872564445 388 IE 389
Cdd:PRK09050 398 IE 399
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-389 9.65e-140

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 403.71  E-value: 9.65e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRD-TVWEVLEDPIHHIMMGET 159
Cdd:PRK08235  81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDlMVADGLTCAFSGVHMGVY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 160 AENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERR-KEVVFSKDEHPRADITAEKLAGLKPAFRKGG 238
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKgDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
3-391 8.39e-127

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 370.58  E-value: 8.39e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   3 NVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGY 82
Cdd:PLN02644   2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  83 TIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRD-TVWEVLEDPIHHIMMGETAE 161
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDgMLKDGLWDVYNDFGMGVCAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 162 NLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITI--KERRKEVVFSKDEHPrADITAEKLAGLKPAFRK-GG 238
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVpgGRGRPSVIVDKDEGL-GKFDPAKLRKLRPSFKEdGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-391 1.30e-126

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 370.23  E-value: 1.30e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFG-GALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEA-NTARTAALAAGFPDT 78
Cdd:PRK07661   1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPyaLKQHrwgqrlqhgEIRDTVWEVLEDPIHHIMMGE 158
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP--MMGH---------VVRPNPRLVEAAPEYYMGMGH 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 159 TAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERR---------KEVVFSKDEHPRADITAEKLAG 229
Cdd:PRK07661 150 TAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennklqeETITFSQDEGVRADTTLEILGK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 230 LKPAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDA 309
Cdd:PRK07661 230 LRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDI 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 310 DLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK07661 310 GLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389

                 ..
gi 872564445 390 AL 391
Cdd:PRK07661 390 LL 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-391 2.60e-126

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 369.72  E-value: 2.60e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTF-GGALKNVTPVELAVPVLQEAVKR-GGVEPHEVDEVILGHCIQRTDEA-NTARTAALAAGFPD 77
Cdd:PRK09052   5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQvPGLDPKLIEDAIVGCAMPEAEQGlNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  78 TVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSP-----YALKQHrwgqrlqhgeirdtVWEVLEDPIH 152
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmmgnkPSMSPA--------------IFARDENVGI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 153 HIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERR----------KEVVFSKDEHPRADI 222
Cdd:PRK09052 151 AYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 223 TAEKLAGLKPAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKV 302
Cdd:PRK09052 231 SLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 303 DWSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGI 382
Cdd:PRK09052 311 GLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGM 390

                 ....*....
gi 872564445 383 GVALFIEAL 391
Cdd:PRK09052 391 GAAGIFERL 399
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-391 1.32e-125

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 368.18  E-value: 1.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIG-TFGGALKNVTPVELAVPVLQEAV-KRGGVEPHEVDEVILGhCIQRTDEA--NTARTAALAAGFp 76
Cdd:PRK07851   1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALdKVPALDPTDIDDLMLG-CGLPGGEQgfNMARVVAVLLGY- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  77 DTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSP--------------YALKQHRWGQRLQHGeirDT 142
Cdd:PRK07851  79 DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAkgnsdslpdtknplFAEAQARTAARAEGG---AE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 143 VW----EVLEDPIHHIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKErrkEVVFSKDEHP 218
Cdd:PRK07851 156 AWhdprEDGLLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPD---GTVVSTDDGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 219 RADITAEKLAGLKPAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKG 298
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 299 LEKVDWSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCV 378
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
                        410
                 ....*....|...
gi 872564445 379 GGGIGVALFIEAL 391
Cdd:PRK07851 393 GGGQGMAMVLERL 405
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
3-390 6.59e-125

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 367.94  E-value: 6.59e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   3 NVVITAAVRSPI-GTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCI----QRtdeANTARTAALAAGFPD 77
Cdd:PLN02287  47 DVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLapgsQR---ANECRMAAFYAGFPE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  78 TVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVwevledpihhIMMG 157
Cdd:PLN02287 124 TVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCL----------LPMG 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 158 ETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIK------ERRKEVVFSKDEHPRADITAEKLAGLK 231
Cdd:PLN02287 194 ITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktGEEKPIVISVDDGIRPNTTLADLAKLK 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 232 PAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADL 311
Cdd:PLN02287 274 PVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 312 LEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEK--GIASLCVGGGIGVALFIE 389
Cdd:PLN02287 354 FEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDCrfGVVSMCIGTGMGAAAVFE 433

                 .
gi 872564445 390 A 390
Cdd:PLN02287 434 R 434
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
4-391 1.33e-121

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 357.42  E-value: 1.33e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:PRK06633   5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSsspyaLKQH----RWGQRLQHGEIRDTV-WEVLEDPIHHIMMGE 158
Cdd:PRK06633  85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-----LGMHgsyiRAGAKFGDIKMVDLMqYDGLTDVFSGVFMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 159 TAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGG 238
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAF 318
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 319 AAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-389 3.92e-120

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 353.64  E-value: 3.92e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFG------GALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGhCIQRTDEANT--ARTAALA 72
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITG-CALQVGENWLygGRHPIFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  73 AGFPDTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYalkqhrwgQRLQHGEIRDTVwevLEDP-- 150
Cdd:PRK06445  80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPM--------GDNPHIEPNPKL---LTDPky 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 151 IHHIM-----MGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAE 225
Cdd:PRK06445 149 IEYDLttgyvMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 226 KLAGLKPAFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWS 305
Cdd:PRK06445 229 KLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLS 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 306 LEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVA 385
Cdd:PRK06445 309 VKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGA 388

                 ....
gi 872564445 386 LFIE 389
Cdd:PRK06445 389 VVLE 392
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-389 6.36e-118

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 347.72  E-value: 6.36e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIG-TFGGALKNVTPVELAVPVLQEAVKRG-GVEPHEVDEVILGhCIQRTDEA--NTARTAALAAGFP 76
Cdd:PRK08947   1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWG-CVQQTLEQgfNIARNAALLAGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  77 DTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPyalkqhrwgqrLQHGeirdtvweVLEDP--IHHI 154
Cdd:PRK08947  80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG--------VDFHPglSKNV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 155 -----MMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPItikERRKE----VVFSKDEHPRADITAE 225
Cdd:PRK08947 141 akaagMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPT---EGHDAdgvlKLFDYDEVIRPETTVE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 226 KLAGLKPAFR-KGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDW 304
Cdd:PRK08947 218 ALAALRPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 305 SLEDADLLEINEAFAAQYLAVEKELGL-DR--EKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGG 381
Cdd:PRK08947 298 SISDIDVFELNEAFAAQSLPCLKDLGLlDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLG 377

                 ....*...
gi 872564445 382 IGVALFIE 389
Cdd:PRK08947 378 QGIATVFE 385
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-391 4.57e-114

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 339.30  E-value: 4.57e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK08170   2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQH--RW----------GQRLQH-GEIRD------ 141
Cdd:PRK08170  82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvRWlagwyaaksiGQKLAAlGKLRPsylapv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 142 -TVWEVLEDPIHHIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDdQIVPITikeRRKEVVFSKDEHPRA 220
Cdd:PRK08170 162 iGLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF---DRDGKFYDHDDGVRP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 221 DITAEKLAGLKPAF-RKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGL 299
Cdd:PRK08170 238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 300 EKVDWSLEDADLLEINEAFAAQYLA----------------VEKELG-LDREKVNVNGSGVGLGHPIGCTGARITVSLIH 362
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLAclaawadeeycreqlgLDGALGeLDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
                        410       420
                 ....*....|....*....|....*....
gi 872564445 363 ELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
4-389 2.38e-109

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 326.46  E-value: 2.38e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRDTVW-EVLEDPIHH-IMMGETAE 161
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFlDGLEDAYDKgRLMGTFAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 162 NLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRAdITAEKLAGLKPAFRKGGSVT 241
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGTVT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 242 AGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQ 321
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564445 322 YLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-389 3.38e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 318.37  E-value: 3.38e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTF--GGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGhCIQRTDE--ANTARTAALAAGFP 76
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGkkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLG-CVTPVGDqgADIARTAVLAAGLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  77 DTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQrlqhgeirdtvwevleDP-----I 151
Cdd:PRK08242  80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAM----------------DPstnfpT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 152 HHIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPItiKERRKEVVFSKDEHPRADITAEKLAGLK 231
Cdd:PRK08242 144 YFVPQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMRPGTTMESLAKLK 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 232 PAFRKGGSV---------------------TAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIG 290
Cdd:PRK08242 222 PSFAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 291 PAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLE 370
Cdd:PRK08242 302 PVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKR 381
                        410
                 ....*....|....*....
gi 872564445 371 KGIASLCVGGGIGVALFIE 389
Cdd:PRK08242 382 TALITLCVGGGMGIATIIE 400
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-391 1.53e-105

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 315.88  E-value: 1.53e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEA-NTARTAALAAGFPDTV 79
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAgNIARTSWLAAGLPEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  80 TGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMS----------------SSPYALKQHrWGQRLQHGEIRDTV 143
Cdd:PRK07801  81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSqipissamtageqlgfTSPFAESKG-WLHRYGDQEVSQFR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 144 wevledpihhimmgeTAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITikerrkevVFSKDEHPRaDIT 223
Cdd:PRK07801 160 ---------------GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG--------GVTVDEGPR-ETS 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 224 AEKLAGLKPaFRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVD 303
Cdd:PRK07801 216 LEKMAGLKP-LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTG 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 304 WSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIG 383
Cdd:PRK07801 295 LSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTA 374

                 ....*...
gi 872564445 384 VALFIEAL 391
Cdd:PRK07801 375 NVTIIERL 382
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-389 2.19e-105

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 316.33  E-value: 2.19e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQR-TDEANTARTAALAAGFPDTV 79
Cdd:PRK08131   1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAgEDSRNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  80 TGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYAL--KQHRWGQRLqhgEIRDTVW-------EVLEDP 150
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMgkAESAFSRDA---KVFDTTIgarfpnpKIVAQY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 151 IHHiMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRK--EVVFSKDEHPRADITAEKLA 228
Cdd:PRK08131 158 GND-SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlpPKLVAEDEHPRPSSTVEALT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 229 GLKPAFrKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLED 308
Cdd:PRK08131 237 KLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 309 ADLLEINEAFAAQYLAVEKELGL--DREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVAL 386
Cdd:PRK08131 316 MDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAM 395

                 ...
gi 872564445 387 FIE 389
Cdd:PRK08131 396 VIE 398
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-261 5.87e-102

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: 302.30  E-value: 5.87e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445    4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQH-RWGQRLQHGEIRD-TVWEVLEDPIHHIMMGETAE 161
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDlLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  162 NLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPRADITAEKLAGLKPAFRKGGSVT 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
                         250       260
                  ....*....|....*....|
gi 872564445  242 AGNASGLNDGSAVLVLMSEE 261
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-389 2.69e-99

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 300.39  E-value: 2.69e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVT 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQH-RWG-QRLQHG--EIRDTVW-EVLEDPIHHIM 155
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDlRWGpKHLLHKnyKIDDAMLvDGLIDAFYFEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 156 MGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITikerrkevVFSKDEHPRaDITAEKLAGLKPAFR 235
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIR-KTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 236 KGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEIN 315
Cdd:PRK06366 232 KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564445 316 EAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-391 4.30e-98

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 297.45  E-value: 4.30e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIG-TFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGhCI--QRTDEANTARTAALAAGFPD 77
Cdd:PRK07108   1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMG-CAnpEGATGANIARQIALRAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  78 TVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRwgqrLQHGeirdtvWEVLEDPIHHIMMG 157
Cdd:PRK07108  80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHM----LREG------WLVEHKPEIYWSML 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 158 ETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKE----------RRKEVVFSKDEHPRADITAEKL 227
Cdd:PRK07108 150 QTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAgvadkatgrlFTKEVTVSADEGIRPDTTLEGV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 228 AGLKPAFrKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLE 307
Cdd:PRK07108 230 SKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 308 DADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALF 387
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGL 388

                 ....
gi 872564445 388 IEAL 391
Cdd:PRK07108 389 FEVL 392
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-391 9.75e-98

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 295.52  E-value: 9.75e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   3 NVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKrgGVEpHEVDEVILGHCIQRTdeANTARTAALAAGFPDTVTGY 82
Cdd:PRK06690   2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLSK--GME-REIDDVILGNVVGPG--GNVARLSALEAGLGLHIPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  83 TIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYAlKQHRWGQrlqhgeirdtvwEVLEDPihhiMMGETAEN 162
Cdd:PRK06690  77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ-NRARFSP------------ETIGDP----DMGVAAEY 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 163 LVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPIT-------IKERRKEVVFSKdehpraditaeklagLKPAFR 235
Cdd:PRK06690 140 VAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNglldesiKKEMNYERIIKR---------------TKPAFL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 236 KGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEIN 315
Cdd:PRK06690 205 HNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEIN 284
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564445 316 EAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK06690 285 EAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
4-390 4.01e-94

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 288.42  E-value: 4.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYAL------------KQHRWGQRL---QHGEIRD--TVWEV 146
Cdd:PRK08963  87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskklaralvdlnKARTLGQRLklfSRLRLRDllPVPPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 147 LEDPIHHIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKevVFSKDEHPRADITAEK 226
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--PLEEDNNIRGDSTLED 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 227 LAGLKPAF-RKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDP-KIMGIGPAPAIRKGLEKVDW 304
Cdd:PRK08963 245 YAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 305 SLEDADLLEINEAFAAQYLA----------VEKELG-------LDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRR 367
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
                        410       420
                 ....*....|....*....|...
gi 872564445 368 GLEKGIASLCVGGGIGVALFIEA 390
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLEV 427
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-389 4.75e-92

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 281.61  E-value: 4.75e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVIlGHCIQRTDEA--NTARTAALAAGFPDT 78
Cdd:PRK07850   1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVI-GGCVTQAGEQsnNITRTAWLHAGLPYH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSP--YALKQHRwgqrlqhGEIRDTVWEvLEDPIHHimm 156
Cdd:PRK07850  80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPlgANAGPGR-------GLPRPDSWD-IDMPNQF--- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 157 gETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKE-------VVFSKDEHPRaDITAEKLAG 229
Cdd:PRK07850 149 -EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEgqptgetRLVTRDQGLR-DTTMEGLAG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 230 LKPAfRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDA 309
Cdd:PRK07850 227 LKPV-LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDI 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 310 DLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK07850 306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-391 1.02e-89

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 275.84  E-value: 1.02e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGhCIQRTDE--ANTARTAALAAGFPDT 78
Cdd:PRK06504   1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMG-CVSQVGEqaTNVARNAVLASKLPES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKqhrwGQRLQHGEIRDTVWEVLEDPIHHIM--- 155
Cdd:PRK06504  80 VPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP----STLPAKNGLGHYKSPGMEERYPGIQfsq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 156 -MGetAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSK-DEHPRADITAEKLAGLKPa 233
Cdd:PRK06504 156 fTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIRFDATLEGIAGVKL- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 234 FRKGGSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLE 313
Cdd:PRK06504 233 IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872564445 314 INEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEAL 391
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-389 1.44e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 258.17  E-value: 1.44e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSP--IGTFG-GALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEA-NTARTAALAAGFP 76
Cdd:PRK06025   1 MAEAYIIDAVRTPrgIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  77 DTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMS-SSPYALKQHRWGQ---RLQHGEIRDTVwevlEDPIH 152
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKpplGMGSGNLRLRA----LHPQS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 153 HimMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRkeVVFSKDEHPRADITAEKLAGLKP 232
Cdd:PRK06025 157 H--QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGS--VALDHEEFPRPQTTAEGLAALKP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 233 AFRK-------------GGSVT-------------AGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVDPKI 286
Cdd:PRK06025 233 AFTAiadyplddkgttyRGLINqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 287 MGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGHPIGCTGARITVSLIHELKR 366
Cdd:PRK06025 313 MLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELER 392
                        410       420
                 ....*....|....*....|...
gi 872564445 367 RGLEKGIASLCVGGGIGVALFIE 389
Cdd:PRK06025 393 RGLKRGLVTMCAAGGMAPAIIIE 415
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
4-390 6.05e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 241.34  E-value: 6.05e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   4 VVITAAVRSPIGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYT 83
Cdd:PRK09268   9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  84 IQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYAL-KQHRW-----------GQRLQH-GEIR--DTVWEV-- 146
Cdd:PRK09268  89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVnEGLRKillelnrakttGDRLKAlGKLRpkHLAPEIpr 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 147 LEDPIHHIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERrkevvfskDEHPRADITAEK 226
Cdd:PRK09268 169 NGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLRPDSSLEK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 227 LAGLKPAFRKG--GSVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAGVD----PKIMGIGPAPAIRKGLE 300
Cdd:PRK09268 241 LAKLKPVFGKGgrATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGLLMAPAYAVPRLLA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 301 KVDWSLEDADLLEINEAFAAQYLAVEK----------ELGL-------DREKVNVNGSGVGLGHPIGCTGARITVSLIHE 363
Cdd:PRK09268 321 RNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLdaplgsiDRSKLNVNGSSLAAGHPFAATGGRIVATLAKL 400
                        410       420
                 ....*....|....*....|....*..
gi 872564445 364 LKRRGLEKGIASLCVGGGIGVALFIEA 390
Cdd:PRK09268 401 LAEKGSGRGLISICAAGGQGVTAILER 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
8-389 2.00e-67

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: 218.52  E-value: 2.00e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   8 AAVRSPIGTFGG---ALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTGYTI 84
Cdd:cd00826    2 GAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  85 QRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHrwgqrlqhgeirdtvWEVledpihhimmgetaENLV 164
Cdd:cd00826   82 NNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKE---------------KHI--------------DVLI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 165 EQYEiTREEQDEVALRSHTLALKAIESGYFDDQIVPITIKERRKEVVFSKDEHPR--ADITAEKLAGLKPAFRKGGSVTA 242
Cdd:cd00826  133 NKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 243 GNASGLNDGSAVLVLMSEEKA-------KEKGLQPLARIVGYSVAGVDPK----IMGIGPAPAIRKGLEKVDWSLEDADL 311
Cdd:cd00826  212 GNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 312 LEINEAFAAQYLAVEKELGLDREK------------------VNVNGSGVGLGHPIGCTGARITVSLIHELKRR-----G 368
Cdd:cd00826  292 IEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEagkrqG 371
                        410       420
                 ....*....|....*....|.
gi 872564445 369 LEKGIASLCVGGGIGVALFIE 389
Cdd:cd00826  372 AGAGLALLCIGGGGGAAMCIE 392
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
268-390 1.14e-60

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: 191.70  E-value: 1.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  268 LQPLARIVGYSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFAAQYLAVEKELGLDREKVNVNGSGVGLGH 347
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 872564445  348 PIGCTGARITVSLIHELKRRGLEKGIASLCVGGGIGVALFIEA 390
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
242-388 4.95e-24

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: 99.83  E-value: 4.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 242 AGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSV----AGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEA 317
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 318 FAAQYLAVEKELGLDREKVNVNGSGVGL---GHPIGCTGARITVSLIHELK-------RRGLEKGIASLCVGGGIGVALF 387
Cdd:cd00327  174 GTPIGDAVELALGLDPDGVRSPAVSATLimtGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253

                 .
gi 872564445 388 I 388
Cdd:cd00327  254 L 254
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
23-367 1.16e-21

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: 95.41  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  23 NVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDTVTgYTIQRQCSSGMQAIMSAAMQI 102
Cdd:cd00829   13 DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGKPA-TRVEAAGASGSAAVRAAAAAI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 103 QLGVSDVVIAGGVEAMSSSPYAlkqHRWGQRLQHGEIRDtvWEVLEDPIHHIMMGETAENLVEQYEITREEQDEVALRSH 182
Cdd:cd00829   92 ASGLADVVLVVGAEKMSDVPTG---DEAGGRASDLEWEG--PEPPGGLTPPALYALAARRYMHRYGTTREDLAKVAVKNH 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 183 TLALKaiesgyfddqivpitikerrkevvfskdeHPRA----DITAEKLAGLKPAfrkGGSVTAGNASGLNDGSAVLVLM 258
Cdd:cd00829  167 RNAAR-----------------------------NPYAqfrkPITVEDVLNSRMI---ADPLRLLDCCPVSDGAAAVVLA 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 259 SEEKAKEKGLQPlARIVG-------YSVAGVDPKIMGIGPAPAIRKGLEKVDWSLEDADLLEINEAFA-AQYLAVEkELG 330
Cdd:cd00829  215 SEERARELTDRP-VWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTiAELLALE-DLG 292
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 872564445 331 LDRE------------------KVNVNGSGVGLGHPIGCTGARITVSLIHELKRR 367
Cdd:cd00829  293 FCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGE 347
PRK12578 PRK12578
thiolase domain-containing protein;
19-367 1.15e-10

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 62.56  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  19 GALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFpdtvTGYT---IQRQCSSGMQAI 95
Cdd:PRK12578  14 GRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGL----TGKVplrVEAMCATGLAAS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  96 MSAAMQIQLGVSDVVIAGGVEAMS-------------SSPYALKQHRWGQRLqhgeirdtvwevledPIHHIMMgetAEN 162
Cdd:PRK12578  90 LTAYTAVASGLVDMAIAVGVDKMTevdtstslaiggrGGNYQWEYHFYGTTF---------------PTYYALY---ATR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 163 LVEQYEITREEQDEVALRSHTLALKAiESGYFDDqivPITIKERRKEVVFSkdeHPraditaeklaglkpafrkggsVTA 242
Cdd:PRK12578 152 HMAVYGTTEEQMALVSVKAHKYGAMN-PKAHFQK---PVTVEEVLKSRAIS---WP---------------------IKL 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 243 GNASGLNDGSAVLVLMSEEKAKEKGLQPLARI--VGYS--VAGVDPKIMGIG---PAPAIRKGLEKVDWSLEDADLLEIN 315
Cdd:PRK12578 204 LDSCPISDGSATAIFASEEKVKELKIDSPVWItgIGYAndYAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVH 283
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872564445 316 EAFA-AQYLAVEkELGLDRE----------------KVNVNGSGvGL---GHPIGCTGaritVSLIHELKRR 367
Cdd:PRK12578 284 DAFTiAEIMGYE-DLGFTEKgkggkfieegqsekggKVGVNLFG-GLkakGHPLGATG----LSMIYEITKQ 349
PRK06064 PRK06064
thiolase domain-containing protein;
1-385 1.92e-10

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 61.84  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   1 MHNVVITAAVRSPIGTfggaLKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCI--QRTDEANTARTAALAAGFPDt 78
Cdd:PRK06064   1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAP- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  79 VTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPY-----ALkqhrwgqrlqhGEIRDTVWEVledpihh 153
Cdd:PRK06064  76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTpdateAI-----------ARAGDYEWEE------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 154 iMMGET--------AENLVEQYEITREEQDEVALRSHTLALKAIESGYfddqivpitikerRKEVvfSKDEHPRADITAE 225
Cdd:PRK06064 138 -FFGATfpglyaliARRYMHKYGTTEEDLALVAVKNHYNGSKNPYAQF-------------QKEI--TVEQVLNSPPVAD 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 226 KLAGLkpafrkggsvtagNASGLNDGSAVLVLMSEEKAKEKGLQPLaRIVGYSVAGvD-------PKIMGIGPAP-AIRK 297
Cdd:PRK06064 202 PLKLL-------------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQAS-DtialhdrKDFTTLDAAVvAAEK 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 298 GLEKVDWSLEDADLLEINEAFA-AQYLAVEkELG---------LDRE-------KVNVNGSGvGL---GHPIGCTGARIT 357
Cdd:PRK06064 267 AYKMAGIEPKDIDVAEVHDCFTiAEILAYE-DLGfakkgeggkLAREgqtyiggDIPVNPSG-GLkakGHPVGATGVSQA 344
                        410       420
                 ....*....|....*....|....*...
gi 872564445 358 VSLIHELKRRGlEKGIASLcVGGGIGVA 385
Cdd:PRK06064 345 VEIVWQLRGEA-EKGRQQV-IGAGYGLT 370
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
29-120 2.95e-08

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: 55.24  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  29 LAVPVLQEAVKRGGVEPHEVDE----VILGHCI--QRTDEANTAR----------------------TAALAAGFPDTVT 80
Cdd:cd00834   74 FALAAAEEALADAGLDPEELDPerigVVIGSGIggLATIEEAYRAllekgprrvspffvpmalpnmaAGQVAIRLGLRGP 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 872564445  81 GYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSS 120
Cdd:cd00834  154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
88-120 1.32e-06

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: 50.09  E-value: 1.32e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 872564445  88 CSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSS 120
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
PRK08256 PRK08256
lipid-transfer protein; Provisional
88-353 1.96e-06

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 49.51  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  88 CSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMssSPYALKQHrWGQRLQ----HGEIRDTVWEVLEDPIHHIMMGETAENL 163
Cdd:PRK08256  80 CSTGSTALFLARQAVRSGAADCALALGFEQM--QPGALGSV-WDDRPSplerFDKALAELQGFDPAPPALRMFGGAGREH 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 164 VEQYEITREeqdevalrshTLAlkaiesgyfddqivPITIKERRKEV-----VFskdehpRADITAEKLAGLKPAFrkgG 238
Cdd:PRK08256 157 MEKYGTTAE----------TFA--------------KIGVKARRHAAnnpyaQF------RDEYTLEDVLASPMIW---G 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 239 SVTAGNASGLNDGSAVLVLMSEEKAKEKGLQPLARIVGYSV--------AGVDP-KIMGIG-PAPAIRKGLEKVDWSLED 308
Cdd:PRK08256 204 PLTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMttdtpstfDGRSMiDLVGYDmTRAAAQQVYEQAGIGPED 283
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872564445 309 ADLLEINEAFAAQYLAVEKELGLDRE----------------KVNVNGSGvGL---GHPIGCTG 353
Cdd:PRK08256 284 IDVVELHDCFSANELLTYEALGLCPEgeaekfiddgdntyggRWVVNPSG-GLlskGHPLGATG 346
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
28-124 2.63e-06

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 48.87  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  28 ELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDT-VTgyTIQRQCSSGMQAIMSAAMQIQLGV 106
Cdd:PRK06157  29 DLMVEAFLEALADAGIEPKDIDAAWFGTHYDEIGSGKSGTPLSRALRLPNIpVT--RVENFCATGSEAFRGAVYAVASGA 106
                         90
                 ....*....|....*...
gi 872564445 107 SDVVIAGGVEAMSSSPYA 124
Cdd:PRK06157 107 YDIALALGVEKLKDTGYG 124
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
248-354 1.51e-05

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 46.71  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 248 LNDGSAVLVLMSEEKAKEKGLQPLARIVGYSVAG-----VDPKIMGIGPAPAIRKGLEKVDWSLEDADLL-------EIN 315
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstPAG 309
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 872564445 316 EAFAAQylAVEKELGLDREKVNVNGSGVGLGHPIGCTGA 354
Cdd:PRK07314 310 DKAETQ--AIKRVFGEHAYKVAVSSTKSMTGHLLGAAGA 346
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
19-365 4.78e-05

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 45.27  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  19 GALKNVTPVELAVPVLQEAVKRGGVEPHE--VDEVILGHCIQR--TDEANTARTAALAAGFPDTVTG------YTIQRQC 88
Cdd:PTZ00455  41 GKKENKTLEELLATAIQGTLENTGLDGKAalVDKVVVGNFLGElfSSQGHLGPAAVGSLGQSGASNAllykpaMRVEGAC 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  89 SSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSSSPYALKQHRWGQRLQHGEIRdtvweVLEDPIHHIMMGETAENLVEQYE 168
Cdd:PTZ00455 121 ASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYRRQR-----KLDDFTFPCLFAKRMKYIQEHGH 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 169 ITREEQDEVALrshtlalKAIESGYFDdqivPITIKERRKevvFSKDEHPRADITAEKLAG---LKPAFRkggsvtAGNA 245
Cdd:PTZ00455 196 FTMEDTARVAA-------KAYANGNKN----PLAHMHTRK---LSLEFCTGASDKNPKFLGnetYKPFLR------MTDC 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 246 SGLNDGSAVLVLMSEEKAKEKGLQP----LARIVGYSVAG-------VDPKIMGIGPAPAiRKGLEKVDWSLEDADLLEI 314
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASgnlyedpPDATRMFTSRAAA-QKALSMAGVKPSDLQVAEV 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872564445 315 NEAFAAQYLAVEKELG------------------LDREKVNVNGSGVGLGHPIGCTGARITVSLIHELK 365
Cdd:PTZ00455 335 HDCFTIAELLMYEALGiaeyghakdlirngatalEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
PRK06066 PRK06066
thiolase domain-containing protein;
78-353 8.63e-05

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 44.36  E-value: 8.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  78 TVTGytiqrqcsSGMQAIMSAAMQIQLGVSDVVIaggVEAmssspyalkqhrwgqrlqHGEIRD--TVWEVLE---DPIH 152
Cdd:PRK06066  83 TVAG--------DGLQGLAHAVMHINSGLANVVV---VEA------------------HSKPSDilTFSDVVKfamDPIY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 153 ---------HIMMGETAENLVEQYEITREEQDEVALRSHTLALKAIESGYfddqIVPITIKE-RRKEVVFskDEHPRADI 222
Cdd:PRK06066 134 vrpigppnpHFIAGLDAVKFMSRKGITREDLALVVEKNKKAGLSNPRASY----ASNISLEDvLSSEYVV--YPLTELDI 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 223 taeklaglkpafrkggsvtagnaSGLNDGSAVLVLMSEEKAKEKGLQPL-ARIVGYSVAGVDPKIMGIGPAPAIRKG--- 298
Cdd:PRK06066 208 -----------------------APFVDGAIVVVLASEEVAKKLTDDPVwIKGIGWSTESSNLETAELGKANYMRIAadm 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872564445 299 ---LEKVDWSLEDADLLEINEAFAAQYLAVEKELGLDRE------------------KVNVNGSGVGLGHPIGCTG 353
Cdd:PRK06066 265 aykMAGIESPRKEVDAAEVDDRYSYKELQHIEALRLSEEpekdsllregnfdpqgelPVNPSGGHLAKGVPLEASG 340
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
246-356 8.66e-05

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 44.29  E-value: 8.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 246 SGLNDGSAVLVLMSEEKAKE-KGLQPLARIVGY--SVAGV--DPKIMGIGPAP--------AIRKGLEKVDWSLEDADLL 312
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDyADARPIPRIKGWghRTAPLglEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDLDGF 299
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872564445 313 EINEAF-AAQYLAVEkELGLD------------------REKVNVNGSGVGLGHPIGCTGARI 356
Cdd:PRK06289 300 EVHDCFtPSEYLAID-HIGLTgpgeswkaiengeiaiggRLPINPSGGLIGGGHPVGASGVRM 361
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
88-120 2.86e-04

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 42.85  E-value: 2.86e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 872564445  88 CSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSS 120
Cdd:PRK07314 162 CATGAHAIGDAARLIAYGDADVMVAGGAEAAIT 194
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
29-120 2.97e-04

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: 41.85  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445   29 LAVPVLQEAVKRGGVEPHEVDE----VILGHCIQRTDEANTAR-TAALAAGFPDTVTG-------------------YTI 84
Cdd:pfam00109  90 LLLEAAWEALEDAGITPDSLDGsrtgVFIGSGIGDYAALLLLDeDGGPRRGSPFAVGTmpsviagrisyflglrgpsVTV 169
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 872564445   85 QRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMSS 120
Cdd:pfam00109 170 DTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLT 205
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
82-115 8.72e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 40.98  E-value: 8.72e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 872564445  82 YTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGV 115
Cdd:PRK09185 154 YTISTACSSSAKVFASARRLLEAGLCDAAIVGGV 187
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
14-115 5.72e-03

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 38.57  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445  14 IGTFGGALKNVTPVELAVPVLQEAVKRGGVEPHEVDEVILGHCIQRTDEANTARTAALAAGFPDtVTGYTIQRQCSSGMQ 93
Cdd:cd00827   36 IGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLTN-AEAFDLKQACYGGTA 114
                         90       100
                 ....*....|....*....|....
gi 872564445  94 AIMSAAMQIQLGVSD--VVIAGGV 115
Cdd:cd00827  115 ALQLAANLVESGPWRyaLVVASDI 138
PRK07937 PRK07937
lipid-transfer protein; Provisional
150-356 6.53e-03

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 38.13  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 150 PIHHIMMGETAENLVEQYEITREEQDEVALRSHTLALKaiesgyfddqivpitikERRKEVVFSKDEHPRADITAEKLag 229
Cdd:PRK07937 136 PDSVSMAGLQARAGLDAGKWTEEQMAEVAARSRADARR-----------------NPSAEPSISVDELLARPYFADPL-- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872564445 230 lkpafrkggsvTAGNASGLNDGSAVLVLMSEEKAKEKGLQPlARIVGYSvAGVDPKIMG---IGPAPAIRKGLEKVDWSL 306
Cdd:PRK07937 197 -----------RRHDIAPITDGAAAVVLAAGDRARELRERP-AWITGIE-HRIESPSLGardLTRSPSTALAAEAATGGD 263
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 872564445 307 EDA-DLLEINEAFAAQYLAVEKELGLDrEKVNVNGSGVGL-GHPIGCTG-ARI 356
Cdd:PRK07937 264 AGGvDVAELHAPFTHQELILREALGLG-DKTKVNPSGGALaANPMFAAGlERI 315
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
68-119 8.57e-03

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 38.11  E-value: 8.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 872564445  68 TAALAAGFPDTVTGYTIQRQCSSGMQAIMSAAMQIQLGVSDVVIAGGVEAMS 119
Cdd:PRK07967 142 SACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELD 193
 
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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