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Conserved domains on  [gi|2676378839|ref|WP_332529008|]
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MULTISPECIES: thiolase family protein [Lactococcus]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

thiolase family protein may 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; such as acetyl-CoA acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl-CoA to another molecule of acetyl-CoA to form acetoacetyl-CoA

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0006635
PubMed:  16356722
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-364 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: 513.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   5 VIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTI 84
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  85 NEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKN------RKTQEETLSMLNDGLVDAFSGISMGIIGETIA 158
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPkarrggRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRPSSSLEKLATLRTAFKENGTVTAGN 230
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVevpgrkGPVVVdrDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 231 SSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLA 310
Cdd:cd00751   241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 311 VNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:cd00751   321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCI 374
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-364 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: 513.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   5 VIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTI 84
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  85 NEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKN------RKTQEETLSMLNDGLVDAFSGISMGIIGETIA 158
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPkarrggRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRPSSSLEKLATLRTAFKENGTVTAGN 230
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVevpgrkGPVVVdrDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 231 SSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLA 310
Cdd:cd00751   241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 311 VNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:cd00751   321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCI 374
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-364 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: 511.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:COG0183     1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL------SMLNDGLVDAFSGISMGIIG 154
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnaklvdPMINPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 ETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRPSSSLEKLATLRTAFKENGTV 226
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevpdrkGEVVVdrDEGPRPDTTLEKLAKLKPAFKKDGTV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 227 TAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAA 306
Cdd:COG0183   241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2676378839 307 SSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:COG0183   321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCI 378
PRK05790 PRK05790
putative acyltransferase; Provisional
1-364 2.17e-169

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 478.11  E-value: 2.17e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK05790    1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII--KNR---KTQEETL--SMLNDGLVDAFSGISMGII 153
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVlpGSRwgqKMGDVELvdTMIHDGLTDAFNGYHMGIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 154 GETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRTAFKENG 224
Cdd:PRK05790  161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtikqrkGDpvvVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK05790  241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK05790  321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCI 380
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-364 2.10e-153

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: 437.43  E-value: 2.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   6 IIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTIN 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  86 EVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQE-------ETLSMLNDGLVDAFSGISMGIIGETIA 158
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkpgnaELEDARLKDLTDANTGLPMGVTAENLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVG--------VDETPRPSSSLEKLATLRTAFKENGTVTAGN 230
Cdd:TIGR01930 161 KKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGrkgpvtvsSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 231 SSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLA 310
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 311 VNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:TIGR01930 321 CIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCI 374
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-247 4.32e-91

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: 274.18  E-value: 4.32e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   4 IVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPAST 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  84 INEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL--------SMLNDGLVDAFSGISMGIIGE 155
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKhgdekkhdLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 156 TIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVG--------VDETPRPSSSLEKLATLRTAFKENGTVT 227
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGrkgkptvdKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
                         250       260
                  ....*....|....*....|
gi 2676378839 228 AGNSSPVNDGASAVILATKD 247
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-364 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: 513.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   5 VIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTI 84
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  85 NEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKN------RKTQEETLSMLNDGLVDAFSGISMGIIGETIA 158
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPkarrggRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRPSSSLEKLATLRTAFKENGTVTAGN 230
Cdd:cd00751   161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVevpgrkGPVVVdrDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 231 SSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLA 310
Cdd:cd00751   241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 311 VNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:cd00751   321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCI 374
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-364 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: 511.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:COG0183     1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL------SMLNDGLVDAFSGISMGIIG 154
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnaklvdPMINPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 ETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRPSSSLEKLATLRTAFKENGTV 226
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevpdrkGEVVVdrDEGPRPDTTLEKLAKLKPAFKKDGTV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 227 TAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAA 306
Cdd:COG0183   241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2676378839 307 SSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:COG0183   321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCI 378
PRK05790 PRK05790
putative acyltransferase; Provisional
1-364 2.17e-169

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 478.11  E-value: 2.17e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK05790    1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII--KNR---KTQEETL--SMLNDGLVDAFSGISMGII 153
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVlpGSRwgqKMGDVELvdTMIHDGLTDAFNGYHMGIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 154 GETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRTAFKENG 224
Cdd:PRK05790  161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtikqrkGDpvvVDTDEHPRPDTTAESLAKLRPAFDKDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK05790  241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK05790  321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCI 380
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-364 2.10e-153

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: 437.43  E-value: 2.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   6 IIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTIN 85
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  86 EVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQE-------ETLSMLNDGLVDAFSGISMGIIGETIA 158
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWgvkpgnaELEDARLKDLTDANTGLPMGVTAENLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVG--------VDETPRPSSSLEKLATLRTAFKENGTVTAGN 230
Cdd:TIGR01930 161 KKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGrkgpvtvsSDEGIRPNTTLEKLAKLKPAFDPDGTVTAGN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 231 SSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLA 310
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 311 VNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:TIGR01930 321 CIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCI 374
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-363 5.41e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 362.88  E-value: 5.41e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK08235    1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII------KNRKTQEETLS-MLNDGLVDAFSGISMGII 153
Cdd:PRK08235   81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYIlpgarwGYRMGDNEVIDlMVADGLTCAFSGVHMGVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 154 GETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRTAFKENG 224
Cdd:PRK08235  161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtipqrkGDpivVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK08235  241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PRK08235  321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAIC 379
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-364 2.26e-121

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 356.57  E-value: 2.26e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIK-SDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNT 78
Cdd:PRK09050    1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNPGVDwEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  79 VPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII---------KNRKTQEETLS--MLNDGLVDAFSG 147
Cdd:PRK09050   81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVmgkadsafsRQAEIFDTTIGwrFVNPLMKAQYGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 148 ISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRT 218
Cdd:PRK09050  161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtipqkkGDpvvVDRDEHPRPETTLEALAKLKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 219 AFKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLF 298
Cdd:PRK09050  241 VFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2676378839 299 EINEAFAASSLAVNRELGL--NESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK09050  321 ELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCI 388
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-364 1.52e-118

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 349.19  E-value: 1.52e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK05656    1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL-------SMLNDGLVDAFSGISMGII 153
Cdd:PRK05656   81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMghaqlvdSMITDGLWDAFNDYHMGIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 154 GETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRTAFKENG 224
Cdd:PRK05656  161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlipqrkGEplaFATDEQPRAGTTAESLAKLKPAFKKDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK05656  241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK05656  321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCI 380
PRK09051 PRK09051
beta-ketothiolase BktB;
1-364 3.01e-114

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 338.09  E-value: 3.01e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNTV 79
Cdd:PRK09051    2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEpRDMYLSRVAAINAGVPQET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  80 PASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIK------NRKTQEETLSMLNDGLVDAFSGISMGII 153
Cdd:PRK09051   82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpaarwgARMGDAKLVDMMVGALHDPFGTIHMGVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 154 GETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDV--GVDETPRPSSSLEKLATLRTAF-KENG 224
Cdd:PRK09051  162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVeiktrkGEVvfDTDEHVRADTTLEDLAKLKPVFkKENG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK09051  242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK09051  322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCI 381
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
2-363 5.83e-113

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 334.75  E-value: 5.83e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   2 KEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPA 81
Cdd:PLN02644    1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  82 STINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL-------SMLNDGLVDAFSGISMGIIG 154
Cdd:PLN02644   81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLghdtvvdGMLKDGLWDVYNDFGMGVCA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 ETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVG--------VDETPRPSS-SLEKLATLRTAFKEN-G 224
Cdd:PLN02644  161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGgrgrpsviVDKDEGLGKfDPAKLRKLRPSFKEDgG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PLN02644  241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PLN02644  321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGIC 379
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-364 3.89e-109

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 325.06  E-value: 3.89e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK06633    2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMS----NAPIIKNRKTQEETLS--MLNDGLVDAFSGISMGIIG 154
Cdd:PRK06633   82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhGSYIRAGAKFGDIKMVdlMQYDGLTDVFSGVFMGITA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 ETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIgDVGV---------DETPRPSSSLEKLATLRTAFKENGT 225
Cdd:PRK06633  162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPI-EVTIkkttslfdhDETVRPDTSLEILSKLRPAFDKNGV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 226 VTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFA 305
Cdd:PRK06633  241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2676378839 306 ASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK06633  321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCI 379
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
2-364 6.14e-108

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


Pssm-ID: 131483  Cd Length: 400  Bit Score: 322.50  E-value: 6.14e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   2 KEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIK-SDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNTV 79
Cdd:TIGR02430   1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNPQLDwAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  80 PASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIK-------NRKTQEETLSM----LNDGLVDAFSGI 148
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMgkadsafSRSAKIEDTTIgwrfINPLMKALYGVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 149 SMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRTA 219
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVvipqkkGEptvVDQDEHPRPETTLEGLAKLKPV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 220 FKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFE 299
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2676378839 300 INEAFAASSLAVNRELGL--NESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCI 387
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-364 5.92e-107

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 319.64  E-value: 5.92e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRY-DGALAEYSAAELGTHVVSNLLSKHENI-KSDVEQVIFGNVL-QAGNGQNIARQIAIHSGLPN 77
Cdd:PRK09052    5 LQDAYIVAATRTPVGKApRGMFKNTRPDDLLAHVLRSAVAQVPGLdPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  78 TVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETLSMLNDGLVDAFSgisMGIIGETI 157
Cdd:PRK09052   85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSPAIFARDENVGIAYG---MGLTAEKV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 158 AEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI-----------GDVGV-------DETPRPSSSLEKLATLRTA 219
Cdd:PRK09052  162 AEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYeiterfpdlatGEVDVktrtvdlDEGPRADTSLEGLAKLKPV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 220 FKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFE 299
Cdd:PRK09052  242 FANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIE 321
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676378839 300 INEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK09052  322 LNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCV 386
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-364 4.88e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 317.70  E-value: 4.88e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK06205    1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKN--RKTQEETLSMLNDGLVDA---FSGISMGIIG- 154
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARGretAGGRRFPVPGg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 -----ETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GD---VGVDETPRPSSSLEKLATLRT-- 218
Cdd:PRK06205  161 mietaENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVtvpqrkGDptvVDRDEHPRADTTLESLAKLRPim 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 219 -AFKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDL 297
Cdd:PRK06205  241 gKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDL 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 298 FEINEAFAASSLAVNRELGLNES---QVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK06205  321 IELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCI 390
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-364 2.89e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 305.14  E-value: 2.89e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYD-GALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVL-QAGNGQNIARQIAIHSGLPNT 78
Cdd:PRK07661    1 MREAVIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  79 VPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNrktqeetLSMLNDGLVDAFSG--ISMGIIGET 156
Cdd:PRK07661   81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGH-------VVRPNPRLVEAAPEyyMGMGHTAEQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 157 IAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIV-------AIGD----------VGVDETPRPSSSLEKLATLRTA 219
Cdd:PRK07661  154 VAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVpvdvtlrTVGEnnklqeetitFSQDEGVRADTTLEILGKLRPA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 220 FKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFE 299
Cdd:PRK07661  234 FNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFE 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676378839 300 INEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK07661  314 LNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCI 378
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-364 8.95e-101

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 303.43  E-value: 8.95e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAE-LGTHVVSNLLSKHENIK-SDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPN 77
Cdd:PRK08947    1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEdLSAHLMRSLLARNPALDpAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  78 TVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPiiknrktqeetlsmLNDGlVDAFSGIS-------- 149
Cdd:PRK08947   81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--------------MNHG-VDFHPGLSknvakaag 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 150 -MGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGD---------VGVDETPRPSSSLEKLATLRTA 219
Cdd:PRK08947  146 mMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGhdadgvlklFDYDEVIRPETTVEALAALRPA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 220 FK-ENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLF 298
Cdd:PRK08947  226 FDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2676378839 299 EINEAFAASSLAVNRELGLNES---QVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK08947  306 ELNEAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCI 374
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-364 6.38e-96

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 291.68  E-value: 6.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNTV 79
Cdd:PRK08131    1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  80 PASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII--KNRKTQEETLSML---------NDGLVDAFSGI 148
Cdd:PRK08131   81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVmgKAESAFSRDAKVFdttigarfpNPKIVAQYGND 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 149 SMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIG----------DVGVDETPRPSSSLEKLATLRT 218
Cdd:PRK08131  161 SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEvpqgrklppkLVAEDEHPRPSSTVEALTKLKP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 219 AFkENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLF 298
Cdd:PRK08131  241 LF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2676378839 299 EINEAFAASSLAVNRELGL--NESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK08131  320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCI 387
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-363 8.88e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 290.46  E-value: 8.88e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGnGQ--NIARQIAIHSGLPNT 78
Cdd:PRK07801    1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  79 VPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETlsmlndGLVDAFSG----------- 147
Cdd:PRK07801   80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQL------GFTSPFAEskgwlhrygdq 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 148 -ISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVGVDETPRpSSSLEKLATLRTaFKENGTV 226
Cdd:PRK07801  154 eVSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVTVDEGPR-ETSLEKMAGLKP-LVEGGRL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 227 TAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAA 306
Cdd:PRK07801  232 TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAP 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2676378839 307 SSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PRK07801  312 VVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMC 368
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-364 7.13e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 289.61  E-value: 7.13e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK08170    2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNR------------KTQEETLSMLND--------- 139
Cdd:PRK08170   82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmvrwlagwyaaKSIGQKLAALGKlrpsylapv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 140 -----GLVDAFSGISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVGV----DETPRPSSSL 210
Cdd:PRK08170  162 igllrGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPLFDRDGKfydhDDGVRPDSSM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 211 EKLATLRTAF-KENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSE 289
Cdd:PRK08170  242 EKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 290 LELSDIDLFEINEAFAASSLAVNR----------ELGL-------NESQVNIYGGAIALGHAIGSSGSKILTTLSYALKR 352
Cdd:PRK08170  322 LTLEDLDLWEINEAFAAQVLACLAawadeeycreQLGLdgalgelDRERLNVDGGAIALGHPVGASGARIVLHLLHALKR 401
                         410
                  ....*....|..
gi 2676378839 353 EQKRYGIASLCI 364
Cdd:PRK08170  402 RGTKRGIAAICI 413
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
3-364 5.99e-93

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 285.89  E-value: 5.99e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   3 EIVIIDALRTPVGRYD-GALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQ-NIARQIAIHSGLPNTVP 80
Cdd:PLN02287   47 DVVIVAAYRTPICKAKrGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKT--QEETLSMLNDGLvdafsgISMGIIGETIA 158
Cdd:PLN02287  127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVnpRVESFSQAQDCL------LPMGITSENVA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 159 EQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGD--------------VGVDETPRPSSSLEKLATLRTAFKENG 224
Cdd:PLN02287  201 ERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpktgeekpivISVDDGIRPNTTLADLAKLKPVFKKNG 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PLN02287  281 TTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAF 360
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQK--RYGIASLCI 364
Cdd:PLN02287  361 ASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKdcRFGVVSMCI 422
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-364 5.04e-92

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 281.40  E-value: 5.04e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK06954    6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII------KNRKTQEETLS-MLNDGLVDAFS-GISMGI 152
Cdd:PRK06954   86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLlpkargGMRMGHGQVLDhMFLDGLEDAYDkGRLMGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 153 IGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGV--DETPRpSSSLEKLATLRTAFKENG 224
Cdd:PRK06954  166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVtvagkkGDTVIdrDEQPF-KANPEKIPTLKPAFSKTG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 225 TVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK06954  245 TVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAF 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK06954  325 AVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCI 384
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-247 4.32e-91

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: 274.18  E-value: 4.32e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   4 IVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPAST 83
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  84 INEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETL--------SMLNDGLVDAFSGISMGIIGE 155
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKhgdekkhdLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 156 TIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVG--------VDETPRPSSSLEKLATLRTAFKENGTVT 227
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGrkgkptvdKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
                         250       260
                  ....*....|....*....|
gi 2676378839 228 AGNSSPVNDGASAVILATKD 247
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-363 1.38e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 277.66  E-value: 1.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK06366    1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII--------------KNRKTQEetlSMLNDGLVDAFS 146
Cdd:PRK06366   81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlpsdlrwgpkhllhKNYKIDD---AMLVDGLIDAFY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 147 GISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVGVDETPRpSSSLEKLATLRTAFKENGTV 226
Cdd:PRK06366  158 FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLDRDEGIR-KTTMEDLAKLPPAFDKNGIL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 227 TAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAA 306
Cdd:PRK06366  237 TAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSI 316
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2676378839 307 SSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PRK06366  317 ASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLC 373
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-364 2.16e-87

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 269.95  E-value: 2.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGR-YDGALAEYSAAELGTHVVSNLLSKHENIK-SDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPn 77
Cdd:PRK07851    1 MPEAVIVSTARSPIGRaFKGSLKDMRPDDLAAQMVRAALDKVPALDpTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  78 TVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMS--------NAPIIKN---RKTQEETLSML--------- 137
Cdd:PRK07851   80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdSLPDTKNplfAEAQARTAARAeggaeawhd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 138 --NDGLV-DAFsgISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEI--VAIGD---VGVDETPRPSSS 209
Cdd:PRK07851  160 prEDGLLpDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREItpVTLPDgtvVSTDDGPRAGTT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 210 LEKLATLRTAFKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVdSTEV-GIDPAIMGVSPIEAIKKLINRS 288
Cdd:PRK07851  238 YEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIV-STGVsGLSPEIMGLGPVEASKQALARA 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2676378839 289 ELELSDIDLFEINEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK07851  317 GMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-364 1.82e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 267.36  E-value: 1.82e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAE------YSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHS 73
Cdd:PRK06445    1 LEDVYLVDFARTAFSRFRPKDPQkdvfnnIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGeNWLYGGRHPIFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  74 GLPNTVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETLSMLNDGLV--DAFSGISMG 151
Cdd:PRK06445   81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPHIEPNPKLLTDPKYIeyDLTTGYVMG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 152 IIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI-----GD---VGVDETPRPSSSLEKLATLRTAFKEN 223
Cdd:PRK06445  161 LTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIeveveGKkkvVDVDQSVRPDTSLEKLAKLPPAFKPD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 224 GTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEA 303
Cdd:PRK06445  241 GVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEA 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2676378839 304 FAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK06445  321 FAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCV 381
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-364 4.78e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 266.36  E-value: 4.78e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGR--YDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGN-GQNIARQIAIHSGLPN 77
Cdd:PRK08242    1 MTEAYIYDAVRTPRGKgkKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  78 TVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPiiknrktqeetlsMLNDG---LVDAFSGIS----- 149
Cdd:PRK08242   81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------------MGSDGgawAMDPSTNFPtyfvp 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 150 MGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDV-GV-----DETPRPSSSLEKLATLRTAFKEN 223
Cdd:PRK08242  148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQnGLtildhDEHMRPGTTMESLAKLKPSFAMM 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 224 GTV---------------------TAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIK 282
Cdd:PRK08242  228 GEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATR 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 283 KLINRSELELSDIDLFEINEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASL 362
Cdd:PRK08242  308 KALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITL 387

                  ..
gi 2676378839 363 CI 364
Cdd:PRK08242  388 CV 389
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
5-362 4.52e-83

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 257.39  E-value: 4.52e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   5 VIIDALRTPVGRYDGALAEYSAAELGTHVVSnLLSKheNIKSDVEQVIFGNVLqaGNGQNIARQIAIHSGLPNTVPASTI 84
Cdd:PRK06690    4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT-FLSK--GMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  85 NEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETLSmlndglvdafsGISMGIIGETIAEQFDIS 164
Cdd:PRK06690   79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIG-----------DPDMGVAAEYVAERYNIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 165 RADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVgVDETPRPSSSLEKL-ATLRTAFKENGTVTAGNSSPVNDGASAVIL 243
Cdd:PRK06690  148 REMQDEYACLSYKRTLQALEKGYIHEEILSFNGL-LDESIKKEMNYERIiKRTKPAFLHNGTVTAGNSCGVNDGACAVLV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 244 ATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLAVNRELGLNESQVN 323
Cdd:PRK06690  227 MEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYEKLN 306
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2676378839 324 IYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASL 362
Cdd:PRK06690  307 VNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATL 345
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-363 1.48e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 254.27  E-value: 1.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNTV 79
Cdd:PRK06504    1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  80 PASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNrktqeETLSMLN-------DGLVDAFSGIS--- 149
Cdd:PRK06504   81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-----STLPAKNglghyksPGMEERYPGIQfsq 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 150 -MGiiGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVG---VDETPRPSSSLEKLATLRTa 219
Cdd:PRK06504  156 fTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLeitradGSGEmhtVDEGIRFDATLEGIAGVKL- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 220 FKENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFE 299
Cdd:PRK06504  233 IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2676378839 300 INEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PRK06504  313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMC 376
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-363 1.59e-76

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 241.55  E-value: 1.59e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNTV 79
Cdd:PRK07850    1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  80 PASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKN-------RKTQEETLSMlndglVDAFSGismgi 152
Cdd:PRK07850   81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANagpgrglPRPDSWDIDM-----PNQFEA----- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 153 iGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVGVDETPRPS--------------SSLEKLATLRT 218
Cdd:PRK07850  151 -AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPTgetrlvtrdqglrdTTMEGLAGLKP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 219 AFkENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLF 298
Cdd:PRK07850  230 VL-EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLV 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676378839 299 EINEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLC 363
Cdd:PRK07850  309 EINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMC 373
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-364 4.99e-73

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 232.35  E-value: 4.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGR-YDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSGLPNT 78
Cdd:PRK07108    1 MTEAVIVSTARTPLAKsWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  79 VPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNApiiknrkTQEETLSMLNDG-LVDAFSGI--SMGIIGE 155
Cdd:PRK07108   81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV-------QNEMNRHMLREGwLVEHKPEIywSMLQTAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 156 TIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIG------------------DVGVDETPRPSSSLEKLATLR 217
Cdd:PRK07108  154 NVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITvtagvadkatgrlftkevTVSADEGIRPDTTLEGVSKIR 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 218 TAFkENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDL 297
Cdd:PRK07108  234 SAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDL 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2676378839 298 FEINEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:PRK07108  313 WELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCI 379
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-363 2.03e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 221.19  E-value: 2.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTP-----VGRydGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQNIARQIAIHSG 74
Cdd:PRK06025    1 MAEAYIIDAVRTPrgigkVGK--GALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  75 LPNTVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMS-NAPIIKNRKTQEETLSMLNDG---LVDAFSGISM 150
Cdd:PRK06025   79 YDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPPLGMGSGnlrLRALHPQSHQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 151 GIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI----GDVGVD--ETPRPSSSLEKLATLRTAFK--- 221
Cdd:PRK06025  159 GVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVyrddGSVALDheEFPRPQTTAEGLAALKPAFTaia 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 222 -----ENGTVT------------------AGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDPAIMGVSPI 278
Cdd:PRK06025  239 dypldDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 279 EAIKKLINRSELELSDIDLFEINEAFAASSLAVNRELGLNESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQKRYG 358
Cdd:PRK06025  319 PAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRG 398

                  ....*
gi 2676378839 359 IASLC 363
Cdd:PRK06025  399 LVTMC 403
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
9-364 6.05e-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: 216.98  E-value: 6.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   9 ALRTPVGRY---DGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPASTIN 85
Cdd:cd00826     3 AAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  86 EVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPiiKNRKTQEETLSMLNDGLvdafsgismgiigetiaeqfdiSR 165
Cdd:cd00826    83 NLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA--ENNAKEKHIDVLINKYG----------------------MR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 166 ADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGVDETP----RPSSSLEKLATLRTAFKENGTVTAGNSSPVN 235
Cdd:cd00826   139 ACPDAFALAGQAGAEAAEKDGRFKDEFAKFgvkgrkGDIHSDADEyiqfGDEASLDEIAKLRPAFDKEDFLTAGNACGLN 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 236 DGASAVILATKDYAEKH-------EIPYLAELVDSTEVGIDPA----IMGVSPIEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:cd00826   219 DGAAAAILMSEAEAQKHglqskarEIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAF 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 305 AASSLAVNRELGL------------------NESQVNIYGGAIALGHAIGSSGSKILTTLSYALKREQK-----RYGIAS 361
Cdd:cd00826   299 AANACATNEALGLcpegqggalvdrgdntygGKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGkrqgaGAGLAL 378

                  ...
gi 2676378839 362 LCI 364
Cdd:cd00826   379 LCI 381
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
4-363 2.86e-64

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 211.00  E-value: 2.86e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   4 IVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVPAST 83
Cdd:PRK08963    7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  84 INEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETLSM-----------------LNDGL----- 141
Cdd:PRK08963   87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLnkartlgqrlklfsrlrLRDLLpvppa 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 142 VDAFS-GISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAI------GDVGVDETPRPSSSLEKLA 214
Cdd:PRK08963  167 VAEYStGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAhvppykQPLEEDNNIRGDSTLEDYA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 215 TLRTAF-KENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGIDP---AIMGvsPIEAIKKLINRSEL 290
Cdd:PRK08963  247 KLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwqdMLLG--PAYATPLALERAGL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 291 ELSDIDLFEINEAFAASSLA----------VNRELGLNE-------SQVNIYGGAIALGHAIGSSGSKILTTLSYALKRE 353
Cdd:PRK08963  325 TLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGRSQaigevdmSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
                         410
                  ....*....|
gi 2676378839 354 QKRYGIASLC 363
Cdd:PRK08963  405 GGGLGLTTAC 414
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-363 7.16e-60

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 199.36  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRYDGALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNTVP 80
Cdd:PRK09268    6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  81 ASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNR------------KTQEETLSMLNDG----LVDA 144
Cdd:PRK09268   86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEglrkillelnraKTTGDRLKALGKLrpkhLAPE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 145 F-------SGISMGIIGETIAEQFDISRADQDAFAQNSQEKAVAASQAGIFKEEIVAIGDVGVDETPRPSSSLEKLATLR 217
Cdd:PRK09268  166 IprngeprTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTRDNNLRPDSSLEKLAKLK 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 218 TAF--KENGTVTAGNSSPVNDGASAVILATKDYAEKHEIPYLAELVDStEV-------GIDPAIMgvSPIEAIKKLINRS 288
Cdd:PRK09268  246 PVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDA-ETaavdfvhGKEGLLM--APAYAVPRLLARN 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 289 ELELSDIDLFEINEAFAASSLAV----------NRELGLNE-------SQVNIYGGAIALGHAIGSSGSKILTTLSYALK 351
Cdd:PRK09268  323 GLTLQDFDFYEIHEAFASQVLATlkawedeeycRERLGLDAplgsidrSKLNVNGSSLAAGHPFAATGGRIVATLAKLLA 402
                         410
                  ....*....|..
gi 2676378839 352 REQKRYGIASLC 363
Cdd:PRK09268  403 EKGSGRGLISIC 414
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
255-364 8.51e-43

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: 145.48  E-value: 8.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 255 PYLAELVDSTEVGIDPAIMGVSPIEAIKKLINRSELELSDIDLFEINEAFAASSLAVNRELGLNESQVNIYGGAIALGHA 334
Cdd:pfam02803   2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2676378839 335 IGSSGSKILTTLSYALKREQKRYGIASLCI 364
Cdd:pfam02803  82 LGASGARILVTLLHELKRRGGKYGLASLCI 111
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
12-339 1.41e-18

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: 86.16  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  12 TPVGRYDGalaeYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNtVPASTINEVCGSG 91
Cdd:cd00829     6 TPFGRRSD----RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  92 MKAVILAKQLLQLGEAEVVIAGGTESMSNAPIIKNRKTQEETLSMLNDGLVDAFSGISM-GIIGETIAEQFDISRADQDA 170
Cdd:cd00829    81 SAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEAGGRASDLEWEGPEPPGGLTPPALyALAARRYMHRYGTTREDLAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 171 FAQNSQEKAVAASQAgIFKEEIvaigDVGVDETPRPSSSleklatlrtafkengTVTAGNSSPVNDGASAVILATKDYAE 250
Cdd:cd00829   161 VAVKNHRNAARNPYA-QFRKPI----TVEDVLNSRMIAD---------------PLRLLDCCPVSDGAAAVVLASEERAR 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 251 KHEIPY-----LAELVDSTEVGIDPAIMGVSPI-EAIKKLINRSELELSDIDLFEINEAFAASSLAVNRELGL---NESQ 321
Cdd:cd00829   221 ELTDRPvwilgVGAASDTPSLSERDDFLSLDAArLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFcekGEGG 300
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2676378839 322 ---------------VNIYGGAIALGHAIGSSG 339
Cdd:cd00829   301 klvregdtaiggdlpVNTSGGLLSKGHPLGATG 333
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
45-355 1.34e-16

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: 78.64  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  45 KSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNtVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTEsmsnapii 124
Cdd:cd00327    26 KGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISG-GPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSE-------- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 125 knrktqeetlsmlndglvdafsgismgiigetiaeqfdisradqdafaqnsqekavaasqagifkeeivaigdvgvdetp 204
Cdd:cd00327       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 205 rpsssleklatlrtafkengtvtagnSSPVNDGASAVILATKDYAEKHEIPYLAELVDSTEVGID----PAIMGVSPIEA 280
Cdd:cd00327    97 --------------------------EFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARA 150
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2676378839 281 IKKLINRSELELSDIDLFEINEAFAASSLAVNRELGLNESQV---NIYGGAIALGHAIGSSGSKILTTLSYALKREQK 355
Cdd:cd00327   151 ARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFI 228
PRK06064 PRK06064
thiolase domain-containing protein;
1-339 5.77e-11

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 63.38  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839   1 MKEIVIIDALRTPVGRydgaLAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAG-NGQ-NIARQIAIHSGLPNt 78
Cdd:PRK06064    1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGLAP- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  79 VPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPiiknRKTQEETLSMLNDGLVDAFSGISM----GIIG 154
Cdd:PRK06064   76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP----TPDATEAIARAGDYEWEEFFGATFpglyALIA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 155 ETIAEQFDISRADQDAFAQNSQEKAVAASQAgIFKEEIVaigdvgVDETPRPSSSLEKLATLrtafkengtvtagNSSPV 234
Cdd:PRK06064  152 RRYMHKYGTTEEDLALVAVKNHYNGSKNPYA-QFQKEIT------VEQVLNSPPVADPLKLL-------------DCSPI 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 235 NDGASAVILATKDYAEKH--EIPYlaelVDSTEVGIDPAIMGVSP--------IEAIKKLINRSELELSDIDLFEINEAF 304
Cdd:PRK06064  212 TDGAAAVILASEEKAKEYtdTPVW----IKASGQASDTIALHDRKdfttldaaVVAAEKAYKMAGIEPKDIDVAEVHDCF 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2676378839 305 AASSLAVNRELG----------LNESQ--------VNIYGGAIALGHAIGSSG 339
Cdd:PRK06064  288 TIAEILAYEDLGfakkgeggklAREGQtyiggdipVNPSGGLKAKGHPVGATG 340
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
65-124 1.38e-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: 49.71  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676378839  65 IARQIAIHSGL--PNTVPASTinevCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII 124
Cdd:COG0304   140 AAGHVSIRFGLkgPNYTVSTA----CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGL 197
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
65-124 1.47e-06

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 49.84  E-value: 1.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  65 IARQIAIHSGLpnTVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNAPII 124
Cdd:cd00834   140 AAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTL 197
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
49-118 4.63e-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: 41.47  E-value: 4.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2676378839  49 EQVIFGNVLQAGNGQN-IARQIAIHSGLpnTVPASTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESM 118
Cdd:pfam00109 135 GGPRRGSPFAVGTMPSvIAGRISYFLGL--RGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
65-121 9.16e-04

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 40.93  E-value: 9.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2676378839  65 IARQIAIHSGL--PNtvpaSTINEVCGSGMKAVILAKQLLQLGEAEVVIAGGTESMSNA 121
Cdd:PRK07314  141 AAGHVSIRYGAkgPN----HSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITP 195
PRK07937 PRK07937
lipid-transfer protein; Provisional
228-330 1.99e-03

lipid-transfer protein; Provisional


Pssm-ID: 181173 [Multi-domain]  Cd Length: 352  Bit Score: 39.67  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839 228 AGNSSPVNDGASAVILATKDYAEKH-EIPylaELVDSTEVGIDPAIMGV-------SPIEAIKKLINRSeleLSDIDLFE 299
Cdd:PRK07937  198 RHDIAPITDGAAAVVLAAGDRARELrERP---AWITGIEHRIESPSLGArdltrspSTALAAEAATGGD---AGGVDVAE 271
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2676378839 300 INEAFAASSLAVNRELGLNES-QVNIYGGAIA 330
Cdd:PRK07937  272 LHAPFTHQELILREALGLGDKtKVNPSGGALA 303
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
20-115 4.26e-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: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676378839  20 ALAEYSAAELGTHVVSNLLSKHENIKSDVEQVIFGNVLQAGNGQNIARQIAIHSGLPNtVPASTINEVCGSGMKAVILAK 99
Cdd:cd00827    42 AGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLTN-AEAFDLKQACYGGTAALQLAA 120
                          90
                  ....*....|....*...
gi 2676378839 100 QLLQLGEAE--VVIAGGT 115
Cdd:cd00827   121 NLVESGPWRyaLVVASDI 138
 
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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