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Conserved domains on  [gi|1253006213|ref|WP_096901568|]
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MULTISPECIES: acetyl-CoA C-acetyltransferase [Acinetobacter]

Protein Classification

acetyl-CoA acetyltransferase( domain architecture ID 11483181)

acetyl-CoA acetyltransferase catalyzes the reversible condensation of two acetyl-CoA units to form acetoacetyl-CoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


:

Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 742.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK08242    1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDFIPQGIGADLIATLDG 160
Cdd:PRK08242   81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 161 YSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGVVILAQDEFIKPQTTAESLAQLKPSFANMGQM-GFDAIALQK 239
Cdd:PRK08242  161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 240 YPEAGQVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDI 319
Cdd:PRK08242  241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 320 DLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIE 399
Cdd:PRK08242  321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                  ..
gi 1253006213 400 RV 401
Cdd:PRK08242  401 RV 402
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 742.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK08242    1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDFIPQGIGADLIATLDG 160
Cdd:PRK08242   81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 161 YSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGVVILAQDEFIKPQTTAESLAQLKPSFANMGQM-GFDAIALQK 239
Cdd:PRK08242  161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 240 YPEAGQVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDI 319
Cdd:PRK08242  241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 320 DLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIE 399
Cdd:PRK08242  321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                  ..
gi 1253006213 400 RV 401
Cdd:PRK08242  401 RV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-401 2.98e-172

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: 486.50  E-value: 2.98e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDN 80
Cdd:COG0183     1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNM-----------ACDFIPQG 149
Cdd:COG0183    78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLvdpminpgltdPYTGLSMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 150 IGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFANM 227
Cdd:COG0183   158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 228 GqmgfdaialqkypeagqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARK 307
Cdd:COG0183   238 G--------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 308 ALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLC 387
Cdd:COG0183   298 ALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
                         410
                  ....*....|....
gi 1253006213 388 VGGGMGIATIIERV 401
Cdd:COG0183   378 IGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-400 3.40e-157

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: 448.08  E-value: 3.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   5 YIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAG 84
Cdd:cd00751     1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  85 VQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDF-----------IPQGIGAD 153
Cdd:cd00751    78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMlddgltdpftgLSMGITAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 154 LIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQA--GVVILAQDEFIKPQTTAESLAQLKPSFANmgqmg 231
Cdd:cd00751   158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGrkGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 232 fdaialqkypeagqvNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAK 311
Cdd:cd00751   233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 312 AGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGG 391
Cdd:cd00751   298 AGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGG 377

                  ....*....
gi 1253006213 392 MGIATIIER 400
Cdd:cd00751   378 QGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-399 1.74e-144

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: 415.86  E-value: 1.74e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQgADIAKTAAIAAGWDNDVAGV 85
Cdd:TIGR01930   1 IVAAARTPIGKFG--GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMG-SDGGAWAFDP-----------ETNMACDFIPQGIGAD 153
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPgnaeledarlkDLTDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 154 LIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFAnmgqmg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVtvKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFD------ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 232 fdaialqkypeagqVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAK 311
Cdd:TIGR01930 232 --------------PDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 312 AGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGG 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGG 377

                  ....*...
gi 1253006213 392 MGIATIIE 399
Cdd:TIGR01930 378 QGAAVILE 385
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
278-400 1.83e-54

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: 176.29  E-value: 1.83e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 278 LKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGH 357
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1253006213 358 PLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIER 400
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 742.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK08242    1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDFIPQGIGADLIATLDG 160
Cdd:PRK08242   81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 161 YSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGVVILAQDEFIKPQTTAESLAQLKPSFANMGQM-GFDAIALQK 239
Cdd:PRK08242  161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 240 YPEAGQVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDI 319
Cdd:PRK08242  241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 320 DLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIE 399
Cdd:PRK08242  321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                  ..
gi 1253006213 400 RV 401
Cdd:PRK08242  401 RV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-401 2.98e-172

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: 486.50  E-value: 2.98e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDN 80
Cdd:COG0183     1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNM-----------ACDFIPQG 149
Cdd:COG0183    78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLvdpminpgltdPYTGLSMG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 150 IGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFANM 227
Cdd:COG0183   158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 228 GqmgfdaialqkypeagqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARK 307
Cdd:COG0183   238 G--------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 308 ALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLC 387
Cdd:COG0183   298 ALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
                         410
                  ....*....|....
gi 1253006213 388 VGGGMGIATIIERV 401
Cdd:COG0183   378 IGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-400 3.40e-157

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: 448.08  E-value: 3.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   5 YIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAG 84
Cdd:cd00751     1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  85 VQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDF-----------IPQGIGAD 153
Cdd:cd00751    78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMlddgltdpftgLSMGITAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 154 LIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQA--GVVILAQDEFIKPQTTAESLAQLKPSFANmgqmg 231
Cdd:cd00751   158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGrkGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 232 fdaialqkypeagqvNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAK 311
Cdd:cd00751   233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 312 AGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGG 391
Cdd:cd00751   298 AGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGG 377

                  ....*....
gi 1253006213 392 MGIATIIER 400
Cdd:cd00751   378 QGAAMVIER 386
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-401 3.27e-152

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 436.51  E-value: 3.27e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKK-DGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWD 79
Cdd:PRK06025    1 MAEAYIIDAVRTPRGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  80 NDVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMACDFIP---------QGI 150
Cdd:PRK06025   81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPLGMGSGNLRlralhpqshQGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 151 GADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGVVILAQDEFIKPQTTAESLAQLKPSFANMGQM 230
Cdd:PRK06025  161 CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAIADY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 231 GFD-------AIALQKYPEAgQVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAP 303
Cdd:PRK06025  241 PLDdkgttyrGLINQKYPDL-EIKHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 304 AARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGM 383
Cdd:PRK06025  320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGL 399
                         410
                  ....*....|....*...
gi 1253006213 384 ATLCVGGGMGIATIIERV 401
Cdd:PRK06025  400 VTMCAAGGMAPAIIIERV 417
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-399 1.74e-144

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: 415.86  E-value: 1.74e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQgADIAKTAAIAAGWDNDVAGV 85
Cdd:TIGR01930   1 IVAAARTPIGKFG--GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMG-SDGGAWAFDP-----------ETNMACDFIPQGIGAD 153
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPgnaeledarlkDLTDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 154 LIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFAnmgqmg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVtvKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFD------ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 232 fdaialqkypeagqVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAK 311
Cdd:TIGR01930 232 --------------PDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 312 AGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGG 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGG 377

                  ....*...
gi 1253006213 392 MGIATIIE 399
Cdd:TIGR01930 378 QGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
1-401 1.12e-120

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 355.23  E-value: 1.12e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDN 80
Cdd:PRK05790    1 MKDVVIVSAARTPIGKFG--GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSR---VAMGSDGG----------AWAFDPETNMACDfIP 147
Cdd:PRK05790   78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQaphVLPGSRWGqkmgdvelvdTMIHDGLTDAFNG-YH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 148 QGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAG-VVILAQDEFIKPQTTAESLAQLKPSF 224
Cdd:PRK05790  157 MGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtiKQRKGdPVVVDTDEHPRPDTTAESLAKLRPAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 225 AnmgqmgfdaialqkypEAGQVnhvhHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPA 304
Cdd:PRK05790  237 D----------------KDGTV----TAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 305 ARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMA 384
Cdd:PRK05790  297 IRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLA 376
                         410
                  ....*....|....*..
gi 1253006213 385 TLCVGGGMGIATIIERV 401
Cdd:PRK05790  377 TLCIGGGQGVALIVERP 393
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-401 1.72e-119

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 352.09  E-value: 1.72e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPrgKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK07801    1 MAEAYIVDAVRTP--VGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSD---GGAWAFDPETNMACDF--------IPQG 149
Cdd:PRK07801   79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtaGEQLGFTSPFAESKGWlhrygdqeVSQF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 150 IGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDqagvviLAQDEFIKpQTTAESLAQLKPSFanmgq 229
Cdd:PRK07801  159 RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG------VTVDEGPR-ETSLEKMAGLKPLV----- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 230 mgfdaialqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKAL 309
Cdd:PRK07801  227 ------------EGGRLT----AAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYAL 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 310 AKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVG 389
Cdd:PRK07801  291 EKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEG 370
                         410
                  ....*....|..
gi 1253006213 390 GGMGIATIIERV 401
Cdd:PRK07801  371 GGTANVTIIERL 382
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-401 1.95e-106

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 318.83  E-value: 1.95e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdGALHEVKPIRLLTTLLNELQQRH-NLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWD 79
Cdd:PRK08947    1 MEDVVIVDAIRTPMGRSKG-GAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  80 NDVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAM--GSDggawaFDPE--TNMACDFIPQGIGADLI 155
Cdd:PRK08947   80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMnhGVD-----FHPGlsKNVAKAAGMMGLTAEML 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 156 ATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK--DQAGVVILA-QDEFIKPQTTAESLAQLKPSFAnmgqmgf 232
Cdd:PRK08947  155 GKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEghDADGVLKLFdYDEVIRPETTVEALAALRPAFD------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 233 daialqkyPEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKA 312
Cdd:PRK08947  228 --------PVNGTVT----AGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRA 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 313 GLNIEDIDLFEVNEAFAAVVLRFITEL----QVDpAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCV 388
Cdd:PRK08947  296 GLSISDIDVFELNEAFAAQSLPCLKDLglldKMD-EKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCI 374
                         410
                  ....*....|...
gi 1253006213 389 GGGMGIATIIERV 401
Cdd:PRK08947  375 GLGQGIATVFERV 387
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-401 1.78e-105

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 316.90  E-value: 1.78e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPrgKGKKDGALHEVKPIRLLTTLLNELQQRH-NLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWD 79
Cdd:PRK09050    1 MTEAFICDAIRTP--IGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  80 NDVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV--AMGSDGGAWAFDPE---TNMACDFI-------- 146
Cdd:PRK09050   79 VSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRApfVMGKADSAFSRQAEifdTTIGWRFVnplmkaqy 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 147 -----PQGigADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV---KDQAGVVILAQDEFIKPQTTAESLA 218
Cdd:PRK09050  159 gvdsmPET--AENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtipQKKGDPVVVDRDEHPRPETTLEALA 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 219 QLKPSFAnmgqmgfdaialqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIML 298
Cdd:PRK09050  237 KLKPVFR----------------PDGTVT----AGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 299 TGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQV--DPAKVNVNGGAIALGHPLGATGAMILGTLLDELER 376
Cdd:PRK09050  297 IGPAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLER 376
                         410       420
                  ....*....|....*....|....*
gi 1253006213 377 QDKKRGMATLCVGGGMGIATIIERV 401
Cdd:PRK09050  377 TGGRYALCTMCIGVGQGIALAIERV 401
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-401 1.99e-104

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 314.25  E-value: 1.99e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdGALHEVKPIRLL-TTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWD 79
Cdd:PRK09052    5 LQDAYIVAATRTPVGKAPR-GMFKNTRPDDLLaHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  80 NDVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWA---FDPETNMACDFiPQGIGADLIA 156
Cdd:PRK09052   84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMGNKPSMSpaiFARDENVGIAY-GMGLTAEKVA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 157 TLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVP--VKD-----QAGVVILAQ-----DEFIKPQTTAESLAQLKPSF 224
Cdd:PRK09052  163 EQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITErfpdlATGEVDVKTrtvdlDEGPRADTSLEGLAKLKPVF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 225 ANMGQMGfdaialqkypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPA 304
Cdd:PRK09052  243 ANKGSVT--------------------AGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEA 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 305 ARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMA 384
Cdd:PRK09052  303 IPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMV 382
                         410
                  ....*....|....*..
gi 1253006213 385 TLCVGGGMGIATIIERV 401
Cdd:PRK09052  383 TMCVGTGMGAAGIFERL 399
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-401 1.51e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 306.65  E-value: 1.51e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTP-----RGKGKKDgALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIA 75
Cdd:PRK06445    1 LEDVYLVDFARTAfsrfrPKDPQKD-VFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  76 AGWDNDVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSD-----GGAWAFDPET---NMACDFIp 147
Cdd:PRK06445   80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiepNPKLLTDPKYieyDLTTGYV- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 148 QGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAG--VVILAQDEFIKPQTTAESLAQLKPSFA 225
Cdd:PRK06445  159 MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEgkKKVVDVDQSVRPDTSLEKLAKLPPAFK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 226 NMGqmgfdaialqkypeagqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAA 305
Cdd:PRK06445  239 PDG--------------------VITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPAS 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 306 RKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMAT 385
Cdd:PRK06445  299 KKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVAT 378
                         410
                  ....*....|....*.
gi 1253006213 386 LCVGGGMGIATIIERV 401
Cdd:PRK06445  379 LCVGGGQGGAVVLERV 394
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-401 4.09e-101

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 305.11  E-value: 4.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPrgKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK07850    1 MGNPVIVEAVRTP--IGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAFDPET-NMACDFIPQGIGADLIATLD 159
Cdd:PRK07850   79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPdSWDIDMPNQFEAAERIAKRR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 160 GYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK---------DQAGVVILAQDEFIKpQTTAESLAQLKPSFANmgqm 230
Cdd:PRK07850  159 GITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapvldeegqPTGETRLVTRDQGLR-DTTMEGLAGLKPVLEG---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 231 gfdaialqkypeagqvnHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALA 310
Cdd:PRK07850  234 -----------------GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLE 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 311 KAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGG 390
Cdd:PRK07850  297 KAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGG 376
                         410
                  ....*....|.
gi 1253006213 391 GMGIATIIERV 401
Cdd:PRK07850  377 ALSTGTIIERI 387
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-401 1.17e-99

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 301.65  E-value: 1.17e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTprGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK06504    1 MAEAYIVAAART--AGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGS-------DGGAWAFDPETNMACDFI--PQGIG 151
Cdd:PRK06504   79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlpakNGLGHYKSPGMEERYPGIqfSQFTG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 152 ADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK---DQAGVVILAQDEFIKPQTTAESLAQLKPsfanmg 228
Cdd:PRK06504  159 AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEitrADGSGEMHTVDEGIRFDATLEGIAGVKL------ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 229 qmgfdaIAlqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKA 308
Cdd:PRK06504  233 ------IA-----EGGRLT----AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 309 LAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCV 388
Cdd:PRK06504  298 LKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCE 377
                         410
                  ....*....|...
gi 1253006213 389 GGGMGIATIIERV 401
Cdd:PRK06504  378 GGGMANVTIVERL 390
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-400 4.88e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 293.06  E-value: 4.88e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdGALHEVKPIRLLTTLLNE-LQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWD 79
Cdd:PRK07851    1 MPEAVIVSTARSPIGRAFK-GSLKDMRPDDLAAQMVRAaLDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  80 NdVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGG-------------------------AWA 134
Cdd:PRK07851   80 F-LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSlpdtknplfaeaqartaaraeggaeAWH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 135 fDPETN--MACDFIPQGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGVVIlAQDEFIKPQT 212
Cdd:PRK07851  159 -DPREDglLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGTVV-STDDGPRAGT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 213 TAESLAQLKPSFAnmgqmgfdaialqkyPEaGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGT 292
Cdd:PRK07851  237 TYEKVSQLKPVFR---------------PD-GTVT----AGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 293 DPAIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLD 372
Cdd:PRK07851  297 SPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLN 376
                         410       420
                  ....*....|....*....|....*...
gi 1253006213 373 ELERQDKKRGMATLCVGGGMGIATIIER 400
Cdd:PRK07851  377 NLQTHDKTFGLETMCVGGGQGMAMVLER 404
PRK09051 PRK09051
beta-ketothiolase BktB;
1-401 1.79e-93

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 286.09  E-value: 1.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTprGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK09051    2 MREVVVVSGVRT--AIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAW--------AFDPETN-MACDF--IPQG 149
Cdd:PRK09051   80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWgarmgdakLVDMMVGaLHDPFgtIHMG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 150 IGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFANm 227
Cdd:PRK09051  160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVeiKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKK- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 228 gqmgfdaialqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARK 307
Cdd:PRK09051  239 --------------ENGTVT----AGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQK 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 308 ALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLC 387
Cdd:PRK09051  301 ALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMC 380
                         410
                  ....*....|....
gi 1253006213 388 VGGGMGIATIIERV 401
Cdd:PRK09051  381 IGGGQGIAAIFERL 394
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-401 3.38e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 277.40  E-value: 3.38e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK07661    1 MREAVIVAGARTPVGKAKK-GSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDggawAFDPETNMACD----FIPQGIGADLIA 156
Cdd:PRK07661   80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGH----VVRPNPRLVEAapeyYMGMGHTAEQVA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 157 TLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV-----------KDQAGVVILAQDEFIKPQTTAESLAQLKPSFA 225
Cdd:PRK07661  156 VKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdvtlrtvgennKLQEETITFSQDEGVRADTTLEILGKLRPAFN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 226 NMGQMGfdaialqkypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAA 305
Cdd:PRK07661  236 VKGSVT--------------------AGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAI 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 306 RKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMAT 385
Cdd:PRK07661  296 PKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVT 375
                         410
                  ....*....|....*.
gi 1253006213 386 LCVGGGMGIATIIERV 401
Cdd:PRK07661  376 MCIGGGMGAAGVFELL 391
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
6-400 1.07e-88

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 275.49  E-value: 1.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKGKKdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDNDVAGV 85
Cdd:PLN02287   50 IVAAYRTPICKAKR-GGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGawaFDPETN---MACD-FIPQGIGADLIATLDGY 161
Cdd:PLN02287  129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGG---VNPRVEsfsQAQDcLLPMGITSENVAERFGV 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 162 SRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQ--------AGVVILAQDEFIKPQTTAESLAQLKPSFANMGqmgfd 233
Cdd:PLN02287  206 TREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktgeEKPIVISVDDGIRPNTTLADLAKLKPVFKKNG----- 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 234 aialqkypeagqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAG 313
Cdd:PLN02287  281 ---------------TTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAG 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 314 LNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELER--QDKKRGMATLCVGGG 391
Cdd:PLN02287  346 LELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgKDCRFGVVSMCIGTG 425

                  ....*....
gi 1253006213 392 MGIATIIER 400
Cdd:PLN02287  426 MGAAAVFER 434
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-401 1.88e-87

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 270.71  E-value: 1.88e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPrgKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGAdIAKTAAIAAGWDN 80
Cdd:PRK06205    1 MRDAVICEPVRTP--VGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAW-------------AFDPETNMACDF-I 146
Cdd:PRK06205   78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWgvrgggvqlhdrlARGRETAGGRRFpV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 147 PQGI--GADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK---DQAGVVILAQDEFIKPQTTAESLAQLK 221
Cdd:PRK06205  158 PGGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTvpqRKGDPTVVDRDEHPRADTTLESLAKLR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 222 PsfanmgqmgfdaIALQKYPEAgqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGP 301
Cdd:PRK06205  238 P------------IMGKQDPEA-----TVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGP 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 302 APAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPA---KVNVNGGAIALGHPLGATGAMILGTLLDELERQD 378
Cdd:PRK06205  301 VPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQ 380
                         410       420
                  ....*....|....*....|...
gi 1253006213 379 KKRGMATLCVGGGMGIATIIERV 401
Cdd:PRK06205  381 ARYGLETMCIGGGQGLAAVFERV 403
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-401 8.73e-87

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 268.95  E-value: 8.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK08131    1 MLDAYIYDGLRSPFGR--HAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV--AMGSDGGAWA-----FDP-----------ETNMA 142
Cdd:PRK08131   79 TVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRApfVMGKAESAFSrdakvFDTtigarfpnpkiVAQYG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 143 CDFIPQGigADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAG----VVILAQDEFIKPQTTAESLA 218
Cdd:PRK08131  159 NDSMPET--GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGrklpPKLVAEDEHPRPSSTVEALT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 219 QLKPSFanmgqmgfdaialqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIML 298
Cdd:PRK08131  237 KLKPLF-----------------EGGVVT----AGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMG 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 299 TGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQV--DPAKVNVNGGAIALGHPLGATGAMILGTLLDELER 376
Cdd:PRK08131  296 IGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQR 375
                         410       420
                  ....*....|....*....|....*
gi 1253006213 377 QDKKRGMATLCVGGGMGIATIIERV 401
Cdd:PRK08131  376 RGKRYAVVSLCIGVGQGLAMVIERV 400
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
3-401 1.43e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 250.33  E-value: 1.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   3 EAYIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTpIGDQGADIAKTAAIAAGWDNDV 82
Cdd:PRK06633    4 PVYITHAKRTAFGSFM--GSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPKEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  83 AGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWA------------FDPETNMACDFIpQGI 150
Cdd:PRK06633   81 PGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAkfgdikmvdlmqYDGLTDVFSGVF-MGI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 151 GADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK--DQAGVVILAQDEFIKPQTTAESLAQLKPSFANmg 228
Cdd:PRK06633  160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEvtIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK-- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 229 qmgfdaialqkypeagqvNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKA 308
Cdd:PRK06633  238 ------------------NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 309 LAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCV 388
Cdd:PRK06633  300 LSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCI 379
                         410
                  ....*....|...
gi 1253006213 389 GGGMGIATIIERV 401
Cdd:PRK06633  380 GGGMGMAMCVEAV 392
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-399 8.16e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 248.09  E-value: 8.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDN 80
Cdd:PRK08235    1 MSKTVIVSAARTPFGK--FGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGGAWAF---DPET-------NMACDF--IPQ 148
Cdd:PRK08235   78 EVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmgDNEVidlmvadGLTCAFsgVHM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 149 GIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV---KDQAGVVILAQDEFIKPQTTAESLAQLKPSFA 225
Cdd:PRK08235  158 GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtipQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 226 NMGQMGfdaialqkypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAA 305
Cdd:PRK08235  238 KTGTIT--------------------AGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAI 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 306 RKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMAT 385
Cdd:PRK08235  298 NALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAA 377
                         410
                  ....*....|....
gi 1253006213 386 LCVGGGMGIATIIE 399
Cdd:PRK08235  378 ICSGGGQGDAVLIE 391
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-400 2.69e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 241.72  E-value: 2.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDN 80
Cdd:PRK05656    1 MQDVVIVAATRTAIGSFQ--GSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV--------------------AMGSDGGAWAFDpETN 140
Cdd:PRK05656   78 SVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLApyvlpgartglrmghaqlvdSMITDGLWDAFN-DYH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 141 MacdfipqGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV---KDQAGVVILAQDEFIKPQTTAESL 217
Cdd:PRK05656  157 M-------GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlipQRKGEPLAFATDEQPRAGTTAESL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 218 AQLKPSFANMGQMGfdaialqkypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIM 297
Cdd:PRK05656  230 AKLKPAFKKDGSVT--------------------AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 298 LTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQ 377
Cdd:PRK05656  290 GIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRR 369
                         410       420
                  ....*....|....*....|...
gi 1253006213 378 DKKRGMATLCVGGGMGIATIIER 400
Cdd:PRK05656  370 DAKKGLATLCIGGGQGVALAIER 392
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
5-401 3.38e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 242.62  E-value: 3.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   5 YIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQgADIAKTAAIAAGWDNDVAG 84
Cdd:PRK08170    6 YIVDGARTPFLKAR--GGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDE-ANIARVVALRLGCGEKVPA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  85 VQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSR--VAMGSDGGAW------------------AFDPE------ 138
Cdd:PRK08170   83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHapLLFSEKMVRWlagwyaaksigqklaalgKLRPSylapvi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 139 ------TNMACDFIpQGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFeRSIVPVKDQAGVViLAQDEFIKPQT 212
Cdd:PRK08170  163 gllrglTDPVVGLN-MGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLFDRDGKF-YDHDDGVRPDS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 213 TAESLAQLKPSFAnmgqmgfdaialQKYpeaGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGT 292
Cdd:PRK08170  240 SMEKLAKLKPFFD------------RPY---GRVT----AGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAAL 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 293 DPAIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQ-----------------VDPAKVNVNGGAIAL 355
Cdd:PRK08170  301 DPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIAL 380
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1253006213 356 GHPLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIERV 401
Cdd:PRK08170  381 GHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-399 8.13e-73

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 232.74  E-value: 8.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDQGADIAKTAAIAAGWDN 80
Cdd:PRK07108    1 MTEAVIVSTARTPLAKSWR-GAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVA------MGSDGGAWAFDPETNMacdfiPQGIGADL 154
Cdd:PRK07108   80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQnemnrhMLREGWLVEHKPEIYW-----SMLQTAEN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 155 IATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAGV------------VILAQDEFIKPQTTAESLAQLKP 222
Cdd:PRK07108  155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVadkatgrlftkeVTVSADEGIRPDTTLEGVSKIRS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 223 SFanmgqmgfdaialqkypEAGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPA 302
Cdd:PRK07108  235 AL-----------------PGGVIT----AGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPV 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 303 PAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRG 382
Cdd:PRK07108  294 FAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYV 373
                         410
                  ....*....|....*..
gi 1253006213 383 MATLCVGGGMGIATIIE 399
Cdd:PRK07108  374 VVTMCIGGGQGAAGLFE 390
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
6-401 2.73e-67

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 218.42  E-value: 2.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAGV 85
Cdd:PLN02644    5 IVGVARTPIGGFL--GSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSAN-LGQAPARQAALGAGLPPSTICT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMS-------------RVAMGS--DG----GAWafDPETNmacdfI 146
Cdd:PLN02644   82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnapkylpearkgsRLGHDTvvDGmlkdGLW--DVYND-----F 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 147 PQGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAG----VVILAQDEFIKpQTTAESLAQLKP 222
Cdd:PLN02644  155 GMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGrgrpSVIVDKDEGLG-KFDPAKLRKLRP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 223 SFANMGqmgfdaialqkypeaGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPA 302
Cdd:PLN02644  234 SFKEDG---------------GSVT----AGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPA 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 303 PAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRG 382
Cdd:PLN02644  295 LAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYG 374
                         410
                  ....*....|....*....
gi 1253006213 383 MATLCVGGGMGIATIIERV 401
Cdd:PLN02644  375 VAGICNGGGGASAIVVELM 393
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-401 1.08e-65

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 213.47  E-value: 1.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   3 EAYIIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHnldTSQVDDIVLGCVTpigDQGADIAKTAAIAAGWDNDV 82
Cdd:PRK06690    2 RAVIVEAKRTPIGK--KNGMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV---GPGGNVARLSALEAGLGLHI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  83 AGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMGSDGgawAFDPETNMACDFipqGIGADLIATLDGYS 162
Cdd:PRK06690   74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRA---RFSPETIGDPDM---GVAAEYVAERYNIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 163 RTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDQAgvvilaqDEFIKPQTTAESLAQ-LKPSFANMGQMGfdaialqkyp 241
Cdd:PRK06690  148 REMQDEYACLSYKRTLQALEKGYIHEEILSFNGLL-------DESIKKEMNYERIIKrTKPAFLHNGTVT---------- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 242 eagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDIDL 321
Cdd:PRK06690  211 ----------AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 322 FEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIERV 401
Cdd:PRK06690  281 FEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-401 1.61e-60

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 200.62  E-value: 1.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKdgALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGDqGADIAKTAAIAAGWDN 80
Cdd:PRK06366    1 MKDVYIVSAKRTAIGKFGR--SFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGV-GQNPAGQAAYHAGLPF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVA-MGSDGGAWA--------FDPETNMACD------- 144
Cdd:PRK06366   78 GVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPfLLPSDLRWGpkhllhknYKIDDAMLVDglidafy 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 145 FIPQGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDqagvviLAQDEFIKpQTTAESLAQLKPSF 224
Cdd:PRK06366  158 FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND------LDRDEGIR-KTTMEDLAKLPPAF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 225 ANMGqmgfdaialqkypeagqvnhVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPAPA 304
Cdd:PRK06366  231 DKNG--------------------ILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPA 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 305 ARKALAKAGLNIEDIDLFEVNEAF--AAVVLRfiTELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRG 382
Cdd:PRK06366  291 TRKLLEKQNKSIDYYDLVEHNEAFsiASIIVR--DQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTG 368
                         410
                  ....*....|....*....
gi 1253006213 383 MATLCVGGGMGIATIIERV 401
Cdd:PRK06366  369 LATLCHGGGGAHTLTLEMV 387
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
278-400 1.83e-54

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: 176.29  E-value: 1.83e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 278 LKPRAKVLATALVGTDPAIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGH 357
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1253006213 358 PLGATGAMILGTLLDELERQDKKRGMATLCVGGGMGIATIIER 400
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
6-399 2.83e-54

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 184.71  E-value: 2.83e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAGV 85
Cdd:PRK06954   11 IASAARTPMAAFQ--GEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGCT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMS-------------RVAMGS-------DGGAWAFDPETNMacdf 145
Cdd:PRK06954   88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTnapyllpkarggmRMGHGQvldhmflDGLEDAYDKGRLM---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 146 ipqGIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVK--DQAGVVILAQDEfiKP-QTTAESLAQLKP 222
Cdd:PRK06954  164 ---GTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTvaGKKGDTVIDRDE--QPfKANPEKIPTLKP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 223 SFANMGQMGfdaialqkypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTDPAIMLTGPA 302
Cdd:PRK06954  239 AFSKTGTVT--------------------AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 303 PAARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQDKKRG 382
Cdd:PRK06954  299 GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRG 378
                         410
                  ....*....|....*..
gi 1253006213 383 MATLCVGGGMGIATIIE 399
Cdd:PRK06954  379 VASLCIGGGEATAMGIE 395
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
9-399 3.22e-50

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: 173.83  E-value: 3.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   9 AIRTPRGK-GKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAGVQI 87
Cdd:cd00826     3 AAMTAFGKfGGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAG-EGQNCAQQAAMHAGGLQEAPAIGM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  88 NRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMgSDGGAWAFDPETNMACdfipqgigadliatldgySRTEVD 167
Cdd:cd00826    82 NNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAE-NNAKEKHIDVLINKYG------------------MRACPD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 168 QFAAASQHKAAAAQAQGHFERSIVP--VKDQAGVVILAQDEFIKPQTTA--ESLAQLKPSFANMGQMGfdaialqkypea 243
Cdd:cd00826   143 AFALAGQAGAEAAEKDGRFKDEFAKfgVKGRKGDIHSDADEYIQFGDEAslDEIAKLRPAFDKEDFLT------------ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 244 gqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLK-------PRAKVLATALVGTDPA----IMLTGPAPAARKALAKA 312
Cdd:cd00826   211 --------AGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKA 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 313 GLNIEDIDLFEVNEAFAAVVLRFITELQVDPAK------------------VNVNGGAIALGHPLGATGAMILGTLLDEL 374
Cdd:cd00826   283 GLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFEL 362
                         410       420       430
                  ....*....|....*....|....*....|
gi 1253006213 375 ERQDKKR-----GMATLCVGGGMGIATIIE 399
Cdd:cd00826   363 KGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
6-400 9.55e-46

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 162.85  E-value: 9.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   6 IIDAIRTPRGKgkKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIgDQGADIAKTAAIAAGWDNDVAGV 85
Cdd:PRK08963    9 IVSGLRTPFAK--QATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQM-PEAPNIAREIVLGTGMNVHTDAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  86 QINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRVAMG-SDGGAWAFdPETNMA---------------CDFIPQ- 148
Cdd:PRK08963   86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvSKKLARAL-VDLNKArtlgqrlklfsrlrlRDLLPVp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 149 ------------GIGADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSI----VPVKDQAgvviLAQDEFIKPQT 212
Cdd:PRK08963  165 pavaeystglrmGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtahVPPYKQP----LEEDNNIRGDS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 213 TAESLAQLKPSFAnmgqmgfdaialQKYpeaGQVNhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGT 292
Cdd:PRK08963  241 TLEDYAKLRPAFD------------RKH---GTVT----AANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 293 DP-AIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVL---------RFITEL--------QVDPAKVNVNGGAIA 354
Cdd:PRK08963  302 DVwQDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLanlqmfaseRFAREKlgrsqaigEVDMSKFNVLGGSIA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1253006213 355 LGHPLGATGA-MILGTlLDELERQDKKRGMATLCVGGGMGIATIIER 400
Cdd:PRK08963  382 YGHPFAATGArMITQT-LHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-271 1.09e-44

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: 155.54  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   5 YIIDAIRTPRGKGKkdGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIGdQGADIAKTAAIAAGWDNDVAG 84
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAG-EGQNPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  85 VQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV--AMGSDGGAWAFDPETNM-----------ACDFIPQGIG 151
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHApyALPTDARSGLKHGDEKKhdllipdgltdAFNGYHMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 152 ADLIATLDGYSRTEVDQFAAASQHKAAAAQAQGHFERSIVPV--KDQAGVVILAQDEFIKPQTTAESLAQLKPSFANMGQ 229
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtvKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGT 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1253006213 230 MgfdaialqkypeagqvnhvhHAGNSSGIVDGAALVLIASEQ 271
Cdd:pfam00108 239 V--------------------TAGNASPINDGAAAVLLMSES 260
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
31-400 6.55e-40

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 146.97  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  31 LLTTLLNELQQRHNLDTSQVDDIVLGCVTpigDQGAD--IAKTAAIAAGWDNDVAGVQINRFCASGLEAVNLAAQKVRSG 108
Cdd:PRK09268   34 MLTAALDGLVDRFGLQGERLGEVVAGAVL---KHSRDfnLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 109 WEDLIVAGGVESMSRVAMGSDGGAWAFDPETNMA---------------CDFIPQ-------------GIGADLIATLDG 160
Cdd:PRK09268  111 QIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAkttgdrlkalgklrpKHLAPEiprngeprtglsmGEHAAITAKEWG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 161 YSRTEVDQFAAASQHKAAAAQAQGHFERSIVPVKDqagvviLAQDEFIKPQTTAESLAQLKPSF--ANMGQMGfdaialq 238
Cdd:PRK09268  191 ISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG------LTRDNNLRPDSSLEKLAKLKPVFgkGGRATMT------- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 239 kypeagqvnhvhhAGNSSGIVDGAALVLIASEQAVQQHNLKPRAKVLA--TALV----GTDPaiMLTGPAPAARKALAKA 312
Cdd:PRK09268  258 -------------AGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDaeTAAVdfvhGKEG--LLMAPAYAVPRLLARN 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 313 GLNIEDIDLFEVNEAFAAVVLrfiTELQ--------------------VDPAKVNVNGGAIALGHPLGATGAMILGTLLD 372
Cdd:PRK09268  323 GLTLQDFDFYEIHEAFASQVL---ATLKawedeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIVATLAK 399
                         410       420
                  ....*....|....*....|....*...
gi 1253006213 373 ELERQDKKRGMATLCVGGGMGIATIIER 400
Cdd:PRK09268  400 LLAEKGSGRGLISICAAGGQGVTAILER 427
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
231-398 1.04e-20

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: 90.58  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 231 GFDAIAL-QKYPEAGQVNHVHHAG-NSSGIVDGAALVLIASEQAVQQHNLKPRAKVLATALVGTD----PAIMLTGPAPA 304
Cdd:cd00327    71 GLTALALaVQQVQNGKADIVLAGGsEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 305 ARKALAKAGLNIEDIDLFEVNEAFAAVVLRFITELQVDPAKV---NVNGGAIALGHPLGATGAMILGTLLDELERQDKKR 381
Cdd:cd00327   151 ARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP 230
                         170       180
                  ....*....|....*....|....
gi 1253006213 382 -------GMATLCVGGGMGIATII 398
Cdd:cd00327   231 tpreprtVLLLGFGLGGTNAAVVL 254
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
44-398 2.54e-16

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: 79.61  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  44 NLDTSQVDDIVLGCVTPIGDQGaDIAKTAAIAAGWDNdVAGVQINRFCASGLEAVNLAAQKVRSGWEDLIVAGGVESMSR 123
Cdd:cd00829    32 GLEPADIDAVVVGNAAGGRFQS-FPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 124 VAMGSDGGAWAFDPEtnmacDFIPQGIGADLIATLDGYSRTEvdqfaaasqhkaaaaqaqgHFERSIVPVKDQAGVVIL- 202
Cdd:cd00829   110 VPTGDEAGGRASDLE-----WEGPEPPGGLTPPALYALAARR-------------------YMHRYGTTREDLAKVAVKn 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 203 ---------AQdeFIKPQTTAESLAQlkpsfanmgQMGFDAIalqkypeagqvnhvhHAGNSSGIVDGAALVLIASEQAV 273
Cdd:cd00829   166 hrnaarnpyAQ--FRKPITVEDVLNS---------RMIADPL---------------RLLDCCPVSDGAAAVVLASEERA 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 274 QQHNLKPrAKVLATAlVGTDPA--------IMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVL------------ 333
Cdd:cd00829   220 RELTDRP-VWILGVG-AASDTPslserddfLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELlaledlgfcekg 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1253006213 334 ---RFITELQVDP---AKVNVNGGAIALGHPLGATGAMILGTLLDEL-----ERQDKKRGMATLCVGGGMGIATII 398
Cdd:cd00829   298 eggKLVREGDTAIggdLPVNTSGGLLSKGHPLGATGLAQAVEAVRQLrgeagARQVPGARVGLAHNIGGTGSAAVV 373
PRK06064 PRK06064
thiolase domain-containing protein;
91-401 5.92e-11

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 63.38  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  91 CASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV-------AMGSDGGA-WafdpETNMACDFIpqGIGAdLIATL--DG 160
Cdd:PRK06064   85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVptpdateAIARAGDYeW----EEFFGATFP--GLYA-LIARRymHK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 161 YSRTEVDQfaaasqhkaaaaqaqghferSIVPVKDQAGVVIlaqdefikpqttaESLAQLKpsfanmgqmgfDAIALQKY 240
Cdd:PRK06064  158 YGTTEEDL--------------------ALVAVKNHYNGSK-------------NPYAQFQ-----------KEITVEQV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 241 PEAGQVNHVHHAGNSSGIVDGAALVLIASEQAVQQHNLKPrAKVLATAlVGTDPAI------MLTGPAP--AARKALAKA 312
Cdd:PRK06064  194 LNSPPVADPLKLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASG-QASDTIAlhdrkdFTTLDAAvvAAEKAYKMA 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 313 GLNIEDIDLFEVNEAF--AAVV----LRFI-------------TELQVDPAkVNVNGGAIALGHPLGATG----AMILGT 369
Cdd:PRK06064  272 GIEPKDIDVAEVHDCFtiAEILayedLGFAkkgeggklaregqTYIGGDIP-VNPSGGLKAKGHPVGATGvsqaVEIVWQ 350
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1253006213 370 LLDELE---RQDKKRGMA-TLCVGGGMGIA--TIIERV 401
Cdd:PRK06064  351 LRGEAEkgrQQVIGAGYGlTHNVGGTGHTAvvHILSRK 388
PRK08256 PRK08256
lipid-transfer protein; Provisional
260-363 2.21e-08

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 55.67  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 260 DGAALVLIASEQAVQQHNLKPRAKVLATALVgTDPAIMLTGPAP-----------AARKALAKAGLNIEDIDLFEVNEAF 328
Cdd:PRK08256  215 CGAAAAIVCSEEFARKHGLDRAVEIVAQAMT-TDTPSTFDGRSMidlvgydmtraAAQQVYEQAGIGPEDIDVVELHDCF 293
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1253006213 329 AAVVLrfIT-------------ELQVDPAK-------VNVNGGAIALGHPLGATG 363
Cdd:PRK08256  294 SANEL--LTyealglcpegeaeKFIDDGDNtyggrwvVNPSGGLLSKGHPLGATG 346
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
256-363 1.41e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 53.36  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 256 SGIVDGAALVLIASEQAVQQHNLKP------RAKVLATALVG-----TDPAIMLTGPApAARKALAKAGLNIEDIDLFEV 324
Cdd:PTZ00455  256 SQVSDGGAGLVLASEEGLQKMGLSPndsrlvEIKSLACASGNlyedpPDATRMFTSRA-AAQKALSMAGVKPSDLQVAEV 334
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006213 325 NEAFAAVVLRFITELQV-DPAK-----------------VNVNGGAIALGHPLGATG 363
Cdd:PTZ00455  335 HDCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATG 391
PRK12578 PRK12578
thiolase domain-containing protein;
91-366 1.79e-07

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 52.93  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  91 CASGLEAVNLAAQKVRSGWEDLIVAGGVESMSRV------AMGSDGGAWAFdpETNMACDFIPQGIGADLIATLDGYSRT 164
Cdd:PRK12578   82 CATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVdtstslAIGGRGGNYQW--EYHFYGTTFPTYYALYATRHMAVYGTT 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 165 EVDQfaaasqhkaaaaqaqghferSIVPVKDQAGVVILAQDEFIKPQTTAESLAQLKPSFAnmgqmgfdaIALQkypeag 244
Cdd:PRK12578  160 EEQM--------------------ALVSVKAHKYGAMNPKAHFQKPVTVEEVLKSRAISWP---------IKLL------ 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 245 qvnhvhhagNSSGIVDGAALVLIASEQAVQQhnLKPRAKVLATAL-VGTDPAIM--------LTGPAPAARKALAKAGLN 315
Cdd:PRK12578  205 ---------DSCPISDGSATAIFASEEKVKE--LKIDSPVWITGIgYANDYAYVarrgewvgFKATQLAARQAYNMAKVT 273
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 316 IEDIDLFEVNEAFAAVVL---------------RFITELQVDP-AKVNVN--GGAIALGHPLGATG-AMI 366
Cdd:PRK12578  274 PNDIEVATVHDAFTIAEImgyedlgftekgkggKFIEEGQSEKgGKVGVNlfGGLKAKGHPLGATGlSMI 343
PRK07516 PRK07516
thiolase domain-containing protein;
256-401 1.08e-05

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 47.25  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 256 SGIVDGAALVLIASEQAVQQhnLKPRAKVLATALVGT-------DPaIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAF 328
Cdd:PRK07516  213 SLVSDGAAALVLADAETARA--LQRAVRFRARAHVNDflplsrrDP-LAFEGPRRAWQRALAQAGVTLDDLSFVETHDCF 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 329 AAVVL---------------RFITELQVDPA---KVNVNGGAIALGHPLGATG-------AMILGTLLDELERQDKKRG- 382
Cdd:PRK07516  290 TIAELieyeamglappgqgaRAIREGWTAKDgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKLAg 369
                         170       180
                  ....*....|....*....|....*
gi 1253006213 383 ---MatlcvgGGMGIA---TIIERV 401
Cdd:PRK07516  370 vfnM------GGAAVAnyvSILERV 388
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
260-377 1.25e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 46.97  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 260 DGAALVLIASEQAVQQHNLKPRAKVLATALvgTDPAIMLTGPAP-------AARKALAKAGLNIEDIDLF-------EVN 325
Cdd:PRK05952  210 EGGAILVLESAELAQKRGAKIYGQILGFGL--TCDAYHMSAPEPdgksaiaAIQQCLARSGLTPEDIDYIhahgtatRLN 287
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1253006213 326 EAFAAVVLRfitelQVDPAKVNVNGGAIALGHPLGATGAMILGTLLDELERQ 377
Cdd:PRK05952  288 DQREANLIQ-----ALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQ 334
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
256-367 2.87e-05

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 45.83  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 256 SGIVDGAALVLIASEQAVQQHnlkPRAKVLA--------TALVGTDPAIMLTGPAP--------AARKALAKAGLNIEDI 319
Cdd:PRK06289  220 SQVTDGGAGVVLASDAYLRDY---ADARPIPrikgwghrTAPLGLEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDL 296
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1253006213 320 DLFEVNEAFAAVVL---------------RFITELQVDPA---KVNVNGGAIALGHPLGATGAMIL 367
Cdd:PRK06289  297 DGFEVHDCFTPSEYlaidhigltgpgeswKAIENGEIAIGgrlPINPSGGLIGGGHPVGASGVRML 362
PRK06066 PRK06066
thiolase domain-containing protein;
256-391 1.94e-04

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 43.20  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 256 SGIVDGAALVLIASEQAVQQHNLKP---RAKVLATALVGTDPAIMltGPAPAARKA--LAK--AGLN--IEDIDLFEVNE 326
Cdd:PRK06066  208 APFVDGAIVVVLASEEVAKKLTDDPvwiKGIGWSTESSNLETAEL--GKANYMRIAadMAYkmAGIEspRKEVDAAEVDD 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 327 AFAAVVLRFITELQVDPA------------------KVNVNGGAIALGHPLGATGamiLGTLLDELERQdkkRGMATLCV 388
Cdd:PRK06066  286 RYSYKELQHIEALRLSEEpekdsllregnfdpqgelPVNPSGGHLAKGVPLEASG---LSLLLDAVEYL---RGEAGARQ 359

                  ...
gi 1253006213 389 GGG 391
Cdd:PRK06066  360 GKA 362
PRK06365 PRK06365
thiolase domain-containing protein;
260-399 3.81e-04

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 42.59  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 260 DGAALVLIASEQAVQQHNLKP-RAKVLATALVGTDPAIMLTGPAP--------------------------AARKALAKA 312
Cdd:PRK06365  227 DGAACAILASEDKAFEITDKPvLIKAIGTGSDTLRLADRPFGEVPllpnespddykdlrypgvhsfragrmAAKEAYEMA 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 313 GLN--IEDIDLFEVNEAFAAVVLRFITELQ----------VDPAK--------VNVNGGAIALGHPLGATGAM------- 365
Cdd:PRK06365  307 GITdpLNDLDLIELHDAYTSSEIQTYEDLGlckygeggqfIESGKpelpgklpVNPSGGLLAAGHAVGATGIMqavfmfw 386
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1253006213 366 -ILGTL-----LDELERQDKKRGMATLCVGGGMGI-ATIIE 399
Cdd:PRK06365  387 qLQGRIkkhfhDDYLQVKNAKRGLIHSHAGTGTYVtVTILE 427
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
91-137 4.43e-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: 4.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1253006213  91 CASGLEAVNLAAQKVRSGWEDLIVAGGVESM---------SRVAMGSDGG-AWAFDP 137
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGGVNLLltplgfagfSAAGMLSPDGpCKAFDP 229
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
216-320 1.02e-03

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 41.17  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 216 SLAQLKP----SFANMGQMGFDAIALQkyPEAGQVNHVHhagNSSGIVDG--AALVLIASEQAVQQHNLKPRAKVLATAL 289
Cdd:PRK07103  194 ALMDLSYwecqALRSLGAMGSDRFADE--PEAACRPFDQ---DRDGFIYGeaCGAVVLESAESARRRGARPYAKLLGWSM 268
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1253006213 290 V-----GTDPAimLTGPAPAARKALAKAGLNIEDID 320
Cdd:PRK07103  269 RldanrGPDPS--LEGEMRVIRAALRRAGLGPEDID 302
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
302-393 1.59e-03

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 40.09  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 302 APAARKALAKAGLNIEDIDLF---EVNEAFAAVVLRfitELQVDPAKVNVNggaIA-LGHplgaTGAMILGTLLDELERQ 377
Cdd:COG0332   227 PEVIREALEKAGLTLDDIDWFiphQANLRIIEAVAK---RLGLPEEKVVVN---IDrYGN----TSAASIPLALDEALRE 296
                          90
                  ....*....|....*..
gi 1253006213 378 DK-KRGMATLCVGGGMG 393
Cdd:COG0332   297 GRiKPGDLVLLAGFGAG 313
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
1-132 2.28e-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: 39.72  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213   1 MSEAYIIDAIRTPRGKGKKDGALHEVKPIRLLTTLLNELQQRHNLDTSQVDDIVLGCVTPIgDQGADIAKTAAIAAGwDN 80
Cdd:cd00827    21 LAEGLGVDPGKYTTGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPI-DKGKSAATYLAELLG-LT 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213  81 DVAGVQINRFCASGLEAVNLAAQKVRSG-WED-LIVAGGV------ESMSRVAMGSDGGA 132
Cdd:cd00827    99 NAEAFDLKQACYGGTAALQLAANLVESGpWRYaLVVASDIasylldEGSALEPTLGDGAA 158
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
91-122 7.19e-03

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 38.29  E-value: 7.19e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1253006213  91 CASGLEAVNLAAQKVRSGWEDLIVAGGVESMS 122
Cdd:cd00834   161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
PRK06158 PRK06158
thiolase; Provisional
261-401 7.53e-03

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 38.09  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1253006213 261 GAALVLIASEQAVQQHnlKPRAKVLATAL------VGTDPAIMLTGPAPAARKALAKAGLNIEDIDLFEVNEAFAAVVLR 334
Cdd:PRK06158  212 AGAVVMVRADRARDLP--RPPVYVLGAAAatwhrqISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINTIL 289
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1253006213 335 FITELQVDP---AKVNVNGGAIALGhplgatGAMILGTlldelerqdkkRGMATLCVGGGM-GIATIIERV 401
Cdd:PRK06158  290 FLEDLGFCAkgeGGAFVEGGRIAPG------GRLPVNT-----------NGGGLSCVHPGMyGLFLLIEAV 343
 
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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