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Conserved domains on  [gi|17535921|ref|NP_495456|]
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Acetyl-CoA C-acetyltransferase [Caenorhabditis elegans]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

thiolase family protein may catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine; such as acetyl-CoA acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl-CoA to another molecule of acetyl-CoA to form acetoacetyl-CoA

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
7-389 3.06e-168

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: 475.43  E-value: 3.06e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTV 86
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  87 NKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPF-GGIQMTDGISKDGLEDIKEKGPMGLCAEKTV 165
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 166 KDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLI-ESKVSSLKPVFVRDgtGTITP 244
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTtLEKLAKLKPAFKKD--GTVTA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 245 ANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTV 323
Cdd:cd00751 239 GNASGINDGAAAVLLMsEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921 324 LAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKK 389
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
7-389 3.06e-168

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: 475.43  E-value: 3.06e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTV 86
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  87 NKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPF-GGIQMTDGISKDGLEDIKEKGPMGLCAEKTV 165
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 166 KDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLI-ESKVSSLKPVFVRDgtGTITP 244
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTtLEKLAKLKPAFKKD--GTVTA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 245 ANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTV 323
Cdd:cd00751 239 GNASGINDGAAAVLLMsEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921 324 LAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKK 389
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
4-390 3.91e-163

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: 462.61  E-value: 3.91e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPFGG-IQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKL--IEsKVSSLKPVFVRDgtG 240
Cdd:COG0183 162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDttLE-KLAKLKPAFKKD--G 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 241 TITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAF 319
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKElGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535921 320 AVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIKKL 390
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELErrGGRYGLATMCIGGGQGIALIIERV 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
8-388 3.11e-146

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: 419.71  E-value: 3.11e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921     8 ILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTVN 87
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    88 KVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP---RGEIPFGGIQMTDGISKDgLEDIKEKGPMGLCAEKT 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrslRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   165 VKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEE-YKKLIESKVSSLKPVFVRDgtGTIT 243
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGiRPNTTLEKLAKLKPAFDPD--GTVT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   244 PANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVT 322
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKElGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921   323 VLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIK 388
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKrrGGRYGLATMCIGGGQGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
4-390 3.47e-138

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 399.53  E-value: 3.47e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCA 161
Cdd:PRK05790  82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  162 EKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKK---LIESkVSSLKPVFVRDg 238
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRpdtTAES-LAKLRPAFDKD- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  239 tGTITPANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNE 317
Cdd:PRK05790 240 -GTVTAGNASGINDGAAAVVVMsEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535921  318 AFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK05790 319 AFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRrgAKKGLATLCIGGGQGVALIVERP 393
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
6-262 1.12e-87

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: 266.09  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921     6 VFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVT 85
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP---RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEE-YKKLIESKVSSLKPVFVRDgtGT 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGiRPPTTAEPLAKLKPAFDKE--GT 238
                         250       260
                  ....*....|....*....|.
gi 17535921   242 ITPANASSLNDGAVATVVVGE 262
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSE 259
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
7-389 3.06e-168

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: 475.43  E-value: 3.06e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTV 86
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  87 NKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPF-GGIQMTDGISKDGLEDIKEKGPMGLCAEKTV 165
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGrLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 166 KDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLI-ESKVSSLKPVFVRDgtGTITP 244
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTtLEKLAKLKPAFKKD--GTVTA 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 245 ANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTV 323
Cdd:cd00751 239 GNASGINDGAAAVLLMsEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921 324 LAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKK 389
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRrgGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
4-390 3.91e-163

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: 462.61  E-value: 3.91e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPFGG-IQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMnAKLVDPMINPGLTDPYTGLSMGETAE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKL--IEsKVSSLKPVFVRDgtG 240
Cdd:COG0183 162 NVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDttLE-KLAKLKPAFKKD--G 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 241 TITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAF 319
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKElGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535921 320 AVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIKKL 390
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELErrGGRYGLATMCIGGGQGIALIIERV 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
8-388 3.11e-146

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: 419.71  E-value: 3.11e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921     8 ILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTVN 87
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    88 KVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP---RGEIPFGGIQMTDGISKDgLEDIKEKGPMGLCAEKT 164
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrslRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   165 VKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEE-YKKLIESKVSSLKPVFVRDgtGTIT 243
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGiRPNTTLEKLAKLKPAFDPD--GTVT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   244 PANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVT 322
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKElGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921   323 VLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIK 388
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKrrGGRYGLATMCIGGGQGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
4-390 3.47e-138

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 399.53  E-value: 3.47e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCA 161
Cdd:PRK05790  82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPgsRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  162 EKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKK---LIESkVSSLKPVFVRDg 238
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRpdtTAES-LAKLRPAFDKD- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  239 tGTITPANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNE 317
Cdd:PRK05790 240 -GTVTAGNASGINDGAAAVVVMsEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535921  318 AFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK05790 319 AFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRrgAKKGLATLCIGGGQGVALIVERP 393
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
4-390 4.76e-130

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 379.05  E-value: 4.76e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCA 161
Cdd:PLN02644  81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPeaRKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  162 EKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSE--VVITEDEEYKKLIESKVSSLKPVFVRDGt 239
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGKFDPAKLRKLRPSFKEDG- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  240 GTITPANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEA 318
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVsGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535921  319 FAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKKL 390
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSknGKYGVAGICNGGGGASAIVVELM 393
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
6-388 9.16e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 332.63  E-value: 9.16e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    6 VFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVT 85
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISKDGLEDIKEKG-PMGLCAE 162
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPkaRGGMRMGHGQVLDHMFLDGLEDAYDKGrLMGTFAE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIESKVSSLKPVFVRDgtGTI 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKT--GTV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  243 TPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAV 321
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRlGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535921  322 TVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIK 388
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRArgGKRGVASLCIGGGEATAMGIE 395
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
5-388 3.25e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 328.21  E-value: 3.25e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    5 KVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAV 84
Cdd:PRK08235   3 KTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   85 TVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGE--IPFGGIQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:PRK08235  83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARwgYRMGDNEVIDLMVADGLTCAFSGVHMGVYGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSE-VVITEDEEYKK--LIEsKVSSLKPVFvrDGT 239
Cdd:PRK08235 163 EVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDpIVVAKDEAPRKdtTIE-KLAKLKPVF--DKT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  240 GTITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEA 318
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDrAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535921  319 FAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIK 388
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRrgGGIGIAAICSGGGQGDAVLIE 391
PRK09051 PRK09051
beta-ketothiolase BktB;
2-390 8.88e-95

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 288.78  E-value: 8.88e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    2 SDKKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVT 80
Cdd:PRK09051   1 MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEpRDMYLSRVAAINAGVPQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   81 TQAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIpfgGIQMTDGISKDG----LEDIKEKGP 156
Cdd:PRK09051  81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARW---GARMGDAKLVDMmvgaLHDPFGTIH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  157 MGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIE-SKVSSLKPVFV 235
Cdd:PRK09051 158 MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTlEDLAKLKPVFK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  236 RDGtGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWE 314
Cdd:PRK09051 238 KEN-GTVTAGNASGINDGAAAVVLAEADAAEArGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIE 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921  315 LNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK09051 317 ANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELqrIGGRYALVTMCIGGGQGIAAIFERL 394
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
4-389 2.36e-89

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 275.06  E-value: 2.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGS------FANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGlgQNVT---RQISLS 74
Cdd:PRK06445   2 EDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVG--ENWLyggRHPIFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   75 AGLPVTTQAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYvprgEIPFGGIQMTDGISKDGLE-DIKE 153
Cdd:PRK06445  80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMG----DNPHIEPNPKLLTDPKYIEyDLTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  154 KGPMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKK--LIEsKVSSLK 231
Cdd:PRK06445 156 GYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPdtSLE-KLAKLP 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  232 PVFVRDGTgtITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDI 310
Cdd:PRK06445 235 PAFKPDGV--ITAGNSSPLNSGASYVLLMSKKAVKKyGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  311 ALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIK 388
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQikGKDYGVATLCVGGGQGGAVVLE 392

                 .
gi 17535921  389 K 389
Cdd:PRK06445 393 R 393
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
4-389 1.27e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 273.30  E-value: 1.27e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK05656   2 QDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCA 161
Cdd:PRK05656  82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPgaRTGLRMGHAQLVDSMITDGLWDAFNDYHMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  162 EKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVI--TEDEEYKKLIESKVSSLKPVFVRDgt 239
Cdd:PRK05656 162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAfaTDEQPRAGTTAESLAKLKPAFKKD-- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  240 GTITPANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEA 318
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMsAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535921  319 FAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIKK 389
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIrrDAKKGLATLCIGGGQGVALAIER 392
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
4-384 1.08e-87

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 271.09  E-value: 1.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK06205   2 RDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP--RGEIPFGGIQMTDGISK----DGLEDIKEKGPM 157
Cdd:PRK06205  82 MQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdmRWGVRGGGVQLHDRLARgretAGGRRFPVPGGM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  158 GLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSE-VVITEDEEYKKLIE-SKVSSLKPVFV 235
Cdd:PRK06205 162 IETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPRADTTlESLAKLRPIMG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  236 R-DGTGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALW 313
Cdd:PRK06205 242 KqDPEATVTAGNASGQNDAAAACLVTTEDKAEElGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLI 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17535921  314 ELNEAFAVTVLAFIKELNIEPS---VVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATA 384
Cdd:PRK06205 322 ELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQrrQARYGLETMCIGGGQGLA 397
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
6-262 1.12e-87

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: 266.09  E-value: 1.12e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921     6 VFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVT 85
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVP---RGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtdaRSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEE-YKKLIESKVSSLKPVFVRDgtGT 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGiRPPTTAEPLAKLKPAFDKE--GT 238
                         250       260
                  ....*....|....*....|.
gi 17535921   242 ITPANASSLNDGAVATVVVGE 262
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSE 259
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
4-382 2.34e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 267.26  E-value: 2.34e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK06366   2 KDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPrGEIPFG-------GIQMTDGISKDGLEDIKEKGP 156
Cdd:PRK06366  82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLP-SDLRWGpkhllhkNYKIDDAMLVDGLIDAFYFEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  157 MGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSvktsrsevVITEDEEYKKLIESKVSSLKPVFVR 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRKTTMEDLAKLPPAFDK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  237 DgtGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWEL 315
Cdd:PRK06366 233 N--GILTAGNSAQLSDGGSALVMASEKAINEyGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535921  316 NEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAPGQL--GVAAICNGGGEA 382
Cdd:PRK06366 311 NEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMktGLATLCHGGGGA 379
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
4-384 8.87e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 263.15  E-value: 8.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIG-AYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLP-AGLGQNVTRQISLSAGLPVTT 81
Cdd:PRK07661   2 REAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   82 QAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPF--YVPRGEIpfggiqmtdgiskdgleDIKEKGP--- 156
Cdd:PRK07661  82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMmgHVVRPNP-----------------RLVEAAPeyy 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  157 --MGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSV---------KTSRSEVVITEDEEYKKLIES 225
Cdd:PRK07661 145 mgMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennKLQEETITFSQDEGVRADTTL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  226 KV-SSLKPVFvrDGTGTITPANASSLNDGAVATVVVG-ENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKS 303
Cdd:PRK07661 225 EIlGKLRPAF--NVKGSVTAGNSSQMSDGAAAVLLMDrEKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  304 GLQVSDIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGE 381
Cdd:PRK07661 303 GLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKrrNEQFGIVTMCIGGGM 382

                 ...
gi 17535921  382 ATA 384
Cdd:PRK07661 383 GAA 385
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-390 1.75e-84

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 262.58  E-value: 1.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    1 MSDkkVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIER-SGVAPEKIEEVIGGCVLPAGL-GQNVTRQISLSAGLP 78
Cdd:PRK09050   1 MTE--AFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   79 VTTQAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPFGgiqmtdgiSKDGLED-------- 150
Cdd:PRK09050  79 VSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFS--------RQAEIFDttigwrfv 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  151 ---IKEK---GPMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIE 224
Cdd:PRK09050 151 nplMKAQygvDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPET 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  225 S--KVSSLKPVFVRDgtGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLK 301
Cdd:PRK09050 231 TleALAKLKPVFRPD--GTVTAGNASGVNDGAAALLLASEAAAKKhGLTPRARILGMATAGVEPRIMGIGPAPATRKLLA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  302 KSGLQVSDIALWELNEAFAVTVLAFIKELNI--EPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICN 377
Cdd:PRK09050 309 RLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERtgGRYALCTMCI 388
                        410
                 ....*....|...
gi 17535921  378 GGGEATAVLIKKL 390
Cdd:PRK09050 389 GVGQGIALAIERV 401
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
4-388 2.01e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 249.56  E-value: 2.01e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK06633   3 KPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPF--YVpRGEIPFGGIQMTDGISKDGLEDIKEKGPMGLCA 161
Cdd:PRK06633  83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHgsYI-RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  162 EKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIESKV-SSLKPVFvrDGTG 240
Cdd:PRK06633 162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEIlSKLRPAF--DKNG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  241 TITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAF 319
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKhNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535921  320 AVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVLIK 388
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLrrAKAKKGLVTLCIGGGMGMAMCVE 390
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
4-390 3.57e-76

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 240.64  E-value: 3.57e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYR-GSFANFGAVELGTVAAKAAIERS-GVAPEKIEEVIGGCV---LPAGLgqNVTRQISLSAGLP 78
Cdd:PRK08947   2 EDVVIVDAIRTPMGRSKgGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVqqtLEQGF--NIARNAALLAGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   79 VTTQAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPfyvprgeipfggiqMTDGI---SKDGLEDIKEKG 155
Cdd:PRK08947  80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--------------MNHGVdfhPGLSKNVAKAAG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  156 PMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEE---YKKLIESkVSSLKP 232
Cdd:PRK08947 146 MMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEvirPETTVEA-LAALRP 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  233 VFvRDGTGTITPANASSLNDGAVATVVV-GENALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIA 311
Cdd:PRK08947 225 AF-DPVNGTVTAGTSSALSDGASAMLVMsESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDID 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  312 LWELNEAFAVTVLAFIKELNIEPSV---VNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVL 386
Cdd:PRK08947 304 VFELNEAFAAQSLPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMERkdAQFGLATMCIGLGQGIATV 383

                 ....
gi 17535921  387 IKKL 390
Cdd:PRK08947 384 FERV 387
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
8-390 5.07e-75

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 238.13  E-value: 5.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    8 ILSGARTPIG-AYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVTTQAVT 85
Cdd:PRK07108   6 IVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVTVPGMT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGeipfggiQMTDGISKDGLEDIKekGPMGLCAEKTV 165
Cdd:PRK07108  86 VNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRH-------MLREGWLVEHKPEIY--WSMLQTAENVA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  166 KDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKT----------SRSEVVITEDEEYKK-LIESKVSSLKPVF 234
Cdd:PRK07108 157 KRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAgvadkatgrlFTKEVTVSADEGIRPdTTLEGVSKIRSAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  235 vrdGTGTITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALW 313
Cdd:PRK07108 237 ---PGGVITAGNASQFSDGASACVVMNAKvAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  314 ELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVnslAYSLAPGQ-----LGVAAICNGGGEATAVLIK 388
Cdd:PRK07108 314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLT---GHALIEGKrrgakYVVVTMCIGGGQGAAGLFE 390

                 ..
gi 17535921  389 KL 390
Cdd:PRK07108 391 VL 392
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
6-390 5.10e-74

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 235.67  E-value: 5.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    6 VFILSGARTPIG-AYRGSFANFGAVELGTVAAKAAIER-SGVAPEKIEEVIGGCVLP-AGLGQNVTRQISLSAGLPVTTQ 82
Cdd:PRK09052   8 AYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQvPGLDPKLIEDAIVGCAMPeAEQGLNVARIGALLAGLPNSVG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   83 AVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFyvprgeipfGG--IQMTDGISKDGlEDIKEKGPMGLC 160
Cdd:PRK09052  88 GVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM---------MGnkPSMSPAIFARD-ENVGIAYGMGLT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  161 AEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIES-----------KVSS 229
Cdd:PRK09052 158 AEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLATGEVDVKTRTVDLdegpradtsleGLAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  230 LKPVFvrDGTGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVS 308
Cdd:PRK09052 238 LKPVF--ANKGSVTAGNSSQTSDGAGAVILVSEKALKQfNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  309 DIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVL 386
Cdd:PRK09052 316 DLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLrrTNLKYGMVTMCVGTGMGAAGI 395

                 ....
gi 17535921  387 IKKL 390
Cdd:PRK09052 396 FERL 399
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
7-390 2.12e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 233.45  E-value: 2.12e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVTTQAVT 85
Cdd:PRK07801   5 YIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEVPGVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVP------FYVPRG-EIPFGGIQMTDgiSKDGLEDIKEKGPMG 158
Cdd:PRK07801  85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPissamtAGEQLGfTSPFAESKGWL--HRYGDQEVSQFRGAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  159 LCAEKtvkdYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVktsrsevvITEDEEYKKLIESKVSSLKPVfvRDG 238
Cdd:PRK07801 163 LIAEK----WGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG--------VTVDEGPRETSLEKMAGLKPL--VEG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  239 tGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNE 317
Cdd:PRK07801 229 -GRLTAAVASQISDGASAVLLASERAVKRhGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINE 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535921  318 AFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK07801 308 AFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELerTGGRYGLQTMCEGGGTANVTIIERL 382
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
8-390 6.55e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 227.96  E-value: 6.55e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    8 ILSGARTPIG-AYRGSFANFGAVELGTVAAKAAIER-SGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPvTTQAV 84
Cdd:PRK07851   6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD-FLPGT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   85 TVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPF----YVPRGEIPF--GGIQMTDGISKDGLE---DIKEKG 155
Cdd:PRK07851  85 TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdSLPDTKNPLfaEAQARTAARAEGGAEawhDPREDG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  156 -------PMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSvkTSRSEVVITEDEEYKKLIESKVS 228
Cdd:PRK07851 165 llpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVT--LPDGTVVSTDDGPRAGTTYEKVS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  229 SLKPVFVRDGTgtITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQV 307
Cdd:PRK07851 243 QLKPVFRPDGT--VTAGNACPLNDGAAAVVIMSDTkARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMSI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  308 SDIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAV 385
Cdd:PRK07851 321 DDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQthDKTFGLETMCVGGGQGMAM 400

                 ....*
gi 17535921  386 LIKKL 390
Cdd:PRK07851 401 VLERL 405
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
6-386 4.56e-69

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 224.26  E-value: 4.56e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    6 VFILSGARTPI-GAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQ-NVTRQISLSAGLPVTTQA 83
Cdd:PLN02287  48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVPV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPfgGIQMTDGiSKDGLEdikekgPMGLCAEK 163
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNP--RVESFSQ-AQDCLL------PMGITSEN 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  164 TVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKT------SRSEVVITEDEEYKKLIE-SKVSSLKPVFVR 236
Cdd:PLN02287 199 VAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpktgEEKPIVISVDDGIRPNTTlADLAKLKPVFKK 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  237 DGTgtITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWEL 315
Cdd:PLN02287 279 NGT--TTAGNSSQVSDGAGAVLLMKRSvAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17535921  316 NEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA----PGQLGVAAICNGGGE-ATAVL 386
Cdd:PLN02287 357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKrrgkDCRFGVVSMCIGTGMgAAAVF 432
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
8-390 1.79e-68

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 221.13  E-value: 1.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    8 ILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVTTQAVTV 86
Cdd:PRK07850   6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGATTI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   87 NKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPfgGIQMTDGISKDgLEDIKEkgpmglCAEKTVK 166
Cdd:PRK07850  86 DCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGR--GLPRPDSWDID-MPNQFE------AAERIAK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  167 DYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSE-------VVITEDEEYKKLIESKVSSLKPVfvRDGt 239
Cdd:PRK07850 157 RRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEgqptgetRLVTRDQGLRDTTMEGLAGLKPV--LEG- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  240 GTITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEA 318
Cdd:PRK07850 234 GIHTAGTSSQISDGAAAVLWMDEDrARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEA 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17535921  319 FAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK07850 314 FASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELerTDKSTALITMCAGGALSTGTIIERI 387
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
4-387 9.25e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 220.27  E-value: 9.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK08170   3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIP-FGGIQMTDGISKD---------------- 146
Cdd:PRK08170  83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRwLAGWYAAKSIGQKlaalgklrpsylapvi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  147 ----GLEDIKEKGPMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEeVVPVSvkTSRSEVVITEDEEYKKL 222
Cdd:PRK08170 163 gllrGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPLF--DRDGKFYDHDDGVRPDS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  223 IESKVSSLKPVFVRDgTGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLK 301
Cdd:PRK08170 240 SMEKLAKLKPFFDRP-YGRVTAGNSSQITDGACWLLLASEEAVKKyGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQ 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  302 KSGLQVSDIALWELNEAFAVTVLAFIKELN-----------------IEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYS 364
Cdd:PRK08170 319 RHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHA 398
                        410       420
                 ....*....|....*....|....*
gi 17535921  365 L--APGQLGVAAICNGGGEATAVLI 387
Cdd:PRK08170 399 LkrRGTKRGIAAICIGGGQGGAMLL 423
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
7-390 2.46e-67

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 218.06  E-value: 2.46e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVTTQAVT 85
Cdd:PRK06504   5 YIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPrgeipfGGIQMTDGISKDGLEDIKEKGP-------MG 158
Cdd:PRK06504  85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP------STLPAKNGLGHYKSPGMEERYPgiqfsqfTG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  159 lcAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVI-TEDE--EYKKLIESkVSSLKPVfv 235
Cdd:PRK06504 159 --AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEgiRFDATLEG-IAGVKLI-- 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  236 RDGtGTITPANASSLNDGAVATVVVGENALPQ-GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWE 314
Cdd:PRK06504 234 AEG-GRLTAATASQICDGASGVMVVNERGLKAlGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921  315 LNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQrgKRYGLQTMCEGGGMANVTIVERL 390
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
7-389 1.84e-65

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 213.49  E-value: 1.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    7 FILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGL-GQNVTRQISLSAGLPVTTQAVT 85
Cdd:PRK08131   5 YIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEIPFGG----IQMTDGISKDGLEDIKEKG--PMGL 159
Cdd:PRK08131  85 VNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRdakvFDTTIGARFPNPKIVAQYGndSMPE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  160 CAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSR--SEVVITEDEEYKKLIE-SKVSSLKPVFvr 236
Cdd:PRK08131 165 TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRklPPKLVAEDEHPRPSSTvEALTKLKPLF-- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  237 DGtGTITPANASSLNDGAvATVVVGENALPQ--GAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWE 314
Cdd:PRK08131 243 EG-GVVTAGNASGINDGA-AALLIGSRAAGEkyGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIE 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535921  315 LNEAFAVTVLAFIKELNI--EPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVAAICNGGGEATAVLIKK 389
Cdd:PRK08131 321 INEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELqrRGKRYAVVSLCIGVGQGLAMVIER 399
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
7-390 2.40e-64

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 210.51  E-value: 2.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    7 FILSGARTPIGAYR--GSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAG-LGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK08242   5 YIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRG------EIPFGGIQMTDGISKDgledikekgpm 157
Cdd:PRK08242  85 VQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGawamdpSTNFPTYFVPQGISAD----------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  158 gLCAEKtvkdYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVsvkTSRSEVVITEDEEYKKL---IESkVSSLKPVF 234
Cdd:PRK08242 154 -LIATK----YGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV---KDQNGLTILDHDEHMRPgttMES-LAKLKPSF 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  235 VR-------DGTGTI------------TPANASSLNDGAvATVVVGENAL--PQGAHPLAELVAFAEAGRAPIDFTVAPV 293
Cdd:PRK08242 225 AMmgemggfDAVALQkypeverinhvhHAGNSSGIVDGA-AAVLIGSEEAgkALGLKPRARIVATATIGSDPTIMLTGPV 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  294 DAVRLLLKKSGLQVSDIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAPGQL--G 371
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKrtA 383
                        410
                 ....*....|....*....
gi 17535921  372 VAAICNGGGEATAVLIKKL 390
Cdd:PRK08242 384 LITLCVGGGMGIATIIERV 402
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
8-390 9.19e-62

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 202.69  E-value: 9.19e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    8 ILSGARTPIGAYRGSFANFGAVELgtvAAKAAIERSGVAPEKIEEVIGGCVLpaGLGQNVTRQISLSAGLPVTTQAVTVN 87
Cdd:PRK06690   5 IVEAKRTPIGKKNGMLKDYEVQQL---AAPLLTFLSKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTID 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   88 KVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFyvprgeipfggiQMTDGISKDGLEDIKekgpMGLCAEKTVKD 167
Cdd:PRK06690  80 RQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF------------QNRARFSPETIGDPD----MGVAAEYVAER 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  168 YGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVktsrsevviTEDEEYKKL--IESKVSSLKPVFvrDGTGTITPA 245
Cdd:PRK06690 144 YNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG---------LLDESIKKEmnYERIIKRTKPAF--LHNGTVTAG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  246 NASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTVL 324
Cdd:PRK06690 213 NSCGVNDGACAVLVMEEGqARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVV 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535921  325 AFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSLA--PGQLGVAAICNGGGEATAVLIKKL 390
Cdd:PRK06690 293 ACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKreDMKYGIATLGIGGGIGLALLFEKV 360
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
5-387 8.81e-61

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 202.14  E-value: 8.81e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    5 KVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAV 84
Cdd:PRK08963   6 RIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   85 TVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRgeiPFGGI-----------QMTDGISKDGLEDIKE 153
Cdd:PRK08963  86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSK---KLARAlvdlnkartlgQRLKLFSRLRLRDLLP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  154 KGP----------MGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSevVITEDEEYKKli 223
Cdd:PRK08963 163 VPPavaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--PLEEDNNIRG-- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  224 ESKVSS---LKPVFVRDgTGTITPANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPI-DFTVAPVDAVRL 298
Cdd:PRK08963 239 DSTLEDyakLRPAFDRK-HGTVTAANSTPLTDGAAAVLLMSESrAKALGLTPLGYLRSYAFAAIDVWqDMLLGPAYATPL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  299 LLKKSGLQVSDIALWELNEAFAVTVLAFIKELN-----------------IEPSVVNVKGGAVAIGHPLGMSGLRIVNSL 361
Cdd:PRK08963 318 ALERAGLTLADLTLIDMHEAFAAQTLANLQMFAserfareklgrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQT 397
                        410       420
                 ....*....|....*....|....*...
gi 17535921  362 AYSLAP--GQLGVAAICNGGGEATAVLI 387
Cdd:PRK08963 398 LHELRRrgGGLGLTTACAAGGLGAAMVL 425
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
7-390 2.12e-49

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 171.88  E-value: 2.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    7 FILSGARTPIG---AYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGL-GQNVTRQISLSAGLPVTTQ 82
Cdd:PRK06025   5 YIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDIKAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   83 AVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRgEIPFGGIQMTDGISKDGLEDIKEKGPMGLCAE 162
Cdd:PRK06025  85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAE-DMAAGKPPLGMGSGNLRLRALHPQSHQGVCGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  163 KTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRsevVITEDEEYKK--LIESKVSSLKPVFVR---- 236
Cdd:PRK06025 164 AIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGS---VALDHEEFPRpqTTAEGLAALKPAFTAiady 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  237 --DGTGTIT------------------PANASSLNDGAVATVVVGEN-ALPQGAHPLAELVAFAEAGRAPIDFTVAPVDA 295
Cdd:PRK06025 241 plDDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAyAEKHGLKPRARIVAMANMGDDPTLMLNAPVPA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  296 VRLLLKKSGLQVSDIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL--APGQLGVA 373
Cdd:PRK06025 321 AKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELerRGLKRGLV 400
                        410
                 ....*....|....*..
gi 17535921  374 AICNGGGEATAVLIKKL 390
Cdd:PRK06025 401 TMCAAGGMAPAIIIERV 417
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
10-387 4.71e-49

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: 170.37  E-value: 4.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  10 SGARTPIGAY---RGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQAVTV 86
Cdd:cd00826   2 GAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  87 NKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGEipfggiQMTDGISKDGledikekgpmglcaektvk 166
Cdd:cd00826  82 NNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEK------HIDVLINKYG------------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 167 dygiTREEQDAYAIESYKKASNAWSSEKFSEEVVPVSVKTSRSEVVITEDEEYKKLIESKVSS---LKPVFvrDGTGTIT 243
Cdd:cd00826 137 ----MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDEASLDEiakLRPAF--DKEDFLT 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 244 PANASSLNDGAVATVVVGE--------NALPQGAHPLAELVAFAEAGRAPIDFTVA----PVDAVRLLLKKSGLQVSDIA 311
Cdd:cd00826 211 AGNACGLNDGAAAAILMSEaeaqkhglQSKAREIQALEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGDLD 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 312 LWELNEAFAVTVLAFIKELNIEP------------------SVVNVKGGAVAIGHPLGMSGLRIVNSLAYSL-------- 365
Cdd:cd00826 291 LIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFELkgeagkrq 370
                       410       420
                ....*....|....*....|..
gi 17535921 366 APGQlGVAAICNGGGEATAVLI 387
Cdd:cd00826 371 GAGA-GLALLCIGGGGGAAMCI 391
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
4-389 1.14e-46

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 164.69  E-value: 1.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    4 KKVFILSGARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTQA 83
Cdd:PRK09268   7 RRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   84 VTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRG-------------------------------EI 132
Cdd:PRK09268  87 YDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGlrkillelnrakttgdrlkalgklrpkhlapEI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  133 PFGGIQMTdGISkdgledikekgpMGLCAEKTVKDYGITREEQDAYAIESYKKASNAWSSEKFSEEVVPvsvktsrsevv 212
Cdd:PRK09268 167 PRNGEPRT-GLS------------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITP----------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  213 itedeeYKKL-----------IEsKVSSLKPVFVRDGTGTITPANASSLNDGAvATVVVG--ENALPQGAHPLAELVaFA 279
Cdd:PRK09268 223 ------FLGLtrdnnlrpdssLE-KLAKLKPVFGKGGRATMTAGNSTPLTDGA-SVVLLAseEWAAEHGLPVLAYLV-DA 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  280 EAgrAPIDFT-------VAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTVLA---------FIKEL--------NIEPS 335
Cdd:PRK09268 294 ET--AAVDFVhgkegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLAtlkawedeeYCRERlgldaplgSIDRS 371
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17535921  336 VVNVKGGAVAIGHPLGMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKK 389
Cdd:PRK09268 372 KLNVNGSSLAAGHPFAATGGRIVATLAKLLAEkgSGRGLISICAAGGQGVTAILER 427
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
271-389 3.85e-44

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: 148.94  E-value: 3.85e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   271 PLAELVAFAEAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTVLAFIKELNIEPSVVNVKGGAVAIGHPL 350
Cdd:pfam02803   3 PLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHPL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 17535921   351 GMSGLRIVNSLAYSLAP--GQLGVAAICNGGGEATAVLIKK 389
Cdd:pfam02803  83 GASGARILVTLLHELKRrgGKYGLASLCIGGGQGVAMIIER 123
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
14-385 4.47e-20

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: 90.79  E-value: 4.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  14 TPIGAYRGSfanfGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTtQAVTVNKVCSSS 93
Cdd:cd00829   6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  94 MKALVTAAVEIKAGYYDTILVVGTENMSQVPF----------YVPRGEIPFGGIQMTdgiskdgledikekGPMGLCAEK 163
Cdd:cd00829  81 SAAVRAAAAAIASGLADVVLVVGAEKMSDVPTgdeaggrasdLEWEGPEPPGGLTPP--------------ALYALAARR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 164 TVKDYGITREEQDAYAIESYKKAS---NAWSSEKFSEEVvpvsVKTSRsevVITEdeeykklieskvsslkPvfvrdgtg 240
Cdd:cd00829 147 YMHRYGTTREDLAKVAVKNHRNAArnpYAQFRKPITVED----VLNSR---MIAD----------------P-------- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 241 tITPANASSLNDGAVATVVVGENALPQGAHPLAELVAFAEAGRAP-----IDFTVAP--VDAVRLLLKKSGLQVSDIALW 313
Cdd:cd00829 196 -LRLLDCCPVSDGAAAVVLASEERARELTDRPVWILGVGAASDTPslserDDFLSLDaaRLAARRAYKMAGITPDDIDVA 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 314 ELNEAFAVTVLAFIKEL---------------NIEPS---VVNVKGGAVAIGHPLGMSGLRIVNSLAYSLApGQLG---- 371
Cdd:cd00829 275 ELYDCFTIAELLALEDLgfcekgeggklvregDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLR-GEAGarqv 353
                       410
                ....*....|....*...
gi 17535921 372 ----VAAICNGGGEATAV 385
Cdd:cd00829 354 pgarVGLAHNIGGTGSAA 371
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
28-387 5.54e-11

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: 62.46  E-value: 5.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  28 AVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTqAVTVNKVCSSSMKALVTAAVEIKAG 107
Cdd:cd00327   7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGP-AYSVNQACATGLTALALAVQQVQNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 108 YYDTILVVGTEnmsqvpfyvprgEIPFGgiqmtdgiskdgledikekgpmglcaektvkdygitreeqdayaiesykkas 187
Cdd:cd00327  86 KADIVLAGGSE------------EFVFG---------------------------------------------------- 101
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 188 nawssekfseevvpvsvktsrsevvitedeeykklieskvsslkpvfvrdgtgtitpanasslnDGAVATVVV-GENALP 266
Cdd:cd00327 102 ----------------------------------------------------------------DGAAAAVVEsEEHALR 117
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 267 QGAHPLAELVAFA----EAGRAPIDFTVAPVDAVRLLLKKSGLQVSDIALWELNEAFAVTVLAFIKELNIEPS---VVNV 339
Cdd:cd00327 118 RGAHPQAEIVSTAatfdGASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDgvrSPAV 197
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17535921 340 KGGAVAIGHPLGMSGLRIVNSLAYSL---------APGQLGVAAICNGGGEATAVLI 387
Cdd:cd00327 198 SATLIMTGHPLGAAGLAILDELLLMLehefipptpREPRTVLLLGFGLGGTNAAVVL 254
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
28-123 3.96e-09

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: 57.43  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  28 AVELGTVAAKAAIERSGVAPEKIEEVIGGCVLP-------AGLgqnVTRQISLSAGLpvttqAVTVNKVCSSSMKALVTA 100
Cdd:COG0332  51 TSDLAVEAARKALEAAGIDPEDIDLIIVATVTPdylfpstACL---VQHKLGAKNAA-----AFDINAACSGFVYALSVA 122
                        90       100
                ....*....|....*....|...
gi 17535921 101 AVEIKAGYYDTILVVGTENMSQV 123
Cdd:COG0332 123 AALIRSGQAKNVLVVGAETLSRI 145
PRK06059 PRK06059
lipid-transfer protein; Provisional
1-136 4.73e-08

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 54.38  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    1 MSDKKVFILSGARTPIGAYRGSFanfgaVELGTVAAKAAIERSGVAPEKIEEVIG---------GCVLPAGLGQNVTRQi 71
Cdd:PRK06059   1 SMPEPVYILGAGMHPWGKWGRDF-----VEYGVVAARAALADAGLDWRDVQLVVGadtirngypGFVAGATFAQALGWN- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535921   72 slsaGLPVTTqavtVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMsqvpfyvPRGEIPFGG 136
Cdd:PRK06059  75 ----GAPVSS----SYAACASGSQALQSARAQILAGLCDVALVVGADTT-------PKGFFAPVG 124
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
12-123 6.85e-08

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 53.71  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   12 ARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPvTTQAVTVNKVCS 91
Cdd:PRK12879  37 QRTGIKERRIAHVEEYTSDLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQVQARLGIP-NAAAFDINAACA 115
                         90       100       110
                 ....*....|....*....|....*....|..
gi 17535921   92 SSMKALVTAAVEIKAGYYDTILVVGTENMSQV 123
Cdd:PRK12879 116 GFLYGLETANGLITSGLYKKVLVIGAERLSKV 147
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
28-121 6.89e-08

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 53.70  E-value: 6.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  28 AVELGTVAAKAAIERSGVAPEKIEEVIGGCV-----LPAGlgqnvtrQISLSAGLPVT-TQAVTVNKVCSSSMKALVTAA 101
Cdd:cd00830  50 TSDLAVEAAKKALEDAGIDADDIDLIIVATStpdylFPAT-------ACLVQARLGAKnAAAFDINAACSGFLYGLSTAA 122
                        90       100
                ....*....|....*....|
gi 17535921 102 VEIKAGYYDTILVVGTENMS 121
Cdd:cd00830 123 GLIRSGGAKNVLVVGAETLS 142
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
13-123 2.52e-07

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 52.00  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   13 RTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVI------------GGCVLPAGLG-QNVTrqislsaglpv 79
Cdd:PRK09352  37 RTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIvatttpdyafpsTACLVQARLGaKNAA----------- 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17535921   80 ttqAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQV 123
Cdd:PRK09352 106 ---AFDLSAACSGFVYALSTADQFIRSGAYKNVLVIGAEKLSRI 146
PLN02326 PLN02326
3-oxoacyl-[acyl-carrier-protein] synthase III
12-135 2.24e-06

3-oxoacyl-[acyl-carrier-protein] synthase III


Pssm-ID: 215185  Cd Length: 379  Bit Score: 49.35  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   12 ARTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGL-GQNVTRQISLSAGLPVttqAVTVNKVC 90
Cdd:PLN02326  80 TRTGIRNRRVLSGDETLTSLAVEAAKKALEMAGVDPEDVDLVLLCTSSPDDLfGSAPQVQAALGCTNAL---AFDLTAAC 156
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17535921   91 SSSMKALVTAAVEIKAGYYDTILVVGTENMSQVPFYVPRGE-IPFG 135
Cdd:PLN02326 157 SGFVLGLVTAARFIRGGGYKNVLVIGADALSRYVDWTDRGTcILFG 202
fabH CHL00203
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
13-122 2.41e-06

3-oxoacyl-acyl-carrier-protein synthase 3; Provisional


Pssm-ID: 164577 [Multi-domain]  Cd Length: 326  Bit Score: 48.79  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   13 RTPIGAYRGSFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGL-GQNVTRQISLSAGLPVttqAVTVNKVCS 91
Cdd:CHL00203  36 RTGIKKRHLAPSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLfGSASQLQAEIGATRAV---AFDITAACS 112
                         90       100       110
                 ....*....|....*....|....*....|.
gi 17535921   92 SSMKALVTAAVEIKAGYYDTILVVGTENMSQ 122
Cdd:CHL00203 113 GFILALVTATQFIQNGSYKNILVVGADTLSK 143
PRK06064 PRK06064
thiolase domain-containing protein;
30-356 3.48e-05

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 45.66  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   30 ELGTVAAKAAIERSGVAPEKIEEVIGGCVLpAGL--GQ-NVTRQISLSAGLPvTTQAVTVNKVCSSSMKALVTAAVEIKA 106
Cdd:PRK06064  24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADYAGLA-PIPATRVEAACASGGAALRQAYLAVAS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  107 GYYDTILVVGTENMSQVPfyvprgeipfgGIQMTDGISKDGleDIKEKGPMG--------LCAEKTVKDYGITREEQDAY 178
Cdd:PRK06064 102 GEADVVLAAGVEKMTDVP-----------TPDATEAIARAG--DYEWEEFFGatfpglyaLIARRYMHKYGTTEEDLALV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  179 AIESYKKASNAwSSEKFSEEvvpvsvktsrsevvITEDEeykklieskvsSLKPVFVRDgtgTITPANASSLNDGAVATV 258
Cdd:PRK06064 169 AVKNHYNGSKN-PYAQFQKE--------------ITVEQ-----------VLNSPPVAD---PLKLLDCSPITDGAAAVI 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  259 VVGENALPQGAHPLAELVAFAEAGRAPI-----DFTV--APVDAVRLLLKKSGLQVSDIALWELNEAF------AVTVLA 325
Cdd:PRK06064 220 LASEEKAKEYTDTPVWIKASGQASDTIAlhdrkDFTTldAAVVAAEKAYKMAGIEPKDIDVAEVHDCFtiaeilAYEDLG 299
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 17535921  326 FIK-----------ELNIEPSV-VNVKGGAVAIGHPLGMSGLR 356
Cdd:PRK06064 300 FAKkgeggklaregQTYIGGDIpVNPSGGLKAKGHPVGATGVS 342
ACP_syn_III pfam08545
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ...
86-123 5.44e-04

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430064 [Multi-domain]  Cd Length: 80  Bit Score: 38.27  E-value: 5.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 17535921    86 VNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQV 123
Cdd:pfam08545   3 INAACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKI 40
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
2-124 6.89e-04

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 41.60  E-value: 6.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921    2 SDKKVFILsgartpiGAYRGSFA------NFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLpaglGQNVTRQISLsA 75
Cdd:PRK06289   1 MSDDVWVL-------GGYQSDFArnwtkeGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHL-G 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17535921   76 GLPVT-------TQAVTVNKVCSSSMKALVTAAVEIKAGYYDTILVVGTENMSQVP 124
Cdd:PRK06289  69 AMPATvhpalwgVPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVP 124
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
22-172 8.33e-04

"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: 40.88  E-value: 8.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921  22 SFANFGAVELGTVAAKAAIERSGVAPEKIEEVIGGCVLPAGLGQNVTRQISLSAGLPVTTqAVTVNKVCSSSMKALVTAA 101
Cdd:cd00827  42 AGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLTNAE-AFDLKQACYGGTAALQLAA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921 102 VEIKAGYYDTILVVGTENMSQVPFYV-----------------PRGEIPFGGIQMTDGISkDGLEDIKEKGPMGLCAEKT 164
Cdd:cd00827 121 NLVESGPWRYALVVASDIASYLLDEGsaleptlgdgaaamlvsRNPGILAAGIVSTHSTS-DPGYDFSPYPVMDGGYPKP 199

                ....*...
gi 17535921 165 VKDYGITR 172
Cdd:cd00827 200 CKLAYAIR 207
PRK07204 PRK07204
beta-ketoacyl-ACP synthase III;
31-118 1.31e-03

beta-ketoacyl-ACP synthase III;


Pssm-ID: 235964  Cd Length: 329  Bit Score: 40.59  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   31 LGTVAAKAAIERSGVAPEKIEEVIGGCvlpaGLGQN--------VTRQISLS-AGLPvttqAVTVNKVCSSSMKALVTAA 101
Cdd:PRK07204  55 MGAEAAKKAVEDAKLTLDDIDCIICAS----GTIQQaipctaslIQEQLGLQhSGIP----CFDINSTCLSFITALDTIS 126
                         90
                 ....*....|....*..
gi 17535921  102 VEIKAGYYDTILVVGTE 118
Cdd:PRK07204 127 YAIECGRYKRVLIISSE 143
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
30-121 6.85e-03

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 236037  Cd Length: 372  Bit Score: 38.32  E-value: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   30 ELGTVAAKAAIERSGVAPEKIEEVIGGCvlpaglgQNVTR-----QISLSAGLPVTTQAVTVNKVCSSSMKALVTAAVEI 104
Cdd:PRK07515  97 EMGVAAARQALARAGRTAEDIDAVIVAC-------SNMQRaypamAIEIQQALGIEGFAFDMNVACSSATFGIQTAANAI 169
                         90
                 ....*....|....*..
gi 17535921  105 KAGYYDTILVVGTENMS 121
Cdd:PRK07515 170 RSGSARRVLVVNPEICS 186
PRK07516 PRK07516
thiolase domain-containing protein;
35-124 8.79e-03

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 38.00  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535921   35 AAKAAIERSGVAPEKIEEVIGGcVLPAGLgqnvTRQIsLSAGLPVT-------TQAVTVNKVCSSSMKALVTAAVEIKAG 107
Cdd:PRK07516  29 VAREALAHAGIAAGDVDGIFLG-HFNAGF----SPQD-FPASLVLQadpalrfKPATRVENACATGSAAVYAALDAIEAG 102
                         90
                 ....*....|....*..
gi 17535921  108 YYDTILVVGTENMSQVP 124
Cdd:PRK07516 103 RARIVLVVGAEKMTATP 119
 
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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