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Conserved domains on  [gi|4504327|ref|NP_000174|]
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trifunctional enzyme subunit beta, mitochondrial isoform 1 precursor [Homo sapiens]

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 ...
55-471 5.58e-174

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: 493.53  E-value: 5.58e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   55 VVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMgqrlsliskfRFNFLAPELPAV 214
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGM----------LDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  215 SefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQM 289
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  290 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLT 369
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  370 MNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG 449
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 4504327  450 GQYGLVAACAAGGQGHAMIVEA 471
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
55-471 5.58e-174

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: 493.53  E-value: 5.58e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   55 VVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMgqrlsliskfRFNFLAPELPAV 214
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGM----------LDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  215 SefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQM 289
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  290 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLT 369
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  370 MNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG 449
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 4504327  450 GQYGLVAACAAGGQGHAMIVEA 471
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
56-470 1.70e-165

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: 472.10  E-value: 1.70e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327     56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 135
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    136 MACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKlMLDLNKAKSMGQRLSLiskfrfnflapelpaVS 215
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRW-GVKPGNAELEDARLKD---------------LT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    216 EFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQMA 290
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    291 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLTM 370
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    371 NDIDAFEFHEAFSGQILANFKAMDsdwfaenymgrktkvglPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGG 450
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
                         410       420
                  ....*....|....*....|
gi 4504327    451 QYGLVAACAAGGQGHAMIVE 470
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
52-471 2.45e-159

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 457.91  E-value: 2.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK08963   5 DRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPEL 211
Cdd:PRK08963  85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVV--PFKVPGKDTVTKDNGIRP-SSLEQ 288
Cdd:PRK08963 165 PAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtAHVPPYKQPLEEDNNIRGdSTLED 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   289 MAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGL 368
Cdd:PRK08963 245 YAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAGL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   369 TMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKE 448
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
                        410       420
                 ....*....|....*....|...
gi 4504327   449 GGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLEV 427
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
52-471 5.58e-153

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: 440.27  E-value: 5.58e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGqrlsliskfrfnflapeL 211
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMI-----------------N 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD---TVTKDNGIRP-SSL 286
Cdd:COG0183 145 PGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTTL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  287 EQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDqLLLGPTYATPKVLEKA 366
Cdd:COG0183 225 EKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALARA 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  367 GLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRLR 446
Cdd:COG0183 303 GLTLDDIDLIEINEAFAAQVLAVLREL----------------GLDP-DKVNVNGGAIALGHPLGASGARILVTLLHELE 365
                       410       420
                ....*....|....*....|....*
gi 4504327  447 KEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:COG0183 366 RRGGRYGLATMCIGGGQGIALIIER 390
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
54-324 3.10e-96

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: 290.74  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327     54 VVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 133
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    134 VTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRklmldlnkaksmgQRLSLISKFRFNFLAPElpA 213
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    214 VSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP---GKDTVTKDNGIRP-SSLEQ 288
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 4504327    289 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEE 324
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
55-471 5.58e-174

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: 493.53  E-value: 5.58e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   55 VVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMgqrlsliskfRFNFLAPELPAV 214
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGM----------LDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  215 SefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQM 289
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  290 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLT 369
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  370 MNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG 449
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 4504327  450 GQYGLVAACAAGGQGHAMIVEA 471
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
56-470 1.70e-165

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: 472.10  E-value: 1.70e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327     56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 135
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    136 MACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKlMLDLNKAKSMGQRLSLiskfrfnflapelpaVS 215
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRW-GVKPGNAELEDARLKD---------------LT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    216 EFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQMA 290
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    291 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLTM 370
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    371 NDIDAFEFHEAFSGQILANFKAMDsdwfaenymgrktkvglPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGG 450
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
                         410       420
                  ....*....|....*....|
gi 4504327    451 QYGLVAACAAGGQGHAMIVE 470
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
52-471 2.45e-159

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 457.91  E-value: 2.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK08963   5 DRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPEL 211
Cdd:PRK08963  85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVV--PFKVPGKDTVTKDNGIRP-SSLEQ 288
Cdd:PRK08963 165 PAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtAHVPPYKQPLEEDNNIRGdSTLED 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   289 MAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGL 368
Cdd:PRK08963 245 YAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAGL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   369 TMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKE 448
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
                        410       420
                 ....*....|....*....|...
gi 4504327   449 GGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLEV 427
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
52-471 5.58e-153

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: 440.27  E-value: 5.58e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:COG0183   2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGqrlsliskfrfnflapeL 211
Cdd:COG0183  82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMI-----------------N 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD---TVTKDNGIRP-SSL 286
Cdd:COG0183 145 PGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTTL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  287 EQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDqLLLGPTYATPKVLEKA 366
Cdd:COG0183 225 EKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALARA 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  367 GLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRLR 446
Cdd:COG0183 303 GLTLDDIDLIEINEAFAAQVLAVLREL----------------GLDP-DKVNVNGGAIALGHPLGASGARILVTLLHELE 365
                       410       420
                ....*....|....*....|....*
gi 4504327  447 KEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:COG0183 366 RRGGRYGLATMCIGGGQGIALIIER 390
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
46-471 7.10e-121

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 359.98  E-value: 7.10e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    46 LAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGF 125
Cdd:PRK09268   1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   126 SDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFN 205
Cdd:PRK09268  81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGDRLKALGKLRPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   206 FLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKvpgkdTVTKDNGIRP- 283
Cdd:PRK09268 161 HLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFL-----GLTRDNNLRPd 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   284 SSLEQMAKLKPAFIK-PYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQD---PKDQLLLGPTYAT 359
Cdd:PRK09268 236 SSLEKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhGKEGLLMAPAYAV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVM 439
Cdd:PRK09268 316 PRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVA 395
                        410       420       430
                 ....*....|....*....|....*....|..
gi 4504327   440 AAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK09268 396 TLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
52-471 1.42e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 338.53  E-value: 1.42e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK08170   3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPE- 210
Cdd:PRK08170  83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKSIGQKLAALGKLRPSYLAPVi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   211 --LPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFkVPGKDTV-TKDNGIRP-SSL 286
Cdd:PRK08170 163 glLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPL-FDRDGKFyDHDDGVRPdSSM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   287 EQMAKLKPAFIKPYGTVTAANSSFLTDGAsAMLIMAEEKALAM-GYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEK 365
Cdd:PRK08170 242 EKLAKLKPFFDRPYGRVTAGNSSQITDGA-CWLLLASEEAVKKyGLPPLGRIVDSQWAALDP-SQMGLGPVHAATPLLQR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   366 AGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRL 445
Cdd:PRK08170 320 HGLTLEDLDLWEINEAFAAQVLACLAAWADEEYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHAL 399
                        410       420
                 ....*....|....*....|....*.
gi 4504327   446 RKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK08170 400 KRRGTKRGIAAICIGGGQGGAMLLER 425
PRK05790 PRK05790
putative acyltransferase; Provisional
52-471 3.99e-106

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 320.95  E-value: 3.99e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP--IRHSR---KMRKL-MLDlnkaksmgqrlSLISkfrfn 205
Cdd:PRK05790  82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRwgqKMGDVeLVD-----------TMIH----- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   206 flapelPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDNG 280
Cdd:PRK05790 146 ------DGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTIKQRKgdpvVVDTDEH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   281 IRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYAT 359
Cdd:PRK05790 220 PRPdTTAESLAKLRPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPA-IMGIGPVPAI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVM 439
Cdd:PRK05790 298 RKALEKAGWSLADLDLIEINEAFAAQALAVEKEL----------------GLDP-EKVNVNGGAIALGHPIGASGARILV 360
                        410       420       430
                 ....*....|....*....|....*....|..
gi 4504327   440 AAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK05790 361 TLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
54-324 3.10e-96

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: 290.74  E-value: 3.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327     54 VVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 133
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    134 VTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRklmldlnkaksmgQRLSLISKFRFNFLAPElpA 213
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    214 VSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP---GKDTVTKDNGIRP-SSLEQ 288
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 4504327    289 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEE 324
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
52-473 1.27e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 271.09  E-value: 1.27e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK06205   2 RDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrHSRKMRK--------LM--LDLNKAKSMGQRLSLISK 201
Cdd:PRK06205  82 MQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEF-YTTDMRWgvrgggvqLHdrLARGRETAGGRRFPVPGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   202 frfnflapelpavsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVT 276
Cdd:PRK06205 161 ---------------------MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVTVPQRKgdptVVD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   277 KDNGIRP-SSLEQMAKLKPAFIK--PYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLL 353
Cdd:PRK06205 220 RDEHPRAdTTLESLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEP-SRMGI 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   354 GPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAEnymgrktkvglpplEKFNNWGGSLSLGHPFGAT 433
Cdd:PRK06205 299 GPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDE--------------ERLNVNGSGISLGHPVGAT 364
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 4504327   434 GCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYP 473
Cdd:PRK06205 365 GGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFERVN 404
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
51-472 2.69e-84

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 265.04  E-value: 2.69e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPI-----RHSRKM-RKLMLDLNKAKSmgqrlsLISKFrf 204
Cdd:PRK08235  81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYilpgaRWGYRMgDNEVIDLMVADG------LTCAF-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   205 nflapelpavsefsTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDN 279
Cdd:PRK08235 153 --------------SGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQRKgdpiVVAKDE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   280 GIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDqLLLGPTYA 358
Cdd:PRK08235 219 APRKdTTIEKLAKLKPVF-DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKD-FPRTPGYA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   359 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAmdsdwfaenymgrktkVGLPPlEKFNNWGGSLSLGHPFGATGCRLV 438
Cdd:PRK08235 297 INALLEKTGKTVEDIDLFEINEAFAAVALASTEI----------------AGIDP-EKVNVNGGAVALGHPIGASGARII 359
                        410       420       430
                 ....*....|....*....|....*....|....
gi 4504327   439 MAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK08235 360 VTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
51-472 1.97e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 257.34  E-value: 1.97e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGTS------YKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT-SNVAREAALGA 123
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   124 GFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIR---HSRKMRKLMLDlnkaksmgqrlslis 200
Cdd:PRK06445  81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdnpHIEPNPKLLTD--------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   201 kfrfnflaPELpAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP---GKDTVT 276
Cdd:PRK06445 146 --------PKY-IEYDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDeILPIEVEvegKKKVVD 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   277 KDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGP 355
Cdd:PRK06445 217 VDQSVRPdTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPP-AIMGKGP 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   356 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKamdsdwfaenymgrktKVGLPPlEKFNNWGGSLSLGHPFGATGC 435
Cdd:PRK06445 295 VPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIK----------------ELGLDP-ETVNIKGGAIAIGHPLGATGA 357
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 4504327   436 RLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK06445 358 RIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
52-470 7.54e-79

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 250.65  E-value: 7.54e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLS-GTSYKDLMPHDLARAALTGLLHRTS--VPKEVVDyIIFGTVIQEVKTS-NVAREAALGAGFSD 127
Cdd:PRK08947   2 EDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPalDPAEIDD-IIWGCVQQTLEQGfNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   128 KTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSrkmrklmLDLNkaksmgqrlsliskfrfnfl 207
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHG-------VDFH-------------------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   208 apelPAVSEFST--SETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPfkVPGKD------TVTKD 278
Cdd:PRK08947 134 ----PGLSKNVAkaAGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNeIIP--TEGHDadgvlkLFDYD 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   279 NGIRP-SSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK08947 208 EVIRPeTTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPS-IMGYGPVP 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaeNYMGRKTkvglpplEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDL-------GLLDKMD-------EKVNLNGGAIALGHPLGCSGARI 352
                        410       420       430
                 ....*....|....*....|....*....|...
gi 4504327   438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08947 353 STTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
PRK09051 PRK09051
beta-ketothiolase BktB;
52-470 1.71e-78

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 249.88  E-value: 1.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK09051   3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPtEPRDMYLSRVAAINAGVPQETP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP-----IRHSRKMrklmldlNKAKSMGQRLSLISkfrfn 205
Cdd:PRK09051  83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPyllpaARWGARM-------GDAKLVDMMVGALH----- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   206 flapelpavSEFSTSEtMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPG-KDTVT--KDNGI 281
Cdd:PRK09051 151 ---------DPFGTIH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVEIKTrKGEVVfdTDEHV 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   282 RPS-SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATP 360
Cdd:PRK09051 221 RADtTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDP-EYMGIGPVPATQ 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK09051 300 KALERAGLTVADLDVIEANEAFAAQACAVTREL----------------GLDP-AKVNPNGSGISLGHPVGATGAIITVK 362
                        410       420       430
                 ....*....|....*....|....*....|
gi 4504327   441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK09051 363 ALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
52-473 9.39e-78

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 248.08  E-value: 9.39e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTP---FLLSGTSYKdlmPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIqevkTSNV----AREAALGAG 124
Cdd:PLN02644   1 RDVCIVGVARTPiggFLGSLSSLS---ATELGSIAIQAALERAGVDPALVQEVFFGNVL----SANLgqapARQAALGAG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   125 FSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrKLMLDLNKAKSMGQrLSLISkfrf 204
Cdd:PLN02644  74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAP--------KYLPEARKGSRLGH-DTVVD---- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   205 NFLAPELPAV-SEFStsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK-----DTVTK 277
Cdd:PLN02644 141 GMLKDGLWDVyNDFG----MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWeIVPVEVPGGrgrpsVIVDK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   278 DNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTY 357
Cdd:PLN02644 217 DEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAP-ELFTTAPAL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLL----------------GLDP-EKVNVHGGAVSLGHPIGCSGARI 358
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 4504327   438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYP 473
Cdd:PLN02644 359 LVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
56-470 2.02e-77

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 246.54  E-value: 2.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:PRK07801   6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTiGPQAGNIARTSWLAAGLPEEVPGVTV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlNKAKSMGQRLSLISKF--------RFNf 206
Cdd:PRK07801  86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPI-------------SSAMTAGEQLGFTSPFaeskgwlhRYG- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   207 lapELPaVSEFstsetmgHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSS 285
Cdd:PRK07801 152 ---DQE-VSQF-------RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPV-----GGVTVDEGPRETS 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   286 LEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVLEK 365
Cdd:PRK07801 216 LEKMAGLKP--LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPV-FMLTAPIPATRYALEK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   366 AGLTMNDIDAFEFHEAFSGQILAnfkamdsdWFAEnymgrktkVGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRL 445
Cdd:PRK07801 293 TGLSIDDIDVVEINEAFAPVVLA--------WLKE--------TGADP-AKVNPNGGAIALGHPLGATGAKLMTTLLHEL 355
                        410       420
                 ....*....|....*....|....*
gi 4504327   446 RKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07801 356 ERTGGRYGLQTMCEGGGTANVTIIE 380
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
53-470 1.84e-74

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 239.24  E-value: 1.84e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK07850   3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSnNITRTAWLHAGLPYHVGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldlnkaKSMGQRLSLISKFRFNFlapEL 211
Cdd:PRK07850  83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLG---------------ANAGPGRGLPRPDSWDI---DM 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   212 PAVSEfstsetmghSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLL-SDVVPFKVPGKD----------TVTKDNG 280
Cdd:PRK07850 145 PNQFE---------AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFdREISPVQAPVLDeegqptgetrLVTRDQG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   281 IRPSSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATP 360
Cdd:PRK07850 216 LRDTTMEGLAGLKP--VLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPY-YHLDGPVQATA 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK07850 293 KVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPD-----------------MDKVNVNGGAIALGHPVGSTGARLITT 355
                        410       420       430
                 ....*....|....*....|....*....|
gi 4504327   441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07850 356 ALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
52-470 3.76e-71

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 231.00  E-value: 3.76e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRT-SVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 129
Cdd:PRK09050   2 TEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNrNVARMSALLAGLPVSV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklmLDLNKAKSMGQRLSLI--SKFRFNFL 207
Cdd:PRK09050  82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAP-----------FVMGKADSAFSRQAEIfdTTIGWRFV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   208 APELPAvsEFSTsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDNGIR 282
Cdd:PRK09050 151 NPLMKA--QYGV-DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEeIVPVTIPQKKgdpvVVDRDEHPR 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   283 PS-SLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPK 361
Cdd:PRK09050 228 PEtTLEALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPR-IMGIGPAPATRK 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   362 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPP-LEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK09050 306 LLARLGLTIDQFDVIELNEAFAAQGLAVLRQL----------------GLADdDARVNPNGGAIALGHPLGMSGARLVLT 369
                        410       420       430
                 ....*....|....*....|....*....|
gi 4504327   441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK09050 370 ALHQLERTGGRYALCTMCIGVGQGIALAIE 399
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
51-470 4.16e-69

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 225.40  E-value: 4.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGT-SYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 128
Cdd:PRK07661   1 MREAVIVAGARTPVGKAKKgSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   129 TPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlnkaksMGQRLSLISKfrfnfLA 208
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM------------------MGHVVRPNPR-----LV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   209 PELPavsEFSTSetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP----GKD--------TV 275
Cdd:PRK07661 138 EAAP---EYYMG--MGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADeIVPVDVTlrtvGENnklqeetiTF 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   276 TKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMyVSQDPKDQLLLG 354
Cdd:PRK07661 213 SQDEGVRAdTTLEILGKLRPAF-NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFA-VAGVPPEVMGIG 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   355 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATG 434
Cdd:PRK07661 291 PIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE-----------------EKVNVNGGAIALGHPLGCTG 353
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 4504327   435 CRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07661 354 AKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
23-471 7.27e-68

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 223.87  E-value: 7.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    23 IRPLSCSSQLRAAPAVQTKTKKTLAKPNI--RNVVVVDGVRTPFLLSGT-SYKDLMPHDLARAALTGLLHRTSV-PKEVV 98
Cdd:PLN02287  15 LRPSSSEPSSLSASACAAGDSAAYHRTTAfgDDVVIVAAYRTPICKAKRgGFKDTYPDDLLAPVLKAVVEKTGLnPSEVG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    99 DyIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsr 177
Cdd:PLN02287  95 D-IVVGTVLAPgSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMA--- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   178 kmrklmldlnkaksmgqrlsliSKFRFNflapelPAVSEFSTSET----MGHSADRLAAAFAVSRLEQDEYALRSHSLAK 253
Cdd:PLN02287 171 ----------------------WEGGVN------PRVESFSQAQDcllpMGITSENVAERFGVTREEQDQAAVESHRKAA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   254 KAQDEGLLSD-VVPFKVPGKD---------TVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMA 322
Cdd:PLN02287 223 AATASGKFKDeIVPVHTKIVDpktgeekpiVISVDDGIRPnTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMK 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   323 EEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQilanfkamdsdwfaenY 402
Cdd:PLN02287 302 RSVAMQKGLPILGVFRSFAAVGVDPA-VMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQ----------------F 364
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504327   403 MGRKTKVGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG--GQYGLVAACAAGGQGHAMIVEA 471
Cdd:PLN02287 365 VYCCKKLGLDP-EKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
51-471 2.40e-64

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 213.33  E-value: 2.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFllsGTS----YKDLMPHDLARAALTGLLHRTSV--PKEVVDYIIfGTVIQEVKTS-NVAREAALGA 123
Cdd:PRK09052   5 LQDAYIVAATRTPV---GKAprgmFKNTRPDDLLAHVLRSAVAQVPGldPKLIEDAIV-GCAMPEAEQGlNVARIGALLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   124 GFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlnkaksMGQRLSLiskfr 203
Cdd:PRK09052  81 GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM------------------MGNKPSM----- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   204 fnflAPELPAVSE-FSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKV----PG------ 271
Cdd:PRK09052 138 ----SPAIFARDEnVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPYEIterfPDlatgev 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   272 ---KDTVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAmLIMAEEKAL-AMGYKPKAYLRDFMyVSQD 346
Cdd:PRK09052 214 dvkTRTVDLDEGPRAdTSLEGLAKLKPVF-ANKGSVTAGNSSQTSDGAGA-VILVSEKALkQFNLTPLARFVSFA-VAGV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   347 PKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKamdsdwfaenymgrktKVGLPPlEKFNNWGGSLSL 426
Cdd:PRK09052 291 PPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIR----------------DLGLDP-SKVNPLGGAIAL 353
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 4504327   427 GHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK09052 354 GHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFER 398
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
55-470 4.60e-62

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 207.55  E-value: 4.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    55 VVVDGVRTPFLLSGT-SYKDLMPHDLA----RAALTgllhrtSVPK---EVVDYIIFGTVIQEVKT-SNVAREAALGAGF 125
Cdd:PRK07851   5 VIVSTARSPIGRAFKgSLKDMRPDDLAaqmvRAALD------KVPAldpTDIDDLMLGCGLPGGEQgFNMARVVAVLLGY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   126 sDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKM---RKLMLDLNKAKSMGQRLSLISKF 202
Cdd:PRK07851  79 -DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFAEAQARTAARAEGGAEAW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   203 RFNFLAPELPAVSEfstseTMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVPGKDTVTKDNGI 281
Cdd:PRK07851 158 HDPREDGLLPDVYI-----AMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFErEITPVTLPDGTVVSTDDGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   282 RP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDfMYVSQDPKDQLLLGPTYATP 360
Cdd:PRK07851 233 RAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVS-TGVSGLSPEIMGLGPVEASK 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK07851 311 QALARAGMSIDDIDLVEINEAFAAQVLPSARELGID-----------------EDKLNVSGGAIALGHPFGMTGARITTT 373
                        410       420       430
                 ....*....|....*....|....*....|
gi 4504327   441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07851 374 LLNNLQTHDKTFGLETMCVGGGQGMAMVLE 403
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
56-470 1.35e-61

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 205.89  E-value: 1.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    56 VVDGVRTPfllSGTSYKD-----LMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQeV--KTSNVAREAALGAGFSDK 128
Cdd:PRK08242   6 IYDAVRTP---RGKGKKDgslheVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTP-VgdQGADIARTAVLAAGLPET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   129 TPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklMLDLNKAKSMGQRLSLISKFrfnflA 208
Cdd:PRK08242  82 VPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP----------MGSDGGAWAMDPSTNFPTYF-----V 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   209 PElpavsefstsetmGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFK-VPGKDTVTKDNGIRP-SS 285
Cdd:PRK08242 147 PQ-------------GISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAkSVVPVKdQNGLTILDHDEHMRPgTT 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   286 LEQMAKLKPAF-------------IKPYGTV-------TAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQ 345
Cdd:PRK08242 214 MESLAKLKPSFammgemggfdavaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGS 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   346 DPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLS 425
Cdd:PRK08242 294 DPT-IMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDI-----------------PHDKVNVNGGAIA 355
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 4504327   426 LGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08242 356 MGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
56-471 7.36e-61

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 203.81  E-value: 7.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:PRK06504   6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVgEQATNVARNAVLASKLPESVPGTSI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklmldlnkaksMGQRLSLISKFRF-NFLAPEL-- 211
Cdd:PRK06504  86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP-------------------MGSPSTLPAKNGLgHYKSPGMee 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   212 --PAVsEFStsETMGhsADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPG----KDTVTKDNGIR-P 283
Cdd:PRK06504 147 ryPGI-QFS--QFTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPLEITRadgsGEMHTVDEGIRfD 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   284 SSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVL 363
Cdd:PRK06504 222 ATLEGIAGVKL--IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPV-IMLEAPLPATERAL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   364 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglpPlEKFNNWGGSLSLGHPFGATGCRLVMAAAN 443
Cdd:PRK06504 299 KKAGMKIDDIDLYEVNEAFASVPLAWLKATGAD----------------P-ERLNVNGGAIALGHPLGASGTKLMTTLVH 361
                        410       420
                 ....*....|....*....|....*...
gi 4504327   444 RLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK06504 362 ALKQRGKRYGLQTMCEGGGMANVTIVER 389
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
53-470 9.55e-61

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 203.86  E-value: 9.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK08131   3 DAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSrNVARNALLLAGLPVTVPG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKS-MGQRlsliskfrfnFLAPE 210
Cdd:PRK08131  83 QTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTtIGAR----------FPNPK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   211 LpaVSEFStSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP--GKDT---VTKDNGIRPS 284
Cdd:PRK08131 153 I--VAQYG-NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADeITPIEVPqgRKLPpklVAEDEHPRPS 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   285 S-LEQMAKLKPAFIKpyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVL 363
Cdd:PRK08131 230 StVEALTKLKPLFEG--GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPR-IMGIGPVEAIKKAL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   364 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwFAEnymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAAN 443
Cdd:PRK08131 307 ARAGLTLDDMDIIEINEAFASQVLGCLKGLGVD-FDD--------------PRVNPNGGAIAVGHPLGASGARLALTAAR 371
                        410       420
                 ....*....|....*....|....*..
gi 4504327   444 RLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08131 372 ELQRRGKRYAVVSLCIGVGQGLAMVIE 398
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
55-470 8.49e-59

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 198.45  E-value: 8.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    55 VVVDGVRTPFllsGTSYKDL--MPH--DLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT-SNVAREAALGAGFSDKT 129
Cdd:PRK07108   5 VIVSTARTPL---AKSWRGAfnMTHgaTLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATgANIARQIALRAGLPVTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVpirhSRKMRKLMLD---LNKAKsmgqrlsliskfrfnf 206
Cdd:PRK07108  82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV----QNEMNRHMLRegwLVEHK---------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   207 laPELpavsefstSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPF--------KVPG-----K 272
Cdd:PRK07108 142 --PEI--------YWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPItvtagvadKATGrlftkE 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   273 DTVTKDNGIRP-SSLEQMAKLKPAFikPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQL 351
Cdd:PRK07108 212 VTVSADEGIRPdTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP-DEM 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   352 LLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaenYMgrKTKVGLPPlEKFNNWGGSLSLGHPFG 431
Cdd:PRK07108 289 GIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVL--------------YC--RDTLGIPM-DRLNVNGGAIAVGHPYG 351
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 4504327   432 ATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07108 352 VSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
51-470 1.13e-57

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 195.61  E-value: 1.13e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR---KLMLDLN-KAKSMGQRLSLISKFRFnf 206
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgpKHLLHKNyKIDDAMLVDGLIDAFYF-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   207 lapelpavsefstsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSS 285
Cdd:PRK06366 159 --------------EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNeIVPF-----NDLDRDEGIRKTT 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   286 LEQMAKLKPAFIKPyGTVTAANSSFLTDGASAmLIMAEEKAL-AMGYKPKAYLRDFMYVSQDPKDqLLLGPTYATPKVLE 364
Cdd:PRK06366 220 MEDLAKLPPAFDKN-GILTAGNSAQLSDGGSA-LVMASEKAInEYGLKPIARITGYESASLDPLD-FVEAPIPATRKLLE 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   365 KAGLTMNDIDAFEFHEAFS--GQILANFKAMDSdwfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAA 442
Cdd:PRK06366 297 KQNKSIDYYDLVEHNEAFSiaSIIVRDQLKIDN-------------------ERFNVNGGAVAIGHPIGNSGSRIIVTLI 357
                        410       420
                 ....*....|....*....|....*...
gi 4504327   443 NRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06366 358 NALKTRHMKTGLATLCHGGGGAHTLTLE 385
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
331-471 1.30e-57

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: 186.31  E-value: 1.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    331 YKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvg 410
Cdd:pfam02803   1 LKPLARIRSYATAGVDP-AIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP------------- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504327    411 lpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:pfam02803  67 ----EKVNVNGGAIALGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
51-471 6.13e-57

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 193.71  E-value: 6.13e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMS----DVPIRHSRKMRKL-MLDLNkaksmgQRLSLISKFRFN 205
Cdd:PRK06633  82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhGSYIRAGAKFGDIkMVDLM------QYDGLTDVFSGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   206 FlapelpavsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKDTVT---KDNGI 281
Cdd:PRK06633 156 F----------------MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDeILPIEVTIKKTTSlfdHDETV 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   282 RP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdqlLLG--PTYA 358
Cdd:PRK06633 220 RPdTSLEILSKLRPAFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPS---IMGtaPVPA 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   359 TPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaenYMGRKTKVGLpplEKFNNWGGSLSLGHPFGATGCRLV 438
Cdd:PRK06633 296 SQKALSKAGWSVNDLEVIEVNEAFAAQSI--------------YVNREMKWDM---EKVNINGGAIAIGHPIGASGGRVL 358
                        410       420       430
                 ....*....|....*....|....*....|...
gi 4504327   439 MAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK06633 359 ITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
54-472 1.45e-54

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 187.41  E-value: 1.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    54 VVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 133
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   134 VTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP-----------IRHSRKMRKLMLD-LNKAKSMGQrlslisk 201
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDgLEDAYDKGR------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   202 frfnflapelpavsefstseTMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVPGKD---TVTK 277
Cdd:PRK06954 162 --------------------LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAwEIAPVTVAGKKgdtVIDR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   278 DNGIRPSSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK06954 222 DEQPFKANPEKIPTLKPAFSKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPS-KFTTAPVG 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK06954 300 AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL-----------------PHEKVNVNGGACALGHPIGASGARI 362
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 4504327   438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK06954 363 LVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
51-470 3.26e-51

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 178.54  E-value: 3.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldLNKAKSmGQRL-------SLISKFR 203
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYV-----------LPGART-GLRMghaqlvdSMITDGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   204 FNflapelpAVSEFStsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKD 278
Cdd:PRK05656 149 WD-------AFNDYH----MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDeITPILIPQRKgeplAFATD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   279 NGIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK05656 218 EQPRAgTTAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPA-IMGIGPVS 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWD-----------------AAKVNVNGGAIALGHPIGASGCRV 358
                        410       420       430
                 ....*....|....*....|....*....|...
gi 4504327   438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK05656 359 LVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
53-470 1.42e-50

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 175.72  E-value: 1.42e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLlhRTSVPKEVvDYIIFGTVIQevKTSNVAREAALGAGFSDKTPAH 132
Cdd:PRK06690   2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMEREI-DDVILGNVVG--PGGNVARLSALEAGLGLHIPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   133 TVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldlnkaksmgqrlsliSKFRFnflAPEL- 211
Cdd:PRK06690  77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ-------------------------NRARF---SPETi 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   212 --PAvsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSSLEQ 288
Cdd:PRK06690 129 gdPD---------MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEeILSF-----NGLLDESIKKEMNYER 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   289 M-AKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQlLLGPTYATPKVLEKAG 367
Cdd:PRK06690 195 IiKRTKPAFLHN-GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLP-GTGPIFAVNKLLNEMN 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   368 LTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRK 447
Cdd:PRK06690 273 MKVEDIDYFEINEAFASKVVACAKELQI-----------------PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKR 335
                        410       420
                 ....*....|....*....|...
gi 4504327   448 EGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06690 336 EDMKYGIATLGIGGGIGLALLFE 358
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
56-470 1.19e-48

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 172.27  E-value: 1.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    56 VVDGVRTPFLLSGT---SYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK06025   6 IIDAVRTPRGIGKVgkgALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYDIKASG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRK----LMLDLNKAksmgqrlsliskfRFNFL 207
Cdd:PRK06025  86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAgkppLGMGSGNL-------------RLRAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   208 APElpavsefstsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVP-GKDTVTKDNGIRP-S 284
Cdd:PRK06025 153 HPQ----------SHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDkSLVPVYRDdGSVALDHEEFPRPqT 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   285 SLEQMAKLKPAF-------IKPYGTVT------------------AANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRD 339
Cdd:PRK06025 223 TAEGLAALKPAFtaiadypLDDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVA 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   340 FMYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSgqilanfkamdsdWFAENYMgRKTKVglpPLEKFNN 419
Cdd:PRK06025 303 MANMGDDPT-LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFA-------------VVAEKFI-RDLDL---DRDKVNV 364
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504327   420 WGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06025 365 NGGAIALGHPIGATGSILIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIE 415
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
60-470 4.07e-41

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: 151.49  E-value: 4.07e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   60 VRTPFLLSGTSYKDLmPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACI 139
Cdd:cd00826   8 FGKFGGENGADANDL-AHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  140 SANQAMTTGVGLIASGQCDVIVAGGVELMSdVPIRHSRKMRKLMLDLNKAKSmgqrlsliskfrfnflapelpavsefst 219
Cdd:cd00826  87 SGLRALALAMQLIAGGDANCILAGGFEKME-TSAENNAKEKHIDVLINKYGM---------------------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  220 setmghsadrlaaafavsRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD---TVTKDNGIR---PSSLEQMAKL 292
Cdd:cd00826 138 ------------------RACPDAFALAGQAGAEAAEKDGRFKDeFAKFGVKGRKgdiHSDADEYIQfgdEASLDEIAKL 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  293 KPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKA-------LAMGYKPKAYLRDFMYVSQDPKDQLLLG---PTYATPKV 362
Cdd:cd00826 200 RPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVGgdgPIEAARKA 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  363 LEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsDWFAENYMGRKTKVGLPPLEK---FNNWGGSLSLGHPFGATGCRLVM 439
Cdd:cd00826 279 LEKAGLGIGDLDLIEAHDAFAANACATNEAL--GLCPEGQGGALVDRGDNTYGGksiINPNGGAIAIGHPIGASGAAICA 356
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 4504327  440 AAANRLRKEGGQY-----GLVAACAAGGQGHAMIVE 470
Cdd:cd00826 357 ELCFELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
76-469 1.55e-19

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: 90.02  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   76 PHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKtPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:cd00829  16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  156 QCDVIVAGGVELMSDVPirhsrkmrklmldlnKAKSMGQRLSLISKFRFN-FLAPELPAVsefstsetMGHSADRLAAAF 234
Cdd:cd00829  95 LADVVLVVGAEKMSDVP---------------TGDEAGGRASDLEWEGPEpPGGLTPPAL--------YALAARRYMHRY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  235 AVSRLEQDEYALRSHSLAKK---AQdegllsdvvpFKVPgkDTVTKDNGIRPSSLeqmaklkpafikPYgtvTAANSSFL 311
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARnpyAQ----------FRKP--ITVEDVLNSRMIAD------------PL---RLLDCCPV 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  312 TDGASAMLIMAEEKALAMGYKPkAYLR------DFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQ 385
Cdd:cd00829 205 SDGAAAVVLASEERARELTDRP-VWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIA 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  386 ILANFKAM------DSDWFAENymGRKTKVGLPPLekfNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQY-----GL 454
Cdd:cd00829 284 ELLALEDLgfcekgEGGKLVRE--GDTAIGGDLPV---NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARqvpgaRV 358
                       410
                ....*....|....*
gi 4504327  455 VAACAAGGQGHAMIV 469
Cdd:cd00829 359 GLAHNIGGTGSAAVV 373
PRK06064 PRK06064
thiolase domain-containing protein;
78-469 1.56e-12

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 68.77  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    78 DLARAALTGLLHRTSVPKEVVDYIIFGTVI--QEVKTSNVAREAALGAGFSDKtPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:PRK06064  24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAPI-PATRVEAACASGGAALRQAYLAVASG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   156 QCDVIVAGGVELMSDVPirhsrkmrklmldlnkaksmgqrlsliskfrfnflAPElpavsefsTSETMGHSADRLAAAFA 235
Cdd:PRK06064 103 EADVVLAAGVEKMTDVP-----------------------------------TPD--------ATEAIARAGDYEWEEFF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   236 ----------VSRLEQDEYALRSHSLAK---KAQDEGLLSDVVPFKvpgkdtvtkdngiRPSSLEQMAKLKPAF--IKPY 300
Cdd:PRK06064 140 gatfpglyalIARRYMHKYGTTEEDLALvavKNHYNGSKNPYAQFQ-------------KEITVEQVLNSPPVAdpLKLL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   301 gtvtaaNSSFLTDGASAMLIMAEEKAlamgykpKAYLRDFMYVS-----------QDPKDQLLLGPT-YATPKVLEKAGL 368
Cdd:PRK06064 207 ------DCSPITDGAAAVILASEEKA-------KEYTDTPVWIKasgqasdtialHDRKDFTTLDAAvVAAEKAYKMAGI 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   369 TMNDIDAFEFHEAFSgqiLANFKAMDSDWFAENYMGRK------TKVG--LPplekFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK06064 274 EPKDIDVAEVHDCFT---IAEILAYEDLGFAKKGEGGKlaregqTYIGgdIP----VNPSGGLKAKGHPVGATGVSQAVE 346
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 4504327   441 AANRLRKE---GGQ------YGLvaACAAGGQGHAMIV 469
Cdd:PRK06064 347 IVWQLRGEaekGRQqvigagYGL--THNVGGTGHTAVV 382
PRK12578 PRK12578
thiolase domain-containing protein;
73-465 3.00e-11

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 64.87  E-value: 3.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327    73 DLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHtVTMACISANQAMTTGVGLI 152
Cdd:PRK12578  18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGLAASLTAYTAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   153 ASGQCDVIVAGGVELMSDVpirhsrkmrklmlDLNKAKSMGQRlSLISKFRFNFLAPELPAVSEFSTSETMghsadrlaA 232
Cdd:PRK12578  97 ASGLVDMAIAVGVDKMTEV-------------DTSTSLAIGGR-GGNYQWEYHFYGTTFPTYYALYATRHM--------A 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   233 AFAVSRLEQDEYALRSH---SLAKKAQdegllsdvvpFKvpgkdtvtkdngiRPSSLEQMakLKPAFIK-PygtVTAANS 308
Cdd:PRK12578 155 VYGTTEEQMALVSVKAHkygAMNPKAH----------FQ-------------KPVTVEEV--LKSRAISwP---IKLLDS 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   309 SFLTDGASAMLIMAEEKALAMGY------KPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAF 382
Cdd:PRK12578 207 CPISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAF 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   383 SgqiLANFKAMDSDWFAENYMGRK----------TKVGLpplekfNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQY 452
Cdd:PRK12578 287 T---IAEIMGYEDLGFTEKGKGGKfieegqsekgGKVGV------NLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKL 357
                        410       420
                 ....*....|....*....|.
gi 4504327   453 --------GLVAacAAGGQGH 465
Cdd:PRK12578 358 qqplkkyiGLVH--NVGGTGH 376
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
305-469 6.42e-09

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: 56.68  E-value: 6.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  305 AANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDfMYVSQDPKDQLLL----GPTYATPKVLEKAGLTMNDIDAFEFHE 380
Cdd:cd00327  94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVS-TAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHG 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327  381 AFSGQILANFKAMDSDWFaenymgrktKVGLPPLEkfnnwGGSLSLGHPFGATG-------CRLVMAAANRLRKEGGQYG 453
Cdd:cd00327 173 TGTPIGDAVELALGLDPD---------GVRSPAVS-----ATLIMTGHPLGAAGlaildelLLMLEHEFIPPTPREPRTV 238
                       170
                ....*....|....*.
gi 4504327  454 LVAACAAGGQGHAMIV 469
Cdd:cd00327 239 LLLGFGLGGTNAAVVL 254
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
130-461 9.21e-08

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 54.13  E-value: 9.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSmgqrlslISKFRFNFL-A 208
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYRRQRK-------LDDFTFPCLfA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   209 PELPAVSEfSTSETMGHSADRLAAAFAVSRLEQdeyalRSHSLAKKAQDEGLlsdvvpfkvpgkdtvtkdNGIRPSSLEQ 288
Cdd:PTZ00455 185 KRMKYIQE-HGHFTMEDTARVAAKAYANGNKNP-----LAHMHTRKLSLEFC------------------TGASDKNPKF 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   289 MAKlkpAFIKPYGTVTaaNSSFLTDGASAMLIMAEEKALAMGYKP--------KAYLRDFMYVSQDPKDQLLLGPTY-AT 359
Cdd:PTZ00455 241 LGN---ETYKPFLRMT--DCSQVSDGGAGLVLASEEGLQKMGLSPndsrlveiKSLACASGNLYEDPPDATRMFTSRaAA 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDsdwFAE-------NYMGRKTKVGLPPLekfNNWGGSLSLGHPFGA 432
Cdd:PTZ00455 316 QKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALG---IAEyghakdlIRNGATALEGRIPV---NTGGGLLSFGHPVGA 389
                        330       340
                 ....*....|....*....|....*....
gi 4504327   433 TGCRLVMAAANRLRKEGGQYGLVAACAAG 461
Cdd:PTZ00455 390 TGVKQIMEVYRQMKGQCGEYQMKNIPALG 418
PRK07516 PRK07516
thiolase domain-containing protein;
309-441 5.59e-07

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 51.49  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   309 SFLTDGASAMLIMAEEKALAM----GYKPKAYLRDFMYVSQdpKDQLLL-GPTYATPKVLEKAGLTMNDIDAFEFHEAFS 383
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSR--RDPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504327   384 GQILANFKAM------------DSDWFAENymGRktkvgLPplekFNNWGGSLSLGHPFGATGCRL-VMAA 441
Cdd:PRK07516 291 IAELIEYEAMglappgqgaraiREGWTAKD--GK-----LP----VNPSGGLKAKGHPIGATGVSMhVLAA 350
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
112-166 2.48e-06

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 49.46  E-value: 2.48e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4504327  112 TSNVAREAALGAGFsdKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVE 166
Cdd:cd00834 137 PNMAAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
130-166 2.89e-06

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 49.32  E-value: 2.89e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 4504327  130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVE 166
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
130-168 1.67e-05

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


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 46.09  E-value: 1.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 4504327    130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELM 168
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
72-171 1.77e-05

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: 46.64  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   72 KDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT----SNVAREaaLGAgfsDKTPAHTVTMACISANQAMTT 147
Cdd:COG0332  47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFpstaCLVQHK--LGA---KNAAAFDINAACSGFVYALSV 121
                        90       100
                ....*....|....*....|....*
gi 4504327  148 GVGLIASGQCD-VIVAGGvELMSDV 171
Cdd:COG0332 122 AAALIRSGQAKnVLVVGA-ETLSRI 145
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
77-167 2.39e-05

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: 45.90  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   77 HDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSdKTPAHTVTMACISANQAMTTGVGLIASGQ 156
Cdd:cd00327   8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGK 86
                        90
                ....*....|.
gi 4504327  157 CDVIVAGGVEL 167
Cdd:cd00327  87 ADIVLAGGSEE 97
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
130-192 2.83e-03

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


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 40.11  E-value: 2.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4504327  130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSM 192
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEEPEEM 216
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
78-171 4.05e-03

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: 39.06  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   78 DLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVARE--AALGAGfsdKTPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:cd00830  52 DLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLvqARLGAK---NAAAFDINAACSGFLYGLSTAAGLIRSG 128
                        90
                ....*....|....*..
gi 4504327  156 QCD-VIVAGGvELMSDV 171
Cdd:cd00830 129 GAKnVLVVGA-ETLSRI 144
PRK08256 PRK08256
lipid-transfer protein; Provisional
358-434 4.82e-03

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 39.11  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504327   358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPP---LEKF--------------NNW 420
Cdd:PRK08256 269 AAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEAL----------------GLCPegeAEKFiddgdntyggrwvvNPS 332
                         90
                 ....*....|....
gi 4504327   421 GGSLSLGHPFGATG 434
Cdd:PRK08256 333 GGLLSKGHPLGATG 346
 
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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