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Conserved domains on  [gi|26345684|dbj|BAC36493|]
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unnamed protein product [Mus musculus]

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 ...
56-472 8.00e-177

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: 500.85  E-value: 8.00e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKaktlgqrlslLSKFRLNFLSPELPAV 215
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT----------LDGMLDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 216 AefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQM 290
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 291 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLT 370
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 371 MNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG 450
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 26345684 451 GQYALVAACAAGGQGHAMIVEA 472
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
56-472 8.00e-177

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: 500.85  E-value: 8.00e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKaktlgqrlslLSKFRLNFLSPELPAV 215
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT----------LDGMLDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 216 AefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQM 290
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 291 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLT 370
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 371 MNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG 450
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 26345684 451 GQYALVAACAAGGQGHAMIVEA 472
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
57-471 3.09e-172

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: 489.05  E-value: 3.09e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684    57 VVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 136
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   137 MACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkMMLDLNKAKTLGQRLSLLskfrlnflspelpavA 216
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLR-WGVKPGNAELEDARLKDL---------------T 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   217 EFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQMA 291
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   292 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTM 371
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   372 NDIDAFEFHEAFSGQILANFKAMDsdwfaqnymgrktkvgsPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
                         410       420
                  ....*....|....*....|
gi 26345684   452 QYALVAACAAGGQGHAMIVE 471
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
55-472 1.64e-163

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 468.69  E-value: 1.64e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPA 214
Cdd:PRK08963  87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVPPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-----IVPfkvPGKDTVTKDNGIRP-SSLE 288
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDevmtaHVP---PYKQPLEEDNNIRGdSTLE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  289 QMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK08963 244 DYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  369 LTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
                        410       420
                 ....*....|....*....|....
gi 26345684  449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEV 427
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
52-472 2.54e-155

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: 446.44  E-value: 2.54e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:COG0183   1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLnkakTLGQRLSllskfrlnflspe 211
Cdd:COG0183  81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA----KLVDPMI------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 212 LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVTKDNGIRP-SS 286
Cdd:COG0183 144 NPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTT 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 287 LEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEK 366
Cdd:COG0183 224 LEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALAR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 367 AGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRL 446
Cdd:COG0183 302 AGLTLDDIDLIEINEAFAAQVLAVLRELGLDP-----------------DKVNVNGGAIALGHPLGASGARILVTLLHEL 364
                       410       420
                ....*....|....*....|....*.
gi 26345684 447 RKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:COG0183 365 ERRGGRYGLATMCIGGGQGIALIIER 390
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
55-325 7.09e-101

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 302.68  E-value: 7.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684    55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkmmldlnkaktlgQRLSLLSKFRLNFLSPElpA 214
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTVTKDNGIRP-SSLEQ 289
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 26345684   290 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSED 325
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 ...
56-472 8.00e-177

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: 500.85  E-value: 8.00e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:cd00751   1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKaktlgqrlslLSKFRLNFLSPELPAV 215
Cdd:cd00751  81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT----------LDGMLDDGLTDPFTGL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 216 AefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQM 290
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 291 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLT 370
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 371 MNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG 450
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
                       410       420
                ....*....|....*....|..
gi 26345684 451 GQYALVAACAAGGQGHAMIVEA 472
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
57-471 3.09e-172

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: 489.05  E-value: 3.09e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684    57 VVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 136
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   137 MACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkMMLDLNKAKTLGQRLSLLskfrlnflspelpavA 216
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLR-WGVKPGNAELEDARLKDL---------------T 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   217 EFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQMA 291
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   292 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTM 371
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   372 NDIDAFEFHEAFSGQILANFKAMDsdwfaqnymgrktkvgsPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
                         410       420
                  ....*....|....*....|
gi 26345684   452 QYALVAACAAGGQGHAMIVE 471
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
55-472 1.64e-163

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 468.69  E-value: 1.64e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPA 214
Cdd:PRK08963  87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVPPA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-----IVPfkvPGKDTVTKDNGIRP-SSLE 288
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDevmtaHVP---PYKQPLEEDNNIRGdSTLE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  289 QMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK08963 244 DYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  369 LTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
                        410       420
                 ....*....|....*....|....
gi 26345684  449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEV 427
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
52-472 2.54e-155

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: 446.44  E-value: 2.54e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:COG0183   1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLnkakTLGQRLSllskfrlnflspe 211
Cdd:COG0183  81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA----KLVDPMI------------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 212 LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVTKDNGIRP-SS 286
Cdd:COG0183 144 NPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTT 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 287 LEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEK 366
Cdd:COG0183 224 LEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALAR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 367 AGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRL 446
Cdd:COG0183 302 AGLTLDDIDLIEINEAFAAQVLAVLRELGLDP-----------------DKVNVNGGAIALGHPLGASGARILVTLLHEL 364
                       410       420
                ....*....|....*....|....*.
gi 26345684 447 RKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:COG0183 365 ERRGGRYGLATMCIGGGQGIALIIER 390
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
47-472 5.19e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 368.07  E-value: 5.19e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   47 LAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGF 126
Cdd:PRK09268   1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  127 SDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLN 206
Cdd:PRK09268  81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGDRLKALGKLRPK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  207 FLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKvpgkdTVTKDNGIRP- 284
Cdd:PRK09268 161 HLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFL-----GLTRDNNLRPd 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  285 SSLEQMAKLKPAFIK-PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQD---PKDQLLLGPTYAT 360
Cdd:PRK09268 236 SSLEKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhGKEGLLMAPAYAV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK09268 316 PRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVA 395
                        410       420       430
                 ....*....|....*....|....*....|..
gi 26345684  441 AAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09268 396 TLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
51-472 5.93e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 336.99  E-value: 5.93e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   51 NMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKT 130
Cdd:PRK08170   1 MARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSP 210
Cdd:PRK08170  81 PAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKSIGQKLAALGKLRPSYLAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  211 E---LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFkVPGKDTV-TKDNGIRP-S 285
Cdd:PRK08170 161 ViglLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPL-FDRDGKFyDHDDGVRPdS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  286 SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLE 365
Cdd:PRK08170 240 SMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDP-SQMGLGPVHAATPLLQ 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  366 KAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK08170 319 RHGLTLEDLDLWEINEAFAAQVLACLAAWADEEYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHA 398
                        410       420
                 ....*....|....*....|....*..
gi 26345684  446 LRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08170 399 LKRRGTKRGIAAICIGGGQGGAMLLER 425
PRK05790 PRK05790
putative acyltransferase; Provisional
52-472 3.26e-109

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 329.04  E-value: 3.26e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDlnkaktlgqrlsllskfrl 205
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRWGQKMgdveLVD------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  206 nflSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDN 280
Cdd:PRK05790 142 ---TMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTIKQRKgdpvVVDTDE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  281 GIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYA 359
Cdd:PRK05790 219 HPRPdTTAESLAKLRPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPA-IMGIGPVPA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PRK05790 297 IRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLD-----------------PEKVNVNGGAIALGHPIGASGARIL 359
                        410       420       430
                 ....*....|....*....|....*....|...
gi 26345684  440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK05790 360 VTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
55-325 7.09e-101

Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 302.68  E-value: 7.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684    55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkmmldlnkaktlgQRLSLLSKFRLNFLSPElpA 214
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTVTKDNGIRP-SSLEQ 289
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 26345684   290 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSED 325
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
52-474 2.86e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 275.33  E-value: 2.86e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrHSRNMRKmmldlnKAKTLGQRLS-LLSKFRlnflsp 210
Cdd:PRK06205  81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEF-YTTDMRW------GVRGGGVQLHdRLARGR------ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  211 ELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDNGIRP- 284
Cdd:PRK06205 148 ETAGGRRFPVPGGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVTVPQRKgdptVVDRDEHPRAd 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  285 SSLEQMAKLKPAFIK--PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPK 362
Cdd:PRK06205 228 TTLESLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEP-SRMGIGPVPATEK 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  363 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAA 442
Cdd:PRK06205 307 ALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADD--------------EERLNVNGSGISLGHPVGATGGRILATL 372
                        410       420       430
                 ....*....|....*....|....*....|..
gi 26345684  443 ANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PRK06205 373 LRELQRRQARYGLETMCIGGGQGLAAVFERVN 404
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
52-473 5.68e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 269.27  E-value: 5.68e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK08235   1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDLNKAKTLgqrlsllskfrl 205
Cdd:PRK08235  81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyiLPGARWGYRMgdneVIDLMVADGL------------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  206 nflspelpaVAEFSTNEtMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDN 280
Cdd:PRK08235 149 ---------TCAFSGVH-MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQRKgdpiVVAKDE 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  281 GIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYA 359
Cdd:PRK08235 219 APRKdTTIEKLAKLKPVF-DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKD-FPRTPGYA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PRK08235 297 INALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGID-----------------PEKVNVNGGAVALGHPIGASGARII 359
                        410       420       430
                 ....*....|....*....|....*....|....
gi 26345684  440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK08235 360 VTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
PRK09051 PRK09051
beta-ketothiolase BktB;
51-471 1.40e-81

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 257.97  E-value: 1.40e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   51 NMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDK 129
Cdd:PRK09051   1 MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPtEPRDMYLSRVAAINAGVPQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKMmldlNKAKTLGQRLSLLSkfrlnf 207
Cdd:PRK09051  81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPylLPAARWGARM----GDAKLVDMMVGALH------ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  208 lSPelpavaeFSTNEtMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPG-KDTVT--KDNGIR 283
Cdd:PRK09051 151 -DP-------FGTIH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVEIKTrKGEVVfdTDEHVR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  284 PS-SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPK 362
Cdd:PRK09051 222 ADtTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDP-EYMGIGPVPATQK 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  363 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsPplEKFNIWGGSLSLGHPFGATGCRLVMAA 442
Cdd:PRK09051 301 ALERAGLTVADLDVIEANEAFAAQACAVTRELGLD---------------P--AKVNPNGSGISLGHPVGATGAIITVKA 363
                        410       420
                 ....*....|....*....|....*....
gi 26345684  443 ANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09051 364 LYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
52-471 2.16e-81

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 257.34  E-value: 2.16e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 130
Cdd:PRK07850   1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSnNITRTAWLHAGLPYHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktLGQRLSL-LSKFRLNFLS 209
Cdd:PRK07850  81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP-------------------LGANAGPgRGLPRPDSWD 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  210 PELPAVAEfstnetmghSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHL-SDIVPFKVPGKD----------TVTK 278
Cdd:PRK07850 142 IDMPNQFE---------AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFdREISPVQAPVLDeegqptgetrLVTR 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  279 DNGIRPSSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTY 358
Cdd:PRK07850 213 DQGLRDTTMEGLAGLKP--VLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPY-YHLDGPVQ 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  359 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILAnfkamdsdwFAQnymgrktkVGSPPLEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK07850 290 ATAKVLEKAGMKIGDIDLVEINEAFASVVLS---------WAQ--------VHEPDMDKVNVNGGAIALGHPVGSTGARL 352
                        410       420       430
                 ....*....|....*....|....*....|...
gi 26345684  439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07850 353 ITTALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
52-473 4.12e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 256.57  E-value: 4.12e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTS------YKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGA 124
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  125 GFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHS----RNMrKMMLDlnkaktlgqrlSLL 200
Cdd:PRK06445  81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiePNP-KLLTD-----------PKY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  201 SKFRLNflspelpavaefsTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTV 276
Cdd:PRK06445 149 IEYDLT-------------TGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDeILPIEVEvegKKKVV 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  277 TKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLG 355
Cdd:PRK06445 216 DVDQSVRPdTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPP-AIMGKG 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  356 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATG 435
Cdd:PRK06445 294 PVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD-----------------PETVNIKGGAIAIGHPLGATG 356
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 26345684  436 CRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06445 357 ARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
52-471 2.57e-80

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 254.50  E-value: 2.57e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLS-GTSYKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSD 128
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGfNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  129 KTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSrnmrkmmLDLNKAktlgqrlslLSKFrlnfl 208
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHG-------VDFHPG---------LSKN----- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  209 spelpaVAEFSTNetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPfkVPGKD------TVTKDNG 281
Cdd:PRK08947 140 ------VAKAAGM--MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNeIIP--TEGHDadgvlkLFDYDEV 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  282 IRP-SSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYAT 360
Cdd:PRK08947 210 IRPeTTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPS-IMGYGPVPAT 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqNYMGRKTkvgspplEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK08947 289 QKALKRAGLSISDIDVFELNEAFAAQSLPCLKDL-------GLLDKMD-------EKVNLNGGAIALGHPLGCSGARIST 354
                        410       420       430
                 ....*....|....*....|....*....|.
gi 26345684  441 AAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08947 355 TLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
52-471 7.37e-80

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 253.09  E-value: 7.37e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKT 130
Cdd:PRK07801   1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTiGPQAGNIARTSWLAAGLPEEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrhSRNMrkmmldlnkakTLGQRLSLLSKFrlnflSP 210
Cdd:PRK07801  81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPI--SSAM-----------TAGEQLGFTSPF-----AE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  211 ELPAVAEFSTNE-TMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSLE 288
Cdd:PRK07801 143 SKGWLHRYGDQEvSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPV-----GGVTVDEGPRETSLE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  289 QMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAG 368
Cdd:PRK07801 218 KMAGLKP--LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPV-FMLTAPIPATRYALEKTG 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  369 LTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK07801 295 LSIDDIDVVEINEAFAPVVLAWLKETGAD-----------------PAKVNPNGGAIALGHPLGATGAKLMTTLLHELER 357
                        410       420
                 ....*....|....*....|...
gi 26345684  449 DGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07801 358 TGGRYGLQTMCEGGGTANVTIIE 380
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
53-474 2.17e-76

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 244.62  E-value: 2.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   53 KNIVVVEGVRIP---FLLSGTSYKdlmPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIqevkTSNV----AREAALGAG 125
Cdd:PLN02644   1 RDVCIVGVARTPiggFLGSLSSLS---ATELGSIAIQAALERAGVDPALVQEVFFGNVL----SANLgqapARQAALGAG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  126 FSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrKMMLDLNKAKTLGQRLSLLSKFRL 205
Cdd:PLN02644  74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAP--------KYLPEARKGSRLGHDTVVDGMLKD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  206 NFLSPelpavaefSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK-----DTVTKD 279
Cdd:PLN02644 146 GLWDV--------YNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWeIVPVEVPGGrgrpsVIVDKD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  280 NGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYA 359
Cdd:PLN02644 218 EGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAP-ELFTTAPALA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqnymgrktkvGSPPlEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PLN02644 297 IPKALKHAGLEASQVDYYEINEAFSVVALANQKLL----------------GLDP-EKVNVHGGAVSLGHPIGCSGARIL 359
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 26345684  440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PLN02644 360 VTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
52-471 9.69e-73

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 235.23  E-value: 9.69e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNrNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPI-------RHSRNMRkmMLDlnkaKTLGQRlsllsk 202
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFvmgkadsAFSRQAE--IFD----TTIGWR------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  203 frlnFLSPELPAvaEFSTnETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVT 277
Cdd:PRK09050 149 ----FVNPLMKA--QYGV-DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEeIVPVTIPQKKgdpvVVD 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  278 KDNGIRPS-SLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PRK09050 222 RDEHPRPEtTLEALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPR-IMGIGP 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAM---DSDwfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGA 433
Cdd:PRK09050 300 APATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLglaDDD------------------ARVNPNGGAIALGHPLGM 361
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 26345684  434 TGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09050 362 SGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
52-471 9.52e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 221.93  E-value: 9.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK07661   1 MREAVIVAGARTPVGKAKKgSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMldlnkaktlGQRLsllskfRLNfls 209
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP---------MM---------GHVV------RPN--- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  210 pelPAVAEFSTN--ETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP----GKD-------- 274
Cdd:PRK07661 134 ---PRLVEAAPEyyMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADeIVPVDVTlrtvGENnklqeeti 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  275 TVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLL 353
Cdd:PRK07661 211 TFSQDEGVRAdTTLEILGKLRPAF-NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFA-VAGVPPEVMG 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  354 LGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGA 433
Cdd:PRK07661 289 IGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE-----------------EKVNVNGGAIALGHPLGC 351
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 26345684  434 TGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07661 352 TGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
54-472 6.87e-67

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 221.56  E-value: 6.87e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   54 NIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTP 131
Cdd:PLN02287  47 DVVIVAAYRTPICKAKRgGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPgSQRANECRMAAFYAGFPETVP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldlnkaktlgqrlsllSKFRLNflspe 211
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMA-------------------------WEGGVN----- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  212 lPAVAEFSTNET----MGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---------TVT 277
Cdd:PLN02287 177 -PRVESFSQAQDcllpMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDeIVPVHTKIVDpktgeekpiVIS 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  278 KDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PLN02287 256 VDDGIRPnTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPA-VMGIGP 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGC 436
Cdd:PLN02287 334 AVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDP-----------------EKVNVNGGAIALGHPLGATGA 396
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 26345684  437 RLVMAAANRLRKDG--GQYALVAACAAGGQGHAMIVEA 472
Cdd:PLN02287 397 RCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
52-471 1.08e-64

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 214.48  E-value: 1.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGT-SYKDLMPHDLA----RAALSGLLHRTniPKDVVDyIIFGTVIQEVKT-SNVAREAALGAG 125
Cdd:PRK07851   1 MPEAVIVSTARSPIGRAFKgSLKDMRPDDLAaqmvRAALDKVPALD--PTDIDD-LMLGCGLPGGEQgFNMARVVAVLLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  126 FsDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNM---RKMMLDLNKAKTLGQRLSLLSK 202
Cdd:PRK07851  78 Y-DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFAEAQARTAARAEGGAEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  203 FRLNFLSPELPAVAEfstneTMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVPGKDTVTKDNG 281
Cdd:PRK07851 157 WHDPREDGLLPDVYI-----AMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFErEITPVTLPDGTVVSTDDG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  282 IRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDfIYVSQDPKDQLLLGPTYAT 360
Cdd:PRK07851 232 PRAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVS-TGVSGLSPEIMGLGPVEAS 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGID-----------------EDKLNVSGGAIALGHPFGMTGARITT 372
                        410       420       430
                 ....*....|....*....|....*....|.
gi 26345684  441 AAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07851 373 TLLNNLQTHDKTFGLETMCVGGGQGMAMVLE 403
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
72-472 1.45e-64

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 213.71  E-value: 1.45e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   72 YKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTA 149
Cdd:PRK09052  26 FKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGlNVARIGALLAGLPNSVGGVTVNRFCASGLQAVAMA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  150 VGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMldlnkaktlGQRLSLlskfrlnflSPELpavaeFSTNET------ 223
Cdd:PRK09052 106 ADRIRVGEADVMIAAGVESMSMVP---------MM---------GNKPSM---------SPAI-----FARDENvgiayg 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  224 MGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKV----PG---------KDTVTKDNGIRP-SSLE 288
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPYEIterfPDlatgevdvkTRTVDLDEGPRAdTSLE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  289 QMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK09052 234 GLAKLKPVF-ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFA-VAGVPPEIMGIGPIEAIPAALKQAG 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  369 LTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK09052 312 LKQDDLDWIELNEAFAAQSLAVIRDLGLD-----------------PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRR 374
                        410       420
                 ....*....|....*....|....
gi 26345684  449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09052 375 TNLKYGMVTMCVGTGMGAAGIFER 398
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
52-471 2.27e-64

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 213.49  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 130
Cdd:PRK08131   1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSrNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPI-------RHSRNMRkmMLDlnkaKTLGQRlsllskf 203
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFvmgkaesAFSRDAK--VFD----TTIGAR------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  204 rlnFLSPELpaVAEFStNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP--GKDT---VT 277
Cdd:PRK08131 148 ---FPNPKI--VAQYG-NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADeITPIEVPqgRKLPpklVA 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  278 KDNGIRPSS-LEQMAKLKPAFIKpyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PRK08131 222 EDEHPRPSStVEALTKLKPLFEG--GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPR-IMGIGP 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGC 436
Cdd:PRK08131 299 VEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDD---------------PRVNPNGGAIAVGHPLGASGA 363
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 26345684  437 RLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08131 364 RLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
77-471 3.57e-64

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 212.82  E-value: 3.57e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQeV--KTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIA 154
Cdd:PRK08242  28 PVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTP-VgdQGADIARTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVR 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  155 SGQCDVVVAGGVELMSDVPIRHSRnmRKMMLDLNKAktlgqrlsllskFRLNFLsPElpavaefstnetmGHSADRLAAA 234
Cdd:PRK08242 107 SGWDDLVIAGGVESMSRVPMGSDG--GAWAMDPSTN------------FPTYFV-PQ-------------GISADLIATK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  235 FAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVpfkVPGKD-----TVTKDNGIRP-SSLEQMAKLKPAF----------- 297
Cdd:PRK08242 159 YGFSREDVDAYAVESQQRAAAAWAEGYFAKSV---VPVKDqngltILDHDEHMRPgTTMESLAKLKPSFammgemggfda 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  298 --IKPYGTV-------TAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAG 368
Cdd:PRK08242 236 vaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPT-IMLTGPVPATRKALAKAG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  369 LTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDI-----------------PHDKVNVNGGAIAMGHPLGATGAMILGTVLDELER 377
                        410       420
                 ....*....|....*....|...
gi 26345684  449 DGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08242 378 RGKRTALITLCVGGGMGIATIIE 400
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
77-472 1.42e-63

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 211.13  E-value: 1.42e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIAS 155
Cdd:PRK06504  26 PADLAAQVLDALVDRSGADPALIEDVIMGCVSQVgEQATNVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMS 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  156 GQCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktLGQRLSLLSKFRL-NFLSPELPA---VAEFStnETMGhsADRL 231
Cdd:PRK06504 106 GTMDIVIAAGVESMTRVP-------------------MGSPSTLPAKNGLgHYKSPGMEErypGIQFS--QFTG--AEMM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  232 AAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPG----KDTVTKDNGIR-PSSLEQMAKLKPafIKPYGTVT 305
Cdd:PRK06504 163 AKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPLEITRadgsGEMHTVDEGIRfDATLEGIAGVKL--IAEGGRLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  306 AANSSFLTDGASAMLIMSEdRAL-AMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFS 384
Cdd:PRK06504 241 AATASQICDGASGVMVVNE-RGLkALGVKPLARIHHMTVIGGDPV-IMLEAPLPATERALKKAGMKIDDIDLYEVNEAFA 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  385 GQILANFKAMDSDwfaqnymgrktkvgsPplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQ 464
Cdd:PRK06504 319 SVPLAWLKATGAD---------------P--ERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGM 381

                 ....*...
gi 26345684  465 GHAMIVEA 472
Cdd:PRK06504 382 ANVTIVER 389
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
52-471 3.36e-61

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 204.62  E-value: 3.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFllsGTSYKDL--MPH--DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGAGF 126
Cdd:PRK07108   1 MTEAVIVSTARTPL---AKSWRGAfnMTHgaTLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATgANIARQIALRAGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  127 SDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVpirhSRNMRKMMLD---LNKAKtlgqrlsllskf 203
Cdd:PRK07108  78 PVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV----QNEMNRHMLRegwLVEHK------------ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  204 rlnflsPELpavaefstNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPF--------KVPG-- 272
Cdd:PRK07108 142 ------PEI--------YWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPItvtagvadKATGrl 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  273 ---KDTVTKDNGIRP-SSLEQMAKLKPAFikPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDP 348
Cdd:PRK07108 208 ftkEVTVSADEGIRPdTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  349 kDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMgrKTKVGSPPlEKFNIWGGSLSLG 428
Cdd:PRK07108 286 -DEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVL--------------YC--RDTLGIPM-DRLNVNGGAIAVG 347
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 26345684  429 HPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07108 348 HPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
332-472 4.66e-59

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: 190.16  E-value: 4.66e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   332 YKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvg 411
Cdd:pfam02803   1 LKPLARIRSYATAGVDP-AIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP------------- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26345684   412 spplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:pfam02803  67 ----EKVNVNGGAIALGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
52-471 5.23e-58

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 196.38  E-value: 5.23e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR---KMMLDLNkaktlgqrlsllSKFRLNFL 208
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgpKHLLHKN------------YKIDDAML 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  209 SPELPAVAEFstnETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSL 287
Cdd:PRK06366 149 VDGLIDAFYF---EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNeIVPF-----NDLDRDEGIRKTTM 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  288 EQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEKA 367
Cdd:PRK06366 221 EDLAKLPPAFDKN-GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLD-FVEAPIPATRKLLEKQ 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  368 GLTMNDIDAFEFHEAFS--GQILANFKAMDSdwfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK06366 299 NKSIDYYDLVEHNEAFSiaSIIVRDQLKIDN-------------------ERFNVNGGAVAIGHPIGNSGSRIIVTLINA 359
                        410       420
                 ....*....|....*....|....*.
gi 26345684  446 LRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06366 360 LKTRHMKTGLATLCHGGGGAHTLTLE 385
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
52-472 4.61e-56

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 191.40  E-value: 4.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06633   2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSdvPIRHSRNMRK-------MMLDLNkaktlgQRLSLLSKFR 204
Cdd:PRK06633  82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS--LGMHGSYIRAgakfgdiKMVDLM------QYDGLTDVFS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  205 LNFlspelpavaefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKDTVT---KDN 280
Cdd:PRK06633 154 GVF----------------MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDeILPIEVTIKKTTSlfdHDE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  281 GIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdqlLLG--PT 357
Cdd:PRK06633 218 TVRPdTSLEILSKLRPAFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPS---IMGtaPV 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  358 YATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMGRKTKVGsppLEKFNIWGGSLSLGHPFGATGCR 437
Cdd:PRK06633 294 PASQKALSKAGWSVNDLEVIEVNEAFAAQSI--------------YVNREMKWD---MEKVNINGGAIAIGHPIGASGGR 356
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 26345684  438 LVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK06633 357 VLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
55-473 1.11e-55

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 190.49  E-value: 1.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP-----------IRHSRNMRKMMLD-LNKAKTLGQrlsllsk 202
Cdd:PRK06954  89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDgLEDAYDKGR------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  203 frlnflspelpavaefstneTMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVPGKD---TVTK 278
Cdd:PRK06954 162 --------------------LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAwEIAPVTVAGKKgdtVIDR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  279 DNGIRPSSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTY 358
Cdd:PRK06954 222 DEQPFKANPEKIPTLKPAFSKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPS-KFTTAPVG 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  359 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK06954 300 AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL-----------------PHEKVNVNGGACALGHPIGASGARI 362
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 26345684  439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06954 363 LVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
52-471 6.32e-53

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 183.17  E-value: 6.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldLNKAKTlGQRLSLLSKFRLNFLSPE 211
Cdd:PRK05656  81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYV-----------LPGART-GLRMGHAQLVDSMITDGL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  212 LPAVAEFStnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDNGIRP-S 285
Cdd:PRK05656 149 WDAFNDYH----MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDeITPILIPQRKgeplAFATDEQPRAgT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  286 SLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLE 365
Cdd:PRK05656 225 TAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPA-IMGIGPVSATRRCLD 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  366 KAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK05656 303 KAGWSLAELDLIEANEAFAAQSLAVGKELGWD-----------------AAKVNVNGGAIALGHPIGASGCRVLVTLLHE 365
                        410       420
                 ....*....|....*....|....*.
gi 26345684  446 LRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK05656 366 MIRRDAKKGLATLCIGGGQGVALAIE 391
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
74-471 5.11e-52

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 181.13  E-value: 5.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   74 DLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGL 152
Cdd:PRK06025  26 HLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  153 IASGQCDVVVAGGVELMSdvpirhsrnMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPElpavaefstnETMGHSADRLA 232
Cdd:PRK06025 106 IMSGMEDLVIAGGTEMMS---------YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQ----------SHQGVCGDAIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  233 AAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVP-GKDTVTKDNGIRP-SSLEQMAKLKPAF-------IKPYG 302
Cdd:PRK06025 167 TMEGITREALDALGLESQRRAARAIKEGRFDkSLVPVYRDdGSVALDHEEFPRPqTTAEGLAALKPAFtaiadypLDDKG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  303 TVT------------------AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVL 364
Cdd:PRK06025 247 TTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT-LMLNAPVPAAKKVL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  365 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAAN 444
Cdd:PRK06025 326 AKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDR-----------------DKVNVNGGAIALGHPIGATGSILIGTVLD 388
                        410       420
                 ....*....|....*....|....*..
gi 26345684  445 RLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06025 389 ELERRGLKRGLVTMCAAGGMAPAIIIE 415
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
54-471 4.56e-51

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 177.27  E-value: 4.56e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   54 NIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLlhRTNIPKDVvDYIIFGTVIQevKTSNVAREAALGAGFSDKTPAH 133
Cdd:PRK06690   2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMEREI-DDVILGNVVG--PGGNVARLSALEAGLGLHIPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  134 TVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldlNKAKtlgqrlsllskfrlnfLSPELP 213
Cdd:PRK06690  77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ------------NRAR----------------FSPETI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  214 AvaefstNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSLEQM-A 291
Cdd:PRK06690 129 G------DPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEeILSF-----NGLLDESIKKEMNYERIiK 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  292 KLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLlGPTYATPKVLEKAGLTM 371
Cdd:PRK06690 198 RTKPAFLHN-GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGT-GPIFAVNKLLNEMNMKV 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  372 NDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:PRK06690 276 EDIDYFEINEAFASKVVACAKELQI-----------------PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDM 338
                        410       420
                 ....*....|....*....|
gi 26345684  452 QYALVAACAAGGQGHAMIVE 471
Cdd:PRK06690 339 KYGIATLGIGGGIGLALLFE 358
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
68-471 2.56e-39

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: 146.48  E-value: 2.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  68 SGTSYKDLmPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMT 147
Cdd:cd00826  15 NGADANDL-AHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 148 TAVGLIASGQCDVVVAGGVELMSdvpirhsrnmrkmMLDLNKAKTlGQRLSLLSKFRlnflspelpavaefstnetmghs 227
Cdd:cd00826  94 LAMQLIAGGDANCILAGGFEKME-------------TSAENNAKE-KHIDVLINKYG----------------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 228 adrlaaafavSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVTKDNGIR---PSSLEQMAKLKPAFIKP 300
Cdd:cd00826 137 ----------MRACPDAFALAGQAGAEAAEKDGRFKDeFAKFGVKGRKgdiHSDADEYIQfgdEASLDEIAKLRPAFDKE 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 301 yGTVTAANSSFLTDGASAMLIMSEDRA-------LAMGYKPKAYLRDFIYVSQDPKDQLLLG---PTYATPKVLEKAGLT 370
Cdd:cd00826 207 -DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVGgdgPIEAARKALEKAGLG 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 371 MNDIDAFEFHEAFSGQILANFKAMdsDWFAQNYMGRKTKVGSPPLEK---FNIWGGSLSLGHPFGATGCRLVMAAANRLR 447
Cdd:cd00826 286 IGDLDLIEAHDAFAANACATNEAL--GLCPEGQGGALVDRGDNTYGGksiINPNGGAIAIGHPIGASGAAICAELCFELK 363
                       410       420
                ....*....|....*....|....*....
gi 26345684 448 KDGGQYA-----LVAACAAGGQGHAMIVE 471
Cdd:cd00826 364 GEAGKRQgagagLALLCIGGGGGAAMCIE 392
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
77-470 2.67e-22

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: 98.10  E-value: 2.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00829  16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASG 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 157 QCDVVVAGGVELMSDVPirhsrnmrkmmldlnKAKTLGQRLSLLSKFRlnflsPELPAvaefstnetmGHSADRLAAAFA 236
Cdd:cd00829  95 LADVVLVVGAEKMSDVP---------------TGDEAGGRASDLEWEG-----PEPPG----------GLTPPALYALAA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 237 VSRMEQdeYALRSHSLAK---KAQDEGHLSDIVPFKVPgkDTVTKDNGIRPSSLeqmaklkpafikPYgtvTAANSSFLT 313
Cdd:cd00829 145 RRYMHR--YGTTREDLAKvavKNHRNAARNPYAQFRKP--ITVEDVLNSRMIAD------------PL---RLLDCCPVS 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 314 DGASAMLIMSEDRALAMGYKPkAYLR------DFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQI 387
Cdd:cd00829 206 DGAAAVVLASEERARELTDRP-VWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAE 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 388 LANFKAM------DSDWFAQNymGRKTKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYA-----LV 456
Cdd:cd00829 285 LLALEDLgfcekgEGGKLVRE--GDTAIGGDLPV---NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQvpgarVG 359
                       410
                ....*....|....
gi 26345684 457 AACAAGGQGHAMIV 470
Cdd:cd00829 360 LAHNIGGTGSAAVV 373
PRK06064 PRK06064
thiolase domain-containing protein;
79-449 7.85e-16

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 79.17  E-value: 7.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   79 DLARAALSGLLHRTNIPKDVVDYIIFGTVI--QEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK06064  24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAPI-PATRVEAACASGGAALRQAYLAVASG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  157 QCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktlgqrlsllskfrlnflSPElpavaefsTNETMGHSADRLAAAFA 236
Cdd:PRK06064 103 EADVVLAAGVEKMTDVP-----------------------------------TPD--------ATEAIARAGDYEWEEFF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  237 ----------VSRMEQDEYALRSHSLAK---KAQDEGHLSDIVPFKvpgkdtvtkdngiRPSSLEQMAKLKPAF--IKPY 301
Cdd:PRK06064 140 gatfpglyalIARRYMHKYGTTEEDLALvavKNHYNGSKNPYAQFQ-------------KEITVEQVLNSPPVAdpLKLL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  302 gtvtaaNSSFLTDGASAMLIMSEDRAlamgykpKAYLRDFIYVS-----------QDPKDQLLLGPT-YATPKVLEKAGL 369
Cdd:PRK06064 207 ------DCSPITDGAAAVILASEEKA-------KEYTDTPVWIKasgqasdtialHDRKDFTTLDAAvVAAEKAYKMAGI 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  370 TMNDIDAFEFHEAFSgqiLANFKAMDSDWFAQNYMGRK------TKVGSppleKF--NIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK06064 274 EPKDIDVAEVHDCFT---IAEILAYEDLGFAKKGEGGKlaregqTYIGG----DIpvNPSGGLKAKGHPVGATGVSQAVE 346

                 ....*...
gi 26345684  442 AANRLRKD 449
Cdd:PRK06064 347 IVWQLRGE 354
PRK12578 PRK12578
thiolase domain-containing protein;
74-466 8.21e-11

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 63.71  E-value: 8.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   74 DLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHtVTMACISSNQAMTTAVGLI 153
Cdd:PRK12578  18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGLAASLTAYTAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  154 ASGQCDVVVAGGVELMSDVpirhsrnmrkmmlDLNKAKTLGQRL-SLLSKFrlNFLSPELPAVAEFStnetmghsADRLA 232
Cdd:PRK12578  97 ASGLVDMAIAVGVDKMTEV-------------DTSTSLAIGGRGgNYQWEY--HFYGTTFPTYYALY--------ATRHM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  233 AAFAVSRMEQDEYALRSHSLAKKaQDEGHLSdivpfkvpgkdtvtkdngiRPSSLEQMakLKPAFIK-PygtVTAANSSF 311
Cdd:PRK12578 154 AVYGTTEEQMALVSVKAHKYGAM-NPKAHFQ-------------------KPVTVEEV--LKSRAISwP---IKLLDSCP 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  312 LTDGASAMLIMSEDRALAMGY------KPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSg 385
Cdd:PRK12578 209 ISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFT- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  386 qiLANFKAMDSDWFAQNYMGRK-------TKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG--QYALV 456
Cdd:PRK12578 288 --IAEIMGYEDLGFTEKGKGGKfieegqsEKGGKVGV---NLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGklQQPLK 362
                        410
                 ....*....|....
gi 26345684  457 AACA----AGGQGH 466
Cdd:PRK12578 363 KYIGlvhnVGGTGH 376
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
306-470 4.37e-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: 57.07  E-value: 4.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 306 AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLL---GPTYATPKVLEKAGLTMNDIDAFEFHEA 382
Cdd:cd00327  94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684 383 FSGQILANFKAMDSDWFAQNYMgrktkvgspplekfNIWGGSLSLGHPFGATG-------CRLVMAAANRLRKDGGQYAL 455
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSP--------------AVSATLIMTGHPLGAAGlaildelLLMLEHEFIPPTPREPRTVL 239
                       170
                ....*....|....*
gi 26345684 456 VAACAAGGQGHAMIV 470
Cdd:cd00327 240 LLGFGLGGTNAAVVL 254
PRK07516 PRK07516
thiolase domain-containing protein;
310-442 9.93e-08

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 53.80  E-value: 9.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  310 SFLTDGASAMLIMSEDRALAM----GYKPKAYLRDFIYVSQdpKDQLLL-GPTYATPKVLEKAGLTMNDIDAFEFHEAFS 384
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSR--RDPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26345684  385 GQILANFKAMDSDWFAQNYM----GRKTKVGSPPLekfNIWGGSLSLGHPFGATGCRL-VMAA 442
Cdd:PRK07516 291 IAELIEYEAMGLAPPGQGARaireGWTAKDGKLPV---NPSGGLKAKGHPIGATGVSMhVLAA 350
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
96-462 1.55e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 53.36  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   96 KDVVDYIIFGTVIQEVKTS--NVAREAALGAGFSDKT------PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PTZ00455  69 AALVDKVVVGNFLGELFSSqgHLGPAAVGSLGQSGASnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  168 LMSDVPIRHSRNMRKMMLDLNKAKTLGqrlsllskfrlNFLSPELPAVAEFSTNETmGHSAdrlaaafavsrMEQDEYal 247
Cdd:PTZ00455 149 VQTTVSARVGGDYLARAADYRRQRKLD-----------DFTFPCLFAKRMKYIQEH-GHFT-----------MEDTAR-- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  248 rshsLAKKAQDEGHLSDIVPFKVpGKDTVTKDNGIRPSSLEQMAKlkpAFIKPYGTVTaaNSSFLTDGASAMLIMSEDRA 327
Cdd:PTZ00455 204 ----VAAKAYANGNKNPLAHMHT-RKLSLEFCTGASDKNPKFLGN---ETYKPFLRMT--DCSQVSDGGAGLVLASEEGL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  328 LAMGYKP--------KAYLRDFIYVSQDPKDQLLLGPTY-ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMD-SD 397
Cdd:PTZ00455 274 QKMGLSPndsrlveiKSLACASGNLYEDPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGiAE 353
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26345684  398 WFAQNYMGRK---TKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAG 462
Cdd:PTZ00455 354 YGHAKDLIRNgatALEGRIPV---NTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNIPALG 418
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
113-167 1.82e-07

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: 53.31  E-value: 1.82e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26345684 113 TSNVAREAALGAGFsdKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:cd00834 137 PNMAAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
131-167 2.19e-07

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: 52.79  E-value: 2.19e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 26345684 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
131-169 3.00e-07

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: 51.48  E-value: 3.00e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 26345684   131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELM 169
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
78-168 8.85e-07

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: 50.14  E-value: 8.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  78 HDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSdKTPAHTVTMACISSNQAMTTAVGLIASGQ 157
Cdd:cd00327   8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGK 86
                        90
                ....*....|.
gi 26345684 158 CDVVVAGGVEL 168
Cdd:cd00327  87 ADIVLAGGSEE 97
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
73-172 9.30e-07

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: 50.49  E-value: 9.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  73 KDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT----SNVAREaaLGAgfsDKTPAHTVTMACISSNQAMTT 148
Cdd:COG0332  47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFpstaCLVQHK--LGA---KNAAAFDINAACSGFVYALSV 121
                        90       100
                ....*....|....*....|....*
gi 26345684 149 AVGLIASGQCD-VVVAGGvELMSDV 172
Cdd:COG0332 122 AAALIRSGQAKnVLVVGA-ETLSRI 145
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
131-181 5.75e-05

"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: 45.12  E-value: 5.75e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 26345684 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR 181
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMG 204
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
131-166 2.16e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 43.29  E-value: 2.16e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 26345684  131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGV 166
Cdd:PRK09185 152 PAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGV 187
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
79-172 8.07e-04

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: 41.37  E-value: 8.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684  79 DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAGfsdKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00830  52 DLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLvqARLGAK---NAAAFDINAACSGFLYGLSTAAGLIRSG 128
                        90
                ....*....|....*.
gi 26345684 157 QCDVVVAGGVELMSDV 172
Cdd:cd00830 129 GAKNVLVVGAETLSRI 144
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
131-171 9.72e-04

polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 41.39  E-value: 9.72e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 26345684 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSD 171
Cdd:cd00833 162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILS 202
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
79-172 2.81e-03

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


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 39.85  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345684   79 DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAgfsDKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK12879  55 DLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQvqARLGI---PNAAAFDINAACAGFLYGLETANGLITSG 131
                         90
                 ....*....|....*.
gi 26345684  157 QCDVVVAGGVELMSDV 172
Cdd:PRK12879 132 LYKKVLVIGAERLSKV 147
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
129-167 4.34e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 39.39  E-value: 4.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 26345684  129 KTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PRK07314 152 KGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE 190
 
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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