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Conserved domains on  [gi|345112616|gb|AEN73448|]
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acetyl-CoA acetyltransferase [Rhodothermus marinus SG0.5JP17-172]

Protein Classification

acetyl-CoA acetyltransferase( domain architecture ID 11483181)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
4-404 0e+00

acetyl-CoA C-acetyltransferase;


:

Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 761.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPMMLDPAVSMQIGFVPQGIGADLIATIEGFT 163
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYGFS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 164 REDVDRYALCSQQRAAHARANGYF-KSIVPVRDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGAM-GFDDVALQKYV 241
Cdd:PRK08242 163 REDVDAYAVESQQRAAAAWAEGYFaKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQKYP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 242 TVERINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:PRK08242 243 EVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATII 401
Cdd:PRK08242 323 FELNEAFASVVLRFMQALDIPH---DKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATII 399

                 ...
gi 345112616 402 ERV 404
Cdd:PRK08242 400 ERV 402
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
4-404 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 761.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPMMLDPAVSMQIGFVPQGIGADLIATIEGFT 163
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYGFS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 164 REDVDRYALCSQQRAAHARANGYF-KSIVPVRDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGAM-GFDDVALQKYV 241
Cdd:PRK08242 163 REDVDAYAVESQQRAAAAWAEGYFaKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQKYP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 242 TVERINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:PRK08242 243 EVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATII 401
Cdd:PRK08242 323 FELNEAFASVVLRFMQALDIPH---DKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATII 399

                 ...
gi 345112616 402 ERV 404
Cdd:PRK08242 400 ERV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
4-404 0e+00

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 530.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSV 83
Cdd:COG0183    3 EVVIVDAVRTPFGRFG--GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGP-----------MMLDPAVSMQIGFVPQGIG 152
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARwgyrmnaklvdPMINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 153 ADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPV--RDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGa 229
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDdEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDG- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 230 mgfddvalqkyvtverinhVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKAL 309
Cdd:COG0183  239 -------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 310 QKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITL 389
Cdd:COG0183  300 ARAGLTLDDIDLIEINEAFAAQVLAVLRELGLD---PDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATM 376
                        410
                 ....*....|....*
gi 345112616 390 CVGGGMGIATIIERV 404
Cdd:COG0183  377 CIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
6-403 5.23e-172

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: 485.83  E-value: 5.23e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   6 YVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEqGGNIAKTAALYAGWDLSVPG 85
Cdd:cd00751    1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  86 VQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPM-----------MLDPAVSMQIGFVPQGIGAD 154
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRggrlglntldgMLDDGLTDPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 155 LIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDQN--GLVVLAEDEHIRPDTTLEALAALPPAFEMmgamg 231
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGrkGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 232 fddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQK 311
Cdd:cd00751  233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 312 AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCV 391
Cdd:cd00751  298 AGLTLDDIDLIEINEAFAAQALACLKELGLD---PEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCI 374
                        410
                 ....*....|..
gi 345112616 392 GGGMGIATIIER 403
Cdd:cd00751  375 GGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
7-402 5.09e-152

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: 435.12  E-value: 5.09e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616    7 VFDAIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGgNIAKTAALYAGWDLSVPGV 86
Cdd:TIGR01930   1 IVAAARTPIG--KFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   87 QINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMG-SDGGPMMLDPAVS-----------MQIGFVPQGIGAD 154
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPGNAeledarlkdltDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  155 LIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDQ--NGLVVLAEDEHIRPDTTLEALAALPPAFemmgamg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKgrKGPVTVSSDEGIRPNTTLEKLAKLKPAF------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  232 fddvalqkyvtveRINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQK 311
Cdd:TIGR01930 231 -------------DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  312 AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLedeGPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCV 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGL---DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCI 374
                         410
                  ....*....|.
gi 345112616  392 GGGMGIATIIE 402
Cdd:TIGR01930 375 GGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
6-271 1.56e-54

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: 181.35  E-value: 1.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616    6 YVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPiGEQGGNIAKTAALYAGWDLSVPG 85
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQ-AGEGQNPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   86 VQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGP-------------MMLDPAVSMQIGFVPQGIG 152
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDArsglkhgdekkhdLLIPDGLTDAFNGYHMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  153 ADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVR--DQNGLVVLAEDEHIRPDTTLEALAALPPAFemmga 229
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTvkGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF----- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 345112616  230 mgfddvalQKYVTVerinhvhTAGNSSGIVDGAALVLIGSKE 271
Cdd:pfam00108 234 --------DKEGTV-------TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
4-404 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 761.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK08242   3 EAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPMMLDPAVSMQIGFVPQGIGADLIATIEGFT 163
Cdd:PRK08242  83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYGFS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 164 REDVDRYALCSQQRAAHARANGYF-KSIVPVRDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGAM-GFDDVALQKYV 241
Cdd:PRK08242 163 REDVDAYAVESQQRAAAAWAEGYFaKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQKYP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 242 TVERINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:PRK08242 243 EVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATII 401
Cdd:PRK08242 323 FELNEAFASVVLRFMQALDIPH---DKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATII 399

                 ...
gi 345112616 402 ERV 404
Cdd:PRK08242 400 ERV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
4-404 0e+00

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 530.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSV 83
Cdd:COG0183    3 EVVIVDAVRTPFGRFG--GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGP-----------MMLDPAVSMQIGFVPQGIG 152
Cdd:COG0183   80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARwgyrmnaklvdPMINPGLTDPYTGLSMGET 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 153 ADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPV--RDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGa 229
Cdd:COG0183  160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDdEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDG- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 230 mgfddvalqkyvtverinhVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKAL 309
Cdd:COG0183  239 -------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 310 QKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITL 389
Cdd:COG0183  300 ARAGLTLDDIDLIEINEAFAAQVLAVLRELGLD---PDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATM 376
                        410
                 ....*....|....*
gi 345112616 390 CVGGGMGIATIIERV 404
Cdd:COG0183  377 CIGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
6-403 5.23e-172

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: 485.83  E-value: 5.23e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   6 YVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEqGGNIAKTAALYAGWDLSVPG 85
Cdd:cd00751    1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  86 VQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPM-----------MLDPAVSMQIGFVPQGIGAD 154
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRggrlglntldgMLDDGLTDPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 155 LIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDQN--GLVVLAEDEHIRPDTTLEALAALPPAFEMmgamg 231
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGrkGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 232 fddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQK 311
Cdd:cd00751  233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 312 AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCV 391
Cdd:cd00751  298 AGLTLDDIDLIEINEAFAAQALACLKELGLD---PEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCI 374
                        410
                 ....*....|..
gi 345112616 392 GGGMGIATIIER 403
Cdd:cd00751  375 GGGQGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
7-402 5.09e-152

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: 435.12  E-value: 5.09e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616    7 VFDAIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGgNIAKTAALYAGWDLSVPGV 86
Cdd:TIGR01930   1 IVAAARTPIG--KFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   87 QINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMG-SDGGPMMLDPAVS-----------MQIGFVPQGIGAD 154
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPGNAeledarlkdltDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  155 LIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDQ--NGLVVLAEDEHIRPDTTLEALAALPPAFemmgamg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKgrKGPVTVSSDEGIRPNTTLEKLAKLKPAF------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  232 fddvalqkyvtveRINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQK 311
Cdd:TIGR01930 231 -------------DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  312 AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLedeGPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCV 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGL---DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCI 374
                         410
                  ....*....|.
gi 345112616  392 GGGMGIATIIE 402
Cdd:TIGR01930 375 GGGQGAAVILE 385
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
4-404 1.12e-151

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 435.36  E-value: 1.12e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKT-TGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLS 82
Cdd:PRK06025   3 EAYIIDAVRTPRGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMS------RVPMGSDGGPMMLDPAVSMQIGFVPQ---GIGA 153
Cdd:PRK06025  83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaamaAEDMAAGKPPLGMGSGNLRLRALHPQshqGVCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 154 DLIATIEGFTREDVDRYALCSQQRAAHARANGYF-KSIVPVRDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGAMGF 232
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFdKSLVPVYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAIADYPL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 233 DD-------VALQKYVTVErINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPAS 305
Cdd:PRK06025 243 DDkgttyrgLINQKYPDLE-IKHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 306 KKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTA 385
Cdd:PRK06025 322 KKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDR---DKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRG 398
                        410
                 ....*....|....*....
gi 345112616 386 LITLCVGGGMGIATIIERV 404
Cdd:PRK06025 399 LVTMCAAGGMAPAIIIERV 417
PRK05790 PRK05790
putative acyltransferase; Provisional
4-404 3.68e-134

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 389.90  E-value: 3.68e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRgkTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSV 83
Cdd:PRK05790   3 DVVIVSAARTPIGK--FGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP---MGSDGGPMMLDPAV--SM-------QIGFVPQGI 151
Cdd:PRK05790  80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvlPGSRWGQKMGDVELvdTMihdgltdAFNGYHMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 152 GADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVR--DQNG-LVVLAEDEHIRPDTTLEALAALPPAFEMM 227
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTikQRKGdPVVVDTDEHPRPDTTAESLAKLRPAFDKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 228 GamgfddvalqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKK 307
Cdd:PRK05790 240 G-------------TV-------TAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRK 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 308 ALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALI 387
Cdd:PRK05790 300 ALEKAGWSLADLDLIEINEAFAAQALAVEKELGLD---PEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLA 376
                        410
                 ....*....|....*..
gi 345112616 388 TLCVGGGMGIATIIERV 404
Cdd:PRK05790 377 TLCIGGGQGVALIVERP 393
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
4-404 6.11e-124

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 364.27  E-value: 6.11e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRgkTTGSLYEVKPIDLLTTLFAELKRRH-ELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLS 82
Cdd:PRK09050   3 EAFICDAIRTPIGR--YGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP--MGSDGGPM--------------MLDPAVSMQIGF 146
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGKADSAFsrqaeifdttigwrFVNPLMKAQYGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 147 VPQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYF-KSIVPV---RDQNGLVVLAEDEHIRPDTTLEALAALPP 222
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLaEEIVPVtipQKKGDPVVVDRDEHPRPETTLEALAKLKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 223 AFEMMGamgfddvalqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPA 302
Cdd:PRK09050 241 VFRPDG-------------TV-------TAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 303 PASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDEGPeRVNVNGGAIAMGHPLGATGAMLLGTALDELERRDL 382
Cdd:PRK09050 301 PATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADDDA-RVNPNGGAIALGHPLGMSGARLVLTALHQLERTGG 379
                        410       420
                 ....*....|....*....|..
gi 345112616 383 STALITLCVGGGMGIATIIERV 404
Cdd:PRK09050 380 RYALCTMCIGVGQGIALAIERV 401
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-404 1.29e-122

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 360.18  E-value: 1.29e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   1 MAcEAYVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWD 80
Cdd:PRK07801   1 MA-EAYIVDAVRTPVGKRK--GGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  81 LSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSD---GGPMMLDPAVSMQIGF--------VPQ 149
Cdd:PRK07801  78 EEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtaGEQLGFTSPFAESKGWlhrygdqeVSQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 150 GIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDqnglvvLAEDEHIRpDTTLEALAALPPAFEMmG 228
Cdd:PRK07801 158 FRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPVGG------VTVDEGPR-ETSLEKMAGLKPLVEG-G 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 229 AMgfddvalqkyvtverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKA 308
Cdd:PRK07801 230 RL--------------------TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYA 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 309 LQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALIT 388
Cdd:PRK07801 290 LEKTGLSIDDIDVVEINEAFAPVVLAWLKETGAD---PAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQT 366
                        410
                 ....*....|....*.
gi 345112616 389 LCVGGGMGIATIIERV 404
Cdd:PRK07801 367 MCEGGGTANVTIIERL 382
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
4-404 2.22e-121

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 357.11  E-value: 2.22e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK07850   3 NPVIVEAVRTPIG--KRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGPMMLDP-AVSMQIGFVPQGIGADLIATIEGF 162
Cdd:PRK07850  81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPrPDSWDIDMPNQFEAAERIAKRRGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 163 TREDVDRYALCSQQRAAHARANGYFKS-----IVPVRDQNG-----LVVLAEDEHIRpDTTLEALAALPPAFEmmgamgf 232
Cdd:PRK07850 161 TREDVDAFGLRSQRRAAQAWAEGRFDReispvQAPVLDEEGqptgeTRLVTRDQGLR-DTTMEGLAGLKPVLE------- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 233 ddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKA 312
Cdd:PRK07850 233 --------------GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 313 GMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVG 392
Cdd:PRK07850 299 GMKIGDIDLVEINEAFASVVLSWAQVHEPD---MDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAG 375
                        410
                 ....*....|..
gi 345112616 393 GGMGIATIIERV 404
Cdd:PRK07850 376 GALSTGTIIERI 387
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
4-404 2.03e-117

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 346.95  E-value: 2.03e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTtGSLYEVKPIDLLTTLFAEL-KRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLS 82
Cdd:PRK08947   3 DVVIVDAIRTPMGRSKG-GAFRNVRAEDLSAHLMRSLlARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPM--GSDggpmmLDPAVSMQIGFVP--QGIGADLIAT 158
Cdd:PRK08947  82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMnhGVD-----FHPGLSKNVAKAAgmMGLTAEMLGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 159 IEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVR--DQNG-LVVLAEDEHIRPDTTLEALAALPPAFEMMGAmgfdd 234
Cdd:PRK08947 157 MHGISREQQDAFAARSHQRAWAATQEGRFKNeIIPTEghDADGvLKLFDYDEVIRPETTVEALAALRPAFDPVNG----- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 235 valqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGM 314
Cdd:PRK08947 232 -------TV-------TAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 315 TLDDIDLIEVNEAFAAVVLKFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGG 394
Cdd:PRK08947 298 SISDIDVFELNEAFAAQSLPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLG 377
                        410
                 ....*....|
gi 345112616 395 MGIATIIERV 404
Cdd:PRK08947 378 QGIATVFERV 387
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
4-404 5.78e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 333.23  E-value: 5.78e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTP--RGRGK--TTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQ---GGniaKTAALY 76
Cdd:PRK06445   3 DVYLVDFARTAfsRFRPKdpQKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwlyGG---RHPIFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  77 AGWDLSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSdgGP-------MMLDPAVS---MQIGF 146
Cdd:PRK06445  80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGD--NPhiepnpkLLTDPKYIeydLTTGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 147 VpQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPVRDQ-NGLV-VLAEDEHIRPDTTLEALAALPPA 223
Cdd:PRK06445 158 V-MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKdEILPIEVEvEGKKkVVDVDQSVRPDTSLEKLAKLPPA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 224 FEMMGamgfddvalqkyvtverinhVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAP 303
Cdd:PRK06445 237 FKPDG--------------------VITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 304 ASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLS 383
Cdd:PRK06445 297 ASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD---PETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKD 373
                        410       420
                 ....*....|....*....|.
gi 345112616 384 TALITLCVGGGMGIATIIERV 404
Cdd:PRK06445 374 YGVATLCVGGGQGGAVVLERV 394
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
11-404 3.01e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 329.26  E-value: 3.01e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  11 IRTPRGRgkTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGnIAKTAALYAGWDLSVPGVQINR 90
Cdd:PRK06205  10 VRTPVGR--FGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPVTVPGMQLDR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  91 FCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPM-------GSDGGPMMLDPAVS---MQIGFVPQGIGADLIATIE 160
Cdd:PRK06205  87 RCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwGVRGGGVQLHDRLArgrETAGGRRFPVPGGMIETAE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 161 ------GFTREDVDRYALCSQQRAAHARANGYFKS-IVPV--RDQNG-LVVLAEDEHIRPDTTLEALAALPPAfemmgaM 230
Cdd:PRK06205 167 nlrreyGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVtvPQRKGdPTVVDRDEHPRADTTLESLAKLRPI------M 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 231 GFDDvalqKYVTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQ 310
Cdd:PRK06205 241 GKQD----PEATV-------TAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALA 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 311 KAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLC 390
Cdd:PRK06205 310 RAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMC 389
                        410
                 ....*....|....
gi 345112616 391 VGGGMGIATIIERV 404
Cdd:PRK06205 390 IGGGQGLAAVFERV 403
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
4-404 4.35e-110

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 328.66  E-value: 4.35e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRgkTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK08131   3 DAYIYDGLRSPFGR--HAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP--MG--------------SDGGPMMLDPAVSMQIGFV 147
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGkaesafsrdakvfdTTIGARFPNPKIVAQYGND 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 148 PQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPVRDQNG----LVVLAEDEHIRPDTTLEALAALPP 222
Cdd:PRK08131 161 SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFAdEITPIEVPQGrklpPKLVAEDEHPRPSSTVEALTKLKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 223 AFEmmgamgfddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPA 302
Cdd:PRK08131 241 LFE---------------------GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPV 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 303 PASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDEGPeRVNVNGGAIAMGHPLGATGAMLLGTALDELERRDL 382
Cdd:PRK08131 300 EAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDDP-RVNPNGGAIAVGHPLGASGARLALTAARELQRRGK 378
                        410       420
                 ....*....|....*....|..
gi 345112616 383 STALITLCVGGGMGIATIIERV 404
Cdd:PRK08131 379 RYAVVSLCIGVGQGLAMVIERV 400
PRK09051 PRK09051
beta-ketothiolase BktB;
1-404 2.34e-107

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 321.52  E-value: 2.34e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   1 MACEAYVFDAIRTprGRGKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWD 80
Cdd:PRK09051   1 MMREVVVVSGVRT--AIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  81 LSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP-----------MGSDGGPMMLDPAVSMQIGFVPQ 149
Cdd:PRK09051  79 QETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPyllpaarwgarMGDAKLVDMMVGALHDPFGTIHM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 150 GIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPV--RDQNGLVVLAEDEHIRPDTTLEALAALPPAFEM 226
Cdd:PRK09051 159 GVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVeiKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 227 MGAmgfddvalqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASK 306
Cdd:PRK09051 239 ENG------------TV-------TAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQ 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 307 KALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTAL 386
Cdd:PRK09051 300 KALERAGLTVADLDVIEANEAFAAQACAVTRELGLD---PAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYAL 376
                        410
                 ....*....|....*...
gi 345112616 387 ITLCVGGGMGIATIIERV 404
Cdd:PRK09051 377 VTMCIGGGQGIAAIFERL 394
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
4-404 1.61e-106

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 319.64  E-value: 1.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTtGSLYEVKPIDLL-TTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLS 82
Cdd:PRK09052   7 DAYIVAATRTPVGKAPR-GMFKNTRPDDLLaHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGsdGGPMMLDPA-------VSMQIGFvpqGIGADL 155
Cdd:PRK09052  86 VGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM--GNKPSMSPAifardenVGIAYGM---GLTAEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 156 IATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVP--VRD-----QNGLVVLAE-----DEHIRPDTTLEALAALPP 222
Cdd:PRK09052 161 VAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPyeITErfpdlATGEVDVKTrtvdlDEGPRADTSLEGLAKLKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 223 AFEMMGAMgfddvalqkyvtverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPA 302
Cdd:PRK09052 241 VFANKGSV--------------------TAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPI 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 303 PASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDL 382
Cdd:PRK09052 301 EAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLD---PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNL 377
                        410       420
                 ....*....|....*....|..
gi 345112616 383 STALITLCVGGGMGIATIIERV 404
Cdd:PRK09052 378 KYGMVTMCVGTGMGAAGIFERL 399
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
4-403 8.39e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 318.10  E-value: 8.39e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGR-GKttGSLYEVKPIDLLTTLF-AELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDl 81
Cdd:PRK07851   3 EAVIVSTARSPIGRaFK--GSLKDMRPDDLAAQMVrAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  82 SVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMG-SDGGPMMLDPAVS------------------- 141
Cdd:PRK07851  80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnSDSLPDTKNPLFAeaqartaaraeggaeawhd 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 142 -MQIGFVPQ-----GIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYF-KSIVPVRDQNGLVVlAEDEHIRPDTTL 214
Cdd:PRK07851 160 pREDGLLPDvyiamGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFeREITPVTLPDGTVV-STDDGPRAGTTY 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 215 EALAALPPAFEMMGamgfddvalqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEP 294
Cdd:PRK07851 239 EKVSQLKPVFRPDG-------------TV-------TAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSP 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 295 TIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTAL 374
Cdd:PRK07851 299 EIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGID---EDKLNVSGGAIALGHPFGMTGARITTTLL 375
                        410       420
                 ....*....|....*....|....*....
gi 345112616 375 DELERRDLSTALITLCVGGGMGIATIIER 403
Cdd:PRK07851 376 NNLQTHDKTFGLETMCVGGGQGMAMVLER 404
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-404 9.55e-105

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 314.74  E-value: 9.55e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   1 MAcEAYVFDAIRTPRGRgkTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWD 80
Cdd:PRK06504   1 MA-EAYIVAAARTAGGR--KGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  81 LSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGS-------DGGPMMLDPAVSMQ---IGFvPQG 150
Cdd:PRK06504  78 ESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlpakNGLGHYKSPGMEERypgIQF-SQF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 151 IGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVP--VRDQNGLVVLAE-DEHIRPDTTLEALAALPPAFEm 226
Cdd:PRK06504 157 TGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPleITRADGSGEMHTvDEGIRFDATLEGIAGVKLIAE- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 227 mgamgfddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASK 306
Cdd:PRK06504 236 --------------------GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATE 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 307 KALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTAL 386
Cdd:PRK06504 296 RALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGAD---PERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGL 372
                        410
                 ....*....|....*...
gi 345112616 387 ITLCVGGGMGIATIIERV 404
Cdd:PRK06504 373 QTMCEGGGMANVTIVERL 390
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
4-404 4.27e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 305.52  E-value: 4.27e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGRGKTtGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK07661   3 EAVIVAGARTPVGKAKK-GSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYTV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGsdGGPMMLDPAVSMQIGFVPQGIG--ADLIATIEG 161
Cdd:PRK07661  82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--GHVVRPNPRLVEAAPEYYMGMGhtAEQVAVKYG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 162 FTREDVDRYALCSQQRAAHARANGYFK-SIVPVR-------DQNGL----VVLAEDEHIRPDTTLEALAALPPAFEMMGA 229
Cdd:PRK07661 160 ISREDQDAFAVRSHQRAAKALAEGKFAdEIVPVDvtlrtvgENNKLqeetITFSQDEGVRADTTLEILGKLRPAFNVKGS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 230 MgfddvalqkyvtverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKAL 309
Cdd:PRK07661 240 V--------------------TAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKAL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 310 QKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITL 389
Cdd:PRK07661 300 KLAGLELSDIGLFELNEAFASQSIQVIRELGLD---EEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTM 376
                        410
                 ....*....|....*
gi 345112616 390 CVGGGMGIATIIERV 404
Cdd:PRK07661 377 CIGGGMGAAGVFELL 391
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
10-403 2.99e-91

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 282.42  E-value: 2.99e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  10 AIRTPRGRGKTtGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSVPGVQIN 89
Cdd:PLN02287  53 AYRTPICKAKR-GGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVRTVN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  90 RFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGpmmLDPAVSM----QIGFVPQGIGADLIATIEGFTRE 165
Cdd:PLN02287 132 RQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGG---VNPRVESfsqaQDCLLPMGITSENVAERFGVTRE 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 166 DVDRYALCSQQRAAHARANGYFKS-IVPVRDQ--------NGLVVLAEDEHIRPDTTLEALAALPPAFEMMGamgfddva 236
Cdd:PLN02287 209 EQDQAAVESHRKAAAATASGKFKDeIVPVHTKivdpktgeEKPIVISVDDGIRPNTTLADLAKLKPVFKKNG-------- 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 237 lqkyvtverinhVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTL 316
Cdd:PLN02287 281 ------------TTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLEL 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 317 DDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERR--DLSTALITLCVGGG 394
Cdd:PLN02287 349 DDIDLFEINEAFASQFVYCCKKLGLD---PEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTG 425

                 ....*....
gi 345112616 395 MGIATIIER 403
Cdd:PLN02287 426 MGAAAVFER 434
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
10-402 8.69e-86

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 266.19  E-value: 8.69e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  10 AIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSVPGVQIN 89
Cdd:PRK08235   9 AARTPFG--KFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPWEVQTETVN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  90 RFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP-----------MGsDGG--PMMLDPAVSMQIGFVPQGIGADLI 156
Cdd:PRK08235  86 KVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyilpgarwgyrMG-DNEviDLMVADGLTCAFSGVHMGVYGGEV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 157 ATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDQN---GLVVLAEDEHIRPDTTLEALAALPPAFEMMGAMgf 232
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQrkgDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTI-- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 233 ddvalqkyvtverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKA 312
Cdd:PRK08235 243 ------------------TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKT 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 313 GMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVG 392
Cdd:PRK08235 305 GKTVEDIDLFEINEAFAAVALASTEIAGID---PEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSG 381
                        410
                 ....*....|
gi 345112616 393 GGMGIATIIE 402
Cdd:PRK08235 382 GGQGDAVLIE 391
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
6-404 1.55e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 266.88  E-value: 1.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   6 YVFDAIRTP--RGRGKTTgslyEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEQGgNIAKTAALYAGWDLSV 83
Cdd:PRK08170   6 YIVDGARTPflKARGGPG----PFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEA-NIARVVALRLGCGEKV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP--------------MGSDGG-----------PMMLDP 138
Cdd:PRK08170  81 PAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvrwlagwYAAKSIgqklaalgklrPSYLAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 139 AVSMQIGF----VPQGIG--ADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKSIVPVRDQNGlVVLAEDEHIRPDT 212
Cdd:PRK08170 161 VIGLLRGLtdpvVGLNMGqtAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPLFDRDG-KFYDHDDGVRPDS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 213 TLEALAALPPAFEmmgamgfddvalQKYVTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGT 292
Cdd:PRK08170 240 SMEKLAKLKPFFD------------RPYGRV-------TAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAAL 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 293 EPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVL---------KFMRDM-GLEDE----GPERVNVNGGAIAM 358
Cdd:PRK08170 301 DPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLaclaawadeEYCREQlGLDGAlgelDRERLNVDGGAIAL 380
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 345112616 359 GHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATIIERV 404
Cdd:PRK08170 381 GHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-404 1.57e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 258.04  E-value: 1.57e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   1 MACEAYVFDAIRTprGRGKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTpIGEQGGNIAKTAALYAGWD 80
Cdd:PRK06633   1 MTKPVYITHAKRT--AFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  81 LSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMS------RVPMGSDGGP------MMLDPAVSMQIGfVP 148
Cdd:PRK06633  78 KEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhgsYIRAGAKFGDikmvdlMQYDGLTDVFSG-VF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 149 QGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPVR--DQNGLVVLAEDEHIRPDTTLEALAALPPAFE 225
Cdd:PRK06633 157 MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKdEILPIEvtIKKTTSLFDHDETVRPDTSLEILSKLRPAFD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 226 MmgamgfddvalqkyvtveriNHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPAS 305
Cdd:PRK06633 237 K--------------------NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPAS 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 306 KKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTA 385
Cdd:PRK06633 297 QKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWD---MEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKG 373
                        410
                 ....*....|....*....
gi 345112616 386 LITLCVGGGMGIATIIERV 404
Cdd:PRK06633 374 LVTLCIGGGMGMAMCVEAV 392
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
43-402 1.37e-79

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 250.46  E-value: 1.37e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  43 RHELDTSQVDDVILGCVTPIGEQGGNIAKTAALYAGWDLSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESM 122
Cdd:PRK07108  41 RAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 123 SRVP------MGSDGGPMMLDPAVSMqigfvPQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRD 195
Cdd:PRK07108 121 SCVQnemnrhMLREGWLVEHKPEIYW-----SMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPITV 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 196 QNGL------------VVLAEDEHIRPDTTLEALAALPPAFEmmgamgfddvalqkyvtveriNHVHTAGNSSGIVDGAA 263
Cdd:PRK07108 196 TAGVadkatgrlftkeVTVSADEGIRPDTTLEGVSKIRSALP---------------------GGVITAGNASQFSDGAS 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 264 LVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEd 343
Cdd:PRK07108 255 ACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIP- 333
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 345112616 344 egPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATIIE 402
Cdd:PRK07108 334 --MDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
18-403 1.53e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 250.19  E-value: 1.53e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  18 GKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSVPGVQINRFCASGLD 97
Cdd:PRK05656  15 GSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  98 AVNLAAMKVRSGWEDLVVAGGVESMSRVPM---GSDGGPMM-----LDPAVS--MQIGF--VPQGIGADLIATIEGFTRE 165
Cdd:PRK05656  94 ALHLAAQAIRCGDAEVIIAGGQENMSLAPYvlpGARTGLRMghaqlVDSMITdgLWDAFndYHMGITAENLVEKYGISRE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 166 DVDRYALCSQQRAAHARANGYFKS-IVPV---RDQNGLVVLAEDEHIRPDTTLEALAALPPAFEMMGAMgfddvalqkyv 241
Cdd:PRK05656 174 AQDAFAAASQQKAVAAIEAGRFDDeITPIlipQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDGSV----------- 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 242 tverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:PRK05656 243 ---------TAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATII 401
Cdd:PRK05656 314 IEANEAFAAQSLAVGKELGWD---AAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAI 390

                 ..
gi 345112616 402 ER 403
Cdd:PRK05656 391 ER 392
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
4-404 2.28e-76

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 240.82  E-value: 2.28e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHEldtSQVDDVILGCVTpigEQGGNIAKTAALYAGWDLSV 83
Cdd:PRK06690   2 RAVIVEAKRTPIG--KKNGMLKDYEVQQLAAPLLTFLSKGME---REIDDVILGNVV---GPGGNVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  84 PGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGgpmMLDPAVsmqIGFVPQGIGADLIATIEGFT 163
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRA---RFSPET---IGDPDMGVAAEYVAERYNIT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 164 REDVDRYALCSQQRAAHARANGYFK-SIVPVrdqNGLvvlaEDEHIRPDTTLEAL-AALPPAFEMMGAMgfddvalqkyv 241
Cdd:PRK06690 148 REMQDEYACLSYKRTLQALEKGYIHeEILSF---NGL----LDESIKKEMNYERIiKRTKPAFLHNGTV----------- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 242 tverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:PRK06690 210 ---------TAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDY 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATII 401
Cdd:PRK06690 281 FEINEAFASKVVACAKELQIPY---EKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLF 357

                 ...
gi 345112616 402 ERV 404
Cdd:PRK06690 358 EKV 360
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
10-404 1.34e-66

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 216.88  E-value: 1.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  10 AIRTPRGrgKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSVPGVQIN 89
Cdd:PLN02644   8 VARTPIG--GFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSAN-LGQAPARQAALGAGLPPSTICTTVN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  90 RFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPM---GSDGGPMMLDPAVS---MQIGF------VPQGIGADLIA 157
Cdd:PLN02644  85 KVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKylpEARKGSRLGHDTVVdgmLKDGLwdvyndFGMGVCAELCA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 158 TIEGFTREDVDRYALCSQQRAAHARANGYFK-SIVPVRDQNG----LVVLAEDEHI-RPDttLEALAALPPAFEMMGAmg 231
Cdd:PLN02644 165 DQYSISREEQDAYAIQSYERAIAAQEAGAFAwEIVPVEVPGGrgrpSVIVDKDEGLgKFD--PAKLRKLRPSFKEDGG-- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 232 fddvalqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQK 311
Cdd:PLN02644 241 ----------SV-------TAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKH 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 312 AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCV 391
Cdd:PLN02644 304 AGLEASQVDYYEINEAFSVVALANQKLLGLD---PEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICN 380
                        410
                 ....*....|...
gi 345112616 392 GGGMGIATIIERV 404
Cdd:PLN02644 381 GGGGASAIVVELM 393
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
7-403 4.00e-66

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 216.39  E-value: 4.00e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   7 VFDAIRTPRGRGKTtgSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEqGGNIAKTAALYAGWDLSVPGV 86
Cdd:PRK08963   9 IVSGLRTPFAKQAT--AFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGMNVHTDAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  87 QINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMG-------------------------SDGGP---MMLDP 138
Cdd:PRK08963  86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvskklaralvdlnkartlgqrlklfSRLRLrdlLPVPP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 139 AVSMQIGFVPQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK-----SIVPVRDQnglvVLAEDEHIRPDTT 213
Cdd:PRK08963 166 AVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDdevmtAHVPPYKQ----PLEEDNNIRGDST 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 214 LEALAALPPAFEmmgamgfddvalQKYVTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTE 293
Cdd:PRK08963 242 LEDYAKLRPAFD------------RKHGTV-------TAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAID 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 294 PTI-MLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVL--------------KFMRDMGLEDEGPERVNVNGGAIAM 358
Cdd:PRK08963 303 VWQdMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLanlqmfaserfareKLGRSQAIGEVDMSKFNVLGGSIAY 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 345112616 359 GHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATIIER 403
Cdd:PRK08963 383 GHPFAATGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
4-404 2.25e-63

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 208.33  E-value: 2.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   4 EAYVFDAIRTPRGR-GKttgSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLS 82
Cdd:PRK06366   3 DVYIVSAKRTAIGKfGR---SFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAG-VGQNPAGQAAYHAGLPFG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVP--MGSD--GGP------------MMLDPAVSMQIGF 146
Cdd:PRK06366  79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPflLPSDlrWGPkhllhknykiddAMLVDGLIDAFYF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 147 VPQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYF-KSIVPVRDqnglvvLAEDEHIRpDTTLEALAALPPAFE 225
Cdd:PRK06366 159 EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFrNEIVPFND------LDRDEGIR-KTTMEDLAKLPPAFD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 226 MMGAMgfddvalqkyvtverinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPAS 305
Cdd:PRK06366 232 KNGIL--------------------TAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPAT 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 306 KKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDegpERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTA 385
Cdd:PRK06366 292 RKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDN---ERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTG 368
                        410
                 ....*....|....*....
gi 345112616 386 LITLCVGGGMGIATIIERV 404
Cdd:PRK06366 369 LATLCHGGGGAHTLTLEMV 387
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
6-271 1.56e-54

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: 181.35  E-value: 1.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616    6 YVFDAIRTPRGRGKttGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPiGEQGGNIAKTAALYAGWDLSVPG 85
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQ-AGEGQNPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616   86 VQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDGGP-------------MMLDPAVSMQIGFVPQGIG 152
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDArsglkhgdekkhdLLIPDGLTDAFNGYHMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  153 ADLIATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVR--DQNGLVVLAEDEHIRPDTTLEALAALPPAFemmga 229
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTvkGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF----- 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 345112616  230 mgfddvalQKYVTVerinhvhTAGNSSGIVDGAALVLIGSKE 271
Cdd:pfam00108 234 --------DKEGTV-------TAGNASPINDGAAAVLLMSES 260
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
43-402 4.33e-54

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 184.33  E-value: 4.33e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  43 RHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGWDLSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESM 122
Cdd:PRK06954  45 RAGLKPEQIDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESM 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 123 SRVPM---GSDGG----------PMMLDPAVSMQIGFVPQGIGADLIATIEGFTREDVDRYALCSQQRAAHARANGYFK- 188
Cdd:PRK06954 124 TNAPYllpKARGGmrmghgqvldHMFLDGLEDAYDKGRLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAw 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 189 SIVPVR--DQNGLVVLAEDEHIRpDTTLEALAALPPAFEMMGAMgfddvalqkyvtverinhvhTAGNSSGIVDGAALVL 266
Cdd:PRK06954 204 EIAPVTvaGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTV--------------------TAANSSSISDGAAALV 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 267 IGSKEKGEALGLKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDegp 346
Cdd:PRK06954 263 MMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPH--- 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 345112616 347 ERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATIIE 402
Cdd:PRK06954 340 EKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
18-402 3.64e-51

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: 176.53  E-value: 3.64e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  18 GKTTGSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGCVTPIGEqGGNIAKTAALYAGWDLSVPGVQINRFCASGLD 97
Cdd:cd00826   12 GGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  98 AVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSdggpmmldpAVSMQIGFVPQGIGadliatiegfTREDVDRYALCSQQR 177
Cdd:cd00826   91 ALALAMQLIAGGDANCILAGGFEKMETSAENN---------AKEKHIDVLINKYG----------MRACPDAFALAGQAG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 178 AAHARANGYFKS-IVP--VRDQNGLVVLAEDEHIR--PDTTLEALAALPPAFEMMGAMgfddvalqkyvtverinhvhTA 252
Cdd:cd00826  152 AEAAEKDGRFKDeFAKfgVKGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFL--------------------TA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 253 GNSSGIVDGAALVLIGSKE-------KGEALGLKPRARIISAALVGTEPT----IMLTGPAPASKKALQKAGMTLDDIDL 321
Cdd:cd00826  212 GNACGLNDGAAAAILMSEAeaqkhglQSKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 322 IEVNEAFAAVVLKFMRDMGLEDEGPER---------------VNVNGGAIAMGHPLGATGAMLLGTALDELERRDLSTA- 385
Cdd:cd00826  292 IEAHDAFAANACATNEALGLCPEGQGGalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQg 371
                        410       420
                 ....*....|....*....|.
gi 345112616 386 ----LITLCVGGGMGIATIIE 402
Cdd:cd00826  372 agagLALLCIGGGGGAAMCIE 392
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
278-403 7.06e-51

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: 167.05  E-value: 7.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  278 LKPRARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEdegPERVNVNGGAIA 357
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGID---PEKVNVNGGAIA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 345112616  358 MGHPLGATGAMLLGTALDELERRDLSTALITLCVGGGMGIATIIER 403
Cdd:pfam02803  78 LGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
31-403 7.48e-48

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 168.54  E-value: 7.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  31 DLLTTLFAELKRRHELDTSQVDDVILGCVTPiGEQGGNIAKTAALYAGWDLSVPGVQINRFCASGLDAVNLAAMKVRSGW 110
Cdd:PRK09268  33 DMLTAALDGLVDRFGLQGERLGEVVAGAVLK-HSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQ 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 111 EDLVVAGGVESMSRVPMG-SDG------------------------GPMMLDPAV----------SMqigfvpqGIGADL 155
Cdd:PRK09268 112 IDSGIAGGVDTTSDAPIAvNEGlrkillelnrakttgdrlkalgklRPKHLAPEIprngeprtglSM-------GEHAAI 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 156 IATIEGFTREDVDRYALCSQQRAAHARANGYFKS-IVPVRDqnglvvLAEDEHIRPDTTLEALAALPPAFemmgamGFDD 234
Cdd:PRK09268 185 TAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFLG------LTRDNNLRPDSSLEKLAKLKPVF------GKGG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 235 VAlqkyvTVerinhvhTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISA--ALV----GTEPtiMLTGPAPASKKA 308
Cdd:PRK09268 253 RA-----TM-------TAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetAAVdfvhGKEG--LLMAPAYAVPRL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 309 LQKAGMTLDDIDLIEVNEAFAAVVL---------KFMRD-MGLEdeGP------ERVNVNGGAIAMGHPLGATGAMLLGT 372
Cdd:PRK09268 319 LARNGLTLQDFDFYEIHEAFASQVLatlkawedeEYCRErLGLD--APlgsidrSKLNVNGSSLAAGHPFAATGGRIVAT 396
                        410       420       430
                 ....*....|....*....|....*....|.
gi 345112616 373 ALDELERRDLSTALITLCVGGGMGIATIIER 403
Cdd:PRK09268 397 LAKLLAEKGSGRGLISICAAGGQGVTAILER 427
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
252-401 8.42e-23

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: 96.36  E-value: 8.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 252 AGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPT----IMLTGPAPASKKALQKAGMTLDDIDLIEVNEA 327
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 328 FAAVVLKFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGAMLLGTALDELERRDLS-------TALITLCVGGGMGIATI 400
Cdd:cd00327  174 GTPIGDAVELALGLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptpreprTVLLLGFGLGGTNAAVV 253

                 .
gi 345112616 401 I 401
Cdd:cd00327  254 L 254
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
46-377 1.43e-20

Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 92.33  E-value: 1.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  46 LDTSQVDDVILGCVTPiGEQGGNIAKTAALYAGwDLSVPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRV 125
Cdd:cd00829   33 LEPADIDAVVVGNAAG-GRFQSFPGALIAEYLG-LLGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 126 PMGSDGGPMMLDPAVSMQI---GFVPQGIGAdLIAT--IE--GFTREDVDRYALcsQQRAaHARANGYfksivpvrdqng 198
Cdd:cd00829  111 PTGDEAGGRASDLEWEGPEppgGLTPPALYA-LAARryMHryGTTREDLAKVAV--KNHR-NAARNPY------------ 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 199 lvvlAedeHIRPDTTLEALAALPPAFEMMGAMgfddvalqkyvtverinhvhtagNSSGIVDGAALVLIGSKEKGEALGL 278
Cdd:cd00829  175 ----A---QFRKPITVEDVLNSRMIADPLRLL-----------------------DCCPVSDGAAAVVLASEERARELTD 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 279 KPrARIISAALVGTEPTIM-------LTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGL--EDEGPER- 348
Cdd:cd00829  225 RP-VWILGVGAASDTPSLSerddflsLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFceKGEGGKLv 303
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 345112616 349 ------------VNVNGGAIAMGHPLGATGAMLLGTALDEL 377
Cdd:cd00829  304 regdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQL 344
PRK06064 PRK06064
thiolase domain-containing protein;
68-366 6.32e-14

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 72.62  E-value: 6.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  68 NIAKTAALYAGwdLS-VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPmGSDGGPMM---LDPAVSMQ 143
Cdd:PRK06064  62 HIAALIADYAG--LApIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP-TPDATEAIaraGDYEWEEF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 144 IGFVPQGIGAdLIATIE----GFTREDvdryaLCsqQRAAHARANGyfksivpvrdqnglvVLAEDEHIRPDTTLEALAA 219
Cdd:PRK06064 139 FGATFPGLYA-LIARRYmhkyGTTEED-----LA--LVAVKNHYNG---------------SKNPYAQFQKEITVEQVLN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 220 LPPafemmgamgfddVA--LQKYvtverinhvhtagNSSGIVDGAALVLIGSKEKGEALGLKPrARIIS-------AALV 290
Cdd:PRK06064 196 SPP------------VAdpLKLL-------------DCSPITDGAAAVILASEEKAKEYTDTP-VWIKAsgqasdtIALH 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 291 GTEPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMG---------LEDEGPER------VNVNGGA 355
Cdd:PRK06064 250 DRKDFTTLDAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGfakkgeggkLAREGQTYiggdipVNPSGGL 329
                        330
                 ....*....|.
gi 345112616 356 IAMGHPLGATG 366
Cdd:PRK06064 330 KAKGHPVGATG 340
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
22-366 1.14e-10

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 62.74  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  22 GSLYEVKPIDLLTTLFAELKRRHELDTSQVDDVILGcvTPIGEQGGNIAKTAALYAgwdLSVPGVQINR---FCASGLDA 98
Cdd:PRK06157  20 GERWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFG--THYDEIGSGKSGTPLSRA---LRLPNIPVTRvenFCATGSEA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  99 VNLAAMKVRSGWEDLVVAGGVESM-----SRVPMGSDGGPM-MLDPAVSMQIGFvpqGIGADLIATIEGFTREDVDRyAL 172
Cdd:PRK06157  95 FRGAVYAVASGAYDIALALGVEKLkdtgyGGLPVANPGTLAdMTMPNVTAPGNF---AQLASAYAAKYGVSREDLKR-AM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 173 CsqQRAAHARANGyfksivpvrdqnglvVLAEDEHIRPDTTLEALAALPPAFEMMGAMgfddvalqkyvtverinhvhta 252
Cdd:PRK06157 171 A--HVSVKSHANG---------------ARNPKAHLRKAVTEEQVLKAPMIAGPLGLF---------------------- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 253 gNSSGIVDGAALVLIGSKEKGEALGlKPRARIISAALVGTEPTIMLTGPA----------PASKKALQKAGMT--LDDID 320
Cdd:PRK06157 212 -DCCGVSDGAAAAIVTTPEIARALG-KKDPVYVKALQLAVSNGWELQYNGwdgsyfpttrIAARKAYREAGITdpREELS 289
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345112616 321 LIEVNEAFAAVVLKFMRDMGLEDEG-----------------PerVNVNGGAIAMGHPLGATG 366
Cdd:PRK06157 290 MAEVHDCFSITELVTMEDLGLSERGqawrdvldgffdadgglP--CQIDGGLKCFGHPIGASG 350
PRK12578 PRK12578
thiolase domain-containing protein;
76-366 1.73e-09

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 59.09  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  76 YAGWDLSVPgVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVpmgsdggpmmlDPAVSMQIGfvpqGIGADL 155
Cdd:PRK12578  67 YSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEV-----------DTSTSLAIG----GRGGNY 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 156 IATIEGFTREDVDRYALCSqqrAAHARANGyfksivpvrdqnglvvlaedehirpdTTLEALAALPPAFEMMGAMGfDDV 235
Cdd:PRK12578 131 QWEYHFYGTTFPTYYALYA---TRHMAVYG--------------------------TTEEQMALVSVKAHKYGAMN-PKA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 236 ALQKYVTVER------INHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIIS-------AALVGTEPTIMLTGPA 302
Cdd:PRK12578 181 HFQKPVTVEEvlksraISWPIKLLDSCPISDGSATAIFASEEKVKELKIDSPVWITGigyandyAYVARRGEWVGFKATQ 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345112616 303 PASKKALQKAGMTLDDIDLIEVNEAFAAVVL---------------KFMRDMGLEDEGPERVNVNGGAIAMGHPLGATG 366
Cdd:PRK12578 261 LAARQAYNMAKVTPNDIEVATVHDAFTIAEImgyedlgftekgkggKFIEEGQSEKGGKVGVNLFGGLKAKGHPLGATG 339
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
62-366 3.00e-09

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 58.37  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  62 IGEQGGNIAKTAALYAgwdlsvPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPmGSDGGPMMLDPAvs 141
Cdd:PTZ00455  96 VGSLGQSGASNALLYK------PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVS-ARVGGDYLARAA-- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 142 mqiGFVPQGIGADL------------IATIEGFTREDVDRYAlcsqqraAHARANGyfksivpvrDQNGLVVLaedeHIR 209
Cdd:PTZ00455 167 ---DYRRQRKLDDFtfpclfakrmkyIQEHGHFTMEDTARVA-------AKAYANG---------NKNPLAHM----HTR 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 210 PDTTLEALAALPPAFEMMGAmgfddvalqkyvtvERINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPR-ARII--- 285
Cdd:PTZ00455 224 KLSLEFCTGASDKNPKFLGN--------------ETYKPFLRMTDCSQVSDGGAGLVLASEEGLQKMGLSPNdSRLVeik 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 286 -SAALVGT------EPTIMLTGPApASKKALQKAGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDEGPER---------- 348
Cdd:PTZ00455 290 sLACASGNlyedppDATRMFTSRA-AAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKdlirngatal 368
                        330       340
                 ....*....|....*....|...
gi 345112616 349 -----VNVNGGAIAMGHPLGATG 366
Cdd:PTZ00455 369 egripVNTGGGLLSFGHPVGATG 391
PRK07516 PRK07516
thiolase domain-containing protein;
256-404 3.89e-09

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 58.03  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 256 SGIVDGAALVLIGSKEKGEALglkPRA-RIISAALVGT-------EPTIMlTGPAPASKKALQKAGMTLDDIDLIEVNEA 327
Cdd:PRK07516 213 SLVSDGAAALVLADAETARAL---QRAvRFRARAHVNDflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDC 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 328 FAAVVLKFMRDMGLE---------DEGPER------VNVNGGAIAMGHPLGATG-------AM-LLGTAlDELERRDLST 384
Cdd:PRK07516 289 FTIAELIEYEAMGLAppgqgaraiREGWTAkdgklpVNPSGGLKAKGHPIGATGvsmhvlaAMqLTGEA-GGMQIPGAKL 367
                        170       180
                 ....*....|....*....|...
gi 345112616 385 ALITLCvgGGMGIA---TIIERV 404
Cdd:PRK07516 368 AGVFNM--GGAAVAnyvSILERV 388
PRK08256 PRK08256
lipid-transfer protein; Provisional
83-366 2.47e-07

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 52.21  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  83 VPGVQINRFCASGLDAVNLAAMKVRSGWEDLVVAGGVESMSRVPMGSDG----GPMM-LDPAVSMQIGFVPQGIGADLIA 157
Cdd:PRK08256  71 IPIVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWddrpSPLErFDKALAELQGFDPAPPALRMFG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 158 tieGFTREDVDRYALCSQQRAA-------HARANGY--FKSIVPVRDqnglvVLAEDEHIRPDTTLEALaalPPAfemmg 228
Cdd:PRK08256 151 ---GAGREHMEKYGTTAETFAKigvkarrHAANNPYaqFRDEYTLED-----VLASPMIWGPLTRLQCC---PPT----- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 229 amgfddvalqkyvtverinhvhtagnssgivDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPT-------IMLTGp 301
Cdd:PRK08256 215 -------------------------------CGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPStfdgrsmIDLVG- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 302 APASKKALQK----AGMTLDDIDLIEVNEAFAAVVLKFMRDMGLEDEG-PER--------------VNVNGGAIAMGHPL 362
Cdd:PRK08256 263 YDMTRAAAQQvyeqAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGeAEKfiddgdntyggrwvVNPSGGLLSKGHPL 342

                 ....
gi 345112616 363 GATG 366
Cdd:PRK08256 343 GATG 346
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
256-370 1.07e-06

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 50.46  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 256 SGIVDGAALVLIGSKEKGEALGLK-PRARII----SAALVGTEPTIMLTGPAP--------ASKKALQKAGMTLDDIDLI 322
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYADArPIPRIKgwghRTAPLGLEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDLDGF 299
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345112616 323 EVNEAFAAVVL---------------KFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGA-MLL 370
Cdd:PRK06289 300 EVHDCFTPSEYlaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVrMLL 363
PRK06365 PRK06365
thiolase domain-containing protein;
304-380 1.77e-06

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 49.91  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 304 ASKKALQKAGMT--LDDIDLIEVNEAFAAVVLKFMRDMGL---------------EDEGPERVNVNGGAIAMGHPLGATG 366
Cdd:PRK06365 298 AAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkpELPGKLPVNPSGGLLAAGHAVGATG 377
                         90
                 ....*....|....
gi 345112616 367 AMLLGTALDELERR 380
Cdd:PRK06365 378 IMQAVFMFWQLQGR 391
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
260-392 2.38e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 46.20  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 260 DGAALVLIGSKEKGEALGLKPRARIISAALV-----GTEPTIMLTGPAPASKKALQKAGMTLDDIDLI-------EVNEA 327
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345112616 328 FAAVVLK--FmrdmgledegPERVNVNGGAIAMGHPLGATGAMllGTALDELErrdLSTALITLCVG 392
Cdd:PRK05952 290 REANLIQalF----------PHRVAVSSTKGATGHTLGASGAL--GVAFSLLA---LRHQQLPPCVG 341
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
42-171 2.92e-05

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 45.50  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616  42 RRHELDTSQVDDVILGCVTPIGeQGGNIAKTAALYAGwDLSVPGVQINRFCASGLDAVNLAAMKVRSG-WED-LVVAGGV 119
Cdd:cd00827   61 ERAGIDPDDIGLLIVATESPID-KGKSAATYLAELLG-LTNAEAFDLKQACYGGTAALQLAANLVESGpWRYaLVVASDI 138
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 345112616 120 eSMSRVPMGSDGGPMMLDPAVSMQIGFVPQGIGADLIATIEGFTREDVDRYA 171
Cdd:cd00827  139 -ASYLLDEGSALEPTLGDGAAAMLVSRNPGILAAGIVSTHSTSDPGYDFSPY 189
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
245-378 1.38e-04

decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 43.39  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 245 RINHVHTAGNSSGIVDGAALVLIGSKEKGEALGLKPRARIISAALVGTEPTIMLTGP-----APASKKALQKAGMTLDDI 319
Cdd:cd00825  146 ASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPsaeglARAAKEALAVAGLTVWDI 225
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 345112616 320 DLIEVNEAFAAVVLKFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGAMLLGTALDELE 378
Cdd:cd00825  226 DYLVAHGTGTPIGDVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
92-133 2.06e-03

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: 39.54  E-value: 2.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 345112616   92 CASGLDAVNLAAMKVRSGWEDLVVAGGVESM---------SRVPMGSDGGP 133
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGGVNLLltplgfagfSAAGMLSPDGP 223
PRK06066 PRK06066
thiolase domain-containing protein;
256-377 2.26e-03

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 39.73  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 256 SGIVDGAALVLIGSKEKGEALGLKPRarIISAALVGTEPTIMLT---GPAP----ASKKALQKAGMT--LDDIDLIEVNE 326
Cdd:PRK06066 208 APFVDGAIVVVLASEEVAKKLTDDPV--WIKGIGWSTESSNLETaelGKANymriAADMAYKMAGIEspRKEVDAAEVDD 285
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 345112616 327 AFA---------------AVVLKFMRDMGLEDEGPERVNVNGGAIAMGHPLGATGAMLLGTALDEL 377
Cdd:PRK06066 286 RYSykelqhiealrlseePEKDSLLREGNFDPQGELPVNPSGGHLAKGVPLEASGLSLLLDAVEYL 351
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
92-123 2.41e-03

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 39.83  E-value: 2.41e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 345112616  92 CASGLDAVNLAAMKVRSGWEDLVVAGGVESMS 123
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
260-367 4.70e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 39.00  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 260 DGAALVLIGSKEKGEALGLKPRARIISAALVG-----TEPTIMLTGPAPASKKALQKAGMTLDDIDLI----------EV 324
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpagDK 311
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 345112616 325 NEAfAAVVLKFmrdmgleDEGPERVNVNGGAIAMGHPLGATGA 367
Cdd:PRK07314 312 AET-QAIKRVF-------GEHAYKVAVSSTKSMTGHLLGAAGA 346
PRK06158 PRK06158
thiolase; Provisional
258-394 6.39e-03

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 38.47  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 258 IVDGAALVLIGSKEKGEALGLKP-----RARIISAALVGTEPTIMLTGPAPASKKALQKAGMTLDDIDLIEVNEAFAAVV 332
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPPvyvlgAAAATWHRQISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 333 LKFMRDMGL--EDEG---------------PerVNVNGGAIAMGHPlGATGAMLLGTALDELE----RRDLSTALITLCV 391
Cdd:PRK06158 288 ILFLEDLGFcaKGEGgafveggriapggrlP--VNTNGGGLSCVHP-GMYGLFLLIEAVRQLRgeagERQVAGAEVALAH 364

                 ...
gi 345112616 392 GGG 394
Cdd:PRK06158 365 GNG 367
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
256-368 9.05e-03

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 37.90  E-value: 9.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 256 SGIV--DGAALVLIGSKEKGEALGLKPRARIISAALVG-----TEPTIMLTGPAPASKKALQKAGMTLDDIDLI------ 322
Cdd:cd00834  225 DGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDYInahgts 304
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 345112616 323 ----EVNEAFAavvlkfMRDMGLEDEGPERVNVNGGAIamGHPLGATGAM 368
Cdd:cd00834  305 tplnDAAESKA------IKRVFGEHAKKVPVSSTKSMT--GHLLGAAGAV 346
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
259-354 9.40e-03

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 37.97  E-value: 9.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345112616 259 VDGAALVLIGSKEKGEALGLkPRARII----SAALVgtEPTIMLTGPAPAS--------KKALQKAGMTLDDIDLIEVNE 326
Cdd:PRK08257 243 VDQGAAVLLTSVAKARRLGV-PEDRWVylhgGADAH--DPYDILERPDLHRspairaagRRALALAGLGIDDIDAFDLYS 319
                         90       100
                 ....*....|....*....|....*...
gi 345112616 327 AFAAVVLKFMRDMGLEDEGPERVNVNGG 354
Cdd:PRK08257 320 CFPSAVQVAARELGLDLDDPRPLTVTGG 347
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
92-122 9.81e-03

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: 37.77  E-value: 9.81e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 345112616  92 CASGLDAVNLAAMKVRSGWEDLVVAGGVESM 122
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAA 191
 
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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