NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|167614485|ref|NP_006102|]
View 

3-ketoacyl-CoA thiolase, mitochondrial [Homo sapiens]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

thiolase family protein such as acetyl-CoA C-acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl-CoA to another molecule of acetyl-CoA to form acetoacetyl-CoA

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-394 0e+00

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: 577.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALT 87
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQ-NPARQAALLAGLPESVPATT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDiKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:cd00751  159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-394 0e+00

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: 577.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALT 87
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQ-NPARQAALLAGLPESVPATT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDiKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:cd00751  159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
5-393 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 564.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSdAIYLARHVGLRVGIPKETP 84
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGsDIKLEDSL-WVSLTDQHVQLPMAM 163
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 164 TAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVFKKD 242
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 243 GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 323 FAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIV 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
9-394 8.10e-170

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: 479.80  E-value: 8.10e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALTI 88
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGsDIKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485  328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
7-266 1.08e-117

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


Pssm-ID: 395058 [Multi-domain]  Cd Length: 260  Bit Score: 342.74  E-value: 1.08e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTA 165
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|.
gi 167614485  246 TAGNASGVADGAGAVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism];
5-393 9.97e-115

Acetyl-CoA acetyltransferase [Lipid transport and metabolism];


Pssm-ID: 223261 [Multi-domain]  Cd Length: 392  Bit Score: 340.04  E-value: 9.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYG-GLLKDFTATDLSEFAAKAALS--AGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPK 81
Cdd:COG0183    2 RDVAIVGAGRTPFGKFGdGSLAELAAEALGAALIDAGLEraPADVDAADVDDVILGCVLQAGEQGQNIARQAALAAGLPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  82 ETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnVRFGTKLGSDIklEDSLWVS-LTDQHVQLP 160
Cdd:COG0183   82 SVPAVTVNRACASGLAAVRLAAQAIASGEADVVLAGGVEKMSDAPM----GREGVRVLDSA--VDPMFEDpLGDATPGYL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFnDEMAPIEVKTKkgkqTMQVDEHARPQ--TTLEQLQKLPPV 238
Cdd:COG0183  156 MGLTAERYAKRYGISREDQDEVAVKSHKNAAANPKAGFF-DEITPEDVLNS----PVVADPLRRLDcsPTSDGAAALVPA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKK-DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMgIGPVPAISGALKKAGLS-LKDMDL 316
Cdd:COG0183  231 FEEvGGTVTAGNASGINDGAAALLLMSESKAKELGLAPLAAIRAYAMAGVDPSIM-DGPVAAVHDALTIAGLLaLEDLGL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 317 VEVNEAFAPQYLAVERslDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGG----KYAVGSACIGGG-QGIAV 391
Cdd:COG0183  310 AEKGEAFAAVALGVTK--ILGDLPVNPSGGAIALGHPIGATGARILVELARQLRGRGQvvakRRGLATLCIGGGgQGVAA 387

                 ..
gi 167614485 392 II 393
Cdd:COG0183  388 VL 389
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-394 0e+00

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: 577.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALT 87
Cdd:cd00751    1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQ-NPARQAALLAGLPESVPATT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDiKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:cd00751   80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:cd00751  159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00751  239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:cd00751  319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
5-393 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 564.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSdAIYLARHVGLRVGIPKETP 84
Cdd:PRK05790   2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGsDIKLEDSL-WVSLTDQHVQLPMAM 163
Cdd:PRK05790  81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 164 TAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVFKKD 242
Cdd:PRK05790 160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 243 GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 323 FAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIV 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
9-394 8.10e-170

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: 479.80  E-value: 8.10e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPALTI 88
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGsDIKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485  328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK09051 PRK09051
beta-ketothiolase BktB;
5-394 8.46e-165

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 467.51  E-value: 8.46e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK09051   3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQETP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGsDIKLEDSLWVSLTDQHVQLPMAMT 164
Cdd:PRK09051  83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMG-DAKLVDMMVGALHDPFGTIHMGVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKD-G 243
Cdd:PRK09051 162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 244 TVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAF 323
Cdd:PRK09051 242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 324 APQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK09051 322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
4-394 5.87e-137

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 397.02  E-value: 5.87e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSA-GKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK09050   1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnvRFGTKLGSDIKLEDSL--W----VSLTDQH 156
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG--KADSAFSRQAEIFDTTigWrfvnPLMKAQY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKL 235
Cdd:PRK09050 159 GVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVvVDRDEHPRPETTLEALAKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMD 315
Cdd:PRK09050 239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 316 LVEVNEAFAPQYLAVERSLDL--DISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVII 393
Cdd:PRK09050 319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAI 398

                 .
gi 167614485 394 Q 394
Cdd:PRK09050 399 E 399
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
4-397 1.53e-136

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 395.90  E-value: 1.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGnvlQS--SSDAIYLARHVGLRVGIPK 81
Cdd:PRK06205   1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGypNGEAPAIGRVAALDAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  82 ETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSdIKLEDSLWVS-LTDQHVQLP 160
Cdd:PRK06205  78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGG-VQLHDRLARGrETAGGRRFP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 ----MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKL 235
Cdd:PRK06205 157 vpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVvDRDEHPRADTTLESLAKL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKK---DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLK 312
Cdd:PRK06205 237 RPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 313 DMDLVEVNEAFAPQYLAVERSL---DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGI 389
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWgfgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396

                 ....*...
gi 167614485 390 AVIIQSTA 397
Cdd:PRK06205 397 AAVFERVN 404
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
9-394 2.01e-130

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 380.21  E-value: 2.01e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPALTI 88
Cdd:PRK08235   6 IVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQI-PSRQAARAAGIPWEVQTETV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlpMAMT 164
Cdd:PRK08235  85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDneviDLMVADGLTCAFSGVH----MGVY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFKKDG 243
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPiVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 244 TVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAF 323
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167614485 324 APQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
5-394 7.35e-130

3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.


Pssm-ID: 131483  Cd Length: 400  Bit Score: 378.74  E-value: 7.35e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKET 83
Cdd:TIGR02430   1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   84 PALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnvRFGTKLGSDIKLEDSL--WVSLTDQHVQL-- 159
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMG--KADSAFSRSAKIEDTTigWRFINPLMKALyg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  160 --PMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKLP 236
Cdd:TIGR02430 159 vdSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  237 PVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDL 316
Cdd:TIGR02430 239 PVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  317 VEVNEAFAPQYLAVERSLDL--DISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
3-395 9.62e-121

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 355.49  E-value: 9.62e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   3 LLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKE 82
Cdd:PRK06633   1 MTKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQ-NPARQTLIHAGIPKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMS---QAPYcvrnVRFGTKLGsDIKLEDSL-WVSLTDQHVQ 158
Cdd:PRK06633  80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSY----IRAGAKFG-DIKMVDLMqYDGLTDVFSG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 159 LPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPV 238
Cdd:PRK06633 155 VFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PRK06633 235 FDKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIE 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK06633 315 VNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
7-394 1.00e-119

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 353.15  E-value: 1.00e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALS-AGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK09052   8 AYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAqVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNSVG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnvrfgtkLGSDIKLEDSLWVSltDQHVQLP--MA 162
Cdd:PRK09052  88 GVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFAR--DENVGIAygMG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKK----------GKQTMQVDEHARPQTTLEQL 232
Cdd:PRK09052 156 LTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLEGL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 233 QKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLK 312
Cdd:PRK09052 236 AKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQD 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 313 DMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVI 392
Cdd:PRK09052 316 DLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGI 395

                 ..
gi 167614485 393 IQ 394
Cdd:PRK09052 396 FE 397
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
7-266 1.08e-117

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


Pssm-ID: 395058 [Multi-domain]  Cd Length: 260  Bit Score: 342.74  E-value: 1.08e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTA 165
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|.
gi 167614485  246 TAGNASGVADGAGAVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
8-394 1.45e-117

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 347.54  E-value: 1.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK08131   5 YIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTVPGQT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRfgTKLGSDIKLEDSLWVS------LTDQHVQLPM 161
Cdd:PRK08131  85 VNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAE--SAFSRDAKVFDTTIGArfpnpkIVAQYGNDSM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 162 AMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQV--DEHARPQTTLEQLQKLPPVF 239
Cdd:PRK08131 163 PETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKLVaeDEHPRPSSTVEALTKLKPLF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PRK08131 243 E-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEI 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDLDI--SKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08131 322 NEAFASQVLGCLKGLGVDFddPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
7-394 8.55e-116

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 342.64  E-value: 8.55e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAiYLARHVGLRVGIPKETPAL 86
Cdd:PRK05656   4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQ-NPARQAAIKAGLPHSVPAM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlpMA 162
Cdd:PRK05656  83 TLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHaqlvDSMITDGLWDAFNDYH----MG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFKK 241
Cdd:PRK05656 159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPlAFATDEQPRAGTTAESLAKLKPAFKK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 242 DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNE 321
Cdd:PRK05656 239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614485 322 AFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK05656 319 AFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism];
5-393 9.97e-115

Acetyl-CoA acetyltransferase [Lipid transport and metabolism];


Pssm-ID: 223261 [Multi-domain]  Cd Length: 392  Bit Score: 340.04  E-value: 9.97e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYG-GLLKDFTATDLSEFAAKAALS--AGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPK 81
Cdd:COG0183    2 RDVAIVGAGRTPFGKFGdGSLAELAAEALGAALIDAGLEraPADVDAADVDDVILGCVLQAGEQGQNIARQAALAAGLPG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  82 ETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnVRFGTKLGSDIklEDSLWVS-LTDQHVQLP 160
Cdd:COG0183   82 SVPAVTVNRACASGLAAVRLAAQAIASGEADVVLAGGVEKMSDAPM----GREGVRVLDSA--VDPMFEDpLGDATPGYL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFnDEMAPIEVKTKkgkqTMQVDEHARPQ--TTLEQLQKLPPV 238
Cdd:COG0183  156 MGLTAERYAKRYGISREDQDEVAVKSHKNAAANPKAGFF-DEITPEDVLNS----PVVADPLRRLDcsPTSDGAAALVPA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKK-DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMgIGPVPAISGALKKAGLS-LKDMDL 316
Cdd:COG0183  231 FEEvGGTVTAGNASGINDGAAALLLMSESKAKELGLAPLAAIRAYAMAGVDPSIM-DGPVAAVHDALTIAGLLaLEDLGL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 317 VEVNEAFAPQYLAVERslDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGG----KYAVGSACIGGG-QGIAV 391
Cdd:COG0183  310 AEKGEAFAAVALGVTK--ILGDLPVNPSGGAIALGHPIGATGARILVELARQLRGRGQvvakRRGLATLCIGGGgQGVAA 387

                 ..
gi 167614485 392 II 393
Cdd:COG0183  388 VL 389
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
5-394 8.65e-113

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 335.01  E-value: 8.65e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK08947   2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcVRNVRFGTKLGSDIKLEDSLwvsltdqhvqlpMA 162
Cdd:PRK08947  82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPM-NHGVDFHPGLSKNVAKAAGM------------MG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 MTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKG-KQTMQVDEHARPQTTLEQLQKLPPVFK- 240
Cdd:PRK08947 149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAFDp 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVN 320
Cdd:PRK08947 229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 321 EAFAPQYLAVERSLDLDIS---KTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK08947 309 EAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
5-395 4.23e-111

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 331.98  E-value: 4.23e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSsDAIYLARHVGLRVGIPKETP 84
Cdd:PRK08170   3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSP-DEANIARVVALRLGCGEKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRN--VR----------FGTKLGSDIKLEDS----- 147
Cdd:PRK08170  82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmVRwlagwyaaksIGQKLAALGKLRPSylapv 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 148 --LWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNdEMAPIevKTKKGKQTMQvDEHARP 225
Cdd:PRK08170 162 igLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL--FDRDGKFYDH-DDGVRP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 226 QTTLEQLQKLPPVF-KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGAL 304
Cdd:PRK08170 238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 305 KKAGLSLKDMDLVEVNEAFAPQYLAVERSLD-----------------LDISKTNVNGGAIALGHPLGGSGSRITAHLVH 367
Cdd:PRK08170 318 QRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
                        410       420
                 ....*....|....*....|....*...
gi 167614485 368 ELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK08170 398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
4-394 3.69e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 328.60  E-value: 3.69e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFGAYGGllKD-----FTATDLSEFAA---KAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGL 75
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRP--KDpqkdvFNNIRPEELAAmliNRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  76 RVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAP-YCVRNVRFGTKLGSDIKLEDslwvslTD 154
Cdd:PRK06445  79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmGDNPHIEPNPKLLTDPKYIE------YD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 155 QHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQK 234
Cdd:PRK06445 153 LTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 235 LPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDM 314
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 315 DLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
5-397 5.87e-109

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 325.51  E-value: 5.87e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   5 RGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLqSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PLN02644   1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVL-SANLGQAPARQAALGAGLPPSTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGS----DIKLEDSLWVSLTDQHvqlp 160
Cdd:PLN02644  80 CTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHdtvvDGMLKDGLWDVYNDFG---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARP-QTTLEQLQKLPPVF 239
Cdd:PLN02644 156 MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLgKFDPAKLRKLRPSF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKD-GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PLN02644 236 KEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYE 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA 397
Cdd:PLN02644 316 INEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
4-390 8.54e-109

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 324.78  E-value: 8.54e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKE 82
Cdd:PRK07661   1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  83 TPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrnvrfgtkLGSDIKLEdslwVSLTDQHVQLPMA 162
Cdd:PRK07661  81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGHVVRPN----PRLVEAAPEYYMG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 163 M--TAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEV---------KTKKGKQTMQVDEHARPQTTLEQ 231
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennKLQEETITFSQDEGVRADTTLEI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 232 LQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSL 311
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 312 KDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
8-394 2.41e-105

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 315.88  E-value: 2.41e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK07801   5 YIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCvRNVRFGTKLG-SDIKLEDSLWVS-LTDQHVQLPMAmtA 165
Cdd:PRK07801  85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIS-SAMTAGEQLGfTSPFAESKGWLHrYGDQEVSQFRG--A 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTkkgkqtmqVDEHARpQTTLEQLQKLPPVFKkDGTV 245
Cdd:PRK07801 162 ELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVT--------VDEGPR-ETSLEKMAGLKPLVE-GGRL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 246 TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAP 325
Cdd:PRK07801 232 TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAP 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 326 QYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK07801 312 VVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
7-394 2.80e-102

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 310.16  E-value: 2.80e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPF-GAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPA 85
Cdd:PLN02287  48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  86 LTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcVRNVRFGTKLGSDIKLEDSLwvsltdqhvqLPMAMTA 165
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPM-AWEGGVNPRVESFSQAQDCL----------LPMGITS 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ------TMQVDEHARPQTTLEQLQKLPPVF 239
Cdd:PLN02287 197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTgeekpiVISVDDGIRPNTTLADLAKLKPVF 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PLN02287 277 KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRG--GKYAVGSACIGGGQGIAVIIQ 394
Cdd:PLN02287 357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFE 433
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
9-394 3.26e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 298.46  E-value: 3.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   9 VVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSagKV---SPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPkETP 84
Cdd:PRK07851   6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALD--KVpalDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD-FLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYC-------VRNVRFGTKLGSDIKLEDSLWVSLTDQH- 156
Cdd:PRK07851  83 GTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnsdslpdTKNPLFAEAQARTAARAEGGAEAWHDPRe 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 ------VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKqTMQVDEHARPQTTLE 230
Cdd:PRK07851 163 dgllpdVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDGT-VVSTDDGPRAGTTYE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 231 QLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLS 310
Cdd:PRK07851 240 KVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 311 LKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07851 320 IDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMA 399

                 ....
gi 167614485 391 VIIQ 394
Cdd:PRK07851 400 MVLE 403
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
9-390 4.62e-98

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 297.45  E-value: 4.62e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   9 VVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK07108   6 IVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVPGMT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapyCVRNvrfgtklGSDIKLEDSLWVSLTDQHVQLPMAMTAEN 167
Cdd:PRK07108  86 VNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQN-------EMNRHMLREGWLVEHKPEIYWSMLQTAEN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQ----------TMQVDEHARPQTTLEQLQKLPP 237
Cdd:PRK07108 155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkevTVSADEGIRPDTTLEGVSKIRS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 238 VFKkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLV 317
Cdd:PRK07108 235 ALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167614485 318 EVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIA 390
Cdd:PRK07108 314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
7-394 3.99e-96

fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]


Pssm-ID: 131498  Cd Length: 385  Bit Score: 292.23  E-value: 3.99e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485    7 VFVVAAKRTPFG-AYGGLLKDFTATDLSEFAAKAALSAG-KVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:TIGR02445   2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARNpKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrnvrfgTKLGSDIKLEDSLWVSLTDQHvqlpMAMT 164
Cdd:TIGR02445  82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP---------MMHGVDFHPGMSLHVAKAAGM----MGLT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGK-QTMQVDEHARPQTTLEQLQKLPPVFK-KD 242
Cdd:TIGR02445 149 AEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEVIRPETTVESLAALRPAFDpKN 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  243 GTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167614485  323 FAPQYLAVERSL---DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:TIGR02445 309 FAAQALPCLKDLgllDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
8-394 4.49e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 292.56  E-value: 4.49e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFG--AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPA 85
Cdd:PRK08242   5 YIYDAVRTPRGkgKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETVPG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  86 LTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrnvrfgtkLGSDikleDSLWVslTDQHVQL-----P 160
Cdd:PRK08242  85 VQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-----------MGSD----GGAWA--MDPSTNFptyfvP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK08242 148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTV---------------------TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPA 299
Cdd:PRK08242 226 MMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 300 ISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK08242 306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
                        410
                 ....*....|....*
gi 167614485 380 SACIGGGQGIAVIIQ 394
Cdd:PRK08242 386 TLCVGGGMGIATIIE 400
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
8-394 4.87e-93

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 284.70  E-value: 4.87e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALT 87
Cdd:PRK06504   5 YIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGTS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  88 INRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVrNVRFGTKLGSDIKLEDSLWVSLTDqhVQLPMAMTAEN 167
Cdd:PRK06504  85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS-PSTLPAKNGLGHYKSPGMEERYPG--IQFSQFTGAEM 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 168 LAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVfKKDGTVT 246
Cdd:PRK06504 162 MAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKLI-AEGGRLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 247 AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQ 326
Cdd:PRK06504 241 AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASV 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167614485 327 YLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06504 321 PLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
4-388 1.73e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 280.36  E-value: 1.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQS---SSDAIYLARHVGLRVGIP 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAgvgQNPAGQAAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  81 KetpaLTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV-RNVRFGTK--LGSDIKLEDSLWVS-LTDQH 156
Cdd:PRK06366  81 K----YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKhlLHKNYKIDDAMLVDgLIDAF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 157 VQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEvktkkgkqTMQVDEHARpQTTLEQLQKLP 236
Cdd:PRK06366 157 YFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIR-KTTMEDLAKLP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 237 PVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDL 316
Cdd:PRK06366 228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167614485 317 VEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
7-394 1.31e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 265.60  E-value: 1.31e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:PRK06954   9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQA-PARQAALGAGLPLSVGCT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQ-LPMAMTA 165
Cdd:PRK06954  88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKgRLMGTFA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 166 ENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARpQTTLEQLQKLPPVFKKDGTV 245
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 246 TAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAP 325
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167614485 326 QYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
7-396 1.79e-81

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 256.06  E-value: 1.79e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSsDAIYLARHVGLRVGIPKETPAL 86
Cdd:PRK08963   7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMP-EAPNIAREIVLGTGMNVHTDAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV--------------RNVRFGTKLGSDIKLEDSLWV-- 150
Cdd:PRK08963  86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskklaralvdlnkaRTLGQRLKLFSRLRLRDLLPVpp 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 151 SLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMapIEVKTKKGKQTMQVDEHARPQTTLE 230
Cdd:PRK08963 166 AVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPPYKQPLEEDNNIRGDSTLE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 231 QLQKLPPVF-KKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDP-SIMGIGPVPAISGALKKAG 308
Cdd:PRK08963 244 DYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 309 LSLKDMDLVEVNEAFAPQYLA----------VERSL-------DLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRR 371
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
                        410       420
                 ....*....|....*....|....*
gi 167614485 372 RGGKYAVGSACIGGGQGIAVIIQST 396
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEVE 428
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
9-394 2.05e-79

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 249.25  E-value: 2.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   9 VVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTI 88
Cdd:PRK07850   6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGATTI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  89 NRLCGSGFQS--IVNGCqeICVKEAEVVLCGGTESMSQAPycvrnvrFGTKLGSDIKL--EDSLWVSLTDQHVqlpmamT 164
Cdd:PRK07850  86 DCQCGSAQQAnhLVAGL--IAAGAIDVGIACGVEAMSRVP-------LGANAGPGRGLprPDSWDIDMPNQFE------A 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIE--VKTKKGKQTMQVDEHARPQ----TTLEQLQKLPPV 238
Cdd:PRK07850 151 AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTGETRLVTRDQglrdTTMEGLAGLKPV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 239 FKkDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVE 318
Cdd:PRK07850 231 LE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVE 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK07850 310 INEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
9-394 3.49e-79

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 248.14  E-value: 3.49e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   9 VVAAKRTPFGAYGGLLKDFTATDLsefAAKAALSAGKVSPETVDSVIMGNVLQSSSDaiyLARHVGLRVGIPKETPALTI 88
Cdd:PRK06690   5 IVEAKRTPIGKKNGMLKDYEVQQL---AAPLLTFLSKGMEREIDDVILGNVVGPGGN---VARLSALEAGLGLHIPGVTI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  89 NRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRnVRFGTKlgsdikledslWVSLTDqhvqlpMAMTAENL 168
Cdd:PRK06690  79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNR-ARFSPE-----------TIGDPD------MGVAAEYV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 169 AVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEvktkkgkqtMQVDEHARPQTTLEQL-QKLPPVFKKDGTVTA 247
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN---------GLLDESIKKEMNYERIiKRTKPAFLHNGTVTA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 248 GNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 328 LAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
8-394 1.50e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 230.05  E-value: 1.50e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   8 FVVAAKRTPFG---AYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETP 84
Cdd:PRK06025   5 YIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIKAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  85 ALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMT 164
Cdd:PRK06025  85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS---YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQSHQGVC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 165 AENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKK--- 241
Cdd:PRK06025 162 GDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiad 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 242 ----DGTVT-------------------AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVP 298
Cdd:PRK06025 240 ypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 299 AISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAV 378
Cdd:PRK06025 320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGL 399
                        410
                 ....*....|....*.
gi 167614485 379 GSACIGGGQGIAVIIQ 394
Cdd:PRK06025 400 VTMCAAGGMAPAIIIE 415
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
273-394 4.15e-67

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: 208.65  E-value: 4.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  273 FTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGH 352
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 167614485  353 PLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQ 394
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
10-395 7.68e-64

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: 209.27  E-value: 7.68e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  10 VAAKRTPFGAYGGLLKDFTATDLSEFAAKA---ALSAGKVSPETVDSVIMGNVLQSSSDAIyLARHVGLRVGIPKETPAL 86
Cdd:cd00826    1 AGAAMTAFGKFGGENGADANDLAHEAGAKAiaaALEPAGVAAGAVEEACLGQVLGAGEGQN-CAQQAAMHAGGLQEAPAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  87 TINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSqapYCVRNVRFGTKLgsdikledslwvsltdqhvqlpmamtae 166
Cdd:cd00826   80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---TSAENNAKEKHI---------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 167 NLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQT--TLEQLQKLPPVFKKDGT 244
Cdd:cd00826  129 DVLINKYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPAFDKEDF 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 245 VTAGNASGVADGAGAVIIASEDAVKKHNFT-------PLARIVGYFVSGCDPS----IMGIGPVPAISGALKKAGLSLKD 313
Cdd:cd00826  209 LTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 314 MDLVEVNEAFAPQYLAVERSLDLD------------------ISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGK 375
Cdd:cd00826  289 LDLIEAHDAFAANACATNEALGLCpegqggalvdrgdntyggKSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
                        410       420
                 ....*....|....*....|....*
gi 167614485 376 YAVGSA-----CIGGGQGIAVIIQS 395
Cdd:cd00826  369 RQGAGAglallCIGGGGGAAMCIES 393
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-395 3.61e-62

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 205.90  E-value: 3.61e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   1 MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDaIYLARHVGLRVGIP 80
Cdd:PRK09268   3 MPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRD-FNLTRECVLGSALS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  81 KETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCV------------RNVRFGTKLGSDIKLEDSL 148
Cdd:PRK09268  82 PYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVneglrkillelnRAKTTGDRLKALGKLRPKH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 149 WVSLTDQHVQ----LPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKkgkqtmqvDEHAR 224
Cdd:PRK09268 162 LAPEIPRNGEprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 225 PQTTLEQLQKLPPVFKK--DGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGY------FVSGCDPSIMGigP 296
Cdd:PRK09268 234 PDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetaavdFVHGKEGLLMA--P 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 297 VPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAV-----------ER-SLD-----LDISKTNVNGGAIALGHPLGGSGS 359
Cdd:PRK09268 312 AYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlkawedeeycrERlGLDaplgsIDRSKLNVNGSSLAAGHPFAATGG 391
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 167614485 360 RITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQS 395
Cdd:PRK09268 392 RIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
15-393 1.70e-23

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: 100.42  E-value: 1.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  15 TPFGAYGGLlkdfTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSD---AIYLARHVGLRVGipketPALTINRL 91
Cdd:cd00829    6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQsfpGALIAEYLGLLGK-----PATRVEAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  92 CGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYcvrNVRFGTKLGSdikLEDSLWVSLTDQHVQLPMAMTAENLAVK 171
Cdd:cd00829   77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPT---GDEAGGRASD---LEWEGPEPPGGLTPPALYALAARRYMHR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 172 HKISREECDKYALQsQQRWKAANDAGYFNDEMapievktkkgkqtmqvdeharpqtTLEQLQKLPPVFkkdGTVTAGNAS 251
Cdd:cd00829  151 YGTTREDLAKVAVK-NHRNAARNPYAQFRKPI------------------------TVEDVLNSRMIA---DPLRLLDCC 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 252 GVADGAGAVIIASEDAVKKHnFTPLARIVG-------YFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFA 324
Cdd:cd00829  203 PVSDGAAAVVLASEERAREL-TDRPVWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 325 PQ-YLAVE--------------RSLDLDIS---KTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIG-- 384
Cdd:cd00829  282 IAeLLALEdlgfcekgeggklvREGDTAIGgdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGla 361
                        410
                 ....*....|..
gi 167614485 385 ---GGQGIAVII 393
Cdd:cd00829  362 hniGGTGSAAVV 373
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
247-393 3.49e-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: 97.51  E-value: 3.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 247 AGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPS----IMGIGPVPAISGALKKAGLSLKDMDLVEVNEA 322
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 323 FAPQYLAVERSLDLDISK---TNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKY-------AVGSACIGGGQGIAVI 392
Cdd:cd00327  174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253

                 .
gi 167614485 393 I 393
Cdd:cd00327  254 L 254
PRK06064 PRK06064
thiolase domain-containing protein;
4-388 5.37e-14

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 72.62  E-value: 5.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   4 LRGVFVVAAKRTPFGAygglLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVL------QSSSdAIYLARHVGLRv 77
Cdd:PRK06064   1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSaglfvsQEHI-AALIADYAGLA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  78 gipkETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLgsdikleDSLWVSLtdQHV 157
Cdd:PRK06064  75 ----PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG-------DYEWEEF--FGA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 158 QLP--MAMTAenlavkhkisREECDKYalqsqqrwkaandaGYFNDEMAPIEVKTKKgKQTMQVDEHARPQTTLEQLQKL 235
Cdd:PRK06064 142 TFPglYALIA----------RRYMHKY--------------GTTEEDLALVAVKNHY-NGSKNPYAQFQKEITVEQVLNS 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKdgtVTAGNASGVADGAGAVIIASEDAVKKHNFTPL-----ARIVGYFVSGCDPSIMGIGP-VPAISGALKKAGL 309
Cdd:PRK06064 197 PPVADP---LKLLDCSPITDGAAAVILASEEKAKEYTDTPVwikasGQASDTIALHDRKDFTTLDAaVVAAEKAYKMAGI 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 310 SLKDMDLVEVNEAFA-PQYLAVErslDLDISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06064 274 EPKDIDVAEVHDCFTiAEILAYE---DLGFAKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQ 350
                        410       420
                 ....*....|....*....|....*..
gi 167614485 369 LRRR--GGKYAVGSACIG-----GGQG 388
Cdd:PRK06064 351 LRGEaeKGRQQVIGAGYGlthnvGGTG 377
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
236-381 4.84e-10

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 60.86  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 236 PPVFKKDGT---VTAG-----NASGVADGAGAVIIASEDAVKKH-NFTPLARIVGY-------------FVSGCDPSIMg 293
Cdd:PRK06289 197 DEATNDDDAtnpVVEGrlrrqDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIKGWghrtaplgleqklDRSAGDPYVL- 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 294 igpvP----AISGALKKAGLSLKDMDLVEVNEAFAP-QYLAVE--------------RSLDLDISKT---NVNGGAIALG 351
Cdd:PRK06289 276 ----PhvrqAVLDAYRRAGVGLDDLDGFEVHDCFTPsEYLAIDhigltgpgeswkaiENGEIAIGGRlpiNPSGGLIGGG 351
                        170       180       190
                 ....*....|....*....|....*....|
gi 167614485 352 HPLGGSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK06289 352 HPVGASGVRMLLDAAKQVTGTAGDYQVEGA 381
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
254-358 2.24e-08

3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 223381 [Multi-domain]  Cd Length: 412  Bit Score: 55.73  E-value: 2.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 254 ADGAGAVIIASEDAVKKHNFTPLARIVGYFVSG-----CDPSIMGIGPVPAISGALKKAGLSLKDMDLV----------E 318
Cdd:COG0304  231 GEGAGALVLEELEHALARGAKIYAEIVGYGTTSdayhiTAPAPDGEGAIRAMRAALADAGLTPEDIDYInahgtstpanD 310
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 167614485 319 VNEAFAPQYLAVERSLDLDISKTnvnGGAIalGHPLGGSG 358
Cdd:COG0304  311 KAESLAIKRVFGEHAKSLPVSST---KSLT--GHTLGAAG 345
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
255-358 3.96e-07

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 51.71  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 255 DGAGAVIIASEDAVKKHNFTPLARIVGYFVSgCD------PSIMGIGPVPAISGALKKAGLSLKDMDLV----------E 318
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMT-GDayhmtaPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpagD 310
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 167614485 319 VNEAfapqyLAVERSLDLDISKTNVNGGAIALGHPLGGSG 358
Cdd:PRK07314 311 KAET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
PRK07516 PRK07516
thiolase domain-containing protein;
7-358 9.14e-06

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 47.25  E-value: 9.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFGAygglLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGN-----VLQSSSDAIYLARHVGLRVgipk 81
Cdd:PRK07516   4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHfnagfSPQDFPASLVLQADPALRF---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  82 eTPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPycvrNVRFGTKL-GSDIKLEDSlwvsltdqhvQLP 160
Cdd:PRK07516  76 -KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP----TAEVGDILlGASYLKEEG----------DTP 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAenlaVKHKISREECDKYALQSqqrwkaandagyfnDEMAPIEVKTKKgkqtmqvDEHARPqttLEQLQK-LPPVF 239
Cdd:PRK07516 141 GGFAG----VFGRIAQAYFQRYGDQS--------------DALAMIAAKNHA-------NGVANP---YAQMRKdLGFEF 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 240 KKdgTVTAGN-----------ASGVADGAGAVIIASEDAVKK-------------HNFTPLARIvgyfvsgcDPSIMGiG 295
Cdd:PRK07516 193 CR--TVSEKNplvagplrrtdCSLVSDGAAALVLADAETARAlqravrfrarahvNDFLPLSRR--------DPLAFE-G 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 296 PVPAISGALKKAGLSLKDMDLVEVNEAF-------------APQ---YLAVERSLDLDISKTNVN--GGAIALGHPLGGS 357
Cdd:PRK07516 262 PRRAWQRALAQAGVTLDDLSFVETHDCFtiaelieyeamglAPPgqgARAIREGWTAKDGKLPVNpsGGLKAKGHPIGAT 341

                 .
gi 167614485 358 G 358
Cdd:PRK07516 342 G 342
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
254-369 3.82e-05

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: 45.32  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 254 ADGAGAVIIASEDAVKKHNFTPLARIVGYfVSGCDPSIMGI------GPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:cd00825  160 GDGAGALVVEELEHALARGAHIYAEIVGT-AATIDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 167614485 328 LAVERSLDLDISKtnvnGGAIALGHPLGGSGSRITAHLVHEL 369
Cdd:cd00825  239 DVKELKLLRSEFG----DKSPAVSATKAMTGNLSSAAVVLAV 276
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
253-359 6.22e-05

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 44.78  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 253 VADGAGAVIIASEDAVKKHNFTPLARIVGYFVSG-----CDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQY 327
Cdd:PLN02836 253 IGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGdahhiTQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPLG 332
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 167614485 328 LAVERSLDLDISKTNVNGGAIAL-------GHPLGGSGS 359
Cdd:PLN02836 333 DAVEARAIKTVFSEHATSGGLAFsstkgatGHLLGAAGA 371
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
254-359 6.56e-05

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: 44.84  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 254 ADGAGAVIIASEDAVKKHNFTPLARIVGYFVSgCD------PSIMGIGPVPAISGALKKAGLSLKDMDLV---------- 317
Cdd:cd00834  230 GEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDayhitaPDPDGEGAARAMRAALADAGLSPEDIDYInahgtstpln 308
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 167614485 318 EVNEAfapqyLAVERSLDLDISKTNVNG--GAIalGHPLGGSGS 359
Cdd:cd00834  309 DAAES-----KAIKRVFGEHAKKVPVSStkSMT--GHLLGAAGA 345
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
7-387 1.83e-04

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 43.09  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485   7 VFVVAAKRTPFGAYGgllkDFTATDLSEFAAKAALSAGKVSPETVDSVIMG---NVLQSSSDAIYLARHVGLrvgipKET 83
Cdd:PRK06157   9 VAILGMGCTKFGERW----DAGAEDLMVEAFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRL-----PNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485  84 PALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVR-FGTklgsdikLEDSLWVSLTDqhvqlP-- 160
Cdd:PRK06157  80 PVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYGGLPVAnPGT-------LADMTMPNVTA-----Pgn 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 161 MAMTAENLAVKHKISREECdkyalqsqqrwKAAndagyfndeMAPIEVKTKKGKqTMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK06157 148 FAQLASAYAAKYGVSREDL-----------KRA---------MAHVSVKSHANG-ARNPKAHLRKAVTEEQVLKAPMIAG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 241 KDGTVtagNASGVADGAGAVIIASEDAVKKHNFTPLARI------VGYFVSGCDPSIMGIgPVPAISGALKKA----GLS 310
Cdd:PRK06157 207 PLGLF---DCCGVSDGAAAAIVTTPEIARALGKKDPVYVkalqlaVSNGWELQYNGWDGS-YFPTTRIAARKAyreaGIT 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 311 --LKDMDLVEVNEAFAPQYLAVERslDLDISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06157 283 dpREELSMAEVHDCFSITELVTME--DLGLSErgqawrdvldgffdadgglpCQIDGGLKCFGHPIGASGLRMLYEMYLQ 360
                        410       420
                 ....*....|....*....|....
gi 167614485 369 LRRRGGKYAVGSACIG-----GGQ 387
Cdd:PRK06157 361 LLGRAGERQLKNPRLAlthnlGGA 384
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
251-376 4.04e-04

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 42.19  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167614485 251 SGVADGAGAVIIASEDAVKKHNFTPL-ARIVGYFVSGC----------DPSIMgIGPVPAISGALKKAGLSLKDMDLVEV 319
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRM-FTSRAAAQKALSMAGVKPSDLQVAEV 334
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 320 NEAFAPQYLAVERSLDldISK--------------------TNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKY 376
Cdd:PTZ00455 335 HDCFTIAELLMYEALG--IAEyghakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEY 409
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
256-317 7.64e-04

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 41.17  E-value: 7.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167614485 256 GAGAVIIASEDAVKKHNFTPLARIVGYFV-----SGCDPSImgIGPVPAISGALKKAGLSLKDMDLV 317
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMrldanRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYV 304
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH