NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1937369814|ref|NP_569117|]
View 

3-ketoacyl-CoA thiolase, mitochondrial [Rattus norvegicus]

Protein Classification

thiolase family protein( domain architecture ID 10091456)

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

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

Graphical summary

 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 ...
8-395 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: 572.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGALT 87
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDlKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:cd00751    80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTVTA 247
Cdd:cd00751   159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-395 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: 572.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGALT 87
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDlKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:cd00751    80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTVTA 247
Cdd:cd00751   159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
7-395 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 548.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGAL 86
Cdd:COG0183     4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESVPAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGtkFGLDLKLEDTL-WAGLTDQHVKLPMGMTA 165
Cdd:COG0183    83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWG--YRMNAKLVDPMiNPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTV 245
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:COG0183   241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:COG0183   321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
PRK05790 PRK05790
putative acyltransferase; Provisional
5-393 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 548.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSdAAYLARHVGLRVGVPTETG 84
Cdd:PRK05790    2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTL-WAGLTDQHVKLPMGM 163
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 164 TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVFKKE 242
Cdd:PRK05790  160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 243 GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:PRK05790  240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369814 323 FAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLII 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 6.62e-168

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: 474.79  E-value: 6.62e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVmQSSSDAAYLARHVGLRVGVPTETGALTL 88
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNV-LQAGEQQNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  89 NRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGlDLKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 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 1.51e-109

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


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 321.94  E-value: 1.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETGAL 86
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTA 165
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|.
gi 1937369814 246 TAGNASGMSDGAGVVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
8-395 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: 572.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGALT 87
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDlKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:cd00751    80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLN-TLDGMLDDGLTDPFTGLSMGITAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTVTA 247
Cdd:cd00751   159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
7-395 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 548.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGAL 86
Cdd:COG0183     4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPESVPAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGtkFGLDLKLEDTL-WAGLTDQHVKLPMGMTA 165
Cdd:COG0183    83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWG--YRMNAKLVDPMiNPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTV 245
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:COG0183   241 TAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAA 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:COG0183   321 QVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
PRK05790 PRK05790
putative acyltransferase; Provisional
5-393 0e+00

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 548.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSdAAYLARHVGLRVGVPTETG 84
Cdd:PRK05790    2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGA-GQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTL-WAGLTDQHVKLPMGM 163
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMG-DVELVDTMiHDGLTDAFNGYHMGI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 164 TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVFKKE 242
Cdd:PRK05790  160 TAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVvDTDEHPRPDTTAESLAKLRPAFDKD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 243 GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:PRK05790  240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369814 323 FAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLII 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 6.62e-168

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: 474.79  E-value: 6.62e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVmQSSSDAAYLARHVGLRVGVPTETGALTL 88
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNV-LQAGEQQNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  89 NRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGlDLKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVpRSLRWGVKPG-NAELEDARLKDLTDANTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK09051 PRK09051
beta-ketothiolase BktB;
5-394 3.19e-165

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 468.67  E-value: 3.19e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK09051    3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQETP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTLWAGLTDQHVKLPMGMT 164
Cdd:PRK09051   83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMG-DAKLVDMMVGALHDPFGTIHMGVT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKE-G 243
Cdd:PRK09051  162 AENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 244 TVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAF 323
Cdd:PRK09051  242 TVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAF 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369814 324 APQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK09051  322 AAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
4-397 7.43e-136

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 394.35  E-value: 7.43e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGnvmQS--SSDAAYLARHVGLRVGVPT 81
Cdd:PRK06205    1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGypNGEAPAIGRVAALDAGLPV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  82 ETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGlDLKLEDTLWAG-LTDQHVKLP 160
Cdd:PRK06205   78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGG-GVQLHDRLARGrETAGGRRFP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 161 M--GM--TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKL 235
Cdd:PRK06205  157 VpgGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVvDRDEHPRADTTLESLAKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 236 PPVFKK---EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLK 312
Cdd:PRK06205  237 RPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 313 DMDLIDVNEAFAPQFLAVQKSL---DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGI 389
Cdd:PRK06205  317 DIDLIELNEAFAAQVLAVLKEWgfgADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396

                  ....*...
gi 1937369814 390 SLIIQNTA 397
Cdd:PRK06205  397 AAVFERVN 404
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
4-394 1.69e-134

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 390.85  E-value: 1.69e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSA-GKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK09050    1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnvRFGTKFGLDLKLEDTL--W----AGLTDQH 156
Cdd:PRK09050   81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG--KADSAFSRQAEIFDTTigWrfvnPLMKAQY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 157 VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKL 235
Cdd:PRK09050  159 GVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVvVDRDEHPRPETTLEALAKL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 236 PPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMD 315
Cdd:PRK09050  239 KPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 316 LIDVNEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLII 393
Cdd:PRK09050  319 VIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAI 398

                  .
gi 1937369814 394 Q 394
Cdd:PRK09050  399 E 399
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
5-394 1.43e-128

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: 375.66  E-value: 1.43e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTET 83
Cdd:TIGR02430   1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  84 GALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnvRFGTKFGLDLKLEDTL--WAGLTDQHVKL-- 159
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMG--KADSAFSRSAKIEDTTigWRFINPLMKALyg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 160 --PMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQT-MQVDEHARPQTTLEQLQKLP 236
Cdd:TIGR02430 159 vdSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 237 PVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDL 316
Cdd:TIGR02430 239 PVVRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 317 IDVNEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
7-394 1.09e-123

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 363.17  E-value: 1.09e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSagKVP---PETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK09052    8 AYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVA--QVPgldPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrfGTKFGLDLKLEDTlwagltDQHVKLP-- 160
Cdd:PRK09052   86 VGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM------GNKPSMSPAIFAR------DENVGIAyg 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKK----------GKQTMQVDEHARPQTTLE 230
Cdd:PRK09052  154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRADTSLE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 231 QLQKLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLS 310
Cdd:PRK09052  234 GLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 311 LKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIS 390
Cdd:PRK09052  314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393

                  ....
gi 1937369814 391 LIIQ 394
Cdd:PRK09052  394 GIFE 397
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
9-394 2.77e-123

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 362.11  E-value: 2.77e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSD---AAYLARHVGLRVGVPTETga 85
Cdd:PRK08235    6 IVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGqipSRQAARAAGIPWEVQTET-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  86 ltLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklpM 161
Cdd:PRK08235   84 --VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGdnevIDLMVADGLTCAFSGVH----M 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK08235  158 GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPiVVAKDEAPRKDTTIEKLAKLKPVFD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 241 KEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PRK08235  238 KTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEIN 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369814 321 EAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08235  318 EAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
3-394 6.34e-118

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 348.17  E-value: 6.34e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   3 LLRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTE 82
Cdd:PRK06633    1 MTKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQN-PARQTLIHAGIPKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvRNVRFGTKFGlDLKLEDTL-WAGLTDQHVKLPM 161
Cdd:PRK06633   80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHG-SYIRAGAKFG-DIKMVDLMqYDGLTDVFSGVFM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKK 241
Cdd:PRK06633  158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 242 EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNE 321
Cdd:PRK06633  238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNE 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369814 322 AFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06633  318 AFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
8-395 2.72e-117

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 346.76  E-value: 2.72e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK08131    5 YIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTVPGQT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRfgTKFGLDLKLEDTLWAG------LTDQHVKLPM 161
Cdd:PRK08131   85 VNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAE--SAFSRDAKVFDTTIGArfpnpkIVAQYGNDSM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 162 GMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQV--DEHARPQTTLEQLQKLPPVF 239
Cdd:PRK08131  163 PETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKLVaeDEHPRPSSTVEALTKLKPLF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 240 KkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PRK08131  243 E-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEI 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 320 NEAFAPQFLAVQKSLDL--DPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:PRK08131  322 NEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
7-394 2.04e-114

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 339.17  E-value: 2.04e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSdAAYLARHVGLRVGVPTETGAL 86
Cdd:PRK05656    4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPHSVPAM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklpMG 162
Cdd:PRK05656   83 TLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGhaqlVDSMITDGLWDAFNDYH----MG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 163 MTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ-TMQVDEHARPQTTLEQLQKLPPVFKK 241
Cdd:PRK05656  159 ITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPlAFATDEQPRAGTTAESLAKLKPAFKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 242 EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNE 321
Cdd:PRK05656  239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937369814 322 AFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK05656  319 AFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
5-395 2.69e-113

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 337.76  E-value: 2.69e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETG 84
Cdd:PRK08170    3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSP-DEANIARVVALRLGCGEKVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSP--YSVRNVR----------FGTKFGLDLKLEDTLWA-- 150
Cdd:PRK08170   82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPllFSEKMVRwlagwyaaksIGQKLAALGKLRPSYLApv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 151 -----GLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEeMAPIevKTKKGKQTMQvDEHARP 225
Cdd:PRK08170  162 igllrGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPL--FDRDGKFYDH-DDGVRP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 226 QTTLEQLQKLPPVF-KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGAL 304
Cdd:PRK08170  238 DSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 305 KKAGLSLKDMDLIDVNEAFAPQFLAVQKSLD-----------------LDPSKTNVSGGAIALGHPLGGSGSRITAHLVH 367
Cdd:PRK08170  318 QRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLH 397
                         410       420
                  ....*....|....*....|....*...
gi 1937369814 368 ELRRRGGKYAVGSACIGGGQGISLIIQN 395
Cdd:PRK08170  398 ALKRRGTKRGIAAICIGGGQGGAMLLER 425
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
4-395 3.07e-110

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 328.60  E-value: 3.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFGAYGGllKD-----FTATDLTEFAA---RAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGL 75
Cdd:PRK06445    1 LEDVYLVDFARTAFSRFRP--KDpqkdvFNNIRPEELAAmliNRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  76 RVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSP-YSVRNVRFGTKFGLDLKLEDTlwagltD 154
Cdd:PRK06445   79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmGDNPHIEPNPKLLTDPKYIEY------D 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 155 QHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQK 234
Cdd:PRK06445  153 LTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 235 LPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDM 314
Cdd:PRK06445  233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 315 DLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06445  313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392

                  .
gi 1937369814 395 N 395
Cdd:PRK06445  393 R 393
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
7-266 1.51e-109

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


Pssm-ID: 459676 [Multi-domain]  Cd Length: 260  Bit Score: 321.94  E-value: 1.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETGAL 86
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQN-PARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTA 165
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKEGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
                         250       260
                  ....*....|....*....|.
gi 1937369814 246 TAGNASGMSDGAGVVIIASED 266
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
5-394 4.59e-108

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 322.69  E-value: 4.59e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK08947    2 EDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrFGTKFGLDLKLEDTLWAGLtdqhvklpMG 162
Cdd:PRK08947   82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMN-----HGVDFHPGLSKNVAKAAGM--------MG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 163 MTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKG-KQTMQVDEHARPQTTLEQLQKLPPVFK- 240
Cdd:PRK08947  149 LTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAFDp 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 241 KEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PRK08947  229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369814 321 EAFAPQFLAVQKSLDLDPS---KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08947  309 EAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
4-388 3.19e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 318.23  E-value: 3.19e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTE 82
Cdd:PRK07661    1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  83 TGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKfgldlkledtlwagLTDQHVKLPMG 162
Cdd:PRK07661   81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPR--------------LVEAAPEYYMG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 163 M--TAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEV---------KTKKGKQTMQVDEHARPQTTLEQ 231
Cdd:PRK07661  147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennKLQEETITFSQDEGVRADTTLEI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 232 LQKLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSL 311
Cdd:PRK07661  227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369814 312 KDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK07661  307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
5-394 6.42e-106

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 317.81  E-value: 6.42e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   5 RGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETG 84
Cdd:PLN02644    1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQA-PARQAALGAGLPPSTI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFG----LDLKLEDTLWAGLTDQHvklp 160
Cdd:PLN02644   80 CTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGhdtvVDGMLKDGLWDVYNDFG---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARP-QTTLEQLQKLPPVF 239
Cdd:PLN02644  156 MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIVDKDEGLgKFDPAKLRKLRPSF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 240 KKE-GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLID 318
Cdd:PLN02644  236 KEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYE 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369814 319 VNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PLN02644  316 INEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVE 391
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
8-394 1.27e-105

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 316.65  E-value: 1.27e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK07801    5 YIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvRNVRFGTKFGLDLKL-EDTLW-AGLTDQHVKLPMGmtA 165
Cdd:PRK07801   85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIS-SAMTAGEQLGFTSPFaESKGWlHRYGDQEVSQFRG--A 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTkkgkqtmqVDEHARpQTTLEQLQKLPPVFKkEGTV 245
Cdd:PRK07801  162 ELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGGVT--------VDEGPR-ETSLEKMAGLKPLVE-GGRL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:PRK07801  232 TAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAP 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369814 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK07801  312 VVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
7-388 1.31e-100

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 305.92  E-value: 1.31e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPF-GAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:PLN02287   48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPV 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNvRFGTKFGLDLKLEDTLwagltdqhvkLPMGMTA 165
Cdd:PLN02287  128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEG-GVNPRVESFSQAQDCL----------LPMGITS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ------TMQVDEHARPQTTLEQLQKLPPVF 239
Cdd:PLN02287  197 ENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDPKTgeekpiVISVDDGIRPNTTLADLAKLKPVF 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 240 KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PLN02287  277 KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEI 356
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369814 320 NEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRG--GKYAVGSACIGGGQG 388
Cdd:PLN02287  357 NEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMG 427
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
9-394 1.72e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 293.83  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSagKVP---PETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK07851    6 IVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALD--KVPaldPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYDFLPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 AlTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQ-------SPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQH- 156
Cdd:PRK07851   84 T-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRfakgnsdSLPDTKNPLFAEAQARTAARAEGGAEAWHDPRe 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 157 ------VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKqTMQVDEHARPQTTLE 230
Cdd:PRK07851  163 dgllpdVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDGT-VVSTDDGPRAGTTYE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 231 QLQKLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLS 310
Cdd:PRK07851  240 KVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 311 LKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIS 390
Cdd:PRK07851  320 IDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMA 399

                  ....
gi 1937369814 391 LIIQ 394
Cdd:PRK07851  400 MVLE 403
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
7-394 5.72e-95

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: 289.53  E-value: 5.72e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAG-KVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:TIGR02445   2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARNpKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSvrnvrFGTKFGLDLKLEDTLWAGLtdqhvklpMGMT 164
Cdd:TIGR02445  82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMM-----HGVDFHPGMSLHVAKAAGM--------MGLT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGK-QTMQVDEHARPQTTLEQLQKLPPVFK-KE 242
Cdd:TIGR02445 149 AEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEVIRPETTVESLAALRPAFDpKN 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 243 GTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:TIGR02445 229 GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369814 323 FAPQFLAVQKSL---DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:TIGR02445 309 FAAQALPCLKDLgllDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
8-394 1.02e-94

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 289.09  E-value: 1.02e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFG--AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:PRK08242    5 YIYDAVRTPRGkgKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETVPG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPysvrnvrFGTKFGLdlkledtlWAglTDQHVKL-----P 160
Cdd:PRK08242   85 VQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-------MGSDGGA--------WA--MDPSTNFptyfvP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 161 MGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFK 240
Cdd:PRK08242  148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 241 KEGTV---------------------TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPA 299
Cdd:PRK08242  226 MMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 300 ITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK08242  306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
                         410
                  ....*....|....*
gi 1937369814 380 SACIGGGQGISLIIQ 394
Cdd:PRK08242  386 TLCVGGGMGIATIIE 400
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
9-388 1.11e-93

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 286.28  E-value: 1.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFG-AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK07108    6 IVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVPGMT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspySVRNvrfgtkfGLDLKLEDTLWAGLTDQHVKLPMGMTAEN 167
Cdd:PRK07108   86 VNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQN-------EMNRHMLREGWLVEHKPEIYWSMLQTAEN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQ----------TMQVDEHARPQTTLEQLQKLPP 237
Cdd:PRK07108  155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkevTVSADEGIRPDTTLEGVSKIRS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 238 VFKKeGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLI 317
Cdd:PRK07108  235 ALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369814 318 DVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQG 388
Cdd:PRK07108  314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQG 384
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
8-394 5.97e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 279.31  E-value: 5.97e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALT 87
Cdd:PRK06504    5 YIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  88 LNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrNVRFGTKFGLDLKLEDTLWAGLTDqhVKLPMGMTAEN 167
Cdd:PRK06504   85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS-PSTLPAKNGLGHYKSPGMEERYPG--IQFSQFTGAEM 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 168 LAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTM-QVDEHARPQTTLEQLQKLPPVfKKEGTVT 246
Cdd:PRK06504  162 MAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKLI-AEGGRLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 247 AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQ 326
Cdd:PRK06504  241 AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASV 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 327 FLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06504  321 PLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
4-394 1.91e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 278.05  E-value: 1.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQS---SSDAAYLARHVGLrvgvP 80
Cdd:PRK06366    1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAgvgQNPAGQAAYHAGL----P 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  81 TETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRFGTKFGL--DLKLEDTLWA-GLTDQH 156
Cdd:PRK06366   77 FGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpSDLRWGPKHLLhkNYKIDDAMLVdGLIDAF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 157 VKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEvktkkgkqTMQVDEHARpQTTLEQLQKLP 236
Cdd:PRK06366  157 YFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIR-KTTMEDLAKLP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 237 PVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDL 316
Cdd:PRK06366  228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369814 317 IDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06366  308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
7-394 1.45e-87

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 270.61  E-value: 1.45e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAyLARHVGLRVGVPTETGAL 86
Cdd:PRK06954    9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQA-PARQAALGAGLPLSVGCT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVK-LPMGMTA 165
Cdd:PRK06954   88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKgRLMGTFA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARpQTTLEQLQKLPPVFKKEGTV 245
Cdd:PRK06954  168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTV 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 246 TAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP 325
Cdd:PRK06954  247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369814 326 QFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06954  327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
9-394 3.63e-80

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 250.45  E-value: 3.63e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAaLSAGKvpPETIDSVIVGNVMQSSSDaayLARHVGLRVGVPTETGALTL 88
Cdd:PRK06690    5 IVEAKRTPIGKKNGMLKDYEVQQLAAPLLTF-LSKGM--EREIDDVILGNVVGPGGN---VARLSALEAGLGLHIPGVTI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  89 NRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRnVRFGTKfgldlkledtlWAGLTDqhvklpMGMTAENL 168
Cdd:PRK06690   79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNR-ARFSPE-----------TIGDPD------MGVAAEYV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 169 AAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEvktkkgkqtMQVDEHARPQTTLEQL-QKLPPVFKKEGTVTA 247
Cdd:PRK06690  141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN---------GLLDESIKKEMNYERIiKRTKPAFLHNGTVTA 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 248 GNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQF 327
Cdd:PRK06690  212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369814 328 LAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK06690  292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
7-394 8.14e-79

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 249.13  E-value: 8.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSsDAAYLARHVGLRVGVPTETGAL 86
Cdd:PRK08963    7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMP-EAPNIAREIVLGTGMNVHTDAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  87 TLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV--------RNVRFGTKFGLDLKLEDTLWA-------- 150
Cdd:PRK08963   86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskklaralVDLNKARTLGQRLKLFSRLRLrdllpvpp 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 151 GLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMapIEVKTKKGKQTMQVDEHARPQTTLE 230
Cdd:PRK08963  166 AVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPPYKQPLEEDNNIRGDSTLE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 231 QLQKLPPVF-KKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAI-MGIGPVPAITGALKKAG 308
Cdd:PRK08963  244 DYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAYATPLALERAG 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 309 LSLKDMDLIDVNEAFAPQFLAVQKSL-----------------DLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRR 371
Cdd:PRK08963  324 LTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
                         410       420
                  ....*....|....*....|...
gi 1937369814 372 RGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK08963  404 RGGGLGLTTACAAGGLGAAMVLE 426
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
9-394 8.34e-76

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 240.01  E-value: 8.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   9 IVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTL 88
Cdd:PRK07850    6 IVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGATTI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  89 NRLCGSGFQS--IVSGCqeICSKDAEVVLCGGTESMSQSPysvrnvrFGTKFGLDLkleDTLWAGltDQHVKLPMGMT-A 165
Cdd:PRK07850   86 DCQCGSAQQAnhLVAGL--IAAGAIDVGIACGVEAMSRVP-------LGANAGPGR---GLPRPD--SWDIDMPNQFEaA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIE--VKTKKGKQTMQVDEHARPQ----TTLEQLQKLPPVF 239
Cdd:PRK07850  152 ERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTGETRLVTRDQglrdTTMEGLAGLKPVL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 240 KkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDV 319
Cdd:PRK07850  232 E-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEI 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369814 320 NEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK07850  311 NEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
8-394 9.50e-70

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 225.42  E-value: 9.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   8 FIVAAKRTPFG---AYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETG 84
Cdd:PRK06025    5 YIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIKAS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  85 ALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMT 164
Cdd:PRK06025   85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMS---YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQSHQGVC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 165 AENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPieVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKK--- 241
Cdd:PRK06025  162 GDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiad 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 242 ----EGTVT-------------------AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVP 298
Cdd:PRK06025  240 ypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 299 AITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAV 378
Cdd:PRK06025  320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGL 399
                         410
                  ....*....|....*.
gi 1937369814 379 GSACIGGGQGISLIIQ 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 1.69e-64

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: 201.72  E-value: 1.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 273 FTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSKTNVSGGAIALGH 352
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937369814 353 PLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
10-394 4.90e-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: 210.04  E-value: 4.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  10 VAAKRTPFGAYGGLLKDFtATDLTEFAARAALSAGKVP----PETIDSVIVGNVMqSSSDAAYLARHVGLRVGVPTETGA 85
Cdd:cd00826     1 AGAAMTAFGKFGGENGAD-ANDLAHEAGAKAIAAALEPagvaAGAVEEACLGQVL-GAGEGQNCAQQAAMHAGGLQEAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  86 LTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSqspYSVRNVrfgtkfgldlkledtlwagltdqhvklPMGMTA 165
Cdd:cd00826    79 IGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME---TSAENN---------------------------AKEKHI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 166 ENLAAKYNiSREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQT--TLEQLQKLPPVFKKEG 243
Cdd:cd00826   129 DVLINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPAFDKED 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 244 TVTAGNASGMSDGAGVVIIASEDAVKKHNFT-------PLARVVGYFVSGCDPA----IMGIGPVPAITGALKKAGLSLK 312
Cdd:cd00826   208 FLTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIG 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 313 DMDLIDVNEAFAPQFLAVQKSLDLDP------------------SKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGG 374
Cdd:cd00826   288 DLDLIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFELKGEAG 367
                         410       420
                  ....*....|....*....|....*
gi 1937369814 375 KYAVGSA-----CIGGGQGISLIIQ 394
Cdd:cd00826   368 KRQGAGAglallCIGGGGGAAMCIE 392
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-394 1.30e-58

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 196.66  E-value: 1.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   1 MALLRGVFIVAAKRTPFGAYGGLLKD------FTATdLTEFAARAALsAGkvppETIDSVIVGNVMQSSSDAAyLARHVG 74
Cdd:PRK09268    3 MPTVRRVAILGGNRIPFARSNGAYADasnqdmLTAA-LDGLVDRFGL-QG----ERLGEVVAGAVLKHSRDFN-LTRECV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  75 LRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSV-RNVRfgtKFGLDLKLEDT------ 147
Cdd:PRK09268   76 LGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVnEGLR---KILLELNRAKTtgdrlk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 148 LWAGLTDQHVK------------LPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKkgkq 215
Cdd:PRK09268  153 ALGKLRPKHLApeiprngeprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR---- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 216 tmqvDEHARPQTTLEQLQKLPPVFKK--EGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGY------FVSGC 287
Cdd:PRK09268  229 ----DNNLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAetaavdFVHGK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 288 DPAIMGigPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKS------------LD-----LDPSKTNVSGGAIAL 350
Cdd:PRK09268  305 EGLLMA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSLAA 382
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1937369814 351 GHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGISLIIQ 394
Cdd:PRK09268  383 GHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
15-392 5.54e-25

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: 104.65  E-value: 5.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  15 TPFGAYGGLlkdfTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSD---AAYLARHVGLRVGVPTETGALtlnrl 91
Cdd:cd00829     6 TPFGRRSDR----SPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQsfpGALIAEYLGLLGKPATRVEAA----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  92 CGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrnvrfgTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAK 171
Cdd:cd00829    77 GASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGD------EAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 172 YNISREDCDRYALQsQQRWKAANEAGYFNEEMapievktkkgkqtmqvdeharpqtTLEQLQKLPPVFkkeGTVTAGNAS 251
Cdd:cd00829   151 YGTTREDLAKVAVK-NHRNAARNPYAQFRKPI------------------------TVEDVLNSRMIA---DPLRLLDCC 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 252 GMSDGAGVVIIASEDAVKKHnFTPLARVVG-------YFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFA 324
Cdd:cd00829   203 PVSDGAAAVVLASEERAREL-TDRPVWILGvgaasdtPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFT 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 325 P---------QFLAVQKSLDLDPS---------KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGG 386
Cdd:cd00829   282 IaellaledlGFCEKGEGGKLVREgdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLA 361

                  ....*.
gi 1937369814 387 QGISLI 392
Cdd:cd00829   362 HNIGGT 367
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
247-393 1.87e-21

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: 92.51  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 247 AGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCD----PAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEA 322
Cdd:cd00327    94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 323 FAPQFLAVQKSLDLDPSK---TNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKY-------AVGSACIGGGQGISLI 392
Cdd:cd00327   174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253

                  .
gi 1937369814 393 I 393
Cdd:cd00327   254 L 254
PRK06064 PRK06064
thiolase domain-containing protein;
4-388 5.18e-16

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 78.79  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   4 LRGVFIVAAKRTPFGAygglLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSD--AAYLARHVGLRvG 78
Cdd:PRK06064    1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMsagLFVSQEhiAALIADYAGLA-P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  79 VPTetgaltlNRL---CGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVrNVRFGTKFGldlkleDTLWAGLtdq 155
Cdd:PRK06064   76 IPA-------TRVeaaCASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPD-ATEAIARAG------DYEWEEF--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 156 hvklpMGMTAENLAAKynISREDCDRYalqsqqrwkaaneaGYFNEEMAPIEVKTKKgKQTMQVDEHARPQTTLEQLQKL 235
Cdd:PRK06064  139 -----FGATFPGLYAL--IARRYMHKY--------------GTTEEDLALVAVKNHY-NGSKNPYAQFQKEITVEQVLNS 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 236 PPVfkkEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPL-----ARVVGYFVSGCDPAIMGIGP-VPAITGALKKAGL 309
Cdd:PRK06064  197 PPV---ADPLKLLDCSPITDGAAAVILASEEKAKEYTDTPVwikasGQASDTIALHDRKDFTTLDAaVVAAEKAYKMAGI 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 310 SLKDMDLIDVNEAFA-PQFLAVQkslDLDPSK--------------------TNVSGGAIALGHPLGGSGSRITAHLVHE 368
Cdd:PRK06064  274 EPKDIDVAEVHDCFTiAEILAYE---DLGFAKkgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQ 350
                         410       420
                  ....*....|....*....|....*..
gi 1937369814 369 LRRR--GGKYAVGSACIG-----GGQG 388
Cdd:PRK06064  351 LRGEaeKGRQQVIGAGYGlthnvGGTG 377
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
31-381 7.49e-12

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 66.25  E-value: 7.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  31 DLTEFAARAALSAGKVPPETIDSVIVGNVmqsssdAAYLARHVGLRVGVPTE-------TGALTLNRLCGSGFQSIVSGC 103
Cdd:PRK06289   28 DLTREVVDGTLAAAGVDADDIEVVHVGNF------FGELFAGQGHLGAMPATvhpalwgVPASRHEAACASGSVATLAAM 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 104 QEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTkfgldlkledTLWAGLTDQHVKLPMGMTAENLAAKYNisredcDRYA 183
Cdd:PRK06289  102 ADLRAGRYDVALVVGVELMKTVPGDVAAEHLGA----------AAWTGHEGQDARFPWPSMFARVADEYD------RRYG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 184 LQSQqRWKAANEAGYFNEEMAPievktkkGKQTMQ---VDEHARPQTTLEqlqklPPVfkkEGTVTAGNASGMSDGAGVV 260
Cdd:PRK06289  166 LDEE-HLRAIAEINFANARRNP-------NAQTRGwafPDEATNDDDATN-----PVV---EGRLRRQDCSQVTDGGAGV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 261 IIASEDAVKKH-NFTPLARVVGYfvsGCDPAIMGIGP-----------VP----AITGALKKAGLSLKDMDLIDVNEAFA 324
Cdd:PRK06289  230 VLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQkldrsagdpyvLPhvrqAVLDAYRRAGVGLDDLDGFEVHDCFT 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369814 325 P-QFLAVQK----------------SLDLDPSK-TNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK06289  307 PsEYLAIDHigltgpgeswkaiengEIAIGGRLpINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTAGDYQVEGA 381
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
253-358 6.02e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 60.57  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:PRK07314  230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMT-GDayhmtaPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpa 308
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937369814 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSGGAIALGHPLGGSG 358
Cdd:PRK07314  309 gDKAET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
253-359 1.06e-08

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


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 56.64  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:COG0304   229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGAS-SDayhitaPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstpl 307
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937369814 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSggAI--ALGHPLGGSGS 359
Cdd:COG0304   308 gDAAET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
253-359 2.04e-07

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 52.54  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLI--------- 317
Cdd:cd00834   229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDayhitaPDPDGEGAARAMRAALADAGLSPEDIDYInahgtstpl 307
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937369814 318 -DVNEAfapqfLAVQKSLDLDPSKTNVSG--GAIalGHPLGGSGS 359
Cdd:cd00834   308 nDAAES-----KAIKRVFGEHAKKVPVSStkSMT--GHLLGAAGA 345
PRK08256 PRK08256
lipid-transfer protein; Provisional
224-381 2.30e-06

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 49.13  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 224 RPQTTLEQLQKLPPVFkkeGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGY-----FVSGCDP--AIMGIG- 295
Cdd:PRK08256  187 RDEYTLEDVLASPMIW---GPLTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQamttdTPSTFDGrsMIDLVGy 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 296 --PVPAITGALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPSK------------------TNVSGGAIALGHPLG 355
Cdd:PRK08256  264 dmTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLG 343
                         170       180
                  ....*....|....*....|....*.
gi 1937369814 356 GSGSRITAHLVHELRRRGGKYAVGSA 381
Cdd:PRK08256  344 ATGLAQCAELTWQLRGTAGARQVEGA 369
PRK06066 PRK06066
thiolase domain-containing protein;
197-379 2.42e-06

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 49.36  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 197 GYFNEEMAPIEVKTKKGKQTMQVDEHARPqTTLEQLQKLPPVFKKegtVTAGNASGMSDGAGVVIIASEDAVKKHNFTPL 276
Cdd:PRK06066  158 GITREDLALVVEKNKKAGLSNPRASYASN-ISLEDVLSSEYVVYP---LTELDIAPFVDGAIVVVLASEEVAKKLTDDPV 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 277 -ARVVGYFVSGCDPAIMGIGPVP----AITGALKKAGLS--LKDMDLIDVNEAF-------------APQFLAVQ--KSL 334
Cdd:PRK06066  234 wIKGIGWSTESSNLETAELGKANymriAADMAYKMAGIEspRKEVDAAEVDDRYsykelqhiealrlSEEPEKDSllREG 313
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1937369814 335 DLDPS---KTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVG 379
Cdd:PRK06066  314 NFDPQgelPVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGARQGK 361
PRK07516 PRK07516
thiolase domain-containing protein;
7-358 1.17e-05

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 46.86  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814   7 VFIVAAKRTPFGAygglLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSDAAYLARHV--GLRvGVPt 81
Cdd:PRK07516    4 ASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFnagFSPQDFPASLVLQAdpALR-FKP- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  82 etgALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPysvrnvrfGTKFGLDLkledtLWAGLTDQHVKLPM 161
Cdd:PRK07516   78 ---ATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP--------TAEVGDIL-----LGASYLKEEGDTPG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 162 GMTA--ENLAAKYNisredcDRYALQSqqrwkaaneagyfnEEMAPIEVKTKKgkqtmqvDEHARPqttLEQLQK-LPPV 238
Cdd:PRK07516  142 GFAGvfGRIAQAYF------QRYGDQS--------------DALAMIAAKNHA-------NGVANP---YAQMRKdLGFE 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 239 FKKegTVTAGN-----------ASGMSDGAGVVIIASED----AVKKHNFTPLARVVGYF-VSGCDPAIMGiGPVPAITG 302
Cdd:PRK07516  192 FCR--TVSEKNplvagplrrtdCSLVSDGAAALVLADAEtaraLQRAVRFRARAHVNDFLpLSRRDPLAFE-GPRRAWQR 268
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369814 303 ALKKAGLSLKDMDLIDVNEAFAPQFLAVQKSLDLDPS------------------KTNVSGGAIALGHPLGGSG 358
Cdd:PRK07516  269 ALAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG 342
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
253-358 1.68e-04

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 43.45  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAGLSLKDMDLIDVNEAFAP- 325
Cdd:PRK06333  242 MGEGAGILVIETLEHALARGAPPLAELVGYGTS-ADayhmtaGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPv 320
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1937369814 326 ----QFLAVqKSLDLDPSKTNVSGGAIALGHPLGGSG 358
Cdd:PRK06333  321 gdlgEVAAI-KKVFGHVSGLAVSSTKSATGHLLGAAG 356
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
25-124 3.06e-04

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 42.40  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814  25 KDFTATDLTEFAARAALSAGKVPPETIDSVIVGNV---MQSSSDAAYLARHVGLRvgvptETGALTLNRLCgSGF-QSIV 100
Cdd:COG0332    47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVtpdYLFPSTACLVQHKLGAK-----NAAAFDINAAC-SGFvYALS 120
                          90       100
                  ....*....|....*....|....
gi 1937369814 101 SGCQEICSKDAEVVLCGGTESMSQ 124
Cdd:COG0332   121 VAAALIRSGQAKNVLVVGAETLSR 144
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
251-395 5.73e-04

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 41.80  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 251 SGMSDGAGVVIIASEDAVKKHNFTP----------LARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN 320
Cdd:PTZ00455  256 SQVSDGGAGLVLASEEGLQKMGLSPndsrlveiksLACASGNLYEDPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 321 EAFAPQFLAVQKSLDL-DPSKT-----------------NVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKY------ 376
Cdd:PTZ00455  336 DCFTIAELLMYEALGIaEYGHAkdlirngatalegripvNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYqmknip 415
                         170       180
                  ....*....|....*....|..
gi 1937369814 377 AVGSACIGGGQ---GISLIIQN 395
Cdd:PTZ00455  416 ALGATLNMGGDdktAVSTVLQN 437
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
246-366 4.17e-03

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


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 38.96  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 246 TAGNASG--MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGcDPAIMGI-----GPVPAITGALKKAGLSLKDMDLI- 317
Cdd:cd00828   220 FDETRDGfvEAEGAGVLVLERAELALARGAPIYGRVAGTASTT-DGAGRSVpaggkGIARAIRTALAKAGLSLDDLDVIs 298
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 318 ---------DVNEAFApqFLAVQKSLDLDPSKTNVSGGaiaLGHPLGGSG--SRITAHLV 366
Cdd:cd00828   299 ahgtstpanDVAESRA--IAEVAGALGAPLPVTAQKAL---FGHSKGAAGalQLIGALQS 353
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
253-359 6.64e-03

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 38.52  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 253 MSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSgCD------PAIMGIGPVPAITGALKKAG-LSLKDMDLIDVNEAFAP 325
Cdd:PTZ00050  237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSS-SDahhitaPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937369814 326 -----QFLAVQKSL-DLDPSKTNVSGGAIALGHPLGGSGS 359
Cdd:PTZ00050  316 igdkiELKAIKKVFgDSGAPKLYVSSTKGGLGHLLGAAGA 355
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
255-370 7.16e-03

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: 38.00  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369814 255 DGAGVVIIASEDAVKKHNFTPLARVVGYfVSGCDPAIMGI------GPVPAITGALKKAGLSLKDMDLIDVNEAFAPQFL 328
Cdd:cd00825   161 DGAGALVVEELEHALARGAHIYAEIVGT-AATIDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937369814 329 AVQKSLDLD---PSKTNVSGGAIALGHPLGGSGSRITAHLVHELR 370
Cdd:cd00825   240 VKELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH