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Conserved domains on  [gi|1958797581|ref|XP_038937924|]
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3-ketoacyl-CoA thiolase B, peroxisomal isoform X1 [Rattus norvegicus]

Protein Classification

3-ketoacyl-CoA thiolase( domain architecture ID 1004030)

3-ketoacyl-CoA thiolase is responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02287 super family cl30635
3-ketoacyl-CoA thiolase
1-333 5.54e-156

3-ketoacyl-CoA thiolase


The actual alignment was detected with superfamily member PLN02287:

Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 446.13  E-value: 5.54e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581   1 MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASAS------DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287    5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  75 DVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287   85 KTGLNPSEVGDIVVGTVLAPGSQRANEcRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 154 TLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDD 233
Cdd:PLN02287  165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 234 K-GDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 312
Cdd:PLN02287  245 KtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGV 324
                         330       340
                  ....*....|....*....|.
gi 1958797581 313 PPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02287  325 DPAVMGIGPAVAIPAAVKAAG 345
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-333 5.54e-156

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 446.13  E-value: 5.54e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581   1 MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASAS------DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287    5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  75 DVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287   85 KTGLNPSEVGDIVVGTVLAPGSQRANEcRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 154 TLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDD 233
Cdd:PLN02287  165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 234 K-GDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 312
Cdd:PLN02287  245 KtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGV 324
                         330       340
                  ....*....|....*....|.
gi 1958797581 313 PPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02287  325 DPAVMGIGPAVAIPAAVKAAG 345
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
39-333 5.40e-135

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: 390.30  E-value: 5.40e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:cd00751     1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEK----------ARDCLIPMGITSENV 188
Cdd:cd00751    80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTldgmlddgltDPFTGLSMGITAENV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:cd00751   160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:cd00751   235 TVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAG 299
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
36-333 1.89e-122

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: 358.61  E-value: 1.89e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:COG0183     2 REVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------ERGNPGNISSRLLENEKARDCLIPMGITS 185
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFK 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:COG0183   236 KDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAG 303
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
40-333 2.75e-113

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: 335.35  E-value: 2.75e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  40 VVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAV 119
Cdd:TIGR01930   1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSERGNPGNISSRLLENEKAR-------DCLIPMGITSENV 188
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSrvpyGVPRSLRWGVKPGNAELEDARlkdltdaNTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttvldDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVT-----VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAG 299
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
38-291 9.33e-104

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: 306.15  E-value: 9.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  38 VVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:pfam00108   1 VVIVSAARTPFGSFG-GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGN-ISSRLLENEKARDCLIP-----------MGITS 185
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGdrktiTVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-----TVDKDEGIRPPTTAEPLAKLKPAFD 234
                         250       260
                  ....*....|....*....|....*.
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRS 291
Cdd:pfam00108 235 KEGTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-333 5.54e-156

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 446.13  E-value: 5.54e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581   1 MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASAS------DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQ 74
Cdd:PLN02287    5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  75 DVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287   85 KTGLNPSEVGDIVVGTVLAPGSQRANEcRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 154 TLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDD 233
Cdd:PLN02287  165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 234 K-GDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 312
Cdd:PLN02287  245 KtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGV 324
                         330       340
                  ....*....|....*....|.
gi 1958797581 313 PPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02287  325 DPAVMGIGPAVAIPAAVKAAG 345
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
39-333 5.40e-135

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: 390.30  E-value: 5.40e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:cd00751     1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEK----------ARDCLIPMGITSENV 188
Cdd:cd00751    80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTldgmlddgltDPFTGLSMGITAENV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:cd00751   160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:cd00751   235 TVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAG 299
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
36-333 1.89e-122

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: 358.61  E-value: 1.89e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:COG0183     2 REVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLS----------ERGNPGNISSRLLENEKARDCLIPMGITS 185
Cdd:COG0183    81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApmllpkarwgYRMNAKLVDPMINPGLTDPYTGLSMGETA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:COG0183   161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFK 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:COG0183   236 KDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAG 303
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
40-333 2.75e-113

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: 335.35  E-value: 2.75e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  40 VVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAV 119
Cdd:TIGR01930   1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT----LSERGNPGNISSRLLENEKAR-------DCLIPMGITSENV 188
Cdd:TIGR01930  80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSrvpyGVPRSLRWGVKPGNAELEDARlkdltdaNTGLPMGVTAENL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 189 AERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttvldDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVT-----VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDG 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAG 299
PRK05790 PRK05790
putative acyltransferase; Provisional
36-333 7.15e-109

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 324.03  E-value: 7.15e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:PRK05790    2 KDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGIT 184
Cdd:PRK05790   81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIhdgltdafngyHMGIT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAF 264
Cdd:PRK05790  161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVT--IKQRKGD--PVVVDTDEHPRPDTTAESLAKLRPAF 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK05790  237 DKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAG 305
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
38-291 9.33e-104

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: 306.15  E-value: 9.33e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  38 VVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:pfam00108   1 VVIVSAARTPFGSFG-GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGN-ISSRLLENEKARDCLIP-----------MGITS 185
Cdd:pfam00108  80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGdrktiTVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-----TVDKDEGIRPPTTAEPLAKLKPAFD 234
                         250       260
                  ....*....|....*....|....*.
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRS 291
Cdd:pfam00108 235 KEGTVTAGNASPINDGAAAVLLMSES 260
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
37-333 4.37e-95

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 289.21  E-value: 4.37e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVK-LKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETV 114
Cdd:PRK09052    7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPNSV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE-RGNPGNISSRLLENEKARDCLIPMGITSENVAERFG 193
Cdd:PRK09052   87 GGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmMGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQWK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVP--VTTTVLDDKG---DRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGG 268
Cdd:PRK09052  167 VSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERFPDLATgevDVKTRTVDLDEGPRADTSLEGLAKLKPVFANKG 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09052  247 SVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAG 311
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
39-333 6.25e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 270.47  E-value: 6.25e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLqPGA--GAAMARIAQFLSGIPETVPL 116
Cdd:PRK07661    5 VIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAM-PEAeqGLNMARNIGALAGLPYTVPA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGnpGNI---SSRLLENekARDCLIPMGITSENVAERFG 193
Cdd:PRK07661   84 ITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--GHVvrpNPRLVEA--APEYYMGMGHTAEQVAVKYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVL----DDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGS 269
Cdd:PRK07661  160 ISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgeNNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKGS 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07661  240 VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
PRK09051 PRK09051
beta-ketothiolase BktB;
34-333 1.34e-80

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 251.80  E-value: 1.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  34 SASDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPE 112
Cdd:PRK09051    1 MMREVVVVSGVRTAIGTFG-GSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPrDMYLSRVAAINAGVPQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 113 TVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCL----------IPMG 182
Cdd:PRK09051   80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMvgalhdpfgtIHMG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 183 ITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVRPSTTMEGLAKLKP 262
Cdd:PRK09051  160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEI-----KTRKGEVVFDTDEHVRADTTLEDLAKLKP 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958797581 263 AF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09051  235 VFkKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAG 306
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
36-333 1.96e-74

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 236.42  E-value: 1.96e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVP 115
Cdd:PRK06205    2 RDAVICEPVRTPVGRFG-GAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE----------RGNPGNISSRLL---ENEKARDCLIPMG 182
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEfyttdmrwgvRGGGVQLHDRLArgrETAGGRRFPVPGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 183 I--TSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKL 260
Cdd:PRK06205  161 MieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVT--VPQRKGD--PTVVDRDEHPRADTTLESLAKL 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 261 KP--AFKDGGST-TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06205  237 RPimGKQDPEATvTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAG 312
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
37-333 3.38e-71

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 227.68  E-value: 3.38e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAG-----RGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMA-RIAQFLSGI 110
Cdd:PRK06445    3 DVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGgRHPIFLARL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 111 PETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERG-NPG-NISSRLLENEKARDCLIP----MGIT 184
Cdd:PRK06445   83 PYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdNPHiEPNPKLLTDPKYIEYDLTtgyvMGLT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgDRKTITVSQDEGVRPSTTMEGLAKLKPAF 264
Cdd:PRK06445  163 AEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-----EGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06445  238 KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAG 306
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
36-333 2.91e-70

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 225.22  E-value: 2.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQ-DVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPET 113
Cdd:PRK09050    2 TEAFICDAIRTPIGRYG-GALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 114 VPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSergnP---GNISSRLLENEKARDCLI----------- 179
Cdd:PRK09050   81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRA----PfvmGKADSAFSRQAEIFDTTIgwrfvnplmka 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 180 -----PMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrkTITVSQDEGVRPSTTM 254
Cdd:PRK09050  157 qygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPV--TIPQKKGD--PVVVDRDEHPRPETTL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 255 EGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGL-PILGVLrSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK09050  233 EALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLtPRARIL-GMATAGVEPRIMGIGPAPATRKLLARLG 311
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
36-333 4.52e-70

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 224.65  E-value: 4.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETV 114
Cdd:PRK07108    2 TEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGI 194
Cdd:PRK07108   82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRYGI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 195 SRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTT--VLDDKGDR---KTITVSQDEGVRPSTTMEGLAKLKPAFKdGGS 269
Cdd:PRK07108  162 SKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTagVADKATGRlftKEVTVSADEGIRPDTTLEGVSKIRSALP-GGV 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07108  241 ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAG 304
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
37-333 9.33e-68

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 218.68  E-value: 9.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVL-QDVKLKPECLGDISVGNVLQPG-AGAAMARIAQFLSGIPETV 114
Cdd:PRK08947    3 DVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLaRNPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVE-----SMTLSERGNPGnissrlLENEKARDCLIpMGITSENVA 189
Cdd:PRK08947   83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEhmghvPMNHGVDFHPG------LSKNVAKAAGM-MGLTAEMLG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 190 ERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTvlDDKGDRKTITVsqDEGVRPSTTMEGLAKLKPAFKD-GG 268
Cdd:PRK08947  156 KMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGH--DADGVLKLFDY--DEVIRPETTVEALAALRPAFDPvNG 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08947  232 TVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAG 296
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
37-333 6.70e-67

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 216.68  E-value: 6.70e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK05656    3 DVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIP-----------MGITS 185
Cdd:PRK05656   82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITdglwdafndyhMGITA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAFK 265
Cdd:PRK05656  162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIL--IPQRKGE--PLAFATDEQPRAGTTAESLAKLKPAFK 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK05656  238 KDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAG 305
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
38-333 4.77e-61

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 201.41  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  38 VVVVHGRRTPIGRAGrgGFKDTTPDELLSAVLTA-VLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK06633    5 VYITHAKRTAFGSFM--GSLSTTPAPMLAAHLIKdILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSR--------LLENEKARDCL--IPMGITSE 186
Cdd:PRK06633   83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKfgdikmvdLMQYDGLTDVFsgVFMGITAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 187 NVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgDRKTITVSQDEGVRPSTTMEGLAKLKPAFKD 266
Cdd:PRK06633  163 NISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI-----KKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958797581 267 GGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06633  238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAG 304
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
37-333 6.11e-61

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 201.39  E-value: 6.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDV-KLKPECLGDISVGnVLQPG--AGAAMARIAQFLSGIPeT 113
Cdd:PRK07851    3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLG-CGLPGgeQGFNMARVVAVLLGYD-F 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 114 VPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSR---LLENEKAR--------------- 175
Cdd:PRK07851   81 LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLPDTknpLFAEAQARtaaraeggaeawhdp 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 176 -------DCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTT---TVlddkgdrktitVSQD 245
Cdd:PRK07851  161 redgllpDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLpdgTV-----------VSTD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 246 EGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAI 325
Cdd:PRK07851  230 DGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309

                  ....*...
gi 1958797581 326 PAALQKAG 333
Cdd:PRK07851  310 KQALARAG 317
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
37-333 2.05e-60

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 199.55  E-value: 2.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PLN02644    2 DVCIVGVARTPIG-GFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGITS 185
Cdd:PLN02644   81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLkdglwdvyndfGMGVCA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddKGDRKTITVSQDEGVRpSTTMEGLAKLKPAFK 265
Cdd:PLN02644  161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPG---GRGRPSVIVDKDEGLG-KFDPAKLRKLRPSFK 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 266 -DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PLN02644  237 eDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAG 305
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
39-333 5.23e-58

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 193.39  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:PRK08235    5 VIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTET 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLI-----------PMGITSEN 187
Cdd:PRK08235   84 VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVadgltcafsgvHMGVYGGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 188 VAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrkTITVSQDEGVRPSTTMEGLAKLKPAFKDG 267
Cdd:PRK08235  164 VAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPV--TIPQRKGD--PIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 268 GSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08235  240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTG 305
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
39-333 1.05e-57

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 192.24  E-value: 1.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPETVPLS 117
Cdd:PRK07850    5 VIVEAVRTPIGKRN-GWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGAT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL--------SERGNPgnissrlleneKARDCLIPMG---ITSE 186
Cdd:PRK07850   84 TIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRvplganagPGRGLP-----------RPDSWDIDMPnqfEAAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 187 NVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDR--KTITVSQDEGVRpSTTMEGLAKLKPAF 264
Cdd:PRK07850  153 RIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPtgETRLVTRDQGLR-DTTMEGLAGLKPVL 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 kDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07850  232 -EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAG 299
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
45-333 4.64e-56

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 188.55  E-value: 4.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  45 RTPIGRAGRGG-FKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPG-AGAAMARIAQFLSGIPETVPLSAVNRQ 122
Cdd:PRK08242   11 RTPRGKGKKDGsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRF 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPG---------NISSRllenekardcLIPMGITSENVAERFG 193
Cdd:PRK08242   91 CASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGgawamdpstNFPTY----------FVPQGISADLIATKYG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 194 ISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTT----TVLDdkgdrktitvsQDEGVRPSTTMEGLAKLKPAFKDGGS 269
Cdd:PRK08242  161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDqnglTILD-----------HDEHMRPGTTMESLAKLKPSFAMMGE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 270 T---------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAA 328
Cdd:PRK08242  230 MggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKA 309

                  ....*
gi 1958797581 329 LQKAG 333
Cdd:PRK08242  310 LAKAG 314
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
37-333 1.89e-55

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 186.91  E-value: 1.89e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAA-MARIAQFLSGIPETVP 115
Cdd:PRK08131    3 DAYIYDGLRSPFGRHA-GALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRnVARNALLLAGLPVTVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 116 LSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE--RGNPGNISSRLLeneKARDCLI-------------- 179
Cdd:PRK08131   82 GQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKAESAFSRDA---KVFDTTIgarfpnpkivaqyg 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 180 --PMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKtitVSQDEGVRPSTTMEGL 257
Cdd:PRK08131  159 ndSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLPPKL---VAEDEHPRPSSTVEAL 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958797581 258 AKLKPAFkDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK08131  236 TKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
38-333 2.67e-55

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 187.11  E-value: 2.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  38 VVVVHGRRTPIGRAGRGgFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:PRK08963    7 IAIVSGLRTPFAKQATA-FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDC--------------LIP--- 180
Cdd:PRK08963   86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLgqrlklfsrlrlrdLLPvpp 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 ----------MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEivpVTTTVLDDKGDrktiTVSQDEGVRP 250
Cdd:PRK08963  166 avaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE---VMTAHVPPYKQ----PLEEDNNIRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 251 STTMEGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPP-DIMGIGPAYAIPAA 328
Cdd:PRK08963  239 DSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLA 318

                  ....*
gi 1958797581 329 LQKAG 333
Cdd:PRK08963  319 LERAG 323
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
37-333 3.24e-50

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 173.66  E-value: 3.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAgRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK08170    4 PVYIVDGARTPFLKA-RGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMT-----LSERG--------NPGNISSRLLENEKAR-DCLIP-- 180
Cdd:PRK08170   83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMShapllFSEKMvrwlagwyAAKSIGQKLAALGKLRpSYLAPvi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 --------------MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGcFRAEIVPVTttvlddkgDRKTITVSQDE 246
Cdd:PRK08170  163 gllrgltdpvvglnMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEG-RLKEVVPLF--------DRDGKFYDHDD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 247 GVRPSTTMEGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAI 325
Cdd:PRK08170  234 GVRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAA 313

                  ....*...
gi 1958797581 326 PAALQKAG 333
Cdd:PRK08170  314 TPLLQRHG 321
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
37-333 2.33e-47

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 165.18  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  37 DVVVVHGRRTPIGRAGRGGFKDTTPdELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPL 116
Cdd:PRK06366    3 DVYIVSAKRTAIGKFGRSFSKIKAP-QLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 117 SAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE-------RGNPGNIssrLLENEKARDCLIP--------- 180
Cdd:PRK06366   82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPfllpsdlRWGPKHL---LHKNYKIDDAMLVdglidafyf 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 181 --MGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTttvlddkgdrktiTVSQDEGVRpSTTMEGLA 258
Cdd:PRK06366  159 ehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN-------------DLDRDEGIR-KTTMEDLA 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 259 KLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06366  225 KLPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQN 299
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
40-333 1.93e-44

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 157.58  E-value: 1.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  40 VVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGA-AMARIAQFLSGIPETVPLSA 118
Cdd:PRK06504    6 IVAAARTAGGRKG-GRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQAtNVARNAVLASKLPESVPGTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNP---------GNISSRLLEnEKARDCLIPMGITSENVA 189
Cdd:PRK06504   85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPstlpaknglGHYKSPGME-ERYPGIQFSQFTGAEMMA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 190 ERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTItvsqDEGVRPSTTMEGLAKLKPaFKDGGS 269
Cdd:PRK06504  164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTV----DEGIRFDATLEGIAGVKL-IAEGGR 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06504  239 LTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAG 302
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
39-325 1.37e-42

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 151.84  E-value: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  39 VVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVklkPECLGDISVGNVLqpGAGAAMARIAQFLSGIPETVPLSA 118
Cdd:PRK06690    4 VIVEAKRTPIGKKN-GMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKardclipMGITSENVAERFGISRQK 198
Cdd:PRK06690   78 IDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-------MGVAAEYVAERYNITREM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 199 QDAFALASQQKAASAQSKGCFRAEIVPVTTTVlddkgdrktitvsqDEGVRPSTTMEGL-AKLKPAFKDGGSTTAGNSSQ 277
Cdd:PRK06690  151 QDEYACLSYKRTLQALEKGYIHEEILSFNGLL--------------DESIKKEMNYERIiKRTKPAFLHNGTVTAGNSCG 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958797581 278 VSDGAAAVLLARRSKAEELGL-PILGVLRSyAVVGVPPDIMGIGPAYAI 325
Cdd:PRK06690  217 VNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAV 264
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
38-333 4.70e-42

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 151.58  E-value: 4.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  38 VVVVHGRRTPIGrAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLS 117
Cdd:PRK06954    9 IVIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 118 AVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSE----------RGNPGNISSRLLEN--EKARDCLIPMGITS 185
Cdd:PRK06954   88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmRMGHGQVLDHMFLDglEDAYDKGRLMGTFA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 186 ENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVttTVLDDKGDrktITVSQDEGVRpSTTMEGLAKLKPAFK 265
Cdd:PRK06954  168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPV--TVAGKKGD---TVIDRDEQPF-KANPEKIPTLKPAFS 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958797581 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK06954  242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNG 309
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
36-333 1.62e-41

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 149.47  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAA-MARIAQFLSGIPETV 114
Cdd:PRK07801    2 AEAYIVDAVRTPVGKRK-GGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGnIARTSWLAAGLPEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 115 PLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL----------SERGNPGNISSRLLENEKARDCLIPMGIT 184
Cdd:PRK07801   81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipissamtagEQLGFTSPFAESKGWLHRYGDQEVSQFRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 185 SENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvlddkGDrktitVSQDEGVRpSTTMEGLAKLKPaF 264
Cdd:PRK07801  161 AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GG-----VTVDEGPR-ETSLEKMAGLKP-L 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958797581 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:PRK07801  226 VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTG 294
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
31-333 1.58e-37

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 140.04  E-value: 1.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  31 PQASASDVVVVHGRRTPIGRAGrGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGI 110
Cdd:PRK09268    2 TMPTVRRVAILGGNRIPFARSN-GAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 111 PETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVES-----MTLSE-----------------------RGNPG 162
Cdd:PRK09268   81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTtsdapIAVNEglrkillelnrakttgdrlkalgKLRPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 163 NISSRLLENEKARDCLiPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvlddKGdrktitV 242
Cdd:PRK09268  161 HLAPEIPRNGEPRTGL-SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LG------L 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 243 SQDEGVRPSTTMEGLAKLKPAF--KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVP----PDI 316
Cdd:PRK09268  227 TRDNNLRPDSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEG 306
                         330
                  ....*....|....*..
gi 1958797581 317 MGIGPAYAIPAALQKAG 333
Cdd:PRK09268  307 LLMAPAYAVPRLLARNG 323
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
36-333 2.16e-35

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 133.75  E-value: 2.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  36 SDVVVVHGRRTP--IGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGA-GAAMARIAQFLSGIPE 112
Cdd:PRK06025    2 AEAYIIDAVRTPrgIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 113 TVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTL-----SERGNPGnISSRLLENEKAR-DCLIPM---GI 183
Cdd:PRK06025   82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYtaamaAEDMAAG-KPPLGMGSGNLRlRALHPQshqGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 184 TSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVtttvLDDKGdrkTITVSQDEGVRPSTTMEGLAKLKPA 263
Cdd:PRK06025  161 CGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV----YRDDG---SVALDHEEFPRPQTTAEGLAALKPA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 264 FK--------DGGST------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIM 317
Cdd:PRK06025  234 FTaiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLM 313
                         330
                  ....*....|....*.
gi 1958797581 318 GIGPAYAIPAALQKAG 333
Cdd:PRK06025  314 LNAPVPAAKKVLAKAG 329
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
45-333 5.75e-29

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: 116.05  E-value: 5.75e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  45 RTPIGRAG--RGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQ 122
Cdd:cd00826     5 MTAFGKFGgeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPgnissrlleNEKARDCLIpmgitsenvaERFGiSRQKQDAF 202
Cdd:cd00826    85 CGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNA---------KEKHIDVLI----------NKYG-MRACPDAF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 203 ALASQQKAASAQSKGCFRAEIVPVTTtvlddKGDRKTITVSQDEGVR--PSTTMEGLAKLKPAFKDGGSTTAGNSSQVSD 280
Cdd:cd00826   145 ALAGQAGAEAAEKDGRFKDEFAKFGV-----KGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTAGNACGLND 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958797581 281 GAAAVLLARRSKAEELGLPI-------LGVLRSYAVVGVPPD----IMGIGPAYAIPAALQKAG 333
Cdd:cd00826   220 GAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAG 283
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
298-333 6.62e-12

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: 61.89  E-value: 6.62e-12
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958797581 298 LPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAG 36
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
46-333 4.81e-08

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: 54.19  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  46 TPIGRAGrggfkDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVL-QPGAGAAMARIAQFLSGIPetVPLSAVNRQCS 124
Cdd:cd00829     6 TPFGRRS-----DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAgGRFQSFPGALIAEYLGLLG--KPATRVEAAGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 125 SGLQAVANIAGGIRNGSYDIGMACGVESMtlSERGNPGNISSRLLENEKARDcLIPMGITSENVA--------ERFGISR 196
Cdd:cd00829    79 SGSAAVRAAAAAIASGLADVVLVVGAEKM--SDVPTGDEAGGRASDLEWEGP-EPPGGLTPPALYalaarrymHRYGTTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 197 qkqDAFAL--ASQQKAASAQSKGCFRAEivpvtttvlddkgdrktITVSQDEGVRPSTTmeglaklkPafkdggsTTAGN 274
Cdd:cd00829   156 ---EDLAKvaVKNHRNAARNPYAQFRKP-----------------ITVEDVLNSRMIAD--------P-------LRLLD 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958797581 275 SSQVSDGAAAVLLARRSKAEELGLP---ILGV---LRSYAVVGVPPDIMGIGPAYAIPAALQKAG 333
Cdd:cd00829   201 CCPVSDGAAAVVLASEERARELTDRpvwILGVgaaSDTPSLSERDDFLSLDAARLAARRAYKMAG 265
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
63-297 2.51e-03

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 39.67  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581  63 ELLSAVLTAVLQDVKLKPECLGDISVGNVlqpgAGAAMARIAQfLSGIPETV-------PLSAVNRQCSSGLQAVANIAG 135
Cdd:PRK06289   28 DLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGH-LGAMPATVhpalwgvPASRHEAACASGSVATLAAMA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 136 GIRNGSYDIGMACGVESM-TLSERGNPGNISSRLLENEKARDCLIP----MGITSENVAERFGISRQKQDAFA---LASQ 207
Cdd:PRK06289  103 DLRAGRYDVALVVGVELMkTVPGDVAAEHLGAAAWTGHEGQDARFPwpsmFARVADEYDRRYGLDEEHLRAIAeinFANA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958797581 208 QKAASAQSKGCFraeiVPVTTTVLDDkgdrktitvsqdegvrpsttmeglaKLKPAFkdGGSTTAGNSSQVSDGAAAVLL 287
Cdd:PRK06289  183 RRNPNAQTRGWA----FPDEATNDDD-------------------------ATNPVV--EGRLRRQDCSQVTDGGAGVVL 231
                         250
                  ....*....|
gi 1958797581 288 ARRSKAEELG 297
Cdd:PRK06289  232 ASDAYLRDYA 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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