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Conserved domains on  [gi|446360888|ref|WP_000438743|]
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MULTISPECIES: acetyl-CoA C-acyltransferase FadA [Enterobacteriaceae]

Protein Classification

acetyl-CoA C-acyltransferase FadA( domain architecture ID 11483478)

acetyl-CoA C-acyltransferase FadA catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed

CATH:  3.40.47.10
EC:  2.3.1.16
Gene Ontology:  GO:0006635|GO:0003988
SCOP:  4000245

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-387 0e+00

3-ketoacyl-CoA thiolase; Reviewed


:

Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 831.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGI 160
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 161 SREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSA 240
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 241 LSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIK 320
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446360888 321 DLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK08947 321 DLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
 
Name Accession Description Interval E-value
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-387 0e+00

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 831.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGI 160
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 161 SREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSA 240
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 241 LSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIK 320
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446360888 321 DLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK08947 321 DLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
3-387 0e+00

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: 748.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    3 QVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSV 82
Cdd:TIGR02445   1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISR 162
Cdd:TIGR02445  81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAKAAGMMGLTAEMLGKMHGISR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  163 EMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSALS 242
Cdd:TIGR02445 161 EQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKNGTVTAGTSSALS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  243 DGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDL 322
Cdd:TIGR02445 241 DGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDL 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446360888  323 GLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:TIGR02445 321 GLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-387 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: 533.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAG-LDPEAVDDVILGCVLQA-GQGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM------------SHGVD--FHPGLSRnvAKAAGM 146
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMllpkarwgyrmnAKLVDpmINPGLTD--PYTGLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 147 MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVlKQFNYDEVIRPETTVEALATLRPAF 226
Cdd:COG0183  156 MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 227 DPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFE 306
Cdd:COG0183  235 KK-DGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIE 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 307 MNEAFAAQILPCIKDLGLMeqiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:COG0183  314 INEAFAAQVLAVLRELGLD---PDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390

                 .
gi 446360888 387 V 387
Cdd:COG0183  391 V 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-386 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: 521.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   5 VIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEqGFNIARNAALLAEVPHSVPA 84
Cdd:cd00751    1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  85 VTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNV------------AKAAGMMGLTAE 152
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNtldgmlddgltdPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 153 MLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVlKQFNYDEVIRPETTVEALATLRPAFDPvSGT 232
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPDTTLEKLAKLKPAFKK-DGT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 233 VTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFA 312
Cdd:cd00751  236 VTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFA 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446360888 313 AQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:cd00751  316 AQALACLKELGLDP---EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-254 2.67e-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: 308.08  E-value: 2.67e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPHSVP 83
Cdd:pfam00108   1 VVIVSAARTPFG-SFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQA-GEGQNPARQAALKAGIPDSAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   84 AVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGM--------------MGL 149
Cdd:pfam00108  78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLlipdgltdafngyhMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  150 TAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLkQFNYDEVIRPETTVEALATLRPAFDPV 229
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKE 236
                         250       260
                  ....*....|....*....|....*
gi 446360888  230 sGTVTAGTSSALSDGAAAMLVMSES 254
Cdd:pfam00108 237 -GTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-387 0e+00

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 831.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGI 160
Cdd:PRK08947  81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 161 SREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSA 240
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 241 LSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIK 320
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446360888 321 DLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK08947 321 DLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
3-387 0e+00

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: 748.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    3 QVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSV 82
Cdd:TIGR02445   1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISR 162
Cdd:TIGR02445  81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAKAAGMMGLTAEMLGKMHGISR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  163 EMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSALS 242
Cdd:TIGR02445 161 EQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKNGTVTAGTSSALS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  243 DGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDL 322
Cdd:TIGR02445 241 DGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDL 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446360888  323 GLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:TIGR02445 321 GLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-385 0e+00

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: 536.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    6 IVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEQgFNIARNAALLAEVPHSVPAV 85
Cdd:TIGR01930   1 IVAAARTPIG-KFGGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   86 TVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM----SHGVDFHPGLSRNV---------AKAAGMMGLTAE 152
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYgvprSLRWGVKPGNAELEdarlkdltdANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  153 MLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVlKQFNYDEVIRPETTVEALATLRPAFDPvSGT 232
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGP-VTVSSDEGIRPNTTLEKLAKLKPAFDP-DGT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  233 VTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFA 312
Cdd:TIGR01930 236 VTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFA 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446360888  313 AQILPCIKDLGLmeqIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFE 385
Cdd:TIGR01930 316 AQVLACIKELGL---DLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-387 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: 533.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:COG0183    1 MREVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAG-LDPEAVDDVILGCVLQA-GQGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM------------SHGVD--FHPGLSRnvAKAAGM 146
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMllpkarwgyrmnAKLVDpmINPGLTD--PYTGLS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 147 MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVlKQFNYDEVIRPETTVEALATLRPAF 226
Cdd:COG0183  156 MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 227 DPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFE 306
Cdd:COG0183  235 KK-DGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIE 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 307 MNEAFAAQILPCIKDLGLMeqiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:COG0183  314 INEAFAAQVLAVLRELGLD---PDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390

                 .
gi 446360888 387 V 387
Cdd:COG0183  391 V 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-386 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: 521.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   5 VIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEqGFNIARNAALLAEVPHSVPA 84
Cdd:cd00751    1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  85 VTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNV------------AKAAGMMGLTAE 152
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNtldgmlddgltdPFTGLSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 153 MLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVlKQFNYDEVIRPETTVEALATLRPAFDPvSGT 232
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGP-VVVDRDEGPRPDTTLEKLAKLKPAFKK-DGT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 233 VTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFA 312
Cdd:cd00751  236 VTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFA 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446360888 313 AQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:cd00751  316 AQALACLKELGLDP---EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
PRK05790 PRK05790
putative acyltransferase; Provisional
1-387 2.52e-150

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 430.34  E-value: 2.52e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKF-GGALKDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQA-GAGQNPARQAALKAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHM----------------GHVPMshgVD--FHPGLSRnvAK 142
Cdd:PRK05790  78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMsqaphvlpgsrwgqkmGDVEL---VDtmIHDGLTD--AF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 143 AAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATL 222
Cdd:PRK05790 153 NGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 223 RPAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDI 302
Cdd:PRK05790 233 RPAFDK-DGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 303 GVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIAT 382
Cdd:PRK05790 312 DLIEINEAFAAQALAVEKELGLDP---EKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVAL 388

                 ....*
gi 446360888 383 VFERV 387
Cdd:PRK05790 389 IVERP 393
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-387 2.37e-135

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 392.39  E-value: 2.37e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK09050   1 MTEAFICDAIRTPIGRY-GGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGvDFHPGLSRN----------------VAKAA 144
Cdd:PRK09050  80 SVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMG-KADSAFSRQaeifdttigwrfvnplMKAQY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 145 GM--MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATL 222
Cdd:PRK09050 159 GVdsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 223 RPAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDI 302
Cdd:PRK09050 239 KPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 303 GVFEMNEAFAAQILPCIKDLGLMEQiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIAT 382
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLADD-DARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIAL 396

                 ....*
gi 446360888 383 VFERV 387
Cdd:PRK09050 397 AIERV 401
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-387 9.43e-135

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 390.65  E-value: 9.43e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAaLDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK07661   1 MREAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGP-IDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM-SHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHG 159
Cdd:PRK07661  80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMmGHVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 160 ISREMQDAFAARSHARAWAATQSGAFKNEIIP---TGGH-DADGVLKQ----FNYDEVIRPETTVEALATLRPAFDpVSG 231
Cdd:PRK07661 160 ISREDQDAFAVRSHQRAAKALAEGKFADEIVPvdvTLRTvGENNKLQEetitFSQDEGVRADTTLEILGKLRPAFN-VKG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 232 TVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAF 311
Cdd:PRK07661 239 SVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAF 318
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446360888 312 AAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK07661 319 ASQSIQVIRELGLDE---EKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-387 9.98e-132

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 383.20  E-value: 9.98e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK09052   5 LQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMS-HGVDFHPGL---SRNVAKAAGmMGLTAEMLAR 156
Cdd:PRK09052  85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgNKPSMSPAIfarDENVGIAYG-MGLTAEKVAE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 157 MHGISREMQDAFAARSHARAWAATQSGAFKNEIIP---------TGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFD 227
Cdd:PRK09052 164 QWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPyeiterfpdLATGEVDVKTRTVDLDEGPRADTSLEGLAKLKPVFA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 228 PvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEM 307
Cdd:PRK09052 244 N-KGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIEL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 308 NEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK09052 323 NEAFAAQSLAVIRDLGLDP---SKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-387 6.65e-131

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 380.99  E-value: 6.65e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSK-----GGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGFNIARNAALL 75
Cdd:PRK06445   1 LEDVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  76 AEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHG--VDFHPG-LSRNVAKAAGM-----M 147
Cdd:PRK06445  80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphIEPNPKlLTDPKYIEYDLttgyvM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 148 GLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGhDADGVLKQFNYDEVIRPETTVEALATLRPAFD 227
Cdd:PRK06445 160 GLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 228 PvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEM 307
Cdd:PRK06445 239 P-DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEI 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 308 NEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK06445 318 NEAFAVVVLYAIKELGLDP---ETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-386 2.90e-128

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 374.72  E-value: 2.90e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK07851   1 MPEAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 sVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHM--------GHVPMSHGVDFHPGLSRNVAKAAG------- 145
Cdd:PRK07851  81 -LPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVsrfakgnsDSLPDTKNPLFAEAQARTAARAEGgaeawhd 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 146 ------------MMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKqfnyDEVIRPE 213
Cdd:PRK07851 160 predgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGTVVST----DDGPRAG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 214 TTVEALATLRPAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALK 293
Cdd:PRK07851 236 TTYEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 294 KAGLSVSDIGVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMC 373
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDE---DKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
                        410
                 ....*....|...
gi 446360888 374 IGLGQGIATVFER 386
Cdd:PRK07851 392 VGGGQGMAMVLER 404
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
3-387 2.13e-125

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: 367.19  E-value: 2.13e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    3 QVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSV 82
Cdd:TIGR02430   2 EAYICDAIRTPIGRY-GGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPgLSRN----------------VAKAAGM 146
Cdd:TIGR02430  81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSA-FSRSakiedttigwrfinplMKALYGV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  147 --MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRP 224
Cdd:TIGR02430 160 dsMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  225 AFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGV 304
Cdd:TIGR02430 240 VVRP-DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  305 FEMNEAFAAQILPCIKDLGLMEQiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVF 384
Cdd:TIGR02430 319 IELNEAFAAQALAVLRELGLADD-DARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAI 397

                  ...
gi 446360888  385 ERV 387
Cdd:TIGR02430 398 ERV 400
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-387 1.56e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 365.08  E-value: 1.56e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGcvqqtleQGFN------IARNAAL 74
Cdd:PRK06205   1 MRDAVICEPVRTPVGRF-GGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFG-------QGYPngeapaIGRVAAL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  75 LAEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM----------SHGVDFHPGLSR------ 138
Cdd:PRK06205  72 DAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwgvrGGGVQLHDRLARgretag 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 139 --NVAKAAGMMGlTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTV 216
Cdd:PRK06205 152 grRFPVPGGMIE-TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 217 EALATLRP---AFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALK 293
Cdd:PRK06205 231 ESLAKLRPimgKQDP-EATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALA 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 294 KAGLSVSDIGVFEMNEAFAAQILPCIKDLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMC 373
Cdd:PRK06205 310 RAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMC 389
                        410
                 ....*....|....
gi 446360888 374 IGLGQGIATVFERV 387
Cdd:PRK06205 390 IGGGQGLAAVFERV 403
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-387 4.52e-123

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 361.12  E-value: 4.52e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSK-GGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVP 79
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKkDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  80 HSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM-SHGVDFhpGLSRNVAKAAGMM--GLTAEMLAR 156
Cdd:PRK08242  80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMgSDGGAW--AMDPSTNFPTYFVpqGISADLIAT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 157 MHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTggHDADGvLKQFNYDEVIRPETTVEALATLRPAF---------D 227
Cdd:PRK08242 158 KYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNG-LTILDHDEHMRPGTTMESLAKLKPSFammgemggfD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 228 PVSGTV-----------TAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAG 296
Cdd:PRK08242 235 AVALQKypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 297 LSVSDIGVFEMNEAFAAQILPCIKDLGLMeqiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGL 376
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDIP---HDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGG 391
                        410
                 ....*....|.
gi 446360888 377 GQGIATVFERV 387
Cdd:PRK08242 392 GMGIATIIERV 402
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
4-386 1.79e-117

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 348.68  E-value: 1.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   4 VVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSVP 83
Cdd:PLN02287  48 VVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKTG-LNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVP 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  84 AVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHP--GLSRNVAKAAGMMGLTAEMLARMHGIS 161
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPrvESFSQAQDCLLPMGITSENVAERFGVT 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 162 REMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDAD---GVLKQF--NYDEVIRPETTVEALATLRPAFDPvSGTVTAG 236
Cdd:PLN02287 207 REEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDpktGEEKPIviSVDDGIRPNTTLADLAKLKPVFKK-NGTTTAG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 237 TSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQIL 316
Cdd:PLN02287 286 NSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFV 365
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446360888 317 PCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMER--KDVQFGLATMCIGLGQGIATVFER 386
Cdd:PLN02287 366 YCCKKLGLDP---EKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgKDCRFGVVSMCIGTGMGAAAVFER 434
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-387 5.24e-117

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 345.15  E-value: 5.24e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK07801   1 MAEAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHgvdfhpglSRNVAKAAGMMGLT---------- 150
Cdd:PRK07801  79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISS--------AMTAGEQLGFTSPFaeskgwlhry 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 151 ----------AEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGhdadgvlkqFNYDEVIRpETTVEALA 220
Cdd:PRK07801 151 gdqevsqfrgAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 221 TLRPAFDpvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVS 300
Cdd:PRK07801 221 GLKPLVE--GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSID 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 301 DIGVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGI 380
Cdd:PRK07801 299 DIDVVEINEAFAPVVLAWLKETGADP---AKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTAN 375

                 ....*..
gi 446360888 381 ATVFERV 387
Cdd:PRK07801 376 VTIIERL 382
PRK09051 PRK09051
beta-ketothiolase BktB;
1-387 3.24e-116

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 343.48  E-value: 3.24e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK09051   2 MREVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMghvpmSHGVDFHPGLsRNVAK------------------ 142
Cdd:PRK09051  80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESM-----SRAPYLLPAA-RWGARmgdaklvdmmvgalhdpf 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 143 AAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLkQFNYDEVIRPETTVEALATL 222
Cdd:PRK09051 154 GTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEV-VFDTDEHVRADTTLEDLAKL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 223 RPAFDPVSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDI 302
Cdd:PRK09051 233 KPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 303 GVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIAT 382
Cdd:PRK09051 313 DVIEANEAFAAQACAVTRELGLDP---AKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAA 389

                 ....*
gi 446360888 383 VFERV 387
Cdd:PRK09051 390 IFERL 394
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-387 5.56e-109

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 325.14  E-value: 5.56e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARNPAlEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK06504   1 MAEAYIVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDRSGA-DPALIEDVIMGCVSQVGEQATNVARNAVLASKLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGM------------MG 148
Cdd:PRK06504  79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGMeerypgiqfsqfTG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 149 ltAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDp 228
Cdd:PRK06504 159 --AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 229 vSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMN 308
Cdd:PRK06504 236 -GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446360888 309 EAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK06504 315 EAFASVPLAWLKATGADP---ERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-387 8.61e-105

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 314.79  E-value: 8.61e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK08131   1 MLDAYIYDGLRSPFGR-HAGALASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGvDFHPGLSRN----------------VAKAA 144
Cdd:PRK08131  79 TVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMG-KAESAFSRDakvfdttigarfpnpkIVAQY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 145 G--MMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEI----IPTGGHDADgvlKQFNYDEVIRPETTVEA 218
Cdd:PRK08131 158 GndSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEItpieVPQGRKLPP---KLVAEDEHPRPSSTVEA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 219 LATLRPAFDpvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLS 298
Cdd:PRK08131 235 LTKLKPLFE--GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 299 VSDIGVFEMNEAFAAQILPCIKDLGLMEQiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQ 378
Cdd:PRK08131 313 LDDMDIIEINEAFASQVLGCLKGLGVDFD-DPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQ 391

                 ....*....
gi 446360888 379 GIATVFERV 387
Cdd:PRK08131 392 GLAMVIERV 400
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
4-254 2.67e-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: 308.08  E-value: 2.67e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888    4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPHSVP 83
Cdd:pfam00108   1 VVIVSAARTPFG-SFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQA-GEGQNPARQAALKAGIPDSAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   84 AVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGM--------------MGL 149
Cdd:pfam00108  78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLlipdgltdafngyhMGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  150 TAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLkQFNYDEVIRPETTVEALATLRPAFDPV 229
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKE 236
                         250       260
                  ....*....|....*....|....*
gi 446360888  230 sGTVTAGTSSALSDGAAAMLVMSES 254
Cdd:pfam00108 237 -GTVTAGNASPINDGAAAVLLMSES 260
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-386 1.15e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 306.43  E-value: 1.15e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQqTLEQGFNIARNAALLAEVPH 80
Cdd:PRK05656   1 MQDVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQT-GLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVP-----------MSHGVDFHPGLSRNVAKAAG--MM 147
Cdd:PRK05656  78 SVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPyvlpgartglrMGHAQLVDSMITDGLWDAFNdyHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 148 GLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFD 227
Cdd:PRK05656 158 GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 228 PvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEM 307
Cdd:PRK05656 238 K-DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEA 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446360888 308 NEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:PRK05656 317 NEAFAAQSLAVGKELGWDA---AKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-387 2.35e-98

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 297.79  E-value: 2.35e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARnPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK07850   1 MGNPVIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMG--LTAEMLARMH 158
Cdd:PRK07850  79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDIDMPNqfEAAERIAKRR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 159 GISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDAD------GVLKQFNYDEVIRpETTVEALATLRPAFDpvSGT 232
Cdd:PRK07850 159 GITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptGETRLVTRDQGLR-DTTMEGLAGLKPVLE--GGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 233 VTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFA 312
Cdd:PRK07850 236 HTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFA 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446360888 313 AQILPCikdLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK07850 316 SVVLSW---AQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
1-387 1.26e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 297.31  E-value: 1.26e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPM--GRSKGGAFRnvrAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQTLEQgFNIARNAALLAEV 78
Cdd:PRK08170   2 ARPVYIVDGARTPFlkARGGPGPFS---ASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMPSPDE-ANIARVVALRLGC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  79 PHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM---SHGVDFHPGLSRnvAKAAG---------- 145
Cdd:PRK08170  77 GEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLlfsEKMVRWLAGWYA--AKSIGqklaalgklr 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 146 ---------------------MMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKnEIIPTggHDADGvlKQF 204
Cdd:PRK08170 155 psylapvigllrgltdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL--FDRDG--KFY 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 205 NYDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGP 284
Cdd:PRK08170 230 DHDDGVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 285 VPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCI----------KDLGLME---QID-EKINLNGGAIALGHPLGCSGA 350
Cdd:PRK08170 310 VHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGLDGalgELDrERLNVDGGAIALGHPVGASGA 389
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 446360888 351 RISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK08170 390 RIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-385 2.93e-95

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 290.13  E-value: 2.93e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARnPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPH 80
Cdd:PRK07108   1 MTEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHV--PMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMH 158
Cdd:PRK07108  80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVqnEMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 159 GISREMQDAFAARSHARAWAATQSGAFKNEIIP---TGGhDADGVLKQF-------NYDEVIRPETTVEALATLRPAFDp 228
Cdd:PRK07108 160 GISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPitvTAG-VADKATGRLftkevtvSADEGIRPDTTLEGVSKIRSALP- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 229 vSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMN 308
Cdd:PRK07108 238 -GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELN 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446360888 309 EAFAAQILPCIKDLGLMeqiDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFE 385
Cdd:PRK07108 317 EAFAVQVLYCRDTLGIP---MDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
1-387 5.84e-92

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 281.53  E-value: 5.84e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLaRNPALEAAALDDIYWGCVQqTLEQGFNIARNAALLAEVPH 80
Cdd:PRK06633   2 TKPVYITHAKRTAFG-SFMGSLSTTPAPMLAAHLIKDIL-QNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHM---------------GHVPMshgVDF--HPGLSRNVAKA 143
Cdd:PRK06633  79 EVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMslgmhgsyiragakfGDIKM---VDLmqYDGLTDVFSGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 144 agMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTgghdaDGVLKQ----FNYDEVIRPETTVEAL 219
Cdd:PRK06633 156 --FMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPI-----EVTIKKttslFDHDETVRPDTSLEIL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 220 ATLRPAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSV 299
Cdd:PRK06633 229 SKLRPAFDK-NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSV 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 300 SDIGVFEMNEAFAAQILPCIKDlglMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQG 379
Cdd:PRK06633 308 NDLEVIEVNEAFAAQSIYVNRE---MKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMG 384

                 ....*...
gi 446360888 380 IATVFERV 387
Cdd:PRK06633 385 MAMCVEAV 392
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-385 7.92e-91

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 278.52  E-value: 7.92e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARnPALEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGKF-GGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQG-GQGQIPSRQAARAAGIPW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVP-----------MSHG--VDF--HPGLSrnVAKAAG 145
Cdd:PRK08235  78 EVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyilpgarwgyrMGDNevIDLmvADGLT--CAFSGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 146 MMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPA 225
Cdd:PRK08235 156 HMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 226 FDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVF 305
Cdd:PRK08235 236 FDK-TGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLF 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 306 EMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFE 385
Cdd:PRK08235 315 EINEAFAAVALASTEIAGIDP---EKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-387 3.65e-86

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 265.48  E-value: 3.65e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   3 QVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRsLLARNPALEaaaLDDIYWGCVqqtLEQGFNIARNAALLAEVPHSV 82
Cdd:PRK06690   2 RAVIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLT-FLSKGMERE---IDDVILGNV---VGPGGNVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAkaagmMGLTAEMLARMHGISR 162
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-----MGVAAEYVAERYNITR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 163 EMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNYDEVIRpettvealaTLRPAFDPvSGTVTAGTSSALS 242
Cdd:PRK06690 149 EMQDEYACLSYKRTLQALEKGYIHEEILSFNGLLDESIKKEMNYERIIK---------RTKPAFLH-NGTVTAGNSCGVN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 243 DGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDL 322
Cdd:PRK06690 219 DGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKEL 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446360888 323 GLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK06690 299 QIPY---EKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
2-386 2.00e-85

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 265.69  E-value: 2.00e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   2 EQVVIVDAIRTPMGRsKGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGfNIARNAALLAEVPHS 81
Cdd:PRK08963   5 DRIAIVSGLRTPFAK-QATAFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPEAP-NIAREIVLGTGMNVH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  82 VPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMshgvdfhpGLSRNVAKA------------------ 143
Cdd:PRK08963  82 TDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPI--------GVSKKLARAlvdlnkartlgqrlklfs 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 144 ------------------AGM-MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQf 204
Cdd:PRK08963 154 rlrlrdllpvppavaeysTGLrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPLEE- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 205 nyDEVIRPETTVEALATLRPAFDPVSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDP-SIMGYG 283
Cdd:PRK08963 233 --DNNIRGDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 284 PVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIK----------DLGLMEQIDE----KINLNGGAIALGHPLGCSG 349
Cdd:PRK08963 311 PAYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQmfaserfareKLGRSQAIGEvdmsKFNVLGGSIAYGHPFAATG 390
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 446360888 350 ARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:PRK08963 391 ARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-387 2.39e-84

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 262.79  E-value: 2.39e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSK--GGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEV 78
Cdd:PRK06025   1 MAEAYIIDAVRTPRGIGKvgKGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  79 PHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGL------SRNVAKAA----GMMG 148
Cdd:PRK06025  80 DIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKpplgmgSGNLRLRAlhpqSHQG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 149 LTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTggHDADGVLKqFNYDEVIRPETTVEALATLRPAFD- 227
Cdd:PRK06025 160 VCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVA-LDHEEFPRPQTTAEGLAALKPAFTa 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 228 ----PVSGTVT--------------------AGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYG 283
Cdd:PRK06025 237 iadyPLDDKGTtyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 284 PVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERK 363
Cdd:PRK06025 317 PVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDR---DKVNVNGGAIALGHPIGATGSILIGTVLDELERR 393
                        410       420
                 ....*....|....*....|....
gi 446360888 364 DVQFGLATMCIGLGQGIATVFERV 387
Cdd:PRK06025 394 GLKRGLVTMCAAGGMAPAIIIERV 417
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
4-387 2.17e-82

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 256.94  E-value: 2.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   4 VVIVDAIRTPMGRSKGgAFRNVRAEDLSAHLMRSLLARNPaLEAAALDDIYWGCVQQT-LEQGfnIARNAALLAEVPHSV 82
Cdd:PLN02644   3 VCIVGVARTPIGGFLG-SLSSLSATELGSIAIQAALERAG-VDPALVQEVFFGNVLSAnLGQA--PARQAALGAGLPPST 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVP-----------MSHG--VD--FHPGLsRNVAKAAGMm 147
Cdd:PLN02644  79 ICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPkylpearkgsrLGHDtvVDgmLKDGL-WDVYNDFGM- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 148 GLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIP---TGGH-------DADGVLKQFNYDEvirpettve 217
Cdd:PLN02644 157 GVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPvevPGGRgrpsvivDKDEGLGKFDPAK--------- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 218 aLATLRPAFDPVSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGL 297
Cdd:PLN02644 228 -LRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 298 SVSDIGVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLG 377
Cdd:PLN02644 307 EASQVDYYEINEAFSVVALANQKLLGLDP---EKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGG 383
                        410
                 ....*....|
gi 446360888 378 QGIATVFERV 387
Cdd:PLN02644 384 GASAIVVELM 393
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-387 2.65e-73

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 233.36  E-value: 2.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLaRNPALEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKF-GRSFSKIKAPQLGGAAIKAVI-DDAKLDPALVQEVIMGNVIQA-GVGQNPAGQAAYHAGLPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPG----LSRNVAKAAGM---------- 146
Cdd:PRK06366  78 GVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGpkhlLHKNYKIDDAMlvdglidafy 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 147 ---MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDadgvlkqfnYDEVIRpETTVEALATLR 223
Cdd:PRK06366 158 fehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLD---------RDEGIR-KTTMEDLAKLP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 224 PAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIG 303
Cdd:PRK06366 228 PAFDK-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYD 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 304 VFEMNEAFAAQILPCIKDLglmeQID-EKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIAT 382
Cdd:PRK06366 307 LVEHNEAFSIASIIVRDQL----KIDnERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTL 382

                 ....*
gi 446360888 383 VFERV 387
Cdd:PRK06366 383 TLEMV 387
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-385 4.57e-68

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 220.15  E-value: 4.57e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGGaFRNVRAEDLSAHLMRSLLARnPALEAAALDDIYWGCVQQTlEQGFNIARNAALLAEVPH 80
Cdd:PRK06954   6 QDPIVIASAARTPMAAFQGE-FASLTAPQLGAAAIAAAVER-AGLKPEQIDEVVMGCVLPA-GQGQAPARQAALGAGLPL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  81 SVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVP-----------MSHGV----DFHPGLSRNVAKAAg 145
Cdd:PRK06954  83 SVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQvldhMFLDGLEDAYDKGR- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 146 MMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPT--GGHDADGVLKQfnyDEVIRpETTVEALATLR 223
Cdd:PRK06954 162 LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVtvAGKKGDTVIDR---DEQPF-KANPEKIPTLK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 224 PAFDPvSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIG 303
Cdd:PRK06954 238 PAFSK-TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 304 VFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATV 383
Cdd:PRK06954 317 LFEINEAFAVVTMAAMKEHGLPH---EKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMG 393

                 ..
gi 446360888 384 FE 385
Cdd:PRK06954 394 IE 395
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
261-386 4.75e-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: 200.56  E-value: 4.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  261 LKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDLGLMEqidEKINLNGGAIA 340
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP---EKVNVNGGAIA 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446360888  341 LGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:pfam02803  78 LGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
7-385 1.25e-57

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: 193.09  E-value: 1.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   7 VDAIRTPMGRSKG--GAFRNVRAEDLSAHLMRSLLARnPALEAAALDDIywgCVQQTLEQGF--NIARNAALLAEVPHSV 82
Cdd:cd00826    1 AGAAMTAFGKFGGenGADANDLAHEAGAKAIAAALEP-AGVAAGAVEEA---CLGQVLGAGEgqNCAQQAAMHAGGLQEA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVpmshgvdfhpglSRNVAKAAGMMGLTAEMLarmhgiSR 162
Cdd:cd00826   77 PAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------------AENNAKEKHIDVLINKYG------MR 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 163 EMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLKQFNyDEVIR--PETTVEALATLRPAFDPvSGTVTAGTSSA 240
Cdd:cd00826  139 ACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDA-DEYIQfgDEASLDEIAKLRPAFDK-EDFLTAGNACG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 241 LSDGAAAMLVMSESRAHELGLK-------PRARVRSMAVVGCDPS----IMGYGPVPASKLALKKAGLSVSDIGVFEMNE 309
Cdd:cd00826  217 LNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHD 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 310 AFAAQILPCIKDLGLMEQIDEK---------------INLNGGAIALGHPLGCSGARISTTLLNLMERKDVQF-----GL 369
Cdd:cd00826  297 AFAANACATNEALGLCPEGQGGalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqgagaGL 376
                        410
                 ....*....|....*.
gi 446360888 370 ATMCIGLGQGIATVFE 385
Cdd:cd00826  377 ALLCIGGGGGAAMCIE 392
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
4-386 9.83e-50

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 172.78  E-value: 9.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   4 VVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALEAAALDDIYWGCVQQtLEQGFNIARNAALLAEVPHSVP 83
Cdd:PRK09268   9 VAILGGNRIPFARS-NGAYADASNQDMLTAALDGLVDRF-GLQGERLGEVVAGAVLK-HSRDFNLTRECVLGSALSPYTP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  84 AVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPM--SHGV--------------------------DFHPG 135
Cdd:PRK09268  86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIavNEGLrkillelnrakttgdrlkalgklrpkHLAPE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 136 LSRNVAKAAGM-MGLTAEMLARMHGISREMQDAFAARSHARAWAATQSGAFKNEIIPTGGHDADGVLkqfnydeviRPET 214
Cdd:PRK09268 166 IPRNGEPRTGLsMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTRDNNL---------RPDS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 215 TVEALATLRPAFD-PVSGTVTAGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMA------VVGCDPSIMGygPVPA 287
Cdd:PRK09268 237 SLEKLAKLKPVFGkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAEtaavdfVHGKEGLLMA--PAYA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 288 SKLALKKAGLSVSDIGVFEMNEAFAAQILP----------CIKDLGL---MEQID-EKINLNGGAIALGHPLGCSGARIS 353
Cdd:PRK09268 315 VPRLLARNGLTLQDFDFYEIHEAFASQVLAtlkawedeeyCRERLGLdapLGSIDrSKLNVNGSSLAAGHPFAATGGRIV 394
                        410       420       430
                 ....*....|....*....|....*....|...
gi 446360888 354 TTLLNLMERKDVQFGLATMCIGLGQGIATVFER 386
Cdd:PRK09268 395 ATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
45-351 4.94e-20

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


Pssm-ID: 238425 [Multi-domain]  Cd Length: 375  Bit Score: 90.40  E-value: 4.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  45 LEAAALDDIYWGCVQQTLEQGFNiarnAALLAEV--PHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMG 122
Cdd:cd00829   33 LEPADIDAVVVGNAAGGRFQSFP----GALIAEYlgLLGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 123 HVPMSHGVDFHPG-------LSRNVAKAAGMMGLTAEMLARMHGISREMQDAFAARshARAWAATQSGAfkneiiptggh 195
Cdd:cd00829  109 DVPTGDEAGGRASdlewegpEPPGGLTPPALYALAARRYMHRYGTTREDLAKVAVK--NHRNAARNPYA----------- 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 196 dadgvlkqfnydeVIRPETTVEALATLRPAFDPVsgtvTAGTSSALSDGAAAMLVMSESRAHELGLKPrARVRSMAVvGC 275
Cdd:cd00829  176 -------------QFRKPITVEDVLNSRMIADPL----RLLDCCPVSDGAAAVVLASEERARELTDRP-VWILGVGA-AS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 276 DPSIMGYGP--------VPASKLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDLGL------MEQIDE---------KI 332
Cdd:cd00829  237 DTPSLSERDdflsldaaRLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFcekgegGKLVREgdtaiggdlPV 316
                        330
                 ....*....|....*....
gi 446360888 333 NLNGGAIALGHPLGCSGAR 351
Cdd:cd00829  317 NTSGGLLSKGHPLGATGLA 335
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
235-383 7.71e-19

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: 85.19  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 235 AGTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPS----IMGYGPVPASKLALKKAGLSVSDIGVFEMNEA 310
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 311 FAAQILPCIKDLGLMEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDV-------QFGLATMCIGLGQGIATV 383
Cdd:cd00327  174 GTPIGDAVELALGLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptprepRTVLLLGFGLGGTNAAVV 253
PRK06064 PRK06064
thiolase domain-containing protein;
72-351 3.09e-17

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 82.25  E-value: 3.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  72 AALLAE---VPHsVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFhpglsrnVAKAA---- 144
Cdd:PRK06064  64 AALIADyagLAP-IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEA-------IARAGdyew 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 145 -GMMGLT----AEMLARMH----GISREMQDAFAARSHARAwAATQSGAFKNEIiptgghdadgvlkqfnydevirpetT 215
Cdd:PRK06064 136 eEFFGATfpglYALIARRYmhkyGTTEEDLALVAVKNHYNG-SKNPYAQFQKEI-------------------------T 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 216 VEALATLRPAFDPVsgtvTAGTSSALSDGAAAMLVMSESRAHELGLKPrARVRSMAV------VGCDPSIMGYGP-VPAS 288
Cdd:PRK06064 190 VEQVLNSPPVADPL----KLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGQasdtiaLHDRKDFTTLDAaVVAA 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446360888 289 KLALKKAGLSVSDIGVFEMNEAFAAQILPCIKDLGLMEQ-------------IDEKI--NLNGGAIALGHPLGCSGAR 351
Cdd:PRK06064 265 EKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLGFAKKgeggklaregqtyIGGDIpvNPSGGLKAKGHPVGATGVS 342
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
83-351 1.63e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 52.97  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFhpglsrnVAKAAGM--------MGLTAEML 154
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDY-------LARAADYrrqrklddFTFPCLFA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 155 ARMHGISRE----MQDAfaARSHARAWAATQSGA----FKNEIIPTGGHDADGVLKQFNYDEVIRPettvealaTLRPAf 226
Cdd:PTZ00455 185 KRMKYIQEHghftMEDT--ARVAAKAYANGNKNPlahmHTRKLSLEFCTGASDKNPKFLGNETYKP--------FLRMT- 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 227 dpvsgtvtagTSSALSDGAAAMLVMSESRAHELGLKPR----ARVRSMAVVGC-------DPSIMgYGPVPASKLALKKA 295
Cdd:PTZ00455 254 ----------DCSQVSDGGAGLVLASEEGLQKMGLSPNdsrlVEIKSLACASGnlyedppDATRM-FTSRAAAQKALSMA 322
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446360888 296 GLSVSDIGVFEMNEAFAAQILPCIKDLGLMEQIDEK---------------INLNGGAIALGHPLGCSGAR 351
Cdd:PTZ00455 323 GVKPSDLQVAEVHDCFTIAELLMYEALGIAEYGHAKdlirngatalegripVNTGGGLLSFGHPVGATGVK 393
PRK08256 PRK08256
lipid-transfer protein; Provisional
82-349 7.91e-07

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 50.67  E-value: 7.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  82 VPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPG-LSRNVAKAAGMMG-LTAEMLARMHG 159
Cdd:PRK08256  71 IPIVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSpLERFDKALAELQGfDPAPPALRMFG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 160 IsremqdafAARSHARAWAATQSG----AFKNEiiptgGHDADGVLKQFnydeviRPETTVEALATLRPAFDPVsgtvTA 235
Cdd:PRK08256 151 G--------AGREHMEKYGTTAETfakiGVKAR-----RHAANNPYAQF------RDEYTLEDVLASPMIWGPL----TR 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 236 GTSSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPS---------IMGYG-PVPASKLALKKAGLSVSDIGVF 305
Cdd:PRK08256 208 LQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPStfdgrsmidLVGYDmTRAAAQQVYEQAGIGPEDIDVV 287
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446360888 306 EMNEAFAAQILPCIKDLGLM-EQIDEK--------------INLNGGAIALGHPLGCSG 349
Cdd:PRK08256 288 ELHDCFSANELLTYEALGLCpEGEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
14-351 9.83e-07

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 50.41  E-value: 9.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  14 MGRSKGGAFRNVRAEDLSAHLMRSLLArNPALEAAALDDIYWGCVQQtlEQGFNIARNAALLAEVPHSVPAVTVNRLCGS 93
Cdd:PRK06157  14 MGCTKFGERWDAGAEDLMVEAFLEALA-DAGIEPKDIDAAWFGTHYD--EIGSGKSGTPLSRALRLPNIPVTRVENFCAT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  94 SMQALHDAARMIMTGDAQACLVGGVEHM-----GHVPMSHGVDFHPGLSRNVAkAAGMMGLTAEMLARMHGISRE-MQDA 167
Cdd:PRK06157  91 GSEAFRGAVYAVASGAYDIALALGVEKLkdtgyGGLPVANPGTLADMTMPNVT-APGNFAQLASAYAAKYGVSREdLKRA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 168 FA---ARSHArawaatqSGAfKNEiiptgghdadgvLKQFnydeviRPETTVEALAtlrpAFDPVSGTVTAGTSSALSDG 244
Cdd:PRK06157 170 MAhvsVKSHA-------NGA-RNP------------KAHL------RKAVTEEQVL----KAPMIAGPLGLFDCCGVSDG 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 245 AAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYG---------PVPASKLALKKAGLS--VSDIGVFEMNEAFAA 313
Cdd:PRK06157 220 AAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQYNgwdgsyfptTRIAARKAYREAGITdpREELSMAEVHDCFSI 299
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446360888 314 QILPCIKDLGLMEQ-------------IDEKI--NLNGGAIALGHPLGCSGAR 351
Cdd:PRK06157 300 TELVTMEDLGLSERgqawrdvldgffdADGGLpcQIDGGLKCFGHPIGASGLR 352
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
82-352 1.25e-06

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 50.07  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  82 VPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDfHPGLSRNVAKAA--------GMMGLTAEM 153
Cdd:PRK06289  81 VPASRHEAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVPGDVAAE-HLGAAAWTGHEGqdarfpwpSMFARVADE 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 154 LARMHGISREMQDAFAARSHARAW----AATQSGAFKNEIiptgghdadgvlkqFNYDEVIRPettvealatlrpafdPV 229
Cdd:PRK06289 160 YDRRYGLDEEHLRAIAEINFANARrnpnAQTRGWAFPDEA--------------TNDDDATNP---------------VV 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 230 SGTVTAGTSSALSDGAAAMLVMSESRAHELglkprARVRSMavvgcdPSIMGYG--PVP---ASKL-------------- 290
Cdd:PRK06289 211 EGRLRRQDCSQVTDGGAGVVLASDAYLRDY-----ADARPI------PRIKGWGhrTAPlglEQKLdrsagdpyvlphvr 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 291 -----ALKKAGLSVSDIGVFEMNEAFAAQILPCIKDLGLME-----------QIDEK----INLNGGAIALGHPLGCSGA 350
Cdd:PRK06289 280 qavldAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTGpgeswkaiengEIAIGgrlpINPSGGLIGGGHPVGASGV 359

                 ..
gi 446360888 351 RI 352
Cdd:PRK06289 360 RM 361
PRK07516 PRK07516
thiolase domain-containing protein;
1-349 1.34e-06

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 49.95  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888   1 MEQVVIVDAIRTPMGRSKGgafrnVRAEDLSAHLMRSLLArNPALEAAALDDIYWGCVQQTL-EQGFNIARNAALLAEVP 79
Cdd:PRK07516   1 MMTASIVGWAHTPFGKLDA-----ETLESLIVRVAREALA-HAGIAAGDVDGIFLGHFNAGFsPQDFPASLVLQADPALR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  80 HsVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMshgvdfhPGLSRNVAKA-------------AGM 146
Cdd:PRK07516  75 F-KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPT-------AEVGDILLGAsylkeegdtpggfAGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 147 MGLTAEMLARMHGISREMQDAFAARSHARAWAatqsgafkneiiptgghdadgvlkqfNYDEVIRPETTVEALATLRPAF 226
Cdd:PRK07516 147 FGRIAQAYFQRYGDQSDALAMIAAKNHANGVA--------------------------NPYAQMRKDLGFEFCRTVSEKN 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 227 DPVSGTVTAGTSSALSDGAAAMLVMSESRAHELglkPRA-RVRSMAVVG-------CDPSIMGyGPVPASKLALKKAGLS 298
Cdd:PRK07516 201 PLVAGPLRRTDCSLVSDGAAALVLADAETARAL---QRAvRFRARAHVNdflplsrRDPLAFE-GPRRAWQRALAQAGVT 276
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446360888 299 VSDIGVFEMNEAFAAQILPCIKDLGLMEQ------IDE---------KINLNGGAIALGHPLGCSG 349
Cdd:PRK07516 277 LDDLSFVETHDCFTIAELIEYEAMGLAPPgqgaraIREgwtakdgklPVNPSGGLKAKGHPIGATG 342
PRK12578 PRK12578
thiolase domain-containing protein;
238-349 2.80e-06

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 49.07  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888 238 SSALSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYG-------PVPASKLALKKAGLSVSDIGVFEMNEA 310
Cdd:PRK12578 206 SCPISDGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVARRGewvgfkaTQLAARQAYNMAKVTPNDIEVATVHDA 285
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446360888 311 FAAQILPCIKDLGLMEQ------IDE---------KINLNGGAIALGHPLGCSG 349
Cdd:PRK12578 286 FTIAEIMGYEDLGFTEKgkggkfIEEgqsekggkvGVNLFGGLKAKGHPLGATG 339
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
83-184 1.21e-04

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


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 43.70  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRN------VAKAAGMM---GLTAEM 153
Cdd:cd00833  162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDgrcrpfDADADGYVrgeGVGVVV 241
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446360888 154 LARmhgisreMQDAFAARSHARA----WAATQSGA 184
Cdd:cd00833  242 LKR-------LSDALRDGDRIYAvirgSAVNQDGR 269
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
83-130 1.47e-04

Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.


Pssm-ID: 425468 [Multi-domain]  Cd Length: 251  Bit Score: 43.01  E-value: 1.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446360888   83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHvPMSHGV 130
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLT-PLGFAG 211
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
83-119 3.56e-03

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 39.06  E-value: 3.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446360888  83 PAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVE 119
Cdd:cd00834  153 PNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
91-119 5.53e-03

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


Pssm-ID: 440073 [Multi-domain]  Cd Length: 409  Bit Score: 38.54  E-value: 5.53e-03
                         10        20
                 ....*....|....*....|....*....
gi 446360888  91 CGSSMQALHDAARMIMTGDAQACLVGGVE 119
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
 
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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