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Conserved domains on  [gi|480057380|gb|ENV96389|]
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hypothetical protein F937_00089 [Acinetobacter calcoaceticus ANC 3680]

Protein Classification

acetyl-CoA acetyltransferase( domain architecture ID 11483181)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


:

Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 759.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFVPQGVGADLIATLDG 160
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 161 YTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMMGQM-GFDAIALQK 239
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 240 YPEAQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDI 319
Cdd:PRK08242 241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 320 DLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIE 399
Cdd:PRK08242 321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                 ..
gi 480057380 400 RV 401
Cdd:PRK08242 401 RV 402
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 759.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFVPQGVGADLIATLDG 160
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 161 YTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMMGQM-GFDAIALQK 239
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 240 YPEAQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDI 319
Cdd:PRK08242 241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 320 DLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIE 399
Cdd:PRK08242 321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                 ..
gi 480057380 400 RV 401
Cdd:PRK08242 401 RV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-401 3.20e-176

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: 496.51  E-value: 3.20e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKgkKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWND 80
Cdd:COG0183    1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSS-----------FVPQG 149
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPminpgltdpytGLSMG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 150 VGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMM 227
Cdd:COG0183  158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 228 GqmgfdaialqkypeaqkinhVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARK 307
Cdd:COG0183  238 G--------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRK 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 308 ALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLC 387
Cdd:COG0183  298 ALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
                        410
                 ....*....|....
gi 480057380 388 VGGGMGIATIIERV 401
Cdd:COG0183  378 IGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-400 1.20e-160

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: 456.56  E-value: 1.20e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   5 YIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAG 84
Cdd:cd00751    1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  85 VQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFV-----------PQGVGAD 153
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLddgltdpftglSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 154 LIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMmgqmg 231
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVevPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 232 fdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEK 311
Cdd:cd00751  233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 312 AGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGG 391
Cdd:cd00751  298 AGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGG 377

                 ....*....
gi 480057380 392 MGIATIIER 400
Cdd:cd00751  378 QGAAMVIER 386
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-399 4.66e-148

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: 424.72  E-value: 4.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380    6 IIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGgDIAKTAAIAAGWNDDVAGV 85
Cdd:TIGR01930   1 IVAAARTPIGKFG--GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   86 QINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG-SDGGPWALDP-----------ETNLKSSFVPQGVGAD 153
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPgnaeledarlkDLTDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  154 LIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDH--SGVVILEKDEFIKGNTTVEGLTKLNPSFemmgqmg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKgrKGPVTVSSDEGIRPNTTLEKLAKLKPAF------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  232 fdaialqkypeaqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEK 311
Cdd:TIGR01930 231 -------------DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  312 AGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGG 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGG 377

                  ....*...
gi 480057380  392 MGIATIIE 399
Cdd:TIGR01930 378 QGAAVILE 385
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
278-400 6.64e-58

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: 185.15  E-value: 6.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  278 LKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGH 357
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 480057380  358 PLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIER 400
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
 
Name Accession Description Interval E-value
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
1-401 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 759.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK08242   1 MTEAYIYDAVRTPRGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFVPQGVGADLIATLDG 160
Cdd:PRK08242  81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKYG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 161 YTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMMGQM-GFDAIALQK 239
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMgGFDAVALQK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 240 YPEAQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDI 319
Cdd:PRK08242 241 YPEVERINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 320 DLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIE 399
Cdd:PRK08242 321 DLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400

                 ..
gi 480057380 400 RV 401
Cdd:PRK08242 401 RV 402
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
1-401 3.20e-176

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: 496.51  E-value: 3.20e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKgkKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWND 80
Cdd:COG0183    1 MREVVIVDAVRTPFGR--FGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAG-QGQNPARQAALLAGLPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSS-----------FVPQG 149
Cdd:COG0183   78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPminpgltdpytGLSMG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 150 VGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMM 227
Cdd:COG0183  158 ETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVevPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 228 GqmgfdaialqkypeaqkinhVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARK 307
Cdd:COG0183  238 G--------------------TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRK 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 308 ALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLC 387
Cdd:COG0183  298 ALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMC 377
                        410
                 ....*....|....
gi 480057380 388 VGGGMGIATIIERV 401
Cdd:COG0183  378 IGGGQGIALIIERV 391
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
5-400 1.20e-160

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: 456.56  E-value: 1.20e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   5 YIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAG 84
Cdd:cd00751    1 VIVSAVRTPIGRFG--GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAG-EGQNPARQAALLAGLPESVPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  85 VQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFV-----------PQGVGAD 153
Cdd:cd00751   78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLddgltdpftglSMGITAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 154 LIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMmgqmg 231
Cdd:cd00751  158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVevPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKK----- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 232 fdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEK 311
Cdd:cd00751  233 ---------------DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 312 AGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGG 391
Cdd:cd00751  298 AGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGG 377

                 ....*....
gi 480057380 392 MGIATIIER 400
Cdd:cd00751  378 QGAAMVIER 386
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
1-401 3.98e-153

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 438.83  E-value: 3.98e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKK-DGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWN 79
Cdd:PRK06025   1 MAEAYIIDAVRTPRGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  80 DDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMS-------------RIPMGSDGGPWALDpETNLKSSfv 146
Cdd:PRK06025  81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaamaaedmaagKPPLGMGSGNLRLR-ALHPQSH-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 147 pQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEM 226
Cdd:PRK06025 158 -QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSVALDHEEFPRPQTTAEGLAALKPAFTA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 227 MGQMGFD-------AIALQKYPEAqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLT 299
Cdd:PRK06025 237 IADYPLDdkgttyrGLINQKYPDL-EIKHVHHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 300 GPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNK 379
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
                        410       420
                 ....*....|....*....|..
gi 480057380 380 KRGLATLCVGGGMGIATIIERV 401
Cdd:PRK06025 396 KRGLVTMCAAGGMAPAIIIERV 417
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
6-399 4.66e-148

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: 424.72  E-value: 4.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380    6 IIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGgDIAKTAAIAAGWNDDVAGV 85
Cdd:TIGR01930   1 IVAAARTPIGKFG--GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   86 QINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG-SDGGPWALDP-----------ETNLKSSFVPQGVGAD 153
Cdd:TIGR01930  78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvPRSLRWGVKPgnaeledarlkDLTDANTGLPMGVTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  154 LIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDH--SGVVILEKDEFIKGNTTVEGLTKLNPSFemmgqmg 231
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKgrKGPVTVSSDEGIRPNTTLEKLAKLKPAF------- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  232 fdaialqkypeaqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEK 311
Cdd:TIGR01930 231 -------------DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKK 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  312 AGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGG 391
Cdd:TIGR01930 298 AGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGG 377

                  ....*...
gi 480057380  392 MGIATIIE 399
Cdd:TIGR01930 378 QGAAVILE 385
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
1-401 5.29e-124

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 363.64  E-value: 5.29e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPrgKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK07801   1 MAEAYIVDAVRTP--VGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSD---GGPWALDPETNLKSSF--------VPQG 149
Cdd:PRK07801  79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAmtaGEQLGFTSPFAESKGWlhrygdqeVSQF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 150 VGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDhsgvviLEKDEFIKgNTTVEGLTKLNPSFEmmgq 229
Cdd:PRK07801 159 RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG------VTVDEGPR-ETSLEKMAGLKPLVE---- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 230 mgfdaialqkypeAQKINhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKAL 309
Cdd:PRK07801 228 -------------GGRLT----AAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYAL 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 310 EKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVG 389
Cdd:PRK07801 291 EKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEG 370
                        410
                 ....*....|..
gi 480057380 390 GGMGIATIIERV 401
Cdd:PRK07801 371 GGTANVTIIERL 382
PRK05790 PRK05790
putative acyltransferase; Provisional
1-401 3.80e-123

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 361.78  E-value: 3.80e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWND 80
Cdd:PRK05790   1 MKDVVIVSAARTPIGKFG--GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAG-AGQNPARQAALKAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIP---MGSDGGPWALDPEtnLKSSFV----------- 146
Cdd:PRK05790  78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvlPGSRWGQKMGDVE--LVDTMIhdgltdafngy 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 147 PQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSG-VVILEKDEFIKGNTTVEGLTKLNPS 223
Cdd:PRK05790 156 HMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVtiKQRKGdPVVVDTDEHPRPDTTAESLAKLRPA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 224 FEMMGQMgfdaialqkypeaqkinhvhHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAP 303
Cdd:PRK05790 236 FDKDGTV--------------------TAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVP 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 304 AARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGL 383
Cdd:PRK05790 296 AIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGL 375
                        410
                 ....*....|....*...
gi 480057380 384 ATLCVGGGMGIATIIERV 401
Cdd:PRK05790 376 ATLCIGGGQGVALIVERP 393
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
1-401 1.37e-109

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 327.30  E-value: 1.37e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPrgKGKKDGSLYEVKPITLLTTLLNELQQRH-QLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWN 79
Cdd:PRK09050   1 MTEAFICDAIRTP--IGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  80 DDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIP--MGSDGGPWALDPE---TNLKSSFV-PQ----- 148
Cdd:PRK09050  79 VSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGKADSAFSRQAEifdTTIGWRFVnPLmkaqy 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 GVG-----ADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV---KDHSGVVILEKDEFIKGNTTVEGLTKL 220
Cdd:PRK09050 159 GVDsmpetAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVtipQKKGDPVVVDRDEHPRPETTLEALAKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 221 NPSFEMMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTG 300
Cdd:PRK09050 239 KPVFRPDGTVT--------------------AGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIG 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 301 PAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVP--PEKVNVNGGAIALGHPLGATGAMILGTLLDELERQN 378
Cdd:PRK09050 299 PAPATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLAddDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTG 378
                        410       420
                 ....*....|....*....|...
gi 480057380 379 KKRGLATLCVGGGMGIATIIERV 401
Cdd:PRK09050 379 GRYALCTMCIGVGQGIALAIERV 401
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
1-401 5.20e-108

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 322.83  E-value: 5.20e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPrgKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK07850   1 MGNPVIVEAVRTP--IGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALDPETNLKSSFVP-QGVGADLIATLD 159
Cdd:PRK07850  79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDIDMPnQFEAAERIAKRR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 160 GYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVK---------DHSGVVILEKDEFIKgNTTVEGLTKLNPSFEmmgqm 230
Cdd:PRK07850 159 GITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapvldeegqPTGETRLVTRDQGLR-DTTMEGLAGLKPVLE----- 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 231 gfdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALE 310
Cdd:PRK07850 233 ----------------GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLE 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 311 KAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGG 390
Cdd:PRK07850 297 KAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGG 376
                        410
                 ....*....|.
gi 480057380 391 GMGIATIIERV 401
Cdd:PRK07850 377 ALSTGTIIERI 387
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
1-401 1.02e-106

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 319.75  E-value: 1.02e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTP-----RGKGKKDgSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQ---GGdiaKTA 72
Cdd:PRK06445   1 LEDVYLVDFARTAfsrfrPKDPQKD-VFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwlyGG---RHP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  73 AIAAGWNDDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSdgGP-------WALDPET---NLK 142
Cdd:PRK06445  77 IFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGD--NPhiepnpkLLTDPKYieyDLT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 143 SSFVpQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSG--VVILEKDEFIKGNTTVEGLTKL 220
Cdd:PRK06445 155 TGYV-MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEgkKKVVDVDQSVRPDTSLEKLAKL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 221 NPSFemmgqmgfdaialqkypeaqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTG 300
Cdd:PRK06445 234 PPAF--------------------KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKG 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 301 PAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKK 380
Cdd:PRK06445 294 PVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKD 373
                        410       420
                 ....*....|....*....|.
gi 480057380 381 RGLATLCVGGGMGIATIIERV 401
Cdd:PRK06445 374 YGVATLCVGGGQGGAVVLERV 394
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
1-401 3.56e-104

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 313.06  E-value: 3.56e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdGSLYEVKPITLLTTLLNELQQRH-QLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWN 79
Cdd:PRK08947   1 MEDVVIVDAIRTPMGRSKG-GAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  80 DDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPM--GSDggpwaLDPETNL---KSSFVpQGVGADL 154
Cdd:PRK08947  80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMnhGVD-----FHPGLSKnvaKAAGM-MGLTAEM 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 155 IATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDH--SGVVIL-EKDEFIKGNTTVEGLTKLNPSFEmmgqmg 231
Cdd:PRK08947 154 LGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHdaDGVLKLfDYDEVIRPETTVEALAALRPAFD------ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 232 fdaialqkypeaqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEK 311
Cdd:PRK08947 228 -------------PVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKR 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 312 AGLTIDDIDLFEVNEAFAA---VVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCV 388
Cdd:PRK08947 295 AGLSISDIDVFELNEAFAAqslPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCI 374
                        410
                 ....*....|...
gi 480057380 389 GGGMGIATIIERV 401
Cdd:PRK08947 375 GLGQGIATVFERV 387
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-401 7.33e-104

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 312.71  E-value: 7.33e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdGSLYEVKPITL-LTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWN 79
Cdd:PRK09052   5 LQDAYIVAATRTPVGKAPR-GMFKNTRPDDLlAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  80 DDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGsdGGPWALDPETNLKSSFVP----QGVGADLI 155
Cdd:PRK09052  84 NSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMM--GNKPSMSPAIFARDENVGiaygMGLTAEKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 156 ATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVP--VKDH-----SGVVILEK-----DEFIKGNTTVEGLTKLNPS 223
Cdd:PRK09052 162 AEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERfpdlaTGEVDVKTrtvdlDEGPRADTSLEGLAKLKPV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 224 FEMMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAP 303
Cdd:PRK09052 242 FANKGSVT--------------------AGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIE 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 304 AARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGL 383
Cdd:PRK09052 302 AIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGM 381
                        410
                 ....*....|....*...
gi 480057380 384 ATLCVGGGMGIATIIERV 401
Cdd:PRK09052 382 VTMCVGTGMGAAGIFERL 399
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
1-401 2.49e-101

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 305.88  E-value: 2.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTprGKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK06504   1 MAEAYIVAAART--AGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSdggPWALDPETNLKSSFVP------------Q 148
Cdd:PRK06504  79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGS---PSTLPAKNGLGHYKSPgmeerypgiqfsQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVK----DHSGVvILEKDEFIKGNTTVEGLTklnpsf 224
Cdd:PRK06504 156 FTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEitraDGSGE-MHTVDEGIRFDATLEGIA------ 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 225 emmgqmGFDAIAlqkypEAQKINhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPA 304
Cdd:PRK06504 229 ------GVKLIA-----EGGRLT----AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPA 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 305 ARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLA 384
Cdd:PRK06504 294 TERALKKAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQ 373
                        410
                 ....*....|....*..
gi 480057380 385 TLCVGGGMGIATIIERV 401
Cdd:PRK06504 374 TMCEGGGMANVTIVERL 390
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
1-400 1.23e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 299.61  E-value: 1.23e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdGSLYEVKPITLLTTLLNE-LQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWn 79
Cdd:PRK07851   1 MPEAVIVSTARSPIGRAFK-GSLKDMRPDDLAAQMVRAaLDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGY- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  80 DDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG-SDGGP------------------------WA 134
Cdd:PRK07851  79 DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGnSDSLPdtknplfaeaqartaaraeggaeaWH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 135 lDPETN--LKSSFVPQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGVVIlEKDEFIKGNT 212
Cdd:PRK07851 159 -DPREDglLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGTVV-STDDGPRAGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 213 TVEGLTKLNPSFEMMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGT 292
Cdd:PRK07851 237 TYEKVSQLKPVFRPDGTVT--------------------AGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 293 DPTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLD 372
Cdd:PRK07851 297 SPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLN 376
                        410       420
                 ....*....|....*....|....*...
gi 480057380 373 ELERQNKKRGLATLCVGGGMGIATIIER 400
Cdd:PRK07851 377 NLQTHDKTFGLETMCVGGGQGMAMVLER 404
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
1-401 1.36e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 293.97  E-value: 1.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK07661   1 MREAVIVAGARTPVGKAKK-GSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDggpwALDPETNLKSS----FVPQGVGADLIA 156
Cdd:PRK07661  80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGH----VVRPNPRLVEAapeyYMGMGHTAEQVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 157 TLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--------KDHSGV---VILEKDEFIKGNTTVEGLTKLNPSFE 225
Cdd:PRK07661 156 VKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdvtlrtvgENNKLQeetITFSQDEGVRADTTLEILGKLRPAFN 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 226 MMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAA 305
Cdd:PRK07661 236 VKGSVT--------------------AGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAI 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 306 RKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLAT 385
Cdd:PRK07661 296 PKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVT 375
                        410
                 ....*....|....*.
gi 480057380 386 LCVGGGMGIATIIERV 401
Cdd:PRK07661 376 MCIGGGMGAAGVFELL 391
PRK09051 PRK09051
beta-ketothiolase BktB;
1-401 3.34e-96

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 293.02  E-value: 3.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTprGKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK09051   2 MREVVVVSGVRT--AIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPW--------ALDPETN-LKSSF--VPQG 149
Cdd:PRK09051  80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWgarmgdakLVDMMVGaLHDPFgtIHMG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 150 VGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFemm 227
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVeiKTRKGEVVFDTDEHVRADTTLEDLAKLKPVF--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 228 gqmgfdaialqkypeaQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARK 307
Cdd:PRK09051 237 ----------------KKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQK 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 308 ALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLC 387
Cdd:PRK09051 301 ALERAGLTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMC 380
                        410
                 ....*....|....
gi 480057380 388 VGGGMGIATIIERV 401
Cdd:PRK09051 381 IGGGQGIAAIFERL 394
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
1-401 6.72e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 277.25  E-value: 6.72e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPrgKGKKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGdIAKTAAIAAGWND 80
Cdd:PRK06205   1 MRDAVICEPVRTP--VGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPW-----------ALDP--ETNLKSSF-V 146
Cdd:PRK06205  78 TVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWgvrgggvqlhdRLARgrETAGGRRFpV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 147 PQGV--GADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVK---DHSGVVILEKDEFIKGNTTVEGLTKLN 221
Cdd:PRK06205 158 PGGMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTvpqRKGDPTVVDRDEHPRADTTLESLAKLR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 222 PsfemmgqmgfdaIALQKYPEAqkinhVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGP 301
Cdd:PRK06205 238 P------------IMGKQDPEA-----TVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGP 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 302 APAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPP---EKVNVNGGAIALGHPLGATGAMILGTLLDELERQN 378
Cdd:PRK06205 301 VPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQ 380
                        410       420
                 ....*....|....*....|...
gi 480057380 379 KKRGLATLCVGGGMGIATIIERV 401
Cdd:PRK06205 381 ARYGLETMCIGGGQGLAAVFERV 403
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
1-401 6.18e-87

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 269.34  E-value: 6.18e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKgkKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK08131   1 MLDAYIYDGLRSPFGR--HAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIP--MGSDGGPWALDPE---TNLKSSF---------- 145
Cdd:PRK08131  79 TVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKAESAFSRDAKvfdTTIGARFpnpkivaqyg 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 146 ---VPQGvgADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSG----VVILEKDEFIKGNTTVEGLT 218
Cdd:PRK08131 159 ndsMPET--GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGrklpPKLVAEDEHPRPSSTVEALT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 219 KLNPSFEmmgqmgfdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIML 298
Cdd:PRK08131 237 KLKPLFE---------------------GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMG 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 299 TGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVP--PEKVNVNGGAIALGHPLGATGAMILGTLLDELER 376
Cdd:PRK08131 296 IGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDfdDPRVNPNGGAIAVGHPLGASGARLALTAARELQR 375
                        410       420
                 ....*....|....*....|....*
gi 480057380 377 QNKKRGLATLCVGGGMGIATIIERV 401
Cdd:PRK08131 376 RGKRYAVVSLCIGVGQGLAMVIERV 400
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
6-400 6.79e-87

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 270.87  E-value: 6.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   6 IIDAIRTPRGKGKKdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWNDDVAGV 85
Cdd:PLN02287  50 IVAAYRTPICKAKR-GGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  86 QINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGpwaLDPETNL----KSSFVPQGVGADLIATLDGY 161
Cdd:PLN02287 129 TVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGG---VNPRVESfsqaQDCLLPMGITSENVAERFGV 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 162 TREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDH--------SGVVILEKDEFIKGNTTVEGLTKLNPSFemmgqmgfd 233
Cdd:PLN02287 206 TREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKivdpktgeEKPIVISVDDGIRPNTTLADLAKLKPVF--------- 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 234 aialqkypeaqKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAG 313
Cdd:PLN02287 277 -----------KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAG 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 314 LTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNK--KRGLATLCVGGG 391
Cdd:PLN02287 346 LELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKdcRFGVVSMCIGTG 425

                 ....*....
gi 480057380 392 MGIATIIER 400
Cdd:PLN02287 426 MGAAAVFER 434
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
1-399 2.53e-82

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 257.33  E-value: 2.53e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKgkKDGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWND 80
Cdd:PRK08235   1 MSKTVIVSAARTPFGK--FGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWAL---DPET-------NLKSSF--VPQ 148
Cdd:PRK08235  78 EVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYrmgDNEVidlmvadGLTCAFsgVHM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV---KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFE 225
Cdd:PRK08235 158 GVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVtipQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 226 MMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAA 305
Cdd:PRK08235 238 KTGTIT--------------------AGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 306 RKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLAT 385
Cdd:PRK08235 298 NALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAA 377
                        410
                 ....*....|....
gi 480057380 386 LCVGGGMGIATIIE 399
Cdd:PRK08235 378 ICSGGGQGDAVLIE 391
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
3-401 3.05e-78

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 246.87  E-value: 3.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   3 EAYIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTpIGDQGGDIAKTAAIAAGWNDDV 82
Cdd:PRK06633   4 PVYITHAKRTAFGSFM--GSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPKEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  83 AGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMS------RIPMGSDGGPWAL------DPETNLKSSfVPQGV 150
Cdd:PRK06633  81 PGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhgsYIRAGAKFGDIKMvdlmqyDGLTDVFSG-VFMGI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 151 GADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKD--HSGVVILEKDEFIKGNTTVEGLTKLNPSFEMmg 228
Cdd:PRK06633 160 TAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVtiKKTTSLFDHDETVRPDTSLEILSKLRPAFDK-- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 229 qmgfdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKA 308
Cdd:PRK06633 238 ------------------NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKA 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 309 LEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCV 388
Cdd:PRK06633 300 LSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCI 379
                        410
                 ....*....|...
gi 480057380 389 GGGMGIATIIERV 401
Cdd:PRK06633 380 GGGMGMAMCVEAV 392
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
5-401 4.15e-76

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 242.23  E-value: 4.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   5 YIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGgDIAKTAAIAAGWNDDVAG 84
Cdd:PRK08170   6 YIVDGARTPFLKAR--GGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEA-NIARVVALRLGCGEKVPA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  85 VQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPM--GSDGGPW------ALDPETNLKS--SFVPQ------ 148
Cdd:PRK08170  83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLlfSEKMVRWlagwyaAKSIGQKLAAlgKLRPSylapvi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 ---------------GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQsVVPVKDHSGVViLEKDEFIKGNTT 213
Cdd:PRK08170 163 gllrgltdpvvglnmGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPLFDRDGKF-YDHDDGVRPDSS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 214 VEGLTKLNPSFEmmgqmgfdaialQKYPEAQkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTD 293
Cdd:PRK08170 241 MEKLAKLKPFFD------------RPYGRVT-------AGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALD 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 294 PTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELN-----------------VPPEKVNVNGGAIALG 356
Cdd:PRK08170 302 PSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALG 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 480057380 357 HPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIERV 401
Cdd:PRK08170 382 HPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
1-399 1.03e-73

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 235.05  E-value: 1.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDQGGDIAKTAAIAAGWND 80
Cdd:PRK07108   1 MTEAVIVSTARTPLAKSWR-GAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSD----GGPWALDPETNLKSSFVPQgvgADLIA 156
Cdd:PRK07108  80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNrhmlREGWLVEHKPEIYWSMLQT---AENVA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 157 TLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSGV------------VILEKDEFIKGNTTVEGLTKLNPSF 224
Cdd:PRK07108 157 KRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVadkatgrlftkeVTVSADEGIRPDTTLEGVSKIRSAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 225 EmmgqmgfdaialqkypeaqkiNHVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPA 304
Cdd:PRK07108 237 P---------------------GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFA 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 305 ARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLA 384
Cdd:PRK07108 296 VPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVV 375
                        410
                 ....*....|....*
gi 480057380 385 TLCVGGGMGIATIIE 399
Cdd:PRK07108 376 TMCIGGGQGAAGLFE 390
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
1-400 2.64e-72

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 231.32  E-value: 2.64e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWND 80
Cdd:PRK05656   1 MQDVVIVAATRTAIGSFQ--GSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSDGGPWALD-PETNLKSSFVPQ----------- 148
Cdd:PRK05656  78 SVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRmGHAQLVDSMITDglwdafndyhm 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV---KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFE 225
Cdd:PRK05656 158 GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIlipQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 226 MMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAA 305
Cdd:PRK05656 238 KDGSVT--------------------AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSAT 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 306 RKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLAT 385
Cdd:PRK05656 298 RRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLAT 377
                        410
                 ....*....|....*
gi 480057380 386 LCVGGGMGIATIIER 400
Cdd:PRK05656 378 LCIGGGQGVALAIER 392
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
1-401 4.91e-69

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 222.96  E-value: 4.91e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   1 MSEAYIIDAIRTPRGKGKKdgSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGDqGGDIAKTAAIAAGWND 80
Cdd:PRK06366   1 MKDVYIVSAKRTAIGKFGR--SFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGV-GQNPAGQAAYHAGLPF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  81 DVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIP--MGSD--GGPWALdPETNLKSS------------ 144
Cdd:PRK06366  78 GVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPflLPSDlrWGPKHL-LHKNYKIDdamlvdglidaf 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 145 -FVPQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDhsgvviLEKDEFIKgNTTVEGLTKLNPS 223
Cdd:PRK06366 157 yFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND------LDRDEGIR-KTTMEDLAKLPPA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 224 FEMMGqmgfdaialqkypeaqkinhVHHAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAP 303
Cdd:PRK06366 230 FDKNG--------------------ILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIP 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 304 AARKALEKAGLTIDDIDLFEVNEAF--AAVVMRfiNELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKR 381
Cdd:PRK06366 290 ATRKLLEKQNKSIDYYDLVEHNEAFsiASIIVR--DQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKT 367
                        410       420
                 ....*....|....*....|
gi 480057380 382 GLATLCVGGGMGIATIIERV 401
Cdd:PRK06366 368 GLATLCHGGGGAHTLTLEMV 387
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
6-401 2.10e-68

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 221.51  E-value: 2.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   6 IIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAGV 85
Cdd:PLN02644   5 IVGVARTPIGGFL--GSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSAN-LGQAPARQAALGAGLPPSTICT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  86 QINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPM-------GS--------DG----GPWalDPETNlkssfV 146
Cdd:PLN02644  82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKylpearkGSrlghdtvvDGmlkdGLW--DVYND-----F 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 147 PQGVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDHSG----VVILEKDEFIkGNTTVEGLTKLNP 222
Cdd:PLN02644 155 GMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGrgrpSVIVDKDEGL-GKFDPAKLRKLRP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 223 SFEmmgqmgfdaialqkypeaQKINHVHhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPA 302
Cdd:PLN02644 234 SFK------------------EDGGSVT-AGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPA 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 303 PAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRG 382
Cdd:PLN02644 295 LAIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYG 374
                        410
                 ....*....|....*....
gi 480057380 383 LATLCVGGGMGIATIIERV 401
Cdd:PLN02644 375 VAGICNGGGGASAIVVELM 393
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
3-401 1.90e-65

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 212.70  E-value: 1.90e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   3 EAYIIDAIRTPRGKgkKDGSLyevKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTpigDQGGDIAKTAAIAAGWNDDV 82
Cdd:PRK06690   2 RAVIVEAKRTPIGK--KNGML---KDYEVQQLAAPLLTFLSKGMEREIDDVILGNVV---GPGGNVARLSALEAGLGLHI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  83 AGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMGSdggpwaldpetnlKSSFVPQ-------GVGADLI 155
Cdd:PRK06690  74 PGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQN-------------RARFSPEtigdpdmGVAAEYV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 156 ATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVkdhSGVVilekDEFIKGNTTVEGLTK-LNPSFEMMGQMGfda 234
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF---NGLL----DESIKKEMNYERIIKrTKPAFLHNGTVT--- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 235 ialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGL 314
Cdd:PRK06690 211 -----------------AGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNM 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 315 TIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGI 394
Cdd:PRK06690 274 KVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGL 353

                 ....*..
gi 480057380 395 ATIIERV 401
Cdd:PRK06690 354 ALLFEKV 360
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
41-399 1.15e-59

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 198.58  E-value: 1.15e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  41 QRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVES 120
Cdd:PRK06954  44 ERAGLKPEQIDEVVMGCVLPAG-QGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMES 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 121 MSRIP--------------------MGSDGGPWALDpETNLKSSFvpqgvgADLIATLDGYTREDVDTFAVNSQQKAAAA 180
Cdd:PRK06954 123 MTNAPyllpkarggmrmghgqvldhMFLDGLEDAYD-KGRLMGTF------AEECAGEYGFTREAQDAFAIESLARAKRA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 181 QANGYFDQSVVPVK--DHSGVVILEKDEFIKgNTTVEGLTKLNPSFEMMGQMGfdaialqkypeaqkinhvhhAGNSSGI 258
Cdd:PRK06954 196 NEDGSFAWEIAPVTvaGKKGDTVIDRDEQPF-KANPEKIPTLKPAFSKTGTVT--------------------AANSSSI 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 259 VDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINE 338
Cdd:PRK06954 255 SDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKE 334
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480057380 339 LNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIE 399
Cdd:PRK06954 335 HGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
278-400 6.64e-58

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: 185.15  E-value: 6.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  278 LKPRAKVLATALVGTDPTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNGGAIALGH 357
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 480057380  358 PLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIER 400
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
6-400 1.59e-51

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 178.25  E-value: 1.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   6 IIDAIRTPRGKGKKDgsLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIgDQGGDIAKTAAIAAGWNDDVAGV 85
Cdd:PRK08963   9 IVSGLRTPFAKQATA--FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQM-PEAPNIAREIVLGTGMNVHTDAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  86 QINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG----------------SDGGPWALDPETNLKSsFVPQ- 148
Cdd:PRK08963  86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGvskklaralvdlnkarTLGQRLKLFSRLRLRD-LLPVp 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 ------------GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVV-----PVKDHsgvviLEKDEFIKGN 211
Cdd:PRK08963 165 pavaeystglrmGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMtahvpPYKQP-----LEEDNNIRGD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 212 TTVEGLTKLNPSFEmmgqmgfdaialQKYPEAQkinhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVG 291
Cdd:PRK08963 240 STLEDYAKLRPAFD------------RKHGTVT-------AANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 292 TDPTI-MLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVM---------RFINE-LN-------VPPEKVNVNGGAI 353
Cdd:PRK08963 301 IDVWQdMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLanlqmfaseRFAREkLGrsqaigeVDMSKFNVLGGSI 380
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 480057380 354 ALGHPLGATGA-MILGTlLDELERQNKKRGLATLCVGGGMGIATIIER 400
Cdd:PRK08963 381 AYGHPFAATGArMITQT-LHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
40-399 2.66e-48

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: 168.83  E-value: 2.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  40 QQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVE 119
Cdd:cd00826   35 LEPAGVAAGAVEEACLGQVLGAG-EGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 120 SMSRIPMgSDGGPWALDPETNLKSSfvpqgvgadliatldgytREDVDTFAVNSQQKAAAAQANGYFDQSVVP--VKDHS 197
Cdd:cd00826  114 KMETSAE-NNAKEKHIDVLINKYGM------------------RACPDAFALAGQAGAEAAEKDGRFKDEFAKfgVKGRK 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 198 GVVILEKDEFIK--GNTTVEGLTKLNPSFEMMGQMGfdaialqkypeaqkinhvhhAGNSSGIVDGAAVVLLASEKAVKE 275
Cdd:cd00826  175 GDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLT--------------------AGNACGLNDGAAAAILMSEAEAQK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 276 QNLK-------PRAKVLATALVGTDPT----IMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPE 344
Cdd:cd00826  235 HGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPE 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480057380 345 K------------------VNVNGGAIALGHPLGATGAMILGTLLDELERQNKKR-----GLATLCVGGGMGIATIIE 399
Cdd:cd00826  315 GqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
87-400 1.38e-45

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 162.38  E-value: 1.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  87 INRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG-SDGGPWAL-------DPETNLK-------SSFVPQ--- 148
Cdd:PRK09268  89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAvNEGLRKILlelnrakTTGDRLKalgklrpKHLAPEipr 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 149 ----------GVGADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPVKDhsgvviLEKDEFIKGNTTVEGLT 218
Cdd:PRK09268 169 ngeprtglsmGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG------LTRDNNLRPDSSLEKLA 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 219 KLNPSFEmmgqmgfdaialqKYPEAQKInhvhhAGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLA--TALV----GT 292
Cdd:PRK09268 243 KLKPVFG-------------KGGRATMT-----AGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDaeTAAVdfvhGK 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 293 DPtiMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVM---------RFINE---LNVP-----PEKVNVNGGAIAL 355
Cdd:PRK09268 305 EG--LLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLatlkawedeEYCRErlgLDAPlgsidRSKLNVNGSSLAA 382
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 480057380 356 GHPLGATGAMILGTLLDELERQNKKRGLATLCVGGGMGIATIIER 400
Cdd:PRK09268 383 GHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
5-270 4.40e-41

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: 145.91  E-value: 4.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380    5 YIIDAIRTPRGKGKkdGSLYEVKPITLLTTLLNELQQRHQLDTSKVDDIVLGCVTPIGdQGGDIAKTAAIAAGWNDDVAG 84
Cdd:pfam00108   2 VIVSAARTPFGSFG--GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAG-EGQNPARQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380   85 VQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG--SDGGPWALDPETNLKSSFVP-----------QGVG 151
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlpTDARSGLKHGDEKKHDLLIPdgltdafngyhMGLT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  152 ADLIATLDGYTREDVDTFAVNSQQKAAAAQANGYFDQSVVPV--KDHSGVVILEKDEFIKGNTTVEGLTKLNPSFEMMGQ 229
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVtvKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGT 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 480057380  230 MgfdaialqkypeaqkinhvhHAGNSSGIVDGAAVVLLASE 270
Cdd:pfam00108 239 V--------------------TAGNASPINDGAAAVLLMSE 259
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
45-398 2.69e-22

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: 97.33  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  45 LDTSKVDDIVLGCVTPiGDQGGDIAKTAAIAAGWnDDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRI 124
Cdd:cd00829   33 LEPADIDAVVVGNAAG-GRFQSFPGALIAEYLGL-LGKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 125 PMGSDGGPWALDPETNLKSSFVPQGVGAD--LIAT----LDGYTREDVDTFAVnsqqkaaaaqangyfdqsvvpvKDHS- 197
Cdd:cd00829  111 PTGDEAGGRASDLEWEGPEPPGGLTPPALyaLAARrymhRYGTTREDLAKVAV----------------------KNHRn 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 198 GVvilekdefikgnttvegltkLNPSfemmGQMGFDaIALQKYPEAQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEQN 277
Cdd:cd00829  169 AA--------------------RNPY----AQFRKP-ITVEDVLNSRMIADPLRLLDCCPVSDGAAAVVLASEERARELT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 278 LKPrAKVLATAlVGTDPT--------IMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVMRFINEL---------- 339
Cdd:cd00829  224 DRP-VWILGVG-AASDTPslserddfLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLgfcekgeggk 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480057380 340 -----------NVPpekVNVNGGAIALGHPLGATGAMILGTLLDEL-----ERQNKKRGLATLCVGGGMGIATII 398
Cdd:cd00829  302 lvregdtaiggDLP---VNTSGGLLSKGHPLGATGLAQAVEAVRQLrgeagARQVPGARVGLAHNIGGTGSAAVV 373
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
252-398 6.36e-22

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: 94.05  E-value: 6.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 252 AGNSSGIVDGAAVVLLASEKAVKEQNLKPRAKVLATALVGTDPT----IMLTGPAPAARKALEKAGLTIDDIDLFEVNEA 327
Cdd:cd00327   94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 328 FAAVVMRFINELNVPPEKV---NVNGGAIALGHPLGATGAMILGTLLDELERQNKKR-------GLATLCVGGGMGIATI 397
Cdd:cd00327  174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253

                 .
gi 480057380 398 I 398
Cdd:cd00327  254 L 254
PRK06064 PRK06064
thiolase domain-containing protein;
91-363 8.06e-18

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 84.18  E-value: 8.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  91 CASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRIPMG--SDGGPWALDPETNLKSSFVPQGVGAdLIATLD----GYTRE 164
Cdd:PRK06064  85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPdaTEAIARAGDYEWEEFFGATFPGLYA-LIARRYmhkyGTTEE 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 165 DVDTFAVnsqqkaaaaqangyfdqsvvpvKDHSGVVILEKDEFiKGNTTVEglTKLNPSfemmgqmgfdaialqkyPEAQ 244
Cdd:PRK06064 164 DLALVAV----------------------KNHYNGSKNPYAQF-QKEITVE--QVLNSP-----------------PVAD 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 245 KINHVHhagnSSGIVDGAAVVLLASEKAVKEQNLKPrAKVLATAlVGTDpTI-------MLTGPAP--AARKALEKAGLT 315
Cdd:PRK06064 202 PLKLLD----CSPITDGAAAVILASEEKAKEYTDTP-VWIKASG-QASD-TIalhdrkdFTTLDAAvvAAEKAYKMAGIE 274
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480057380 316 IDDIDLFEVNEAFAavvmrfINEL---------------------------NVPpekVNVNGGAIALGHPLGATG 363
Cdd:PRK06064 275 PKDIDVAEVHDCFT------IAEIlayedlgfakkgeggklaregqtyiggDIP---VNPSGGLKAKGHPVGATG 340
PRK08256 PRK08256
lipid-transfer protein; Provisional
260-363 4.60e-09

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 57.60  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 260 DGAAVVLLASEKAVKEQNLKPRAKVLATALVgTDPTIMLTGPAP-----------AARKALEKAGLTIDDIDLFEVNEAF 328
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAQAMT-TDTPSTFDGRSMidlvgydmtraAAQQVYEQAGIGPEDIDVVELHDCF 293
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 480057380 329 AAvvmrfiNE------LNVPPE----------------KVNVN--GGAIALGHPLGATG 363
Cdd:PRK08256 294 SA------NElltyeaLGLCPEgeaekfiddgdntyggRWVVNpsGGLLSKGHPLGATG 346
PRK12578 PRK12578
thiolase domain-containing protein;
91-366 6.28e-08

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 54.08  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  91 CASGLEAVNMAAMKVRSGWEDLVVAGGVESMSRI------PMGSDGGPWALdpETNLKSSFVPQ--GVGADLIATLDGYT 162
Cdd:PRK12578  82 CATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVdtstslAIGGRGGNYQW--EYHFYGTTFPTyyALYATRHMAVYGTT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 163 REDVdtfavnsqqkaaaaqangyfdqSVVPVKDHSGVVILEKDEFIKgnttvegltklnpsfemmgqmgfdAIALQKYPE 242
Cdd:PRK12578 160 EEQM----------------------ALVSVKAHKYGAMNPKAHFQK------------------------PVTVEEVLK 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 243 AQKINHVHHAGNSSGIVDGAAVVLLASEKAVKEqnLKPRAKVLATAL-VGTDPTIM--------LTGPAPAARKALEKAG 313
Cdd:PRK12578 194 SRAISWPIKLLDSCPISDGSATAIFASEEKVKE--LKIDSPVWITGIgYANDYAYVarrgewvgFKATQLAARQAYNMAK 271
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480057380 314 LTIDDIDLFEVNEAFA-AVVM--------------RFINELNVPPE-KVNVN--GGAIALGHPLGATG-AMI 366
Cdd:PRK12578 272 VTPNDIEVATVHDAFTiAEIMgyedlgftekgkggKFIEEGQSEKGgKVGVNlfGGLKAKGHPLGATGlSMI 343
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
256-363 7.33e-08

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 54.13  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 256 SGIVDGAAVVLLASEKAVKEQNLKP------RAKVLATALVG-----TDPTIMLTGPApAARKALEKAGLTIDDIDLFEV 324
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrlvEIKSLACASGNlyedpPDATRMFTSRA-AAQKALSMAGVKPSDLQVAEV 334
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 480057380 325 NEAFAAVVMRFINELNV--------------------PPekVNVNGGAIALGHPLGATG 363
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaeyghakdlirngatalegrIP--VNTGGGLLSFGHPVGATG 391
PRK07516 PRK07516
thiolase domain-containing protein;
256-401 7.79e-08

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 53.80  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 256 SGIVDGAAVVLLASEKAVKEqnLKPRAKVLATALVGT-------DPTIMlTGPAPAARKALEKAGLTIDDIDLFEVNEAF 328
Cdd:PRK07516 213 SLVSDGAAALVLADAETARA--LQRAVRFRARAHVNDflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDCF 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 329 --AAVVM-------------RFINELNVPPE---KVNVNGGAIALGHPLGATG-------AMILGTLLDELERQNKKRGL 383
Cdd:PRK07516 290 tiAELIEyeamglappgqgaRAIREGWTAKDgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKLAG 369
                        170       180
                 ....*....|....*....|.
gi 480057380 384 atLCVGGGMGIA---TIIERV 401
Cdd:PRK07516 370 --VFNMGGAAVAnyvSILERV 388
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
256-367 2.45e-07

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 52.38  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 256 SGIVDGAAVVLLASEKAVKEQnlkPRAKVLA--------TALVGTDPTIMLTGPAP--------AARKALEKAGLTIDDI 319
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDY---ADARPIPrikgwghrTAPLGLEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDL 296
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480057380 320 DLFEVNEAFAAVVMRFINELNV-PPEK-----------------VNVNGGAIALGHPLGATGA-MIL 367
Cdd:PRK06289 297 DGFEVHDCFTPSEYLAIDHIGLtGPGEswkaiengeiaiggrlpINPSGGLIGGGHPVGASGVrMLL 363
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
257-377 3.66e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 48.51  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 257 GIV--DGAAVVLLASEKAVKEQNLKPRAKVL-----ATALVGTDPTIMLTGPAPAARKALEKAGLTIDDIDLF------- 322
Cdd:PRK05952 205 GLVlgEGGAILVLESAELAQKRGAKIYGQILgfgltCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtat 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 480057380 323 EVNEAFAAVVMRfinelNVPPEKVNVNGGAIALGHPLGATGAMILGTLLDELERQ 377
Cdd:PRK05952 285 RLNDQREANLIQ-----ALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQ 334
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
302-392 7.04e-06

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


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 47.41  E-value: 7.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 302 APAARKALEKAGLTIDDIDLF---EVNEAFAAVVMRfinELNVPPEKVNVNggaIA-LGHplgaTGAMILGTLLDELERQ 377
Cdd:COG0332  227 PEVIREALEKAGLTLDDIDWFiphQANLRIIEAVAK---RLGLPEEKVVVN---IDrYGN----TSAASIPLALDEALRE 296
                         90
                 ....*....|....*...
gi 480057380 378 NK-KRG--LATLCVGGGM 392
Cdd:COG0332  297 GRiKPGdlVLLAGFGAGL 314
PRK06365 PRK06365
thiolase domain-containing protein;
260-399 1.23e-05

thiolase domain-containing protein;


Pssm-ID: 235785 [Multi-domain]  Cd Length: 430  Bit Score: 47.21  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 260 DGAAVVLLASEKAVKEQNLKP-RAKVLATALVGTDPTIMLTGPAP--------------------------AARKALEKA 312
Cdd:PRK06365 227 DGAACAILASEDKAFEITDKPvLIKAIGTGSDTLRLADRPFGEVPllpnespddykdlrypgvhsfragrmAAKEAYEMA 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 313 GLT--IDDIDLFEVNEAFAAVVMRFINELNVPPE------------------KVNVNGGAIALGHPLGATGAM------- 365
Cdd:PRK06365 307 GITdpLNDLDLIELHDAYTSSEIQTYEDLGLCKYgeggqfiesgkpelpgklPVNPSGGLLAAGHAVGATGIMqavfmfw 386
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 480057380 366 -ILGTL-----LDELERQNKKRGLATLCVGGGMGI-ATIIE 399
Cdd:PRK06365 387 qLQGRIkkhfhDDYLQVKNAKRGLIHSHAGTGTYVtVTILE 427
PRK06066 PRK06066
thiolase domain-containing protein;
92-391 1.62e-05

thiolase domain-containing protein;


Pssm-ID: 180380 [Multi-domain]  Cd Length: 385  Bit Score: 46.67  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  92 ASGLEAVNMAAMKVRSGWEDLVVaggVESMSR---IPMGSDGGPWALDP----ETNLKSSFVPQGVGADLIATLDGYTRE 164
Cdd:PRK06066  86 GDGLQGLAHAVMHINSGLANVVV---VEAHSKpsdILTFSDVVKFAMDPiyvrPIGPPNPHFIAGLDAVKFMSRKGITRE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 165 DVDTFAVNSQQkaaaaqaNGYFDqsvvPVKDHSGVVILekDEFIKGNTTVEGLTKLNpsfemmgqmgfdaIAlqkypeaq 244
Cdd:PRK06066 163 DLALVVEKNKK-------AGLSN----PRASYASNISL--EDVLSSEYVVYPLTELD-------------IA-------- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 245 kinhvhhagnssGIVDGAAVVLLASEKAVKEQNLKP---RAKVLATALVGTDptIMLTGPAPAARKALEKA----GLT-- 315
Cdd:PRK06066 209 ------------PFVDGAIVVVLASEEVAKKLTDDPvwiKGIGWSTESSNLE--TAELGKANYMRIAADMAykmaGIEsp 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 316 IDDIDLFEVNEAFAAVVMRFINELNVPPE------------------KVNVNGGAIALGHPLGATGamiLGTLLDELERQ 377
Cdd:PRK06066 275 RKEVDAAEVDDRYSYKELQHIEALRLSEEpekdsllregnfdpqgelPVNPSGGHLAKGVPLEASG---LSLLLDAVEYL 351
                        330
                 ....*....|....
gi 480057380 378 nkkRGLATLCVGGG 391
Cdd:PRK06066 352 ---RGEAGARQGKA 362
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
302-398 5.75e-05

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 44.84  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 302 APAARKALEKAGLTIDDIDLF-------EVNEAFAAvvmrfinELNVPPEKVNVNggaialGHPLGATGAMILGTLLDEL 374
Cdd:cd00830  226 PESIEEALEKAGLTPDDIDWFvphqanlRIIEAVAK-------RLGLPEEKVVVN------LDRYGNTSAASIPLALDEA 292
                         90       100
                 ....*....|....*....|....*..
gi 480057380 375 ERQNK-KRG-LATLC-VGGGMGIATII 398
Cdd:cd00830  293 IEEGKlKKGdLVLLLgFGAGLTWGAAL 319
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
260-375 1.13e-04

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


Pssm-ID: 238421 [Multi-domain]  Cd Length: 332  Bit Score: 43.78  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 260 DGAAVVLLASEKAVKEQNLKPRAKVLATALvGTDPTIM------LTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVM 333
Cdd:cd00825  161 DGAGALVVEELEHALARGAHIYAEIVGTAA-TIDGAGMgafapsAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 480057380 334 RFINELNVP---PEKVNVNGGAIALGHPLGATGAMILGTLLDELE 375
Cdd:cd00825  240 VKELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
91-132 2.95e-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: 42.24  E-value: 2.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 480057380   91 CASGLEAVNMAAMKVRSGWEDLVVAGGVESM---------SRIPMGSDGGP 132
Cdd:pfam00109 173 CSSSLVAIHAAVQSIRSGEADVALAGGVNLLltplgfagfSAAGMLSPDGP 223
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
309-398 5.40e-04

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 38.64  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  309 LEKAGLTIDDIDLFEVNEAFAAVVMRFINELNVPPEKVNVNggaiaLGHpLGATGAMILGTLLDELERQNK-KRG-LATL 386
Cdd:pfam08541   1 LEKAGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVN-----LDE-YGNTSAASIPLALDEAVEEGKlKPGdLVLL 74
                          90
                  ....*....|...
gi 480057380  387 C-VGGGMGIATII 398
Cdd:pfam08541  75 VgFGAGLTWGAAL 87
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
254-320 7.61e-04

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 41.56  E-value: 7.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480057380 254 NSSGIVDG--AAVVLLASEKAVKEQNLKPRAKVLATALV-----GTDPTimLTGPAPAARKALEKAGLTIDDID 320
Cdd:PRK07103 231 DRDGFIYGeaCGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPS--LEGEMRVIRAALRRAGLGPEDID 302
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
39-131 8.69e-04

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


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 40.88  E-value: 8.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  39 LQQRHQLDTSKVDDIVLGCVTPIgDQGGDIAKTAAIAAGwNDDVAGVQINRFCASGLEAVNMAAMKVRSG-WED-LVVAG 116
Cdd:cd00827   59 ALERAGIDPDDIGLLIVATESPI-DKGKSAATYLAELLG-LTNAEAFDLKQACYGGTAALQLAANLVESGpWRYaLVVAS 136
                         90       100
                 ....*....|....*....|.
gi 480057380 117 GV------ESMSRIPMGSDGG 131
Cdd:cd00827  137 DIasylldEGSALEPTLGDGA 157
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
256-365 9.75e-04

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: 41.23  E-value: 9.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 256 SGIV--DGAAVVLLASEKAVKEQNLKPRAKVL-------ATALVGTDPTimLTGPAPAARKALEKAGLTIDDIDLfeVN- 325
Cdd:COG0304  225 DGFVlgEGAGVLVLEELEHAKARGAKIYAEVVgygassdAYHITAPAPD--GEGAARAMRAALKDAGLSPEDIDY--INa 300
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 480057380 326 -------------EAFAAVvmrFINELNVPPekVNVNGGAIalGHPLGATGAM 365
Cdd:COG0304  301 hgtstplgdaaetKAIKRV---FGDHAYKVP--VSSTKSMT--GHLLGAAGAI 346
PRK06158 PRK06158
thiolase; Provisional
261-401 1.02e-03

thiolase; Provisional


Pssm-ID: 180434 [Multi-domain]  Cd Length: 384  Bit Score: 40.78  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 261 GAAVVLLASEKAvkeQNL-KPRAKVLATAL------VGTDPTIMLTGPAPAARKALEKAGLTIDDIDLFEVNEAFAAVVM 333
Cdd:PRK06158 212 AGAVVMVRADRA---RDLpRPPVYVLGAAAatwhrqISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINTI 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480057380 334 RFINELNVPPEKVN---VNGGAIALGhplgatGAMILGTlldelerqnKKRGLAtlCVGGGM-GIATIIERV 401
Cdd:PRK06158 289 LFLEDLGFCAKGEGgafVEGGRIAPG------GRLPVNT---------NGGGLS--CVHPGMyGLFLLIEAV 343
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
256-365 1.38e-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: 40.60  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 256 SGIV--DGAAVVLLASEKAVKEQNLKPRAKVLATALVG-----TDPTIMLTGPAPAARKALEKAGLTIDDIDLfeVN--- 325
Cdd:cd00834  225 DGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahg 302
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 480057380 326 -----------EAFAAVvmrFINELNVPPekVNVNGGAIalGHPLGATGAM 365
Cdd:cd00834  303 tstplndaaesKAIKRV---FGEHAKKVP--VSSTKSMT--GHLLGAAGAV 346
PRK08313 PRK08313
thiolase domain-containing protein;
260-366 1.50e-03

thiolase domain-containing protein;


Pssm-ID: 181378 [Multi-domain]  Cd Length: 386  Bit Score: 40.48  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 260 DGAAVVLLASEKAVKEQNLKPRAKVLATALVgTDPTIML-------TGPAPAARKALEKAGLT--IDDIDLFEVNEAFAA 330
Cdd:PRK08313 210 DGACAVVIGDEEAADAAAGRPVAWIHGTAMR-TEPLAFAgrdqvnpQAGRDAAAALWKAAGITdpRDEIDVAEIYVPFSW 288
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 480057380 331 VVMRFINELNVPPE------------------KVNVNGGAIAlGHPLGATGaMI 366
Cdd:PRK08313 289 FEPMWLENLGFAPEgegwklteagetaiggrlPVNPSGGVLS-SNPIGASG-MI 340
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
91-122 1.51e-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: 40.60  E-value: 1.51e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 480057380  91 CASGLEAVNMAAMKVRSGWEDLVVAGGVESMS 122
Cdd:cd00834  161 CASGAHAIGDAARLIRLGRADVVIAGGAEALI 192
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
259-344 3.18e-03

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 39.51  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 259 VD-GAAVVLLASEKA----VKEQNL----------KPRAkVLATALVGTDPTIMLtgpapAARKALEKAGLTIDDIDLFE 323
Cdd:PRK08257 243 VDqGAAVLLTSVAKArrlgVPEDRWvylhggadahDPYD-ILERPDLHRSPAIRA-----AGRRALALAGLGIDDIDAFD 316
                         90       100
                 ....*....|....*....|.
gi 480057380 324 VNEAFAAVVMRFINELNVPPE 344
Cdd:PRK08257 317 LYSCFPSAVQVAARELGLDLD 337
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
91-128 3.33e-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: 39.31  E-value: 3.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 480057380  91 CASGLEAVNMAAMKVRSGWEDLVVAGGVESM-SRIPMGS 128
Cdd:COG0304  161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAiTPLGLAG 199
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
45-384 3.37e-03

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 39.24  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380  45 LDTSKVDDIVLGcvTPIGDQGGDIAKTAAIAAGWNDDVAGVQINRFCASGLEAVNMAAMKVRSGWEDLVVAGGVESM--- 121
Cdd:PRK06157  44 IEPKDIDAAWFG--THYDEIGSGKSGTPLSRALRLPNIPVTRVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLkdt 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 122 --SRIPMGSDGGP-WALDPETNLKSSFVpQGVGAdlIATLDGYTREDVDTFAVNsqqkaaaaqangyfdqsvVPVKDHSG 198
Cdd:PRK06157 122 gyGGLPVANPGTLaDMTMPNVTAPGNFA-QLASA--YAAKYGVSREDLKRAMAH------------------VSVKSHAN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 199 VVILEKDEFIKgNTTVEGLTKlnpSFEMMGQMG-FDAialqkypeaqkinhvhhagnsSGIVDGAAVVLLASEKAVKEQN 277
Cdd:PRK06157 181 GARNPKAHLRK-AVTEEQVLK---APMIAGPLGlFDC---------------------CGVSDGAAAAIVTTPEIARALG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 278 LKPRAKVLATALV----------GTDPTIMLTGPApAARKALEKAGLT--IDDIDLFEVNEAFAAVVMRFINELNVPPE- 344
Cdd:PRK06157 236 KKDPVYVKALQLAvsngwelqynGWDGSYFPTTRI-AARKAYREAGITdpREELSMAEVHDCFSITELVTMEDLGLSERg 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480057380 345 -----------------KVNVNGGAIALGHPLGATGAMILGTLLDEL-----ERQ--NKKRGLA 384
Cdd:PRK06157 315 qawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRMLYEMYLQLlgragERQlkNPRLALT 378
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
302-391 3.71e-03

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 38.90  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480057380 302 APAARKALEKAGLTIDDIDLF-------EVNEAFAavvmrfiNELNVPPEKVNVNggaiaLGHpLGATGAMILGTLLDEL 374
Cdd:PRK09352 222 AKVAREALEAAGLTPEDIDWLvphqanlRIIDATA-------KKLGLPMEKVVVT-----VDK-YGNTSAASIPLALDEA 288
                         90       100
                 ....*....|....*....|
gi 480057380 375 ERQNK-KRG--LATLCVGGG 391
Cdd:PRK09352 289 VRDGRiKRGdlVLLEGFGGG 308
 
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.
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