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Conserved domains on  [gi|1222381029|ref|WP_090433237|]
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acetyl-CoA C-acyltransferase [Ectopseudomonas guguanensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06954 super family cl30647
acetyl-CoA C-acetyltransferase;
1-396 0e+00

acetyl-CoA C-acetyltransferase;


The actual alignment was detected with superfamily member PRK06954:

Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 575.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLS 80
Cdd:PRK06954    2 TAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  81 QAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYERGR 160
Cdd:PRK06954   82 LSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 161 LMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQPPKARPDKIPGLKPAFR 240
Cdd:PRK06954  162 LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:PRK06954  242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEIN 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222381029 321 EAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIELY 396
Cdd:PRK06954  322 EAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
 
Name Accession Description Interval E-value
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-396 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 575.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLS 80
Cdd:PRK06954    2 TAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  81 QAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYERGR 160
Cdd:PRK06954   82 LSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 161 LMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQPPKARPDKIPGLKPAFR 240
Cdd:PRK06954  162 LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:PRK06954  242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEIN 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222381029 321 EAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIELY 396
Cdd:PRK06954  322 EAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
6-394 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 537.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   6 DPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQC 85
Cdd:COG0183     2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMgHGQVLDHMFLDGLEDAYErGRLMGTF 165
Cdd:COG0183    82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYT-GLSMGET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 166 AEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGT 244
Cdd:COG0183   160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPrPDTTLEKLAKLKPAFKKDGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 245 VTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFA 324
Cdd:COG0183   240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 325 VVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:COG0183   320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIE 389
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
9-394 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 520.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTTL 88
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  89 NKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQvLDHMFLDGLEDAYErGRLMGTFAED 168
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT-LDGMLDDGLTDPFT-GLSMGITAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 169 CAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTVTA 247
Cdd:cd00751   159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPrPDTTLEKLAKLKPAFKKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 248 ANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAVVP 327
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 328 MVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
10-394 4.32e-144

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: 414.32  E-value: 4.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTTLN 89
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  90 KMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARA-RGGYRMGHGQVLDHMFLDgLEDAYErGRLMGTFAED 168
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANT-GLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 169 CAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIrPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 248 ANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAVVP 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 328 MVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
8-264 3.03e-91

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: 275.34  E-value: 3.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLAR-ARGGYRMGHGQVLDHMFLDGLEDAYErGRLMGTFA 166
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTdARSGLKHGDEKKHDLLIPDGLTDAFN-GYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 167 EDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIrPPTTAEPLAKLKPAFDKEGTV 239
                         250
                  ....*....|....*....
gi 1222381029 246 TAANASSISDGAAALLLMR 264
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMS 258
 
Name Accession Description Interval E-value
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
1-396 0e+00

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 575.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLS 80
Cdd:PRK06954    2 TAVDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  81 QAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYERGR 160
Cdd:PRK06954   82 LSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 161 LMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQPPKARPDKIPGLKPAFR 240
Cdd:PRK06954  162 LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:PRK06954  242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEIN 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222381029 321 EAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIELY 396
Cdd:PRK06954  322 EAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
6-394 0e+00

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


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 537.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   6 DPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQC 85
Cdd:COG0183     2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMgHGQVLDHMFLDGLEDAYErGRLMGTF 165
Cdd:COG0183    82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYT-GLSMGET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 166 AEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGT 244
Cdd:COG0183   160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPrPDTTLEKLAKLKPAFKKDGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 245 VTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFA 324
Cdd:COG0183   240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 325 VVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:COG0183   320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIE 389
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
9-394 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 520.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTTL 88
Cdd:cd00751     1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  89 NKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQvLDHMFLDGLEDAYErGRLMGTFAED 168
Cdd:cd00751    81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT-LDGMLDDGLTDPFT-GLSMGITAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 169 CAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTVTA 247
Cdd:cd00751   159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPrPDTTLEKLAKLKPAFKKDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 248 ANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAVVP 327
Cdd:cd00751   239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 328 MVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:cd00751   319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
8-395 1.16e-171

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 484.98  E-value: 1.16e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:PLN02644    3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYERGRlMGTFAE 167
Cdd:PLN02644   83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFG-MGVCAE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 168 DCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRER--RLVATDEQPPKARPDKIPGLKPAFRE-GGT 244
Cdd:PLN02644  162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGKFDPAKLRKLRPSFKEdGGS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 245 VTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFA 324
Cdd:PLN02644  242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222381029 325 VVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIEL 395
Cdd:PLN02644  322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
PRK05790 PRK05790
putative acyltransferase; Provisional
8-394 1.08e-170

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 482.34  E-value: 1.08e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:PRK05790    4 VVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYErGRLMGTFAE 167
Cdd:PRK05790   84 INKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFN-GYHMGITAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 168 DCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-ERRLVATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:PRK05790  163 NLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKgDPVVVDTDEHPrPDTTAESLAKLRPAFDKDGTV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 246 TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAV 325
Cdd:PRK05790  243 TAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAA 322
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222381029 326 VPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK05790  323 QALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
10-394 4.32e-144

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: 414.32  E-value: 4.32e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTTLN 89
Cdd:TIGR01930   1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  90 KMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARA-RGGYRMGHGQVLDHMFLDgLEDAYErGRLMGTFAED 168
Cdd:TIGR01930  81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANT-GLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 169 CAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTVTA 247
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIrPNTTLEKLAKLKPAFDPDGTVTA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 248 ANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAVVP 327
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 328 MVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
9-396 2.75e-141

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 407.56  E-value: 2.75e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTTL 88
Cdd:PRK08235    5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  89 NKMCGSGMQALMLGhDQLL-AGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYeRGRLMGTFAE 167
Cdd:PRK08235   85 NKVCASGLRAVTLA-DQIIrAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAF-SGVHMGVYGG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 168 DCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-ERRLVATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:PRK08235  163 EVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKgDPIVVAKDEAPrKDTTIEKLAKLKPVFDKTGTI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 246 TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAV 325
Cdd:PRK08235  243 TAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAA 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222381029 326 VPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIELY 396
Cdd:PRK08235  323 VALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
8-394 1.18e-122

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 360.36  E-value: 1.18e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:PRK05656    4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMFLDGLEDAYERGRlMGTFAE 167
Cdd:PRK05656   84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYH-MGITAE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 168 DCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLV-ATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:PRK05656  163 NLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAfATDEQPrAGTTAESLAKLKPAFKKDGSV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 246 TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAV 325
Cdd:PRK05656  243 TAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAA 322
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222381029 326 VPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK05656  323 QSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
PRK09051 PRK09051
beta-ketothiolase BktB;
8-394 9.11e-114

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 337.70  E-value: 9.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQA-PARQAALGAGLSQAAQCT 86
Cdd:PRK09051    5 VVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMyLSRVAAINAGVPQETPAF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  87 TLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQVLDHMfLDGLEDAYERGRlMGTFA 166
Cdd:PRK09051   85 NVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMM-VGALHDPFGTIH-MGVTA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 167 EDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFR-EGGT 244
Cdd:PRK09051  163 ENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVrADTTLEDLAKLKPVFKkENGT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 245 VTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFA 324
Cdd:PRK09051  243 VTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFA 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 325 VVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK09051  323 AQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
8-394 2.23e-100

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 303.80  E-value: 2.23e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLER-AGLAAEAVDTVLMGCVLQAGQ-GQAPARQAALGAGLSQAAQC 85
Cdd:PRK09050    4 AFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMgHGQVLDHM----FLDGLEDAYERGRL 161
Cdd:PRK09050   84 TTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSR-QAEIFDTTigwrFVNPLMKAQYGVDS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 162 MGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-ERRLVATDEQP-PKARPDKIPGLKPAF 239
Cdd:PRK09050  163 MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKgDPVVVDRDEHPrPETTLEALAKLKPVF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 240 REGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEI 319
Cdd:PRK09050  243 RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVIEL 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 320 NEAFAVVPMVAMRELGIAHD--KLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK09050  323 NEAFAAQGLAVLRQLGLADDdaRVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
8-395 4.33e-98

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 297.31  E-value: 4.33e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:PRK06366    4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLArarGGYRMGHGQVL-------DHMFLDGLEDA--YER 158
Cdd:PRK06366   84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLP---SDLRWGPKHLLhknykidDAMLVDGLIDAfyFEH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 159 grlMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEAsqgrerrlVATDEQPPKARPDKIPGLKPA 238
Cdd:PRK06366  161 ---MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIRKTTMEDLAKLPPA 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 239 FREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFE 318
Cdd:PRK06366  230 FDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVE 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 319 INEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIEL 395
Cdd:PRK06366  310 HNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEM 386
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
8-394 2.19e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 296.13  E-value: 2.19e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGcvlQA-GQGQAPA--RQAALGAGLSQAAQ 84
Cdd:PRK06205    4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG---QGyPNGEAPAigRVAALDAGLPVTVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  85 CTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMGHGQvldhmfldgLEDAYERGRL--- 161
Cdd:PRK06205   81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQ---------LHDRLARGREtag 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 162 ---------MGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-ERRLVATDEQP-PKARPD 230
Cdd:PRK06205  152 grrfpvpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKgDPTVVDRDEHPrADTTLE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 231 KIPGLKP---AFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARI 307
Cdd:PRK06205  232 SLAKLRPimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 308 EWTLETVDLFEINEAFAVVPMVAMRELGIA---HDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIG 384
Cdd:PRK06205  312 GLTLDDIDLIELNEAFAAQVLAVLKEWGFGaddEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIG 391
                         410
                  ....*....|
gi 1222381029 385 GGEATAVAIE 394
Cdd:PRK06205  392 GGQGLAAVFE 401
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
7-394 9.69e-97

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 294.25  E-value: 9.69e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   7 PVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCT 86
Cdd:PRK06633    4 PVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  87 TLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMS---NAPYLlaraRGGYRMGHGQVLDHMFLDGLEDAYErGRLMG 163
Cdd:PRK06633   84 TINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI----RAGAKFGDIKMVDLMQYDGLTDVFS-GVFMG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 164 TFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQppkARPDK----IPGLKPAF 239
Cdd:PRK06633  159 ITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDET---VRPDTsleiLSKLRPAF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 240 REGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEI 319
Cdd:PRK06633  236 DKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEV 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 320 NEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK06633  316 NEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
pcaF TIGR02430
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ...
8-394 2.10e-91

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


Pssm-ID: 131483  Cd Length: 400  Bit Score: 280.52  E-value: 2.10e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLER-AGLAAEAVDTVLMGCVLQAGQ-GQAPARQAALGAGLSQAAQC 85
Cdd:TIGR02430   3 AYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSVPG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMG---HGQVLDHMFLDGLEDAYERGRLM 162
Cdd:TIGR02430  83 TTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSakiEDTTIGWRFINPLMKALYGVDSM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 163 GTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-ERRLVATDEQP-PKARPDKIPGLKPAFR 240
Cdd:TIGR02430 163 PETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKgEPTVVDQDEHPrPETTLEGLAKLKPVVR 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:TIGR02430 243 PDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELN 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222381029 321 EAFAVVPMVAMRELGIAHD--KLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:TIGR02430 323 EAFAAQALAVLRELGLADDdaRVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
8-264 3.03e-91

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: 275.34  E-value: 3.03e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:pfam00108   1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLAR-ARGGYRMGHGQVLDHMFLDGLEDAYErGRLMGTFA 166
Cdd:pfam00108  81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTdARSGLKHGDEKKHDLLIPDGLTDAFN-GYHMGLTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 167 EDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIrPPTTAEPLAKLKPAFDKEGTV 239
                         250
                  ....*....|....*....
gi 1222381029 246 TAANASSISDGAAALLLMR 264
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMS 258
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
10-394 7.16e-89

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 273.51  E-value: 7.16e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGqGQAP--ARQAALGAGLSQAAQCTT 87
Cdd:PRK07801    6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQAGniARTSWLAAGLPEEVPGVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARG-----GYRMGHGQVLDHMFLDGlEDAYERGrlm 162
Cdd:PRK07801   85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGeqlgfTSPFAESKGWLHRYGDQ-EVSQFRG--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 163 gtfAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEAsqgrerrlVATDEQPPKARPDKIPGLKPaFREG 242
Cdd:PRK07801  161 ---AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG--------VTVDEGPRETSLEKMAGLKP-LVEG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 243 GTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEA 322
Cdd:PRK07801  229 GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEA 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222381029 323 FAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK07801  309 FAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
9-394 3.15e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 272.65  E-value: 3.15e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMG-GFLGDLAGFSAAELGAAAIRSSLERA-GLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQc 85
Cdd:PRK07851    5 VIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDFLPG- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMS--------------NAPYLLARARGGYRMGHGQVLDHmfldg 151
Cdd:PRK07851   84 TTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtkNPLFAEAQARTAARAEGGAEAWH----- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 152 leDAYERGRL------MGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRerrLVATDEQPp 225
Cdd:PRK07851  159 --DPREDGLLpdvyiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGT---VVSTDDGP- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 226 kaRP----DKIPGLKPAFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQ 301
Cdd:PRK07851  233 --RAgttyEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASK 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 302 RLLARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASV 381
Cdd:PRK07851  311 QALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETM 390
                         410
                  ....*....|...
gi 1222381029 382 CIGGGEATAVAIE 394
Cdd:PRK07851  391 CVGGGQGMAMVLE 403
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
9-395 8.79e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 271.24  E-value: 8.79e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMG-GFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVL-QAGQGQAPARQAALGAGLSQAAQCT 86
Cdd:PRK07661    5 VIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTVPAI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  87 TLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYllararggyrMGHGQVLDHMFLdglEDAYERGRLMGTFA 166
Cdd:PRK07661   85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGHVVRPNPRLV---EAAPEYYMGMGHTA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 167 EDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR---------ERRLVATDEQ-PPKARPDKIPGLK 236
Cdd:PRK07661  152 EQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennklqeETITFSQDEGvRADTTLEILGKLR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 237 PAFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDL 316
Cdd:PRK07661  232 PAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGL 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222381029 317 FEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIEL 395
Cdd:PRK07661  312 FELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFEL 390
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
9-394 9.69e-86

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 265.82  E-value: 9.69e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQCTT 87
Cdd:PRK07850    5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGATT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYllarargGYRMGHGQVL---DHMFLDgLEDAYERgrlmgt 164
Cdd:PRK07850   85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL-------GANAGPGRGLprpDSWDID-MPNQFEA------ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 165 fAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR-------ERRLVATDEQPPKARPDKIPGLKP 237
Cdd:PRK07850  151 -AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRDTTMEGLAGLKP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 238 AfREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLF 317
Cdd:PRK07850  230 V-LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLV 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 318 EINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK07850  309 EINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
5-394 2.31e-84

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 262.35  E-value: 2.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   5 LDPVVIVSAVRTPMGGFL------GDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQA-PARQAALGA 77
Cdd:PRK06445    1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  78 GLSQAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPyllararggyrMGHGQVLD-HM-FLdgLEDA 155
Cdd:PRK06445   81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP-----------MGDNPHIEpNPkLL--TDPK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 156 YER-----GRLMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDEQppkARPD 230
Cdd:PRK06445  148 YIEydlttGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQS---VRPD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 231 ----KIPGLKPAFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLAR 306
Cdd:PRK06445  225 tsleKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 307 IEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGG 386
Cdd:PRK06445  305 AGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGG 384

                  ....*...
gi 1222381029 387 EATAVAIE 394
Cdd:PRK06445  385 QGGAVVLE 392
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
8-394 1.24e-83

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 260.28  E-value: 1.24e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAE-LGAAAIRSSLER-AGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQ 84
Cdd:PRK08947    4 VVIVDAIRTPMGRSKGGAFRNVRAEdLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSVP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  85 CTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPyllararggyrMGHGqvLDHMFLDGLEDAYERGrLMGT 164
Cdd:PRK08947   84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG--VDFHPGLSKNVAKAAG-MMGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 165 FAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEA--SQGReRRLVATDEQ-PPKARPDKIPGLKPAFR- 240
Cdd:PRK08947  150 TAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGhdADGV-LKLFDYDEViRPETTVEALAALRPAFDp 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:PRK08947  229 VNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 308
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 321 EAFAVVPMVAMRELGI---AHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK08947  309 EAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
1-394 5.11e-83

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 259.16  E-value: 5.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPMG-GFLGDLAGFSAAELGAAAIRSSLERA-GLAAEAVDTVLMGCVL-QAGQGQAPARQAALGA 77
Cdd:PRK09052    1 MSKQLQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  78 GLSQAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYllararggyrMGHGQVLDHMFLDGLED--- 154
Cdd:PRK09052   81 GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENvgi 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 155 AYErgrlMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR----------ERRLVATDEQP 224
Cdd:PRK09052  151 AYG----MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 225 -PKARPDKIPGLKPAFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRL 303
Cdd:PRK09052  227 rADTSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAA 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 304 LARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCI 383
Cdd:PRK09052  307 LKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCV 386
                         410
                  ....*....|.
gi 1222381029 384 GGGEATAVAIE 394
Cdd:PRK09052  387 GTGMGAAGIFE 397
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
10-394 6.72e-83

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 258.51  E-value: 6.72e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQCTTL 88
Cdd:PRK06504    6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTSI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  89 NKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLArARGGYRMGHGqvldHMFLDGLEDAY---ERGRLMGtf 165
Cdd:PRK06504   86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-STLPAKNGLG----HYKSPGMEERYpgiQFSQFTG-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 166 AEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQ--GRERRLVATDEQPPKARPDKIPGLKPaFREGG 243
Cdd:PRK06504  159 AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRadGSGEMHTVDEGIRFDATLEGIAGVKL-IAEGG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 244 TVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAF 323
Cdd:PRK06504  238 RLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAF 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222381029 324 AVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK06504  318 ASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
10-394 2.54e-81

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 254.81  E-value: 2.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFL--GDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQCT 86
Cdd:PRK08242    6 IYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  87 TLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPylLARARGGYRMGHGQVLDHMFLDgledayergrlMGTFA 166
Cdd:PRK08242   86 QINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP--MGSDGGAWAMDPSTNFPTYFVP-----------QGISA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 167 EDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRErrLVATDEQP-PKARPDKIPGLKPAFREGGTV 245
Cdd:PRK08242  153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLT--ILDHDEHMrPGTTMESLAKLKPSFAMMGEM 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 246 ---------------------TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLL 304
Cdd:PRK08242  231 ggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKAL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 305 ARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIG 384
Cdd:PRK08242  311 AKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVG 390
                         410
                  ....*....|
gi 1222381029 385 GGEATAVAIE 394
Cdd:PRK08242  391 GGMGIATIIE 400
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
7-394 4.75e-79

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 249.55  E-value: 4.75e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   7 PVVIVSAVRTPmggFLGDLAG---FSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAA 83
Cdd:PRK08170    4 PVYIVDGARTP---FLKARGGpgpFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  84 QCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARA-----RGGYRM-GHGQVLDHMF--------- 148
Cdd:PRK08170   81 PAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKmvrwlAGWYAAkSIGQKLAALGklrpsylap 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 149 ----LDGLEDAYErGRLMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFAsEIVAVEASQGRerRLVATDEQP 224
Cdd:PRK08170  161 viglLRGLTDPVV-GLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK--FYDHDDGVR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 225 PKARPDKIPGLKPAF-REGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRL 303
Cdd:PRK08170  237 PDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 304 LARIEWTLETVDLFEINEAFAVVPMVAMR----------ELGIAH-------DKLNVHGGACALGHPIGASGARILVTLL 366
Cdd:PRK08170  317 LQRHGLTLEDLDLWEINEAFAAQVLACLAawadeeycreQLGLDGalgeldrERLNVDGGAIALGHPVGASGARIVLHLL 396
                         410       420
                  ....*....|....*....|....*...
gi 1222381029 367 AALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK08170  397 HALKRRGTKRGIAAICIGGGQGGAMLLE 424
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
10-394 2.74e-78

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 247.00  E-value: 2.74e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQ-GQAPARQAALGAGLSQAAQCTTL 88
Cdd:PRK08131    6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  89 NKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARARGGYRMgHGQVLDHM----FLDGLEDAYERGRLMGT 164
Cdd:PRK08131   86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSR-DAKVFDTTigarFPNPKIVAQYGNDSMPE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 165 FAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGR--ERRLVATDEQP-PKARPDKIPGLKPAFrE 241
Cdd:PRK08131  165 TGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRklPPKLVAEDEHPrPSSTVEALTKLKPLF-E 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 242 GGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINE 321
Cdd:PRK08131  244 GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINE 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 322 AFAVVPMVAMRELGIAHD--KLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK08131  324 AFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
10-394 1.83e-75

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 240.06  E-value: 1.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  10 IVSAVRTPMG-GFLGD--LAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAAQC 85
Cdd:PRK06025    6 IIDAVRTPRGiGKVGKgaLAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYDIKASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMS----NAPYLLARARGGYRMGHGqvldHMFLDGLEDAYERGrl 161
Cdd:PRK06025   86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaaMAAEDMAAGKPPLGMGSG----NLRLRALHPQSHQG-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 162 mgTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRerRLVATDEQP-PKARPDKIPGLKPAFR 240
Cdd:PRK06025  160 --VCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGS--VALDHEEFPrPQTTAEGLAALKPAFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 --------EGGTV------------------TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTT 294
Cdd:PRK06025  236 aiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 295 APVAAIQRLLARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGL 374
Cdd:PRK06025  316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
                         410       420
                  ....*....|....*....|
gi 1222381029 375 KRGMASVCIGGGEATAVAIE 394
Cdd:PRK06025  396 KRGLVTMCAAGGMAPAIIIE 415
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-394 2.06e-73

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 235.81  E-value: 2.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPM-----GGFlgdlAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQA-PARQAA 74
Cdd:PLN02287   41 TTAFGDDVVIVAAYRTPIckakrGGF----KDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  75 LGAGLSQAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSnapyllararggyrmghgqvLDHMFLDG--- 151
Cdd:PLN02287  117 FYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMT--------------------TNPMAWEGgvn 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 152 -----LEDAYERGRLMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAV-----EASQGRERRLV--A 219
Cdd:PLN02287  177 prvesFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkivDPKTGEEKPIVisV 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 220 TDEQPPKARPDKIPGLKPAFREGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAA 299
Cdd:PLN02287  257 DDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVA 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 300 IQRLLARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRG--LKRG 377
Cdd:PLN02287  337 IPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFG 416
                         410
                  ....*....|....*..
gi 1222381029 378 MASVCIGGGEATAVAIE 394
Cdd:PLN02287  417 VVSMCIGTGMGAAAVFE 433
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
9-394 1.02e-72

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 231.19  E-value: 1.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMGGFLGDLAGFSAAELGAAAIR---SSLERAglaaeaVDTVLMGCVLqaGQGQAPARQAALGAGLSQAAQC 85
Cdd:PRK06690    4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTflsKGMERE------IDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLlARARggyrmghgqvldhMFLDGLEDAYergrlMGTF 165
Cdd:PRK06690   76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ-NRAR-------------FSPETIGDPD-----MGVA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 166 AEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEAsqgrerrlvATDEQPPKARPDK--IPGLKPAFREGG 243
Cdd:PRK06690  137 AEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG---------LLDESIKKEMNYEriIKRTKPAFLHNG 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 244 TVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAF 323
Cdd:PRK06690  208 TVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAF 287
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222381029 324 AVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK06690  288 ASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
9-390 6.30e-72

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 230.43  E-value: 6.30e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   9 VIVSAVRTPMG----GFLGDLAGfsaAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAG-QGQAPARQAALGAGLSQAA 83
Cdd:PRK07108    5 VIVSTARTPLAkswrGAFNMTHG---ATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVTV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  84 QCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLARarggyrmghgqvldHMFLDG--LEDAYERGRL 161
Cdd:PRK07108   82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNR--------------HMLREGwlVEHKPEIYWS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 162 MGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQG-----------RERRLVATDEQPPKARPD 230
Cdd:PRK07108  148 MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGvadkatgrlftKEVTVSADEGIRPDTTLE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 231 KIPGLKPAFrEGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWT 310
Cdd:PRK07108  228 GVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLK 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 311 LETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATA 390
Cdd:PRK07108  307 VDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
fadA TIGR02445
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ...
8-394 3.00e-70

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


Pssm-ID: 131498  Cd Length: 385  Bit Score: 225.59  E-value: 3.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   8 VVIVSAVRTPMGGFLGDLAGFSAAE-LGAAAIRSSLER-AGLAAEAVDTVLMGCVLQA-GQGQAPARQAALGAGLSQAAQ 84
Cdd:TIGR02445   2 VVIVDFGRTPMGRSKGGAFRNTRAEdLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  85 CTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPyllararggyrMGHGQVLD-HMFLDgledAYERGRLMG 163
Cdd:TIGR02445  82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-----------MMHGVDFHpGMSLH----VAKAAGMMG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 164 TFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVE--ASQGRERRLVATDEQPPKARPDKIPGLKPAFR- 240
Cdd:TIGR02445 147 LTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQghDADGFLKQFDYDEVIRPETTVESLAALRPAFDp 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 241 EGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEIN 320
Cdd:TIGR02445 227 KNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELN 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222381029 321 EAFAVVPMVAMRELGI---AHDKLNVHGGACALGHPIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:TIGR02445 307 EAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
6-394 2.14e-56

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 190.97  E-value: 2.14e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   6 DPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQC 85
Cdd:PRK08963    5 DRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  86 TTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPYLLAR--ARGGYRMGH----GQVLDHMFLDGLED----- 154
Cdd:PRK08963   85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKklARALVDLNKartlGQRLKLFSRLRLRDllpvp 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 155 ----AYERGRLMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRErrlvaTDEQPPKARPD 230
Cdd:PRK08963  165 pavaEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ-----PLEEDNNIRGD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 231 KIPG----LKPAF-REGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAP-NLFTTAPVAAIQRLL 304
Cdd:PRK08963  240 STLEdyakLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLAL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 305 ARIEWTLETVDLFEINEAFAV-----VPMVAMRE-----LG-------IAHDKLNVHGGACALGHPIGASGARILVTLLA 367
Cdd:PRK08963  320 ERAGLTLADLTLIDMHEAFAAqtlanLQMFASERfarekLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQTLH 399
                         410       420
                  ....*....|....*....|....*..
gi 1222381029 368 ALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK08963  400 ELRRRGGGLGLTTACAAGGLGAAMVLE 426
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
11-394 1.15e-53

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: 182.69  E-value: 1.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  11 VSAVRTPMGGFLGDLAGFS---AAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQCTT 87
Cdd:cd00826     1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  88 LNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNApyllarARGGYRMGHgqvldhmfLDGLEDAYErgrlmgtfae 167
Cdd:cd00826    81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAKEKH--------IDVLINKYG---------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 168 dcaqqyrfSREEQDAYALESLRRAQQAIEQGSFASEIVAVEASQGRERRLVATDE---QPPKARPDKIPGLKPAFREGGT 244
Cdd:cd00826   137 --------MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiqFGDEASLDEIAKLRPAFDKEDF 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 245 VTAANASSISDGAAALLLMRLSEAQE-------RGLKPLARIVGHAGHAQAPNLFT----TAPVAAIQRLLARIEWTLET 313
Cdd:cd00826   209 LTAGNACGLNDGAAAAILMSEAEAQKhglqskaREIQALEMITDMASTFEDKKVIKmvggDGPIEAARKALEKAGLGIGD 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 314 VDLFEINEAFAVVPMVAMRELGIAHDK------------------LNVHGGACALGHPIGASGARILVTLLAALQQRGLK 375
Cdd:cd00826   289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
                         410       420
                  ....*....|....*....|....
gi 1222381029 376 R-----GMASVCIGGGEATAVAIE 394
Cdd:cd00826   369 RqgagaGLALLCIGGGGGAAMCIE 392
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
1-394 7.89e-50

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 173.55  E-value: 7.89e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   1 MNQHLDPVVIVSAVRTPMGGFLGDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLS 80
Cdd:PRK09268    2 TMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  81 QAAQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAP---------YLLARARGGYRMGHGQVLDHMFLDG 151
Cdd:PRK09268   82 PYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrkILLELNRAKTTGDRLKALGKLRPKH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 152 LEDAYER------GRLMGTFAEDCAQQYRFSREEQDAYALESLRRAQQAIEQGSFASEIVAVeasqgreRRLVATDEQPP 225
Cdd:PRK09268  162 LAPEIPRngeprtGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LGLTRDNNLRP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 226 KARPDKIPGLKPAF--REGGTVTAANASSISDGAAALLLMRLSEAQERGLKPLARIVghAGHAQAPNLFT------TAPV 297
Cdd:PRK09268  235 DSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV--DAETAAVDFVHgkegllMAPA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 298 AAIQRLLARIEWTLETVDLFEINEAFAVVPMVAMR----------ELG-------IAHDKLNVHGGACALGHPIGASGAR 360
Cdd:PRK09268  313 YAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGldaplgsIDRSKLNVNGSSLAAGHPFAATGGR 392
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1222381029 361 ILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:PRK09268  393 IVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
273-394 1.09e-44

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: 150.49  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 273 LKPLARIVGHAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLFEINEAFAVVPMVAMRELGIAHDKLNVHGGACALGH 352
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222381029 353 PIGASGARILVTLLAALQQRGLKRGMASVCIGGGEATAVAIE 394
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
23-393 3.44e-16

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: 79.23  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  23 GDLAGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSqAAQCTTLNKMCGSGMQALMLG 102
Cdd:cd00829     9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 103 HDQLLAGSADVLVAGGMESMSNAPY-LLARARGGYRMGHGQVLDHMFLDGLEDAYERGRLMGTFAEDCAQQYRFSREeQD 181
Cdd:cd00829    88 AAAIASGLADVVLVVGAEKMSDVPTgDEAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTTREDLAKVAVK-NH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 182 AYALESlRRAQqaieqgsFASEIVA--VEASqgrerRLVAtdeqPPkarpdkipglkpafreggtVTAANASSISDGAAA 259
Cdd:cd00829   167 RNAARN-PYAQ-------FRKPITVedVLNS-----RMIA----DP-------------------LRLLDCCPVSDGAAA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 260 LLLMRLSEAQERGLKPlARIVGHAGHAQAPNLFT-------TAPVAAIQRLLARIEWTLETVDLFEINEAFAVVPMVAMR 332
Cdd:cd00829   211 VVLASEERARELTDRP-VWILGVGAASDTPSLSErddflslDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALE 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 333 ELGIAHD------------------KLNVHGGACALGHPIGASGARILVTLL-------AALQQRGLKRGMASVcIGGGE 387
Cdd:cd00829   290 DLGFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVrqlrgeaGARQVPGARVGLAHN-IGGTG 368

                  ....*.
gi 1222381029 388 ATAVAI 393
Cdd:cd00829   369 SAAVVT 374
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
247-393 1.05e-13

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: 70.55  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 247 AANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFT----TAPVAAIQRLLARIEWTLETVDLFEINEA 322
Cdd:cd00327    94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPavsgEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 323 FAVVPMVAMRELGIAHDK---LNVHGGACALGHPIGASGARILVTLLAALQ-------QRGLKRGMASVCIGGGEATAVA 392
Cdd:cd00327   174 GTPIGDAVELALGLDPDGvrsPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253

                  .
gi 1222381029 393 I 393
Cdd:cd00327   254 L 254
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
32-392 1.21e-08

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 56.44  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  32 ELGAAAIRSSLERAGLAAEA--VDTVLMGCVL-QAGQGQAPARQAALGAGLSQAAQCTTLNK-------MCGSGMQALML 101
Cdd:PTZ00455   50 ELLATAIQGTLENTGLDGKAalVDKVVVGNFLgELFSSQGHLGPAAVGSLGQSGASNALLYKpamrvegACASGGLAVQS 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 102 GHDQLLAGSADVLVAGGMESMSNAPyllARARGGY--RMGHgqvldhmfldgledaYERGRLMGTFAEDC--AQQYRFSR 177
Cdd:PTZ00455  130 AWEALLAGTSDIALVVGVEVQTTVS---ARVGGDYlaRAAD---------------YRRQRKLDDFTFPClfAKRMKYIQ 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 178 EEQDAYALESLRRAQQAIEQGSfASEIVAVEASQGRERRLVATDEQPPKARPDkiPGLKPAFReggtvtAANASSISDGA 257
Cdd:PTZ00455  192 EHGHFTMEDTARVAAKAYANGN-KNPLAHMHTRKLSLEFCTGASDKNPKFLGN--ETYKPFLR------MTDCSQVSDGG 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 258 AALLLMRLSEAQERGLKPL-ARIVGHAGHAQAP-NLFTTAP--------VAAIQRLLARIEWTLETVDLFEINEAFAVVP 327
Cdd:PTZ00455  263 AGLVLASEEGLQKMGLSPNdSRLVEIKSLACASgNLYEDPPdatrmftsRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 328 MVAMRELGIA---HDK---------------LNVHGGACALGHPIGASGA-------RILVTLLAALQQRGLKRGMASVC 382
Cdd:PTZ00455  343 LLMYEALGIAeygHAKdlirngatalegripVNTGGGLLSFGHPVGATGVkqimevyRQMKGQCGEYQMKNIPALGATLN 422
                         410
                  ....*....|
gi 1222381029 383 IGGGEATAVA 392
Cdd:PTZ00455  423 MGGDDKTAVS 432
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
18-392 7.54e-08

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 53.92  E-value: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  18 MGGFLGDLA------GFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCV---LQAGQGQAPARQAALGAGLS-------Q 81
Cdd:PRK06289    8 LGGYQSDFArnwtkeGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPALWgvpasrhE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  82 AAqcttlnkmCGSGMQALMLGHDQLLAGSADVLVAGGMESMSNAPyllaRARGGYRMGHGQVLDHmflDGLEDAYERGRL 161
Cdd:PRK06289   88 AA--------CASGSVATLAAMADLRAGRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTGH---EGQDARFPWPSM 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 162 MGTFAEDCAQQYRFSREEqdayalesLRraqqAIEQGSFAseivaveasqgRERRlvatdeqPPKA--RPDKIPglKPAF 239
Cdd:PRK06289  153 FARVADEYDRRYGLDEEH--------LR----AIAEINFA-----------NARR-------NPNAqtRGWAFP--DEAT 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 240 REGGTVTAA--------NASSISDGAAALLLMRLSEAQE-RGLKPLARIVGHaGHAQAPNLFTT-------APV------ 297
Cdd:PRK06289  201 NDDDATNPVvegrlrrqDCSQVTDGGAGVVLASDAYLRDyADARPIPRIKGW-GHRTAPLGLEQkldrsagDPYvlphvr 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 298 AAIQRLLARIEWTLETVDLFEINEAFAVVPMVAMRELGIA------------------HDKLNVHGGACALGHPIGASGA 359
Cdd:PRK06289  280 QAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLTgpgeswkaiengeiaiggRLPINPSGGLIGGGHPVGASGV 359
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1222381029 360 RIL------VTLLAALQQRGLKRGMASVCIGGGEATAVA 392
Cdd:PRK06289  360 RMLldaakqVTGTAGDYQVEGAKTFGTLNIGGSTTTTVS 398
PRK06064 PRK06064
thiolase domain-containing protein;
250-391 1.35e-06

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 49.90  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 250 ASSISDGAAALLLMRLSEAQERGLKPLaRIVGHAGHAQAPNL-----FTT--APVAAIQRLLARIEWTLETVDLFEINEA 322
Cdd:PRK06064  208 CSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQASDTIALhdrkdFTTldAAVVAAEKAYKMAGIEPKDIDVAEVHDC 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 323 FAVVPMVAMRELGIAHD----KL--------------NVHGGACALGHPIGASGARILVTLLAALQQRGLK--------- 375
Cdd:PRK06064  287 FTIAEILAYEDLGFAKKgeggKLaregqtyiggdipvNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEKgrqqvigag 366
                         170
                  ....*....|....*.
gi 1222381029 376 RGMASvCIGGGEATAV 391
Cdd:PRK06064  367 YGLTH-NVGGTGHTAV 381
PRK06157 PRK06157
acetyl-CoA acetyltransferase; Validated
251-376 5.14e-06

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 180433 [Multi-domain]  Cd Length: 398  Bit Score: 48.10  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 251 SSISDGAAALLLMRLSEAQERG------LKPLARIVGHAGHAQAPNL-FTTAP--VAAIQRLL--ARIEWTLETVDLFEI 319
Cdd:PRK06157  214 CGVSDGAAAAIVTTPEIARALGkkdpvyVKALQLAVSNGWELQYNGWdGSYFPttRIAARKAYreAGITDPREELSMAEV 293
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 320 NEAFAVVPMVAMRELGIA------HDKL------------NVHGGACALGHPIGASGARILVTLLAALQQRGLKR 376
Cdd:PRK06157  294 HDCFSITELVTMEDLGLSergqawRDVLdgffdadgglpcQIDGGLKCFGHPIGASGLRMLYEMYLQLLGRAGER 368
PRK12578 PRK12578
thiolase domain-containing protein;
29-358 1.17e-05

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 47.15  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  29 SAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPARQAALGAGLSQAAQcTTLNKMCGSGMQALMLGHDQLLA 108
Cdd:PRK12578   20 SVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVAS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 109 GSADVLVAGGMESMSNAPYLLARARGGyRMGHGQVLDHMFLDGLEDAYE--RGRLMGTFAedcaqqyrfSREEQDAYALE 186
Cdd:PRK12578   99 GLVDMAIAVGVDKMTEVDTSTSLAIGG-RGGNYQWEYHFYGTTFPTYYAlyATRHMAVYG---------TTEEQMALVSV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 187 SLRRAQQAIEQGSFASEIvaveasqgrerrlvaTDEQPPKARPDKIPglkpafreggtVTAANASSISDGAAALLLMRLS 266
Cdd:PRK12578  169 KAHKYGAMNPKAHFQKPV---------------TVEEVLKSRAISWP-----------IKLLDSCPISDGSATAIFASEE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 267 EAQERGLKPLARIVGhAGHAQapnlfTTAPVAaiqrllARIEW-------------------TLETVDLFEINEAFAVVP 327
Cdd:PRK12578  223 KVKELKIDSPVWITG-IGYAN-----DYAYVA------RRGEWvgfkatqlaarqaynmakvTPNDIEVATVHDAFTIAE 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1222381029 328 MVAMRELGIAH-------------DK-----LNVHGGACALGHPIGASG 358
Cdd:PRK12578  291 IMGYEDLGFTEkgkggkfieegqsEKggkvgVNLFGGLKAKGHPLGATG 339
PRK08257 PRK08257
acetyl-CoA acetyltransferase; Validated
249-346 1.46e-05

acetyl-CoA acetyltransferase; Validated


Pssm-ID: 236204 [Multi-domain]  Cd Length: 498  Bit Score: 46.83  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 249 NASSISDGAAALLLMRLSEAQERGLkPLARIVGHAGHAQA---------PNLFTTAP-VAAIQRLLARIEWTLETVDLFE 318
Cdd:PRK08257  238 NANDMVDQGAAVLLTSVAKARRLGV-PEDRWVYLHGGADAhdpydilerPDLHRSPAiRAAGRRALALAGLGIDDIDAFD 316
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1222381029 319 INEAFAVVPMVAMRELGIAHDK---LNVHGG 346
Cdd:PRK08257  317 LYSCFPSAVQVAARELGLDLDDprpLTVTGG 347
PRK07516 PRK07516
thiolase domain-containing protein;
251-378 2.44e-05

thiolase domain-containing protein;


Pssm-ID: 181013 [Multi-domain]  Cd Length: 389  Bit Score: 46.09  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 251 SSISDGAAALLLmrlseAQERGLKPLARIVGHAGHAQAPNLFT---------TAPVAAIQRLLARIEWTLETVDLFEINE 321
Cdd:PRK07516  213 SLVSDGAAALVL-----ADAETARALQRAVRFRARAHVNDFLPlsrrdplafEGPRRAWQRALAQAGVTLDDLSFVETHD 287
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 322 AFAVVPMVAMRELGIAHD----------------KL--NVHGGACALGHPIGASGARILVtlLAALQQRGLKRGM 378
Cdd:PRK07516  288 CFTIAELIEYEAMGLAPPgqgarairegwtakdgKLpvNPSGGLKAKGHPIGATGVSMHV--LAAMQLTGEAGGM 360
PRK06059 PRK06059
lipid-transfer protein; Provisional
6-122 3.13e-05

lipid-transfer protein; Provisional


Pssm-ID: 180373 [Multi-domain]  Cd Length: 399  Bit Score: 45.91  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029   6 DPVVIVSAVRTPMGGFlgdlaGFSAAELGAAAIRSSLERAGLAAEAVDTVLMGCVLQAGQGQAPArqaalGAGLSQA--- 82
Cdd:PRK06059    4 EPVYILGAGMHPWGKW-----GRDFVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGYPGFVA-----GATFAQAlgw 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222381029  83 --AQCTTLNKMCGSGMQALMLGHDQLLAGSADVLVAGGMESM 122
Cdd:PRK06059   74 ngAPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTT 115
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
253-359 1.28e-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: 40.46  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 253 ISDGAAALLLMRLSEAQERGLKPLARIVGH-----AGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLfeIN------- 320
Cdd:COG0304   229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYgassdAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDY--INahgtstp 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1222381029 321 -----EAfavvpmVAMRE-LGIAHDKLNVHGGACALGHPIGASGA 359
Cdd:COG0304   307 lgdaaET------KAIKRvFGDHAYKVPVSSTKSMTGHLLGAAGA 345
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
247-372 1.48e-03

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


Pssm-ID: 238429 [Multi-domain]  Cd Length: 421  Bit Score: 40.62  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 247 AANASSISDGAAALLLMRLSEAQERGLKPLARI----VGHAGHAQ---APNlfTTAPVAAIQRLLARIEWTLETVDLFE- 318
Cdd:cd00833   227 DADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIrgsaVNQDGRTKgitAPS--GEAQAALIRRAYARAGVDPSDIDYVEa 304
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222381029 319 ---------------INEAFAvvpmvamrelgiahdKLNVHGGACAL-------GHPIGASGARILVTLLAALQQR 372
Cdd:cd00833   305 hgtgtplgdpieveaLAKVFG---------------GSRSADQPLLIgsvksniGHLEAAAGLAGLIKVVLALEHG 365
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
29-118 2.51e-03

"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: 39.72  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  29 SAAELGAAAIRSSLERAGLAAEAVDTVLMGC--VLQAGQGQAPARQAALGAglsQAAQCTTLNKMCGSGMQALMLGHDQL 106
Cdd:cd00827    47 DVPTMAVEAARRALERAGIDPDDIGLLIVATesPIDKGKSAATYLAELLGL---TNAEAFDLKQACYGGTAALQLAANLV 123
                          90
                  ....*....|...
gi 1222381029 107 LAGS-ADVLVAGG 118
Cdd:cd00827   124 ESGPwRYALVVAS 136
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
252-315 2.71e-03

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


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 39.44  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222381029 252 SISDGAAALLLMRLSEAQERGLKPLARIVGH-----AGHAQAPNLFTTAPVAAIQRLLARIEWTLETVD 315
Cdd:cd00834   228 VLGEGAGVLVLESLEHAKARGAKIYAEILGYgassdAYHITAPDPDGEGAARAMRAALADAGLSPEDID 296
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
255-372 3.50e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 39.26  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 255 DGAAALLLMRLSEAQERGLKPLARIVG-----HAGHAQAPNLFTTAPVAAIQRLLARIEWTLETVDLF-------EINEA 322
Cdd:PRK05952  210 EGGAILVLESAELAQKRGAKIYGQILGfgltcDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 323 F-AVVpmvamrelgIAH---DKLNVHGGACALGHPIGASGA-RILVTLLAALQQR 372
Cdd:PRK05952  290 ReANL---------IQAlfpHRVAVSSTKGATGHTLGASGAlGVAFSLLALRHQQ 335
PRK06816 PRK06816
StlD/DarB family beta-ketosynthase;
28-123 4.31e-03

StlD/DarB family beta-ketosynthase;


Pssm-ID: 235866  Cd Length: 378  Bit Score: 39.12  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  28 FSAAELGAAAIRSSLERAGLAAEAVDtvlmgcVLQAGQ--------GQAPARQAALGAGlsqAAQCTTLNKMCGSGMQAL 99
Cdd:PRK06816   61 HSNAQMAAEAIRDLLDDAGFSLGDIE------LLACGTsqpdqlmpGHASMVHGELGAP---PIEVVSSAGVCAAGMMAL 131
                          90       100
                  ....*....|....*....|....
gi 1222381029 100 MLGHDQLLAGSADVLVAGGMESMS 123
Cdd:PRK06816  132 KYAYLSVKAGESRNAVATASELAS 155
PRK08256 PRK08256
lipid-transfer protein; Provisional
33-122 8.54e-03

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 37.96  E-value: 8.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029  33 LGAAAIRSSLERAGLAAEAVDTVLMGCVLqagqGQAPARQAAL-GAGLSqAAQCTTLNKMCGSGMQALMLGHDQLLAGSA 111
Cdd:PRK08256   25 MAAEAGRAALADAGIDYDAVQQAYVGYVY----GDSTSGQRALyEVGMT-GIPIVNVNNNCSTGSTALFLARQAVRSGAA 99
                          90
                  ....*....|.
gi 1222381029 112 DVLVAGGMESM 122
Cdd:PRK08256  100 DCALALGFEQM 110
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
246-371 8.71e-03

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 37.79  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222381029 246 TAANASSISDGAAALLLMRLSEAQERGLKPLARIVGHAGHAQAPNLFTTA-----PVAAIQRLLARIEWTLETV------ 314
Cdd:PRK14691  153 TARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAedgdgAYRAMKIALRQAGITPEQVqhlnah 232
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222381029 315 -------DLFEINeafavvpmvAMRELGIAHDKLNVHGGACALGHPIGASGA-RILVTLLAALQQ 371
Cdd:PRK14691  233 atstpvgDLGEIN---------AIKHLFGESNALAITSTKSATGHLLGAAGGlETIFTVLALRDQ 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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