|
Name |
Accession |
Description |
Interval |
E-value |
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-390 |
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: 537.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVG 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 81 AVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMgHGEIKDHMFLDGLEDAETGRLMGSF 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 161 AQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQPLK-ANLEKIPTLRPAFSKDGT 239
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPdTTLEKLAKLKPAFKKDGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 240 ITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFA 319
Cdd:COG0183 240 VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042405 320 MVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:COG0183 320 AQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-390 |
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: 525.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 5 VIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVTI 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 85 NKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIkDHMFLDGLEDAETGRLMGSFAQDM 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 165 ANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQPLK-ANLEKIPTLRPAFSKDGTITAA 243
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPdTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 244 NSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAM 323
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042405 324 APIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:cd00751 320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-390 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 521.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMFLDGLEDA-ETGRLMGSFAQ 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAyDKGRLMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 163 DMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQPLKANLEKIPTLRPAFSKDGTITA 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKTGTVTA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 243 ANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVA 322
Cdd:PRK06954 249 ANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVT 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042405 323 MAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK06954 329 MAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIEL 396
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-390 |
2.34e-179 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 503.92 E-value: 2.34e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVG 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 81 AVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMFLDGLEDAETGRLMGSF 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 161 AQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKG-VEVIDQDEQP-LKANLEKIPTLRPAFSKDG 238
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDTDEHPrPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 239 TITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAF 318
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042405 319 AMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
4-389 |
3.76e-159 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 453.01 E-value: 3.76e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMFLDGLEDAETGRLMGSFAQD 163
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 164 MANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVE--VIDQDEQPLKANLEKIPTLRPAFSKD-GTI 240
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPsvIVDKDEGLGKFDPAKLRKLRPSFKEDgGSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 241 TAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAM 320
Cdd:PLN02644 243 TAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 321 VAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PLN02644 323 VALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVE 391
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.82e-153 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 438.38 E-value: 1.82e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVG 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 81 AVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMFLDGLEDAETGRLMGSF 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 161 AQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVE-VIDQDEQPLK-ANLEKIPTLRPAFSKDG 238
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPiVVAKDEAPRKdTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 239 TITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAF 318
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042405 319 AMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIEV 392
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-389 |
5.12e-152 |
|
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: 434.35 E-value: 5.12e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 6 IVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVTIN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 86 KLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKA-RGGYRMGHGEIKDHMFLDgLEDAETGRLMGSFAQDM 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 165 ANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQPLKA-NLEKIPTLRPAFSKDGTITAA 243
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNtTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 244 NSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAM 323
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042405 324 APIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-389 |
1.06e-130 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 380.39 E-value: 1.06e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVG 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 81 AVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMFLDGLEDAETGRLMGSF 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 161 AQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVI-DQDEQP-LKANLEKIPTLRPAFSKDG 238
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAfATDEQPrAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 239 TITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAF 318
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042405 319 AMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-389 |
3.53e-122 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 358.89 E-value: 3.53e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVlsagIGQGP-----ARQAMRKASV 75
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHV----IPTEPrdmylSRVAAINAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 76 PDHVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHMfLDGLEDAETGR 155
Cdd:PRK09051 78 PQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMM-VGALHDPFGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 156 LMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQP-LKANLEKIPTLRPAF 234
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVrADTTLEDLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 235 SKD-GTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWE 313
Cdd:PRK09051 237 KKEnGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042405 314 INEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK09051 317 ANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-389 |
1.39e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 326.60 E-value: 1.39e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMT---NAPYIlpkaRGGYRMGHGEIKDHMFLDGLEDAETGRLMGSF 160
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI----RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 161 AQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDE--QPlKANLEKIPTLRPAFSKDG 238
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDEtvRP-DTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 239 TITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAF 318
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042405 319 AMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-389 |
6.85e-105 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 314.97 E-value: 6.85e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQR-AGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDH 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 79 VGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMgHGEIKDHM----FLDGLEDAETG 154
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSR-QAEIFDTTigwrFVNPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 155 -RLMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKG-VEVIDQDEQPLKA-NLEKIPTLR 231
Cdd:PRK09050 160 vDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRDEHPRPEtTLEALAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 232 PAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDA 311
Cdd:PRK09050 240 PVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 312 WEINEAFAMVAMAPIHELGI--DEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK09050 320 IELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
3.06e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 305.40 E-value: 3.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVG 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 81 AVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPkarGGYRMG-------HGEIKDHMFLDGLEDAET 153
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLP---SDLRWGpkhllhkNYKIDDAMLVDGLIDAFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 154 GRLMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVktrkgvevIDQDEQPLKANLEKIPTLRPA 233
Cdd:PRK06366 158 FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIRKTTMEDLAKLPPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 234 FSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWE 313
Cdd:PRK06366 230 FDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488042405 314 INEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK06366 310 HNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEM 386
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-389 |
3.58e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 295.09 E-value: 3.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGF------QGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAG----IGqgpARQAM 70
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGenwlYG---GRHPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 71 RKASVPDHVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPyilpkarggyrMGHG-EIKDHM-FLDGL 148
Cdd:PRK06445 78 FLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP-----------MGDNpHIEPNPkLLTDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 149 E----DAETGRLMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDeQPLKAN- 223
Cdd:PRK06445 147 KyieyDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVD-QSVRPDt 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 224 -LEKIPTLRPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHA 302
Cdd:PRK06445 226 sLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 303 GWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGE 382
Cdd:PRK06445 306 GLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQ 385
|
....*..
gi 488042405 383 ATAVAIE 389
Cdd:PRK06445 386 GGAVVLE 392
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
6-389 |
8.42e-97 |
|
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: 294.38 E-value: 8.42e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 6 IVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQR-AGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDHVGAVT 83
Cdd:TIGR02430 5 ICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSVPGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHgEIKDHM----FLDGLEDAETG-RLMG 158
Cdd:TIGR02430 85 VNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSA-KIEDTTigwrFINPLMKALYGvDSMP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 159 SFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVE-VIDQDEQP-LKANLEKIPTLRPAFSK 236
Cdd:TIGR02430 164 ETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPtVVDQDEHPrPETTLEGLAKLKPVVRP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 237 DGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINE 316
Cdd:TIGR02430 244 DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNE 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488042405 317 AFAMVAMAPIHELGI--DEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:TIGR02430 324 AFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-261 |
2.18e-96 |
|
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: 288.05 E-value: 2.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILP-KARGGYRMGHGEIKDHMFLDGLEDAETGRLMGSFAQ 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPtDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 163 DMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQP-LKANLEKIPTLRPAFSKDGTIT 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIrPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 488042405 242 AANSSSISDGAAALVLTTEE 261
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-389 |
7.12e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 286.22 E-value: 7.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGP-ARQAMRKASVPDHV 79
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNiARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 80 GAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPY---ILPKARGGYRMGHGEIKdhMFLDGLEDAETGRL 156
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIssaMTAGEQLGFTSPFAESK--GWLHRYGDQEVSQF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 157 MGsfAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEvktrkGVEVidqDEQPLKANLEKIPTLRPaFSK 236
Cdd:PRK07801 159 RG--AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG-----GVTV---DEGPRETSLEKMAGLKP-LVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 237 DGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINE 316
Cdd:PRK07801 228 GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488042405 317 AFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK07801 308 AFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-390 |
3.03e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 279.71 E-value: 3.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMG-GFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVL-SAGIGQGPARQAMRKASVPDH 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 79 VGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYilpkarggyrMGHgEIKDHMFLdgLEDA-ETGRLM 157
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGH-VVRPNPRL--VEAApEYYMGM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 158 GSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVE---------VIDQDEQ-PLKANLEKI 227
Cdd:PRK07661 148 GHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetiTFSQDEGvRADTTLEIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 228 PTLRPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVD 307
Cdd:PRK07661 228 GKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 308 EVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVA 387
Cdd:PRK07661 308 DIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGV 387
|
...
gi 488042405 388 IEV 390
Cdd:PRK07661 388 FEL 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-389 |
4.60e-91 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 279.57 E-value: 4.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGcvLSAGIGQGPA--RQAMRKASVPDH 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFG--QGYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 79 VGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGYRMGHGEIKDHmfLD-GLEDAETGRL- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDR--LArGRETAGGRRFp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 157 ----MGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKG-VEVIDQDEQP-LKANLEKIPTL 230
Cdd:PRK06205 157 vpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHPrADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 231 RPAFSK---DGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVD 307
Cdd:PRK06205 237 RPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 308 EVDAWEINEAFAMVAMAPIHELGI---DEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEAT 384
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGL 396
|
....*
gi 488042405 385 AVAIE 389
Cdd:PRK06205 397 AAVFE 401
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-389 |
6.35e-85 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 263.36 E-value: 6.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQ-GSLSALTAPELGAAVIRESIQR-AGVAPDQVDEVIFGCVLSAgIGQG--PARQAMRKASVP 76
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKgGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQT-LEQGfnIARNAALLAGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 77 DHVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPyilpkarggyrMGHGeIKDHMFLdGLEDAETGRL 156
Cdd:PRK08947 80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG-VDFHPGL-SKNVAKAAGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 157 MGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGV-EVIDQDE--QPlKANLEKIPTLRPA 233
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVlKLFDYDEviRP-ETTVEALAALRPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 234 FS-KDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAW 312
Cdd:PRK08947 226 FDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 313 EINEAFAMVAMAPIHELG----IDEaKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAI 388
Cdd:PRK08947 306 ELNEAFAAQSLPCLKDLGlldkMDE-KVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVF 384
|
.
gi 488042405 389 E 389
Cdd:PRK08947 385 E 385
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-389 |
2.03e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 262.36 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDHV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 80 GAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPkARGGYRMGHGEIKDHMFLDGLEDAETGRLMGs 159
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-STLPAKNGLGHYKSPGMEERYPGIQFSQFTG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 160 fAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDEQPLK--ANLEKIPTLRPaFSKD 237
Cdd:PRK06504 159 -AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRfdATLEGIAGVKL-IAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 238 GTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEA 317
Cdd:PRK06504 237 GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488042405 318 FAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK06504 317 FASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-389 |
3.44e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 256.85 E-value: 3.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMG-GFQGSLSALTAPELGAAVIRESIQRA-GVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVpD 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGY-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 78 HVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMT--------------NAPYILPKARGGYRMGHGEIKDHm 143
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtkNPLFAEAQARTAARAEGGAEAWH- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 144 flDGLEDaetGRL------MGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVevkTRKGVEVIDQDE 217
Cdd:PRK07851 159 --DPRED---GLLpdvyiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV---TLPDGTVVSTDD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 218 QPLKA-NLEKIPTLRPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQ 296
Cdd:PRK07851 231 GPRAGtTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 297 KVLEHAGWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAAL 376
Cdd:PRK07851 311 QALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETM 390
|
410
....*....|...
gi 488042405 377 CIGGGEATAVAIE 389
Cdd:PRK07851 391 CVGGGQGMAMVLE 403
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
6-389 |
2.32e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 251.85 E-value: 2.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 6 IVSGSRTAMGGFQGSLSALTAP-ELGAAVIRESIQRA-GVAPDQVDEVIFGCVL-SAGIGQGPARQAMRKASVPDHVGAV 82
Cdd:PRK09052 10 IVAATRTPVGKAPRGMFKNTRPdDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 83 TINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYilpkarggyrMGHG-EIKDHMFlDGLEDAETGRLMGSFA 161
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKpSMSPAIF-ARDENVGIAYGMGLTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 162 QDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTR----KGVEV------IDQDEQPLK-ANLEKIPTL 230
Cdd:PRK09052 159 EKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERfpdlATGEVdvktrtVDLDEGPRAdTSLEGLAKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 231 RPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVD 310
Cdd:PRK09052 239 KPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 311 AWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK09052 319 WIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFE 397
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
4-389 |
4.64e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 252.25 E-value: 4.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:PRK08170 5 VYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPK-----------ARG-GYRMGH-GEIKDHMF------ 144
Cdd:PRK08170 85 VQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmvrwlagwyaAKSiGQKLAAlGKLRPSYLapvigl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 145 LDGLEDAETGRLMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEeIVPVevKTRKGvEVIDQDE--QPlKA 222
Cdd:PRK08170 165 LRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPL--FDRDG-KFYDHDDgvRP-DS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 223 NLEKIPTLRPAFSKD-GTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEH 301
Cdd:PRK08170 240 SMEKLAKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 302 AGWSVDEVDAWEINEAFAMVAMAPI----------HELG-------IDEAKVNIHGGACALGHPIGATGSRIILSLIYAL 364
Cdd:PRK08170 320 HGLTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHLLHAL 399
|
410 420
....*....|....*....|....*
gi 488042405 365 KRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK08170 400 KRRGTKRGIAAICIGGGQGGAMLLE 424
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-389 |
3.10e-79 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 249.31 E-value: 3.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDHV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 80 GAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGGY----RMGHGEIKDHMFLDGLEDAETGR 155
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFsrdaKVFDTTIGARFPNPKIVAQYGND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 156 LMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKT--RKGVEVIDQDEQPL-KANLEKIPTLRP 232
Cdd:PRK08131 161 SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEHPRpSSTVEALTKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 233 AFSkDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAW 312
Cdd:PRK08131 241 LFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDII 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 313 EINEAFAMVAMAPIHELGI--DEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK08131 320 EINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
19-389 |
2.10e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 247.10 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 19 GSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGiGQGP--ARQAMRKASVPDHVGAVTINKLCGSAMKAVL 96
Cdd:PRK08242 21 GSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVG-DQGAdiARTAVLAAGLPETVPGVQINRFCASGLEAVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 97 MASDTLKAGSANIIVAGGMESMTnapyilpkarggyRMGHGEIKDHMFLDGLEDAETGRLMGSFAQDMANTK-GFTREQM 175
Cdd:PRK08242 100 LAAAKVRSGWDDLVIAGGVESMS-------------RVPMGSDGGAWAMDPSTNFPTYFVPQGISADLIATKyGFSREDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 176 DNFAISSLKKAQTAITEGYFKEEIVPVevKTRKGVEVIDQDEQP-LKANLEKIPTLRPAFSKDGTI-------------- 240
Cdd:PRK08242 167 DAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMrPGTTMESLAKLKPSFAMMGEMggfdavalqkypev 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 241 -------TAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWE 313
Cdd:PRK08242 245 erinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488042405 314 INEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK08242 325 LNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-389 |
3.54e-78 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 246.17 E-value: 3.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDHV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 80 GAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAP--YILPKARGGYRMGHGEIKDHmflDGLEDAETgrlm 157
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPlgANAGPGRGLPRPDSWDIDMP---NQFEAAER---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 158 gsfaqdMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRK-------GVEVIDQDEQPLKANLEKIPTL 230
Cdd:PRK07850 154 ------IAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRDTTMEGLAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 231 RPAFsKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVD 310
Cdd:PRK07850 228 KPVL-EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDID 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 311 AWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK07850 307 LVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
4-389 |
2.95e-76 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 243.13 E-value: 2.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAM-----GGFQGSLsaltAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQG-PARQAMRKASVPD 77
Cdd:PLN02287 48 VVIVAAYRTPIckakrGGFKDTY----PDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAGFPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 78 HVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPyilpkarggyrmGHGEIKDHMFLDGLEDAETGRL- 156
Cdd:PLN02287 124 TVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP------------MAWEGGVNPRVESFSQAQDCLLp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 157 MGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKT---RKGVE---VIDQDE--QPlKANLEKIP 228
Cdd:PLN02287 192 MGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIvdpKTGEEkpiVISVDDgiRP-NTTLADLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 229 TLRPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDE 308
Cdd:PLN02287 271 KLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 309 VDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGK--KKGVAALCIGGGEATAV 386
Cdd:PLN02287 351 IDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKdcRFGVVSMCIGTGMGAAA 430
|
...
gi 488042405 387 AIE 389
Cdd:PLN02287 431 VFE 433
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
4-389 |
2.67e-71 |
|
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: 228.29 E-value: 2.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALT-APELGAAVIRESIQR-AGVAPDQVDEVIFGCVlSAGIGQG--PARQAMRKASVPDHV 79
Cdd:TIGR02445 2 VVIVDFGRTPMGRSKGGAFRNTrAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCV-QQTLEQGfnIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 80 GAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPyilpkarggyrMGHG-EIKDHMfldGLEDAETGRLMG 158
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-----------MMHGvDFHPGM---SLHVAKAAGMMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 159 SFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGV-EVIDQDE--QPlKANLEKIPTLRPAFS 235
Cdd:TIGR02445 147 LTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFlKQFDYDEviRP-ETTVESLAALRPAFD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 236 -KDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEI 314
Cdd:TIGR02445 226 pKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 315 NEAFAMVAMAPIHELG----IDEaKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:TIGR02445 306 NEAFAAQALPCLKDLGlldkMDE-KVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-389 |
4.99e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 228.51 E-value: 4.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMG---GFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGP-ARQAMRKASVP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDlGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 77 DHVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMT-NAPYILPKARGG---YRMGHGeikdHMFLDGLEDAE 152
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGkppLGMGSG----NLRLRALHPQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 153 TgrlMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVevKTRKGVEVIDQDEQPL-KANLEKIPTLR 231
Cdd:PRK06025 157 H---QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVALDHEEFPRpQTTAEGLAALK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 232 PAFSK-------DGTIT-------------------AANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPS 285
Cdd:PRK06025 232 PAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 286 EFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALK 365
Cdd:PRK06025 312 LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
|
410 420
....*....|....*....|....
gi 488042405 366 RLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK06025 392 RRGLKRGLVTMCAAGGMAPAIIIE 415
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-390 |
6.49e-68 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 219.64 E-value: 6.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMG-GFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAG-IGQGPARQAMRKASVPDH 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 79 VGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPK--ARGGYRMGHgeiKDHMFLDGLEDAETgrl 156
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRhmLREGWLVEH---KPEIYWSMLQTAEN--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 157 mgsfaqdMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVktRKGV-----------EV-IDQDE--QPlKA 222
Cdd:PRK07108 155 -------VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITV--TAGVadkatgrlftkEVtVSADEgiRP-DT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 223 NLEKIPTLRPAFsKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHA 302
Cdd:PRK07108 225 TLEGVSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 303 GWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGE 382
Cdd:PRK07108 304 GLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQ 383
|
....*...
gi 488042405 383 ATAVAIEV 390
Cdd:PRK07108 384 GAAGLFEV 391
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-389 |
8.90e-68 |
|
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: 219.29 E-value: 8.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 7 VSGSRTAMGGFQGSLSALT---APELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 84 INKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARggyrmghgeikdHMfldgledaetgrlmgsfaqD 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEK------------HI-------------------D 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 164 MANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKGVEVIDQDE---QPLKANLEKIPTLRPAFSKDGTI 240
Cdd:cd00826 130 VLINKYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiqFGDEASLDEIAKLRPAFDKEDFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 241 TAANSSSISDGAAALVLTTEEYAQSHGLNT-------LAKIVATSTHSQHPSEFTIA----PIGAIQKVLEHAGWSVDEV 309
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 310 DAWEINEAFAMVAMAPIHELGIDEAK------------------VNIHGGACALGHPIGATGSRIILSLIYALK-----R 366
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKgeagkR 369
|
410 420
....*....|....*....|...
gi 488042405 367 LGKKKGVAALCIGGGEATAVAIE 389
Cdd:cd00826 370 QGAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-390 |
9.49e-67 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 215.79 E-value: 9.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 5 VIVSGSRTAMGGFQGSLSALTAPELGAAVIResiQRAGVAPDQVDEVIFGCVLsaGIGQGPARQAMRKASVPDHVGAVTI 84
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT---FLSKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 85 NKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYilpKARGgyRMGHGEIKDHMfldgledaetgrlMGSFAQDM 164
Cdd:PRK06690 79 DRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRA--RFSPETIGDPD-------------MGVAAEYV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 165 ANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEvktrkGVEvidqDEQPLKA-NLEK-IPTLRPAFSKDGTITA 242
Cdd:PRK06690 141 AERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFN-----GLL----DESIKKEmNYERiIKRTKPAFLHNGTVTA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 243 ANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVA 322
Cdd:PRK06690 212 GNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKV 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488042405 323 MAPIHELGIDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK06690 292 VACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEK 359
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-390 |
3.78e-51 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 176.71 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 4 IVIVSGSRTAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSagIGQGP--ARQAMRKASVPDHVGA 81
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQ--MPEAPniAREIVLGTGMNVHTDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 82 VTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPYILPKARGgyrmghgeikdHMFLD--------------- 146
Cdd:PRK08963 85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLA-----------RALVDlnkartlgqrlklfs 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 147 --GLED--------AE--TGRLMGSFAQDMANTKGFTREQMDNFAISSLKKAQTAITEGYFKEEIVPVEVKTRKgvEVID 214
Cdd:PRK08963 154 rlRLRDllpvppavAEysTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYK--QPLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 215 QDEQPLK-ANLEKIPTLRPAFS-KDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSE-FTIAP 291
Cdd:PRK08963 232 EDNNIRGdSTLEDYAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 292 IGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIH----------ELG-------IDEAKVNIHGGACALGHPIGATGS 354
Cdd:PRK08963 312 AYATPLALERAGLTLADLTLIDMHEAFAAQTLANLQmfaserfareKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGA 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 488042405 355 RIILSLIYALKRLGKKKGVAALCIGGGEATAVAIEV 390
Cdd:PRK08963 392 RMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
271-389 |
1.99e-48 |
|
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: 160.12 E-value: 1.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 271 LAKIVATSTHSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKVNIHGGACALGHPIG 350
Cdd:pfam02803 4 LARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHPLG 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 488042405 351 ATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:pfam02803 84 ASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
38-389 |
4.76e-42 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 152.36 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 38 IQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMES 117
Cdd:PRK09268 43 VDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 118 MTNAP--------YILPKARGGYRMGH-----GEIKDHMF---LDGLEDAETGRLMGSFAQDMANTKGFTREQMDNFAIS 181
Cdd:PRK09268 123 TSDAPiavneglrKILLELNRAKTTGDrlkalGKLRPKHLapeIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 182 SLKKAQTAITEGYFKEEIVPVEVKTRkgveviDQDEQPlKANLEKIPTLRPAFSK--DGTITAANSSSISDGAAALVLTT 259
Cdd:PRK09268 203 SHQNLAAAYDRGFFDDLITPFLGLTR------DNNLRP-DSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLAS 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 260 EEYAQSHGLNTLAKIVATST----HSQHPSEFTIAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPI--------- 326
Cdd:PRK09268 276 EEWAAEHGLPVLAYLVDAETaavdFVHGKEGLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLkawedeeyc 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042405 327 -HELG-------IDEAKVNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVAALCIGGGEATAVAIE 389
Cdd:PRK09268 356 rERLGldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
19-388 |
1.25e-20 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 92.33 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 19 GSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASvPDHVGAVTINKLCGSAMKAVLMA 98
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLG-LLGKPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 99 SDTLKAGSANIIVAGGMESMTNAPY-ILPKARGGYRMGHGEIKDHMFLdgledaeTGRLMGSFAQDMANTKGFTREQMDN 177
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTgDEAGGRASDLEWEGPEPPGGLT-------PPALYALAARRYMHRYGTTREDLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 178 FAISSLKKAQ---TAitegYFKEEIVPVEV-KTRKGVEvidqdeqPLkanlekiptlrpafskdgtiTAANSSSISDGAA 253
Cdd:cd00829 161 VAVKNHRNAArnpYA----QFRKPITVEDVlNSRMIAD-------PL--------------------RLLDCCPVSDGAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 254 ALVLTTEEYAQSHGlNTLAKIVA------TSTHSQHPSEFTIAPIG-AIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPI 326
Cdd:cd00829 210 AVVLASEERARELT-DRPVWILGvgaasdTPSLSERDDFLSLDAARlAARRAYKMAGITPDDIDVAELYDCFTIAELLAL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 327 HELGI---DEAK---------------VNIHGGACALGHPIGATGSRIILSLIYALKRLGKKKGVA----ALC--IGGGE 382
Cdd:cd00829 289 EDLGFcekGEGGklvregdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPgarvGLAhnIGGTG 368
|
....*.
gi 488042405 383 ATAVAI 388
Cdd:cd00829 369 SAAVVT 374
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
22-388 |
5.04e-17 |
|
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: 79.80 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 22 SALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPdHVGAVTINKLCGSAMKAVLMASDT 101
Cdd:cd00327 3 LGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 102 LKAGSANIIVAGGMESmtnapyilpkarggyrmghgeikdhmfldgledaetgrlmgsfaqdmantkgftreqmdnfais 181
Cdd:cd00327 82 VQNGKADIVLAGGSEE---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 182 slkkaqtaitegyfkeeivpvevktrkgvevidqdeqplkanlekiptlrpafskdgtitaansSSISDGAAALVLTTEE 261
Cdd:cd00327 98 ----------------------------------------------------------------FVFGDGAAAAVVESEE 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 262 YAQSHGLNTLAKIVATSTHSQHPSEFTI----APIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIHELGIDEAKV- 336
Cdd:cd00327 114 HALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVr 193
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488042405 337 --NIHGGACALGHPIGATGSRIILSLIYALKRLGKK-------KGVAALCIGGGEATAVAI 388
Cdd:cd00327 194 spAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptpreprTVLLLGFGLGGTNAAVVL 254
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-353 |
1.52e-13 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 71.52 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 1 MSSIVIVSGSRTAMGgfqgSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGcVLSAG-IGQG-PARQAMrkASVPD- 77
Cdd:PRK07516 1 MMTASIVGWAHTPFG----KLDAETLESLIVRVAREALAHAGIAAGDVDGIFLG-HFNAGfSPQDfPASLVL--QADPAl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 78 -HVGAVTINKLCGSAMKAVLMASDTLKAGSANIIVAGGMESMTNAPY-----ILPKArgGYRMghgeikdhmfldglEDA 151
Cdd:PRK07516 74 rFKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTaevgdILLGA--SYLK--------------EEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 152 ETGrlmGSFAQDMANTKG--FTR--EQMDNFAISSLKKAQTAITEGYfkeeivpveVKTRK--GVEVIDQ--DEQPLKAn 223
Cdd:PRK07516 138 DTP---GGFAGVFGRIAQayFQRygDQSDALAMIAAKNHANGVANPY---------AQMRKdlGFEFCRTvsEKNPLVA- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 224 lekiPTLRpafskdgtitAANSSSISDGAAALVLTTEEYAQshglnTLAKIVATSTHSQ----------HPSEFTiAPIG 293
Cdd:PRK07516 205 ----GPLR----------RTDCSLVSDGAAALVLADAETAR-----ALQRAVRFRARAHvndflplsrrDPLAFE-GPRR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 294 AIQKVLEHAGWSVDEVDAWEINEAFAmvamapIHELGIDEA------------------------KVNIHGGACALGHPI 349
Cdd:PRK07516 265 AWQRALAQAGVTLDDLSFVETHDCFT------IAELIEYEAmglappgqgarairegwtakdgklPVNPSGGLKAKGHPI 338
|
....
gi 488042405 350 GATG 353
Cdd:PRK07516 339 GATG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
28-372 |
2.12e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 67.95 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 28 ELGAAVIRESIQRAGVAPDQVDEVIFGCVLSAGIGQGPARQAMRKASVPDHvGAVTINKLCGSAMKAVLMASDTLKAGSA 107
Cdd:PRK12578 23 ELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGK-VPLRVEAMCATGLAASLTAYTAVASGLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 108 NIIVAGGMESMTNAPYILPKARGGyRMGHGEIKDHMF---LDGLEDAETGRLMGSFaqdmantkGFTREQMdnfAISSLK 184
Cdd:PRK12578 102 DMAIAVGVDKMTEVDTSTSLAIGG-RGGNYQWEYHFYgttFPTYYALYATRHMAVY--------GTTEEQM---ALVSVK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 185 KAQTAIT--EGYFKEEIVPVEVktrkgvevidqdeqpLKANLEKIPtlrpafskdgtITAANSSSISDGAAALVLTTEEY 262
Cdd:PRK12578 170 AHKYGAMnpKAHFQKPVTVEEV---------------LKSRAISWP-----------IKLLDSCPISDGSATAIFASEEK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 263 AQSHGLNTLAKIVATSTHSQHPS-----EFT--IAPIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIHELG----- 330
Cdd:PRK12578 224 VKELKIDSPVWITGIGYANDYAYvarrgEWVgfKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGftekg 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 488042405 331 -----IDEAK--------VNIHGGACALGHPIGATGsriiLSLIYAL-KRLGKKKG 372
Cdd:PRK12578 304 kggkfIEEGQsekggkvgVNLFGGLKAKGHPLGATG----LSMIYEItKQLRDEAG 355
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
34-386 |
4.09e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 60.68 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 34 IRESIQRAGVAPDQVDEVIFGCVLSAGIGQgparQAMRKASVPD-----HVGAVTINKLCGSAMKAVLMASDTLKAGSAN 108
Cdd:PRK06064 30 GLEALEDAGIDGKDIDAMYVGNMSAGLFVS----QEHIAALIADyaglaPIPATRVEAACASGGAALRQAYLAVASGEAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 109 IIVAGGMESMTNAPyilpkarggyrmgHGEIKDhmFLDGLEDAETGRLMG-SF-------AQDMANTKGFTREQMDNFAI 180
Cdd:PRK06064 106 VVLAAGVEKMTDVP-------------TPDATE--AIARAGDYEWEEFFGaTFpglyaliARRYMHKYGTTEEDLALVAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 181 ------SSLKKAQtaitegyFKEEIVPVEVktrkgvevidqdeqplkanLEKIPTLRPafskdgtITAANSSSISDGAAA 254
Cdd:PRK06064 171 knhyngSKNPYAQ-------FQKEITVEQV-------------------LNSPPVADP-------LKLLDCSPITDGAAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 255 LVLTTEEYAQSH---GLNTLAKIVATSTHSQH--PSEFTI-APIGAIQKVLEHAGWSVDEVDAWEINEAFAMVAMAPIHE 328
Cdd:PRK06064 218 VILASEEKAKEYtdtPVWIKASGQASDTIALHdrKDFTTLdAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYED 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 329 LG----------IDEAK--------VNIHGGACALGHPIGATGSRIILSLIYAL-------KRLGKKKGVA-ALCIGGGE 382
Cdd:PRK06064 298 LGfakkgeggklAREGQtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLrgeaekgRQQVIGAGYGlTHNVGGTG 377
|
....
gi 488042405 383 ATAV 386
Cdd:PRK06064 378 HTAV 381
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
25-387 |
1.41e-09 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 59.52 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 25 TAPELGAAVIRESIQRAGVA--PDQVDEVIFGCVLSAGIGQ----GPARQAMRKASVPD----HVGAVTINKLCGSAMKA 94
Cdd:PTZ00455 47 TLEELLATAIQGTLENTGLDgkAALVDKVVVGNFLGELFSSqghlGPAAVGSLGQSGASnallYKPAMRVEGACASGGLA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 95 VLMASDTLKAGSANIIVAGGMESMTNApyilpKARGGyrmghgeikdhmfldgledaetgrlmgsfAQDMANTKGFTRE- 173
Cdd:PTZ00455 127 VQSAWEALLAGTSDIALVVGVEVQTTV-----SARVG-----------------------------GDYLARAADYRRQr 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 174 QMDNFAISSL-KKAQTAITE-GYF-KEEIVPVEVK--------------TRKGVEVIDQDEQPLKANLEKIPTLRPafsk 236
Cdd:PTZ00455 173 KLDDFTFPCLfAKRMKYIQEhGHFtMEDTARVAAKayangnknplahmhTRKLSLEFCTGASDKNPKFLGNETYKP---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 237 dgTITAANSSSISDGAAALVLTTEEYAQSHGL----NTLAKI----VATSTHSQHPSEFT--IAPIGAIQKVLEHAGWSV 306
Cdd:PTZ00455 249 --FLRMTDCSQVSDGGAGLVLASEEGLQKMGLspndSRLVEIkslaCASGNLYEDPPDATrmFTSRAAAQKALSMAGVKP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 307 DEVDAWEINEAFAMVAMAPIHELGIDE---AK---------------VNIHGGACALGHPIGATGSRIILSLIYALK--- 365
Cdd:PTZ00455 327 SDLQVAEVHDCFTIAELLMYEALGIAEyghAKdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKgqc 406
|
410 420
....*....|....*....|....*.
gi 488042405 366 ---RLGKKKGVAA-LCIGGGEATAVA 387
Cdd:PTZ00455 407 geyQMKNIPALGAtLNMGGDDKTAVS 432
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
249-353 |
8.48e-09 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 56.83 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 249 SDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEF----TIAPIG------AIQKVLEHAGWSVDEVDAWEINEAF 318
Cdd:PRK08256 214 TCGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFdgrsMIDLVGydmtraAAQQVYEQAGIGPEDIDVVELHDCF 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488042405 319 AM--------VAMAPIHELG--IDEAK--------VNIHGGACALGHPIGATG 353
Cdd:PRK08256 294 SAnelltyeaLGLCPEGEAEkfIDDGDntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
26-357 |
1.32e-08 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 56.19 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 26 APELGAAVIRESIQRAGVAPDQVDEVIFG---CVLSAGIGQGPARQAMRKASVPdhvgaVT-INKLCGSAMKAVLMASDT 101
Cdd:PRK06157 27 AEDLMVEAFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRLPNIP-----VTrVENFCATGSEAFRGAVYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 102 LKAGSANIIVAGGMESMTNApyilpkargGYRmghgeikdhmfldGLEDAETGRLMGSFAQDMANTKGFTReqmdnfaIS 181
Cdd:PRK06157 102 VASGAYDIALALGVEKLKDT---------GYG-------------GLPVANPGTLADMTMPNVTAPGNFAQ-------LA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 182 SLKKAQTAITEGYFKEEIVPVEVKTRkgvevidqdeqplkANLEKIPT--LRPAFSKDgTITAA----------NSSSIS 249
Cdd:PRK06157 153 SAYAAKYGVSREDLKRAMAHVSVKSH--------------ANGARNPKahLRKAVTEE-QVLKApmiagplglfDCCGVS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 250 DGAAALVLTTEEYAQSHGLNTLAKI------VATSTHSQHPSE-FTIAP--IGAIQKVLEHAGWS--VDEVDAWEINEAF 318
Cdd:PRK06157 218 DGAAAAIVTTPEIARALGKKDPVYVkalqlaVSNGWELQYNGWdGSYFPttRIAARKAYREAGITdpREELSMAEVHDCF 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488042405 319 AMVAMAPIHELGIDEA------------------KVNIHGGACALGHPIGATGSRII 357
Cdd:PRK06157 298 SITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
246-390 |
9.30e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 53.54 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 246 SSISDGAAALVLTTEEYAQSH-GLNTLAKI------VATSTHSQHPSEFTIAPI------GAIQKVLEHAGWSVDEVDAW 312
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYaDARPIPRIkgwghrTAPLGLEQKLDRSAGDPYvlphvrQAVLDAYRRAGVGLDDLDGF 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 313 EINEAFAMVAMAPIHELGIDEA------------------KVNIHGGACALGHPIGATGSRIILSliyALKRLGKKKG-- 372
Cdd:PRK06289 300 EVHDCFTPSEYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRMLLD---AAKQVTGTAGdy 376
|
170 180
....*....|....*....|....*
gi 488042405 373 -------VAALCIGGGEATAVAIEV 390
Cdd:PRK06289 377 qvegaktFGTLNIGGSTTTTVSFVV 401
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
247-310 |
1.58e-03 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 40.21 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 247 SISDGAAALVLTTEEYAQSHGLNTLAKIV--ATSTHSQH---PSEFTIAPIGAIQKVLEHAGWSVDEVD 310
Cdd:cd00834 228 VLGEGAGVLVLESLEHAKARGAKIYAEILgyGASSDAYHitaPDPDGEGAARAMRAALADAGLSPEDID 296
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
231-310 |
1.92e-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: 40.08 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 231 RPaFSK--DGTItaansssISDGAAALVLTTEEYAQSHGLNTLAKIV--ATSTHSQH---PSEFTIAPIGAIQKVLEHAG 303
Cdd:COG0304 218 RP-FDKdrDGFV-------LGEGAGVLVLEELEHAKARGAKIYAEVVgyGASSDAYHitaPAPDGEGAARAMRAALKDAG 289
|
....*..
gi 488042405 304 WSVDEVD 310
Cdd:COG0304 290 LSPEDID 296
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
12-114 |
2.83e-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: 39.34 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 12 TAMGGFQGSLSALTAPELGAAVIRESIQRAGVAPDQVDEVIFGCvlSAGIGQGPARQAM-RKASVPDHVGAVTINKLCGS 90
Cdd:cd00827 34 TGIGQRHMAGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVAT--ESPIDKGKSAATYlAELLGLTNAEAFDLKQACYG 111
|
90 100
....*....|....*....|....*
gi 488042405 91 AMKAVLMASDTLKAGS-ANIIVAGG 114
Cdd:cd00827 112 GTAALQLAANLVESGPwRYALVVAS 136
|
|
| SRP54_G |
cd17875 |
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ... |
29-91 |
5.14e-03 |
|
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.
Pssm-ID: 349784 Cd Length: 193 Bit Score: 37.94 E-value: 5.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488042405 29 LGAAVIRESIQ-RAGVAPDqvdEVIFgcVLSAGIGQGPARQAMR-KASVPdhVGAVTINKLCGSA 91
Cdd:cd17875 96 QEEELFEEMKQiSDAVKPD---EVIL--VIDASIGQAAEDQAKAfKEAVD--IGSVIITKLDGHA 153
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
227-367 |
7.42e-03 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 38.00 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488042405 227 IPTLRPAFSKDGTITAANSSSISDGAAALVLTTEEYAQSHGLNTLAKIVATSTHSQHPSEFTIAPIG-----AIQKVLEH 301
Cdd:cd00825 138 GALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAeglarAAKEALAV 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488042405 302 AGWSVDEVDAWEINEAFAMVAMAPIHELGIDEAK---VNIHGGACALGHPIGATGsriILSLIYALKRL 367
Cdd:cd00825 218 AGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGdksPAVSATKAMTGNLSSAAV---VLAVDEAVLML 283
|
|
| |
