|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
49-425 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 600.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 49 SFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAV 128
Cdd:PRK05790 16 KFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 129 CLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQ 207
Cdd:PRK05790 96 ALAAQAIRAGDADIVVAGGQESMSQAPHvLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 208 DKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANASGINDG 286
Cdd:PRK05790 176 DEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDTDEHPRPDTTAESLAKLRPAFDKDGT--VTAGNASGINDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 287 AAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGL 366
Cdd:PRK05790 254 AAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGL 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 735997436 367 NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK05790 334 DPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
45-425 |
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: 567.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 45 TSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSG 124
Cdd:cd00751 8 TPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTVNRVCGSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 125 LKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSR 204
Cdd:cd00751 88 LQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 205 EDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTPANASGIN 284
Cdd:cd00751 168 EEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAF--KKDGTVTAGNASGIN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKEL 364
Cdd:cd00751 246 DGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALACLKEL 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735997436 365 GLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:cd00751 326 GLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
45-425 |
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 735997436 45 TSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSG 124
Cdd:COG0183 12 TPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 125 LKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKiGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVS 203
Cdd:COG0183 92 LQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPkARWGYR-MNAKLVDPMINPGLTDPYTGLSMGETAENVAERYGIS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 204 REDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANASGI 283
Cdd:COG0183 171 REEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGT--VTAGNASGI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 284 NDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKE 363
Cdd:COG0183 249 NDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRE 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 735997436 364 LGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:COG0183 329 LGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
42-424 |
5.54e-165 |
|
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: 468.63 E-value: 5.54e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 42 FAQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMIC 121
Cdd:TIGR01930 4 AARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVNRQC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 122 GSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAY--LRTGVKIGEMPLTDSILCDgLTDAFHNCHMGITAENVAKK 199
Cdd:TIGR01930 84 ASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrsLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENLAKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 200 WQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTPAN 279
Cdd:TIGR01930 163 YGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAF--DPDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 280 ASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAA 359
Cdd:TIGR01930 241 SSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVLA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 360 IVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 424
Cdd:TIGR01930 321 CIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
43-425 |
1.48e-150 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 432.46 E-value: 1.48e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 43 AQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPV-RQASVGAGIPYSVPAWSCQMIC 121
Cdd:PRK09051 11 VRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLsRVAAINAGVPQETPAFNVNRLC 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 122 GSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLA-YLRTGVKIGEMPLTDSILcDGLTDAFHNCHMGITAENVAKKW 200
Cdd:PRK09051 91 GSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVDMMV-GALHDPFGTIHMGVTAENVAAKY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 201 QVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGtGTVTPANA 280
Cdd:PRK09051 170 GISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEN-GTVTAGNA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:PRK09051 249 SGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFAAQACAV 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 361 VKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK09051 329 TRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
43-425 |
1.67e-145 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 419.68 E-value: 1.67e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 43 AQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICG 122
Cdd:PRK05656 10 TRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMTLNKVCG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 123 SGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQ 201
Cdd:PRK05656 90 SGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYvLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAENLVEKYG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANA 280
Cdd:PRK05656 170 ISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGePLAFATDEQPRAGTTAESLAKLKPAFKKDGS--VTAGNA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:PRK05656 248 SSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQSLAV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 361 VKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK05656 328 GKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
44-424 |
5.91e-141 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 408.26 E-value: 5.91e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 44 QTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGS 123
Cdd:PRK06633 12 RTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 124 GLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVS 203
Cdd:PRK06633 92 GLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAENISKQFNIS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 204 REDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTPANASGI 283
Cdd:PRK06633 172 RQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAF--DKNGVVTAGNASSI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 284 NDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKE 363
Cdd:PRK06633 250 NDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNRE 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735997436 364 LGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 424
Cdd:PRK06633 330 MKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
43-424 |
7.86e-133 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 387.53 E-value: 7.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 43 AQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICG 122
Cdd:PRK08235 10 ARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETVNKVCA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 123 SGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQ 201
Cdd:PRK08235 90 SGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYiLPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEVAKELG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTPANA 280
Cdd:PRK08235 170 ISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGdPIVVAKDEAPRKDTTIEKLAKLKPVF--DKTGTITAGNA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:PRK08235 248 PGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVALAS 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997436 361 VKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 424
Cdd:PRK08235 328 TEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
43-425 |
1.07e-128 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 376.74 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 43 AQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICG 122
Cdd:PLN02644 9 ARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTTVNKVCA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 123 SGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPH-LAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQ 201
Cdd:PLN02644 89 SGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAELCADQYS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG--LIEVKTDEFPRHgSNIEAMSKLKPYFLTDGtGTVTPAN 279
Cdd:PLN02644 169 ISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrpSVIVDKDEGLGK-FDPAKLRKLRPSFKEDG-GSVTAGN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 280 ASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAA 359
Cdd:PLN02644 247 ASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSVVALA 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 735997436 360 IVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PLN02644 327 NQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
50-425 |
1.19e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 351.60 E-value: 1.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 50 FNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK06205 17 FGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQLDRRCGSGLQAVI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKIGEMPLTDSiLCDGLTDAFHNCH-----MGITAENVAKKWQVS 203
Cdd:PRK06205 97 TAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDR-LARGRETAGGRRFpvpggMIETAENLRREYGIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 204 REDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFL-TDGTGTVTPANAS 281
Cdd:PRK06205 176 REEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHPRADTTLESLAKLRPIMGkQDPEATVTAGNAS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 282 GINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIV 361
Cdd:PRK06205 256 GQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVL 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 735997436 362 KELGLNP---EKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK06205 336 KEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
50-425 |
1.64e-114 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 340.78 E-value: 1.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 50 FNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKA 127
Cdd:PRK09050 17 YGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVSVPGTTINRLCGSGMDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 128 VCLAVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTG----VKIG---------EMPLTDSilcdgltdafhnch 188
Cdd:PRK09050 97 VGTAARAIKAGEAELMIAGGVESMSRAPFVmgkadsAFSRQAeifdTTIGwrfvnplmkAQYGVDS-------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 189 MGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYF 267
Cdd:PRK09050 163 MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRDEHPRPETTLEALAKLKPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 268 LTDGTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF 347
Cdd:PRK09050 243 RPDGT--VTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 348 EINEAFAAVSAAIVKELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK09050 321 ELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIER 400
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
43-424 |
3.25e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 332.24 E-value: 3.25e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 43 AQTSRCSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICG 122
Cdd:PRK06954 15 ARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTTVNKMCG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 123 SGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHL-AYLRTGVKIGEMPLTDSILCDGLTDAFHNCH-MGITAENVAKKW 200
Cdd:PRK06954 95 SGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLlPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAEECAGEY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 201 QVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHgSNIEAMSKLKPYFLTDGTgtVTPANA 280
Cdd:PRK06954 175 GFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGT--VTAANS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:PRK06954 252 SSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAA 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997436 361 VKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQ 424
Cdd:PRK06954 332 MKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
51-420 |
2.63e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 319.77 E-value: 2.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLA-AGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK07661 19 KGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYTVPAITINRYCSSGLQSIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPHLAY-LRTGVKIGEmpltdsilcdglTDAFHNCHMGITAENVAKKWQVSREDQD 208
Cdd:PRK07661 99 YGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPRLVE------------AAPEYYMGMGHTAEQVAVKYGISREDQD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 209 KVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-----GLIEVK----TDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPAN 279
Cdd:PRK07661 167 AFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennKLQEETitfsQDEGVRADTTLEILGKLRPAFNVKGS--VTAGN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 280 ASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAA 359
Cdd:PRK07661 245 SSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQ 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735997436 360 IVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 420
Cdd:PRK07661 325 VIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
50-425 |
2.61e-104 |
|
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: 314.80 E-value: 2.61e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 50 FNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKA 127
Cdd:TIGR02430 16 YGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGeDNRNVARMAALLAGLPVSVPGTTVNRLCGSGLDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 128 VCLAVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTgVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQ 201
Cdd:TIGR02430 96 IGMAARAIKAGEADLLIAGGVESMSRAPFVmgkadsAFSRS-AKIEDTTIGWRFINPLMKALYGVDSMPETAENVAEEFG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGL-IEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANA 280
Cdd:TIGR02430 175 ISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEpTVVDQDEHPRPETTLEGLAKLKPVVRPDGT--VTAGNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:TIGR02430 253 SGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNEAFAAQALAV 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 735997436 361 VKELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:TIGR02430 333 LRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
52-426 |
6.09e-104 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 315.55 E-value: 6.09e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 52 GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQ-NPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:PLN02287 64 GGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVPVRTVNRQCSSGLQAVAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPltdsilcdgltDAfHNC--HMGITAENVAKKWQVSREDQD 208
Cdd:PLN02287 144 VAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFS-----------QA-QDCllPMGITSENVAERFGVTREEQD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 209 KVAVLSQNRTENAQKAGHFDKEIVPV---LVSTRKG---LIEVKTDEFPRHGSNIEAMSKLKPYFLTDgtGTVTPANASG 282
Cdd:PLN02287 212 QAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGeekPIVISVDDGIRPNTTLADLAKLKPVFKKN--GTTTAGNSSQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 283 INDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVK 362
Cdd:PLN02287 290 VSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCK 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 735997436 363 ELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSR--GVAALCIGGGMGIAMCVQRE 426
Cdd:PLN02287 370 KLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDCrfGVVSMCIGTGMGAAAVFERG 435
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
49-296 |
1.34e-102 |
|
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: 305.38 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 49 SFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAV 128
Cdd:pfam00108 13 SFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 129 CLAVQSIGIGDSSIVVAGGMENMSKAPHLAY--LRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSRED 206
Cdd:pfam00108 93 YLAAQSIASGDADVVLAGGVESMSHAPYALPtdARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 207 QDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGTGTVTPANASGINDG 286
Cdd:pfam00108 173 QDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAF--DKEGTVTAGNASPINDG 250
|
250
....*....|
gi 735997436 287 AAAVVLMKKS 296
Cdd:pfam00108 251 AAAVLLMSES 260
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
52-425 |
4.79e-101 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 306.70 E-value: 4.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 52 GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:PRK08131 19 GALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTVPGQTVNRLCASGLAAVID 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSKAPHL------AYLRTgVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSR 204
Cdd:PRK08131 99 AARAITCGEGDLYLAGGVESMSRAPFVmgkaesAFSRD-AKVFDTTIGARFPNPKIVAQYGNDSMPETGDNVAAEFGISR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 205 EDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVST--RKGLIEVKTDEFPRHGSNIEAMSKLKPYFltDGtGTVTPANASG 282
Cdd:PRK08131 178 EDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEHPRPSSTVEALTKLKPLF--EG-GVVTAGNASG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 283 INDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVK 362
Cdd:PRK08131 255 INDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLK 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 363 ELGL--NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK08131 335 GLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIER 399
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
61-426 |
1.99e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 299.71 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 61 DLGSTVIKEVLKRATVAPEDVSEVIFGhvLAAGCGQNPV---RQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGI 137
Cdd:PRK06445 34 ELAAMLINRLIEKTGIKPEEIDDIITG--CALQVGENWLyggRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIAT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 138 GDSSIVVAGGMENMSKAPhlAYLRTGVKIGEMPLTDSILCD-GLTDAFHnchMGITAENVAKKWQVSREDQDKVAVLSQN 216
Cdd:PRK06445 112 GMADIVIAGGVEHMTRTP--MGDNPHIEPNPKLLTDPKYIEyDLTTGYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 217 RTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTgtVTPANASGINDGAAAVVLMKKS 296
Cdd:PRK06445 187 LAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKPDGV--ITAGNSSPLNSGASYVLLMSKK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 297 EADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGG 376
Cdd:PRK06445 265 AVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGG 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 735997436 377 AIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE 426
Cdd:PRK06445 345 AIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
51-420 |
3.31e-97 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 296.53 E-value: 3.31e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRA-TVAPEDVSEVIFGHVLA-AGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAV 128
Cdd:PRK09052 23 RGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPeAEQGLNVARIGALLAGLPNSVGGVTVNRFCASGLQAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 129 CLAVQSIGIGDSSIVVAGGMENMSKAPHLaylrtgvkiGEMP-LTDSILC--DGLTDAFHnchMGITAENVAKKWQVSRE 205
Cdd:PRK09052 103 AMAADRIRVGEADVMIAAGVESMSMVPMM---------GNKPsMSPAIFArdENVGIAYG---MGLTAEKVAEQWKVSRE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 206 DQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-----GLIEVKT-----DEFPRHGSNIEAMSKLKPYFltDGTGTV 275
Cdd:PRK09052 171 DQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatGEVDVKTrtvdlDEGPRADTSLEGLAKLKPVF--ANKGSV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 276 TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA 355
Cdd:PRK09052 249 TAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAA 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 356 VSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 420
Cdd:PRK09052 329 QSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
49-425 |
6.69e-96 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 292.64 E-value: 6.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 49 SFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLK 126
Cdd:PRK08947 17 SKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLeQGFNIARNAALLAGIPHSVPAVTVNRLCGSSMQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 127 AVCLAVQSIGIGDSSIVVAGGMENMskaphlaylrtgvkiGEMPLTDSIlcD-----GLTDAFHNCHMGITAENVAKKWQ 201
Cdd:PRK08947 97 ALHDAARAIMTGDGDVFLIGGVEHM---------------GHVPMNHGV--DfhpglSKNVAKAAGMMGLTAEMLGKMHG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFlTDGTGTVTPANA 280
Cdd:PRK08947 160 ISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPETTVEALAALRPAF-DPVNGTVTAGTS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAI 360
Cdd:PRK08947 239 SALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPC 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 735997436 361 VKELGL---NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK08947 319 LKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
51-425 |
2.17e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 292.17 E-value: 2.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK08242 20 DGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRFCASGLEAVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPhlaylrTGVKIGEMPLTDSIlcdgltdAFHNCHM--GITAENVAKKWQVSREDQ 207
Cdd:PRK08242 100 LAAAKVRSGWDDLVIAGGVESMSRVP------MGSDGGAWAMDPST-------NFPTYFVpqGISADLIATKYGFSREDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 208 DKVAVLSQNRTENAQKAGHFDKEIVPVlvSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT-------DGTGTV----- 275
Cdd:PRK08242 167 DAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMmgemggfDAVALQkypev 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 276 -------TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFE 348
Cdd:PRK08242 245 erinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 735997436 349 INEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK08242 325 LNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIER 401
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
51-425 |
1.05e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 289.68 E-value: 1.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGcGQ--NPVRQASVGAGIPYSVPAWSCQMICGSGLKAV 128
Cdd:PRK07801 18 KGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEEVPGVTVDRQCGSSQQAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 129 CLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIG-EMPLTDSILC-----DGLTDAFHNchmgitAENVAKKWQV 202
Cdd:PRK07801 97 HFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGfTSPFAESKGWlhrygDQEVSQFRG------AELIAEKWGI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 203 SREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLvstrkgliEVKTDEFPRHgSNIEAMSKLKPyfLTDGtGTVTPANASG 282
Cdd:PRK07801 171 SREEMERFALESHRRAFAAIRAGRFDNEIVPVG--------GVTVDEGPRE-TSLEKMAGLKP--LVEG-GRLTAAVASQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 283 INDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVK 362
Cdd:PRK07801 239 ISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPVVLAWLK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 735997436 363 ELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK07801 319 ETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
50-425 |
1.34e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 287.67 E-value: 1.34e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 50 FNGALAAVPVQDLGSTVIKEVL-KRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPySVPAWSCQMICGSGLKA 127
Cdd:PRK07851 18 FKGSLKDMRPDDLAAQMVRAALdKVPALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD-FLPGTTVNRYCSSSLQT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 128 VCLAVQSIGIGDSSIVVAGGMENMSKAPH---------------LAYLRTG--VKIGEMPLTDSILCDGLTDAFhnCHMG 190
Cdd:PRK07851 97 TRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdslpdtknplfaEAQARTAarAEGGAEAWHDPREDGLLPDVY--IAMG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 191 ITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVlvSTRKGLIeVKTDEFPRHGSNIEAMSKLKPYFLTD 270
Cdd:PRK07851 175 QTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV--TLPDGTV-VSTDDGPRAGTTYEKVSQLKPVFRPD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 271 GTgtVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEIN 350
Cdd:PRK07851 252 GT--VTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAGMSIDDIDLVEIN 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 351 EAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK07851 330 EAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQGMAMVLER 404
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
51-424 |
2.59e-91 |
|
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: 281.30 E-value: 2.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:cd00826 15 NGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSkaphlaylrtgvkigempltdsilcdgltdafhnchmgITAENVAKKWQV-------- 202
Cdd:cd00826 95 AMQLIAGGDANCILAGGFEKME--------------------------------------TSAENNAKEKHIdvlinkyg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 203 SREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGS--NIEAMSKLKPYFltDGTGTVTPANA 280
Cdd:cd00826 137 MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGDeaSLDEIAKLRPAF--DKEDFLTAGNA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADK-------RGLTPLARIVSWSQVGVEPS----IMGIGPIPAIKQAVTKAGWSLEDVDIFEI 349
Cdd:cd00826 215 CGLNDGAAAAILMSEAEAQKhglqskaREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 350 NEAFAAVSAAIVKELGLNPEK------------------VNIEGGAIALGHPLGASGCRILVTLLHTL-----ERMGRSR 406
Cdd:cd00826 295 HDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELkgeagKRQGAGA 374
|
410
....*....|....*...
gi 735997436 407 GVAALCIGGGMGIAMCVQ 424
Cdd:cd00826 375 GLALLCIGGGGGAAMCIE 392
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
50-418 |
2.70e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 278.43 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 50 FNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK06366 17 FGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYTVNVVCASGMLAVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPHL--AYLRTGVK---IGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSR 204
Cdd:PRK06366 97 SAAREIMLGERDLVIAGGMENMSNAPFLlpSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 205 EDQDKVAVLSQNRTENAQKAGHFDKEIVPVLvstrkgliEVKTDEFPRHgSNIEAMSKLKPYFltDGTGTVTPANASGIN 284
Cdd:PRK06366 177 EMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRK-TTMEDLAKLPPAF--DKNGILTAGNSAQLS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKEL 364
Cdd:PRK06366 246 DGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQL 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 735997436 365 GLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMG 418
Cdd:PRK06366 326 KIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
61-426 |
6.73e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 276.13 E-value: 6.73e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 61 DLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDS 140
Cdd:PRK08170 29 DLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 141 SIVVAGGMENMSKAPHL---AYLR----------TGVKIGEMP------LTDSI-LCDGLTDAFHNCHMGITAENVAKKW 200
Cdd:PRK08170 109 DLVLAGGVEAMSHAPLLfseKMVRwlagwyaaksIGQKLAALGklrpsyLAPVIgLLRGLTDPVVGLNMGQTAEVLAHRF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 201 QVSREDQDKVAVLSQNRTENAQKAGHFdKEIVPVLvsTRKGLIEVKTDEFpRHGSNIEAMSKLKPYFlTDGTGTVTPANA 280
Cdd:PRK08170 189 GITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLF--DRDGKFYDHDDGV-RPDSSMEKLAKLKPFF-DRPYGRVTAGNS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA-VSAA 359
Cdd:PRK08170 264 SQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAqVLAC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 360 IV---------KELGL-------NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCV 423
Cdd:PRK08170 344 LAawadeeycrEQLGLdgalgelDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLL 423
|
...
gi 735997436 424 QRE 426
Cdd:PRK08170 424 ERV 426
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
49-425 |
1.16e-80 |
|
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: 253.71 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 49 SFNGALAAVPVQDLGSTVIKEVLKR-ATVAPEDVSEVIFGHVLAA-GCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLK 126
Cdd:TIGR02445 15 SKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTSAAVTVNRLCGSSMQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 127 AVCLAVQSIGIGDSSIVVAGGMENMSKAPhlayLRTGVKIGEMPLTDSILCDGLtdafhnchMGITAENVAKKWQVSRED 206
Cdd:TIGR02445 95 ALHDAARAIMTGDADVCLVGGVEHMGHVP----MMHGVDFHPGMSLHVAKAAGM--------MGLTAEMLGKMHGISREQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 207 QDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKG-LIEVKTDEFPRHGSNIEAMSKLKPYFLTDGtGTVTPANASGIND 285
Cdd:TIGR02445 163 QDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGfLKQFDYDEVIRPETTVESLAALRPAFDPKN-GTVTAGTSSALSD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 286 GAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELG 365
Cdd:TIGR02445 242 GASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDLG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 735997436 366 L---NPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:TIGR02445 322 LldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
51-425 |
4.84e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 252.34 E-value: 4.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK06504 18 GGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESVPGTSIDRQCGSSQQALH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGemplTDSILCDGLTDAFHNCH----MGitAENVAKKWQVSRE 205
Cdd:PRK06504 98 FAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNG----LGHYKSPGMEERYPGIQfsqfTG--AEMMAKKYGLSKD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 206 DQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKT-DEFPRHGSNIEAMSKLKPyfLTDGtGTVTPANASGIN 284
Cdd:PRK06504 172 QLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIRFDATLEGIAGVKL--IAEG-GRLTAATASQIC 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKEL 364
Cdd:PRK06504 249 DGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPLAWLKAT 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735997436 365 GLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK06504 329 GADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
51-425 |
1.66e-78 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 248.10 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAG-CGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVC 129
Cdd:PRK07850 18 NGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHVGATTIDCQCGSAQQANH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPhlayLRTGVKIGE-MPLTDSILCDgLTDAFHnchmgiTAENVAKKWQVSREDQD 208
Cdd:PRK07850 98 LVAGLIAAGAIDVGIACGVEAMSRVP----LGANAGPGRgLPRPDSWDID-MPNQFE------AAERIAKRRGITREDVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 209 KVAVLSQNRTENAQKAGHFDKEIVPVLVSTRK-------GLIEVKTDEFPRHgSNIEAMSKLKPyfLTDGtGTVTPANAS 281
Cdd:PRK07850 167 AFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRD-TTMEGLAGLKP--VLEG-GIHTAGTSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 282 GINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIV 361
Cdd:PRK07850 243 QISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVVLSWA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997436 362 KELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK07850 323 QVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
52-425 |
1.74e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 243.91 E-value: 1.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 52 GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:PRK06025 22 GALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGeMPLTDSilCDGLTDAFH-NCHMGITAENVAKKWQVSREDQDK 209
Cdd:PRK06025 102 AAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKP-PLGMGS--GNLRLRALHpQSHQGVCGDAIATMEGITREALDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 210 VAVLSQNRTENAQKAGHFDKEIVPVLvsTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLT------DGTGT--------V 275
Cdd:PRK06025 179 LGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEEFPRPQTTAEGLAALKPAFTAiadyplDDKGTtyrglinqK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 276 TP----------ANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVD 345
Cdd:PRK06025 257 YPdleikhvhhaGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDID 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 346 IFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK06025 337 LWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
51-421 |
2.57e-75 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 238.90 E-value: 2.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRAtvaPEDVSEVIFGHVLaaGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:PRK06690 17 NGMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGVTIDRQCGAGLEAIRT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSKAPHLAYLR-TGVKIGEmPltdsilcdgltdafhncHMGITAENVAKKWQVSREDQDK 209
Cdd:PRK06690 92 ACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGD-P-----------------DMGVAAEYVAERYNITREMQDE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 210 VAVLSQNRTENAQKAGHFDKEIVPVlvstrKGLIevktDEFPRHGSNIEAM-SKLKPYFLTDGTgtVTPANASGINDGAA 288
Cdd:PRK06690 154 YACLSYKRTLQALEKGYIHEEILSF-----NGLL----DESIKKEMNYERIiKRTKPAFLHNGT--VTAGNSCGVNDGAC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 289 AVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNP 368
Cdd:PRK06690 223 AVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPY 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 735997436 369 EKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAM 421
Cdd:PRK06690 303 EKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLAL 355
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
49-420 |
4.15e-75 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 239.67 E-value: 4.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 49 SFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGC-GQNPVRQASVGAGIPYSVPAWSCQMICGSGLKA 127
Cdd:PRK07108 17 SWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTVPGMTVNRFCSSGLQT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 128 VCLAVQSIGIGDSSIVVAGGMENMSKAPHlaylrtgvKIGEMPLTDSILCDGLTDAFHNchMGITAENVAKKWQVSREDQ 207
Cdd:PRK07108 97 IALAAQRVIAGEGDVFVAGGVESISCVQN--------EMNRHMLREGWLVEHKPEIYWS--MLQTAENVAKRYGISKERQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 208 DKVAVLSQNRTENAQKAGHFDKEIVPVLV------------STRKglIEVKTDEFPRHGSNIEAMSKLKPYFltdGTGTV 275
Cdd:PRK07108 167 DEYGVQSQQRAAAAQAAGRFDDEIVPITVtagvadkatgrlFTKE--VTVSADEGIRPDTTLEGVSKIRSAL---PGGVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 276 TPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAA 355
Cdd:PRK07108 242 TAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAV 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 356 VSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIA 420
Cdd:PRK07108 322 QVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
53-426 |
1.25e-66 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 218.70 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 53 ALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAV 132
Cdd:PRK08963 23 AFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 133 QSIGIGDSSIVVAGGMENMSKAP------------HLAYLRT---------GVKIGE-MPLTDSI--LCDGLTdafhnch 188
Cdd:PRK08963 103 ESIMAGTIDIGIAGGADSSSVLPigvskklaralvDLNKARTlgqrlklfsRLRLRDlLPVPPAVaeYSTGLR------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 189 MGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEvkTDEFPRHGSNIEAMSKLKPYFL 268
Cdd:PRK08963 176 MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQPLE--EDNNIRGDSTLEDYAKLRPAFD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 269 TDgTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEP-SIMGIGPIPAIKQAVTKAGWSLEDVDIF 347
Cdd:PRK08963 254 RK-HGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGLTLADLTLI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 348 EINEAFAAVSAAIVK----------ELGLN-------PEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAA 410
Cdd:PRK08963 333 DMHEAFAAQTLANLQmfaserfareKLGRSqaigevdMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGLGLTT 412
|
410
....*....|....*.
gi 735997436 411 LCIGGGMGIAMCVQRE 426
Cdd:PRK08963 413 ACAAGGLGAAMVLEVE 428
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
303-425 |
3.39e-62 |
|
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: 196.71 E-value: 3.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 303 LTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGH 382
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 735997436 383 PLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
51-425 |
3.07e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 178.17 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 51 NGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCL 130
Cdd:PRK09268 23 NGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 131 AVQSIGIGDSSIVVAGGMENMSKAP-------------------------HLAYLRTGVKIGEMPLTDSILCdGLTdafh 185
Cdd:PRK09268 103 VANKIALGQIDSGIAGGVDTTSDAPiavneglrkillelnrakttgdrlkALGKLRPKHLAPEIPRNGEPRT-GLS---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 186 nchMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRkglievktDEFPRHGSNIEAMSKLKP 265
Cdd:PRK09268 178 ---MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLRPDSSLEKLAKLKP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 266 YFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVsWSQV-------GVEPSIMGigPIPAIKQAVTKAG 338
Cdd:PRK09268 247 VFGKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV-DAETaavdfvhGKEGLLMA--PAYAVPRLLARNG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 339 WSLEDVDIFEINEAFAAVSAAIVK----------ELGLN-------PEKVNIEGGAIALGHPLGASGCRILVTLLHTLER 401
Cdd:PRK09268 324 LTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLDaplgsidRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAE 403
|
410 420
....*....|....*....|....
gi 735997436 402 MGRSRGVAALCIGGGMGIAMCVQR 425
Cdd:PRK09268 404 KGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
55-423 |
1.53e-24 |
|
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: 101.75 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 55 AAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPySVPAWSCQMICGSGLKAVCLAVQS 134
Cdd:cd00327 3 LGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 135 IGIGDSSIVVAGGMEnmskaphlaylrtgvkigempltdsilcdgltdafhnchmgitaenvakkwqvsredqdkvavls 214
Cdd:cd00327 82 VQNGKADIVLAGGSE----------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 215 qnrtenaqkaghfdkeivpvlvstrkglievktdefprhgsnieamsklkpyfltdgtgtvtpanASGINDGAAAVVLMK 294
Cdd:cd00327 97 -----------------------------------------------------------------EFVFGDGAAAAVVES 111
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 295 KSEADKRGLTPLARIVSWSQVGVEPS----IMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEK 370
Cdd:cd00327 112 EEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDG 191
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 735997436 371 V---NIEGGAIALGHPLGASGCRILVTLLHTLERMGRSR-------GVAALCIGGGMGIAMCV 423
Cdd:cd00327 192 VrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
57-418 |
8.63e-14 |
|
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: 72.30 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 57 VPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYsVPAWSCQMICGSGLKAVCLAVQSIG 136
Cdd:cd00829 14 RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 137 IGDSSIVVAGGMENMSKAPhlaylrTGVKIGEMPLTDSILCDGLTDAFHNCHM-GITAENVAKKWQVSREDQDKVAVlsQ 215
Cdd:cd00829 93 SGLADVVLVVGAEKMSDVP------TGDEAGGRASDLEWEGPEPPGGLTPPALyALAARRYMHRYGTTREDLAKVAV--K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 216 NRtENAQK---AgHFDKEIVP--VLVStrkglievktdefPRHGSnieamsklkPYFLTDgtgtvtpanASGINDGAAAV 290
Cdd:cd00829 165 NH-RNAARnpyA-QFRKPITVedVLNS-------------RMIAD---------PLRLLD---------CCPVSDGAAAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 291 VLMKKSEADKRGLTPlARIVSWSQVGVEPSIMGIGPI-------PAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKE 363
Cdd:cd00829 212 VLASEERARELTDRP-VWILGVGAASDTPSLSERDDFlsldaarLAARRAYKMAGITPDDIDVAELYDCFTIAELLALED 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 735997436 364 LGLNPE------------------KVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVA----ALCIGGGMG 418
Cdd:cd00829 291 LGFCEKgeggklvregdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPgarvGLAHNIGGT 367
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
52-420 |
1.49e-09 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 59.53 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 52 GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCgqnpVRQASVGAGIP-YS----VPAWSCQMICGSGLK 126
Cdd:PRK06064 15 GELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLF----VSQEHIAALIAdYAglapIPATRVEAACASGGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 127 AVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGempltdsilcdgltDAFHNCHMGIT--------AENVAK 198
Cdd:PRK06064 91 ALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAG--------------DYEWEEFFGATfpglyaliARRYMH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 199 KWQVSREDQDKVAVlsqNRTENAQK--AGHFDKEIV--PVLVSTRKGlievktdefprhgsnieamsklKPYFLTDgtgt 274
Cdd:PRK06064 157 KYGTTEEDLALVAV---KNHYNGSKnpYAQFQKEITveQVLNSPPVA----------------------DPLKLLD---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 275 vtpanASGINDGAAAVVLMKKSEADKRGLTPLaRIVSWSQ------VGVEPSIMGIGP-IPAIKQAVTKAGWSLEDVDIF 347
Cdd:PRK06064 208 -----CSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQasdtiaLHDRKDFTTLDAaVVAAEKAYKMAGIEPKDIDVA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 348 EINEAFAAVSAAIVKELGLnPEK-------------------VNIEGGAIALGHPLGASGCRILVTLlhTLERMGRSRGV 408
Cdd:PRK06064 282 EVHDCFTIAEILAYEDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEI--VWQLRGEAEKG 358
|
410
....*....|..
gi 735997436 409 AALCIGGGMGIA 420
Cdd:PRK06064 359 RQQVIGAGYGLT 370
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
281-393 |
3.13e-09 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 58.55 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 281 SGINDGAAAVVLMKKSEA-DKRGLTPLARIVSWSQ----VGVEPSIMGIGPIP--------AIKQAVTKAGWSLEDVDIF 347
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLrDYADARPIPRIKGWGHrtapLGLEQKLDRSAGDPyvlphvrqAVLDAYRRAGVGLDDLDGF 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 735997436 348 EINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIALGHPLGASGCRILV 393
Cdd:PRK06289 300 EVHDCFTPSEYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRMLL 363
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
48-388 |
8.03e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 54.08 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 48 CSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAwSCQMICGSGLKA 127
Cdd:PRK12578 10 NSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPL-RVEAMCATGLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 128 VCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLtdsilcdgltdAFHN------CHMGITAENVAKKWQ 201
Cdd:PRK12578 89 SLTAYTAVASGLVDMAIAVGVDKMTEVDTSTSLAIGGRGGNYQW-----------EYHFygttfpTYYALYATRHMAVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 202 VSREDQDKVAVLSQNRTENAQKAgHFDKEIvpvlvsTRKGLIEVKTDEFPrhgsnieamskLKPYfltdgtgtvtpaNAS 281
Cdd:PRK12578 158 TTEEQMALVSVKAHKYGAMNPKA-HFQKPV------TVEEVLKSRAISWP-----------IKLL------------DSC 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 282 GINDGAAAVVLMKKSEADKRGL-TP--------------LARIVSWsqVGVEPSIMgigpipAIKQAVTKAGWSLEDVDI 346
Cdd:PRK12578 208 PISDGSATAIFASEEKVKELKIdSPvwitgigyandyayVARRGEW--VGFKATQL------AARQAYNMAKVTPNDIEV 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 347 FEINEAFAAVSAAIVKELGL-------------NPEK-----VNIEGGAIALGHPLGASG 388
Cdd:PRK12578 280 ATVHDAFTIAEIMGYEDLGFtekgkggkfieegQSEKggkvgVNLFGGLKAKGHPLGATG 339
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
278-388 |
2.78e-06 |
|
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: 49.07 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 278 ANASGIN--DGAAAVVLMKKSEADKRGLTPLARIVSWSQVG-----VEPSIMGIGPIPAIKQAVTKAGWSLEDVDIfeIN 350
Cdd:cd00834 222 KDRDGFVlgEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--IN 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 351 ------------EafaavSAAIVKELGLNPEKVnieggAI-----ALGHPLGASG 388
Cdd:cd00834 300 ahgtstplndaaE-----SKAIKRVFGEHAKKV-----PVsstksMTGHLLGAAG 344
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
286-345 |
9.82e-06 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 47.33 E-value: 9.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735997436 286 GAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSImgIGPIPAIKQAVTKAGWSLEDVD 345
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDID 302
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
101-390 |
2.83e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 46.04 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 101 QASVGAGIPYSvPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAP------HLA----YLRTGVkigemp 170
Cdd:PTZ00455 101 QSGASNALLYK-PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSarvggdYLAraadYRRQRK------ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 171 ltdsilcdgLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLS-QNRTENAQKAGHfdkeivpvlvsTRKGLIEVKTDE 249
Cdd:PTZ00455 174 ---------LDDFTFPCLFAKRMKYIQEHGHFTMEDTARVAAKAyANGNKNPLAHMH-----------TRKLSLEFCTGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 250 FPRHgSNIEAMSKLKPYFLTdgtgtvtpANASGINDGAAAVVLMKKSEADKRGLTPL-ARIVSWSQVGVEPSIMGIGP-- 326
Cdd:PTZ00455 234 SDKN-PKFLGNETYKPFLRM--------TDCSQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACASGNLYEDPpd 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 327 -------IPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIALG 381
Cdd:PTZ00455 305 atrmftsRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGIAEYghakdlirngatalegriPVNTGGGLLSFG 384
|
....*....
gi 735997436 382 HPLGASGCR 390
Cdd:PTZ00455 385 HPVGATGVK 393
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
285-388 |
3.96e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 45.43 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIF-------EINEA 352
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQ 289
|
90 100 110
....*....|....*....|....*....|....*.
gi 735997436 353 FaavSAAIVKELglNPEKVNIEGGAIALGHPLGASG 388
Cdd:PRK05952 290 R---EANLIQAL--FPHRVAVSSTKGATGHTLGASG 320
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
52-388 |
8.52e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 44.55 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 52 GALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHvLAAGCGQNPVRQASVGAGIP--YSVPAWSCQMICGSGLKAVC 129
Cdd:PRK07516 15 GKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGH-FNAGFSPQDFPASLVLQADPalRFKPATRVENACATGSAAVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 130 LAVQSIGIGDSSIVVAGGMENMSKAPhlaylrtGVKIGEMPLTDSILcdgltdafhnchmgitaenvakkwqvsREDQDK 209
Cdd:PRK07516 94 AALDAIEAGRARIVLVVGAEKMTATP-------TAEVGDILLGASYL---------------------------KEEGDT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 210 VAVLsqnrtenaqkAGHFDKeivpvlvstrkglieVKTDEFPRHGSNIEAMSKL----------KPY------FLTDGTG 273
Cdd:PRK07516 140 PGGF----------AGVFGR---------------IAQAYFQRYGDQSDALAMIaaknhangvaNPYaqmrkdLGFEFCR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 274 TVTPAN-----------ASGINDGAAAVVLMkkSEADKRGLTPLARIVSWSQVGvepSIMGI---------GPIPAIKQA 333
Cdd:PRK07516 195 TVSEKNplvagplrrtdCSLVSDGAAALVLA--DAETARALQRAVRFRARAHVN---DFLPLsrrdplafeGPRRAWQRA 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 735997436 334 VTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPE------------------KVNIEGGAIALGHPLGASG 388
Cdd:PRK07516 270 LAQAGVTLDDLSFVETHDCFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATG 342
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
285-388 |
2.02e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 43.24 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVG-----VEPSIMGIGPIPAIKQAVTKAGWSLEDVD----------IFEI 349
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDyinahgtstpAGDK 311
|
90 100 110
....*....|....*....|....*....|....*....
gi 735997436 350 NEAfaavsAAIVKELGLNPEKVNIEGGAIALGHPLGASG 388
Cdd:PRK07314 312 AET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
285-388 |
2.58e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 42.96 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 285 DGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIP----------AIKQAVTKAGWSLEDVDIFEINEAFA 354
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFDGRSMIdlvgydmtraAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 735997436 355 AVSAAIVKELGLNPEK------------------VNIEGGAIALGHPLGASG 388
Cdd:PRK08256 295 ANELLTYEALGLCPEGeaekfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
278-388 |
3.55e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 42.39 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 278 ANASGIN--DGAAAVVLMKKSEADKRGLTPLARIVSWS-------QVGVEPSimGIGPIPAIKQAVTKAGWSLEDVDIfe 348
Cdd:COG0304 222 KDRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDIDY-- 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 735997436 349 IN------------EAfaavsAAIVKELGLNPEKVNIegGAI--ALGHPLGASG 388
Cdd:COG0304 298 INahgtstplgdaaET-----KAIKRVFGDHAYKVPV--SSTksMTGHLLGAAG 344
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
324-375 |
4.08e-04 |
|
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) and similar proteins; DDRA, also called DDR large subunit, diol dehydratase-reactivase large subunit, diol dehydratase-reactivating factor alpha subunit, or DDR alpha subunit, is the large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. DDR has weak ATPase activity which is required for DD reactivation. DDRA contains the adenosine nucleotide binding site. DDRA has four domains, the ATPase domain, the swiveling domain, the linker domain, and the insert domain. The model corresponds to the ATPase domain. DDRA belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation.
Pssm-ID: 466880 Cd Length: 260 Bit Score: 41.81 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 735997436 324 IGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLnpeKVNIEG 375
Cdd:cd24030 46 PGIIKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELGI---PVEIGG 94
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
328-423 |
5.34e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 38.55 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 328 PAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKV--NIEggaiALGHPLGASgcriLVTLLHTLERMGR- 404
Cdd:COG0332 228 EVIREALEKAGLTLDDIDWFIPHQANLRIIEAVAKRLGLPEEKVvvNID----RYGNTSAAS----IPLALDEALREGRi 299
|
90 100
....*....|....*....|.
gi 735997436 405 SRG-VAALC-IGGGMGIAMCV 423
Cdd:COG0332 300 KPGdLVLLAgFGAGLTWGAAV 320
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
283-400 |
6.53e-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: 38.39 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735997436 283 INDGAAAVVLMKKSEADKRGLTPLARIVSWSQV-----GVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVS 357
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATidgagMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 735997436 358 AAIVKELGLN---PEKVNIEGGAIALGHPLGASGCRILVTLLHTLE 400
Cdd:cd00825 239 DVKELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| |
