|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
4-339 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 541.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMGE 82
Cdd:PRK05790 57 LQAGAGQNPARQAALKAGLPVEVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLpGSRWGQKMGD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 83 ASLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKI 161
Cdd:PRK05790 137 VELVDTMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 162 DEHPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPI 241
Cdd:PRK05790 217 DEHPRPDTTAESLAKLRPAFDKDGT--VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 242 SAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:PRK05790 295 PAIRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKG 374
|
330
....*....|....*...
gi 704582759 322 VAALCIGGGMGIAMCVER 339
Cdd:PRK05790 375 LATLCIGGGQGVALIVER 392
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
4-339 |
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: 524.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEA 83
Cdd:cd00751 53 LQAGEGQNPARQAALLAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 84 SLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKIDE 163
Cdd:cd00751 133 NTLDGMLDDGLTDPFTGLSMGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 164 HPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISA 243
Cdd:cd00751 213 GPRPDTTLEKLAKLKPAF--KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 244 IKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVA 323
Cdd:cd00751 291 IPKALKRAGLTLDDIDLIEINEAFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLA 370
|
330
....*....|....*.
gi 704582759 324 ALCIGGGMGIAMCVER 339
Cdd:cd00751 371 TMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
4-339 |
2.51e-177 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 496.51 E-value: 2.51e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMgE 82
Cdd:COG0183 57 LQAGQGQNPARQAALLAGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLpKARWGYRM-N 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 83 ASLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKID 162
Cdd:COG0183 136 AKLVDPMINPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 163 EHPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS 242
Cdd:COG0183 216 EGPRPDTTLEKLAKLKPAFKKDGT--VTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 243 AIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGV 322
Cdd:COG0183 294 ATRKALARAGLTLDDIDLIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGL 373
|
330
....*....|....*..
gi 704582759 323 AALCIGGGMGIAMCVER 339
Cdd:COG0183 374 ATMCIGGGQGIALIIER 390
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
4-338 |
4.53e-150 |
|
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: 427.41 E-value: 4.53e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIH--MRAGVKMG 81
Cdd:TIGR01930 52 LQAGEQQNIARQAALLAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrsLRWGVKPG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 82 EASLQDTIILDgLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKI 161
Cdd:TIGR01930 132 NAELEDARLKD-LTDANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 162 DEHPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPI 241
Cdd:TIGR01930 211 DEGIRPNTTLEKLAKLKPAF--DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 242 SAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:TIGR01930 289 PAIPKALKKAGLSISDIDLFEINEAFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYG 368
|
330
....*....|....*..
gi 704582759 322 VAALCIGGGMGIAMCVE 338
Cdd:TIGR01930 369 LATMCIGGGQGAAVILE 385
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
6-339 |
4.03e-138 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 397.34 E-value: 4.03e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 6 AGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMGEAS 84
Cdd:PRK05656 59 AGAGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLpGARTGLRMGHAQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 85 LQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKIDE 163
Cdd:PRK05656 139 LVDSMITDGLWDAFNDYHMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGePLAFATDE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 164 HPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISA 243
Cdd:PRK05656 219 QPRAGTTAESLAKLKPAFKKDGS--VTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 244 IKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVA 323
Cdd:PRK05656 297 TRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLA 376
|
330
....*....|....*.
gi 704582759 324 ALCIGGGMGIAMCVER 339
Cdd:PRK05656 377 TLCIGGGQGVALAIER 392
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
14-339 |
2.44e-135 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 390.09 E-value: 2.44e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 14 RQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMGEASLQDtIILD 92
Cdd:PRK09051 69 RVAAINAGVPQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVD-MMVG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 93 GLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKIDEHPRHGSNLE 172
Cdd:PRK09051 148 ALHDPFGTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 173 MMGKLKPCFLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIKKAIDKAG 252
Cdd:PRK09051 228 DLAKLKPVFKKEN-GTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 253 WTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAALCIGGGMG 332
Cdd:PRK09051 307 LTVADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQG 386
|
....*..
gi 704582759 333 IAMCVER 339
Cdd:PRK09051 387 IAAIFER 393
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-338 |
5.51e-132 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 381.69 E-value: 5.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEA 83
Cdd:PRK06633 58 ITGGSGQNPARQTLIHAGIPKEVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 84 SLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKIDE 163
Cdd:PRK06633 138 KMVDLMQYDGLTDVFSGVFMGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 164 HPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISA 243
Cdd:PRK06633 218 TVRPDTSLEILSKLRPAF--DKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 244 IKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVA 323
Cdd:PRK06633 296 SQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLV 375
|
330
....*....|....*
gi 704582759 324 ALCIGGGMGIAMCVE 338
Cdd:PRK06633 376 TLCIGGGMGMAMCVE 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
4-338 |
2.72e-123 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 359.80 E-value: 2.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIH-MRAGVKMGE 82
Cdd:PRK08235 57 LQGGQGQIPSRQAARAAGIPWEVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPgARWGYRMGD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 83 ASLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKI 161
Cdd:PRK08235 137 NEVIDLMVADGLTCAFSGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGdPIVVAK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 162 DEHPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPI 241
Cdd:PRK08235 217 DEAPRKDTTIEKLAKLKPVF--DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 242 SAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:PRK08235 295 YAINALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIG 374
|
330
....*....|....*..
gi 704582759 322 VAALCIGGGMGIAMCVE 338
Cdd:PRK08235 375 IAAICSGGGQGDAVLIE 391
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
11-339 |
1.02e-115 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 340.78 E-value: 1.02e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEASLQDTII 90
Cdd:PRK09050 66 NVARMSALLAGLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSRQAEIFDTTI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 91 ----LDGLTDAfyQY---HMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKID 162
Cdd:PRK09050 146 gwrfVNPLMKA--QYgvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 163 EHPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS 242
Cdd:PRK09050 224 EHPRPETTLEALAKLKPVFRPDGT--VTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 243 AIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKV--NLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKR 320
Cdd:PRK09050 302 ATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRY 381
|
330
....*....|....*....
gi 704582759 321 GVAALCIGGGMGIAMCVER 339
Cdd:PRK09050 382 ALCTMCIGVGQGIALAIER 400
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
6-339 |
8.65e-114 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 335.52 E-value: 8.65e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 6 AGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMGEAS 84
Cdd:PLN02644 58 ANLGQAPARQAALGAGLPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLpEARKGSRLGHDT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 85 LQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG--PIEVKID 162
Cdd:PLN02644 138 VVDGMLKDGLWDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrpSVIVDKD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 163 EHPRHgSNLEMMGKLKPCFLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS 242
Cdd:PLN02644 218 EGLGK-FDPAKLRKLRPSFKEDG-GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPAL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 243 AIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGV 322
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGV 375
|
330
....*....|....*..
gi 704582759 323 AALCIGGGMGIAMCVER 339
Cdd:PLN02644 376 AGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
14-339 |
2.58e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 331.95 E-value: 2.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 14 RQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIH-MRAGVKMGEASLQDTiiLD 92
Cdd:PRK06205 67 RVAALDAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDR--LA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 93 -GLTDAFYQYH-----MGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKIDEHP 165
Cdd:PRK06205 145 rGRETAGGRRFpvpggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 166 RHGSNLEMMGKLKPCFL-TDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAI 244
Cdd:PRK06205 225 RADTTLESLAKLRPIMGkQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPAT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 245 KKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVN---LEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:PRK06205 305 EKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGaddEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYG 384
|
330
....*....|....*...
gi 704582759 322 VAALCIGGGMGIAMCVER 339
Cdd:PRK06205 385 LETMCIGGGQGLAAVFER 402
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
10-339 |
3.60e-108 |
|
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: 321.35 E-value: 3.60e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 10 QNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEASLQDTI 89
Cdd:TIGR02430 64 RNVARMAALLAGLPVSVPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 90 I----LDGLTDAFYQYH-MGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKIDE 163
Cdd:TIGR02430 144 IgwrfINPLMKALYGVDsMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGePTVVDQDE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 164 HPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISA 243
Cdd:TIGR02430 224 HPRPETTLEGLAKLKPVVRPDGT--VTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 244 IKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKV--NLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:TIGR02430 302 TQKLLARAGLSIDQFDVIELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYA 381
|
330
....*....|....*...
gi 704582759 322 VAALCIGGGMGIAMCVER 339
Cdd:TIGR02430 382 LCTMCIGVGQGIALAIER 399
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-338 |
3.32e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 303.35 E-value: 3.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI-HMRAGVKMGE 82
Cdd:PRK06954 62 LPAGQGQAPARQAALGAGLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLpKARGGMRMGH 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 83 ASLQDTIILDGLTDAFYQYH-MGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKI 161
Cdd:PRK06954 142 GQVLDHMFLDGLEDAYDKGRlMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 162 DEHPRHgSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPI 241
Cdd:PRK06954 222 DEQPFK-ANPEKIPTLKPAFSKTGT--VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 242 SAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRG 321
Cdd:PRK06954 299 GAIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRG 378
|
330
....*....|....*..
gi 704582759 322 VAALCIGGGMGIAMCVE 338
Cdd:PRK06954 379 VASLCIGGGEATAMGIE 395
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
9-339 |
1.70e-100 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 301.54 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 9 GQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvihmragvKMGEASLQDT 88
Cdd:PRK09052 69 GLNVARIGALLAGLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP---------MMGNKPSMSP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 89 IILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKK-----GPIEVK--- 160
Cdd:PRK09052 140 AIFARDENVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatGEVDVKtrt 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 161 --IDEHPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMkkSEAA--RRGLMPLARIVSWAQTGIDPSIM 236
Cdd:PRK09052 220 vdLDEGPRADTSLEGLAKLKPVF--ANKGSVTAGNSSQTSDGAGAVILV--SEKAlkQFNLTPLARFVSFAVAGVPPEIM 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 237 GVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERT 316
Cdd:PRK09052 296 GIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRT 375
|
330 340
....*....|....*....|...
gi 704582759 317 GGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK09052 376 NLKYGMVTMCVGTGMGAAGIFER 398
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
6-334 |
1.67e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 298.97 E-value: 1.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 6 AGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAP---HVIhmRAGVKMGE 82
Cdd:PRK07661 61 AEQGLNMARNIGALAGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPmmgHVV--RPNPRLVE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 83 ASLQdtiildgltdafYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKK-----GPI 157
Cdd:PRK07661 139 AAPE------------YYMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennKLQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 158 EVKI----DEHPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDP 233
Cdd:PRK07661 207 EETItfsqDEGVRADTTLEILGKLRPAFNVKGS--VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 234 SIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHAL 313
Cdd:PRK07661 285 EVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEM 364
|
330 340
....*....|....*....|.
gi 704582759 314 ERTGGKRGVAALCIGGGMGIA 334
Cdd:PRK07661 365 KRRNEQFGIVTMCIGGGMGAA 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
14-339 |
9.88e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 292.01 E-value: 9.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 14 RQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvihmragvkMGEASLQDtIILDG 93
Cdd:PRK06445 74 RHPIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP----------MGDNPHIE-PNPKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 94 LTDAFYQ-------YHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKIDEHPR 166
Cdd:PRK06445 143 LTDPKYIeydlttgYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 167 HGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIKK 246
Cdd:PRK06445 223 PDTSLEKLAKLPPAFKPDGV--ITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 247 AIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAALC 326
Cdd:PRK06445 301 ALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLC 380
|
330
....*....|...
gi 704582759 327 IGGGMGIAMCVER 339
Cdd:PRK06445 381 VGGGQGGAVVLER 393
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
5-339 |
1.13e-95 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 291.28 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 5 PAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEAS 84
Cdd:PLN02287 104 PGSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 85 -LQDTIIldgltdafyqyHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPV---LVPSKKG---PI 157
Cdd:PLN02287 184 qAQDCLL-----------PMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGeekPI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 158 EVKIDEHPRHGSNLEMMGKLKPCFLTDgtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMG 237
Cdd:PLN02287 253 VISVDDGIRPNTTLADLAKLKPVFKKN--GTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 238 VGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTG 317
Cdd:PLN02287 331 IGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRG 410
|
330 340
....*....|....*....|....
gi 704582759 318 --GKRGVAALCIGGGMGIAMCVER 339
Cdd:PLN02287 411 kdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
10-339 |
3.58e-95 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 288.21 E-value: 3.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 10 QNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEASLQDTI 89
Cdd:PRK08131 64 RNVARNALLLAGLPVTVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 90 I-----LDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVP--SKKGPIEVKID 162
Cdd:PRK08131 144 IgarfpNPKIVAQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPqgRKLPPKLVAED 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 163 EHPRHGSNLEMMGKLKPCFltDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS 242
Cdd:PRK08131 224 EHPRPSSTVEALTKLKPLF--EG-GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 243 AIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLE--KINVQGGAIALGHPLGASGCRILVTLLHALERTGGKR 320
Cdd:PRK08131 301 AIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRY 380
|
330
....*....|....*....
gi 704582759 321 GVAALCIGGGMGIAMCVER 339
Cdd:PRK08131 381 AVVSLCIGVGQGLAMVIER 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
14-339 |
3.99e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 280.23 E-value: 3.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 14 RQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKaphvihmragVKMGeaSLQDTIILDG 93
Cdd:PRK08242 70 RTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSR----------VPMG--SDGGAWAMDP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 94 LTdAFYQYHM--GITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLvpSKKGPIEVKIDEHPRHGSNL 171
Cdd:PRK08242 138 ST-NFPTYFVpqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGLTILDHDEHMRPGTTM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 172 EMMGKLKPCFLT-------DGTGTV------------TAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGID 232
Cdd:PRK08242 215 ESLAKLKPSFAMmgemggfDAVALQkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 233 PSIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHA 312
Cdd:PRK08242 295 PTIMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDE 374
|
330 340
....*....|....*....|....*..
gi 704582759 313 LERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK08242 375 LERRGKRTALITLCVGGGMGIATIIER 401
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
5-339 |
5.43e-92 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 280.35 E-value: 5.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 5 PAG-AGQNPVRQASVAAGIPySVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPH------------- 70
Cdd:PRK07851 60 PGGeQGFNMARVVAVLLGYD-FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdslpdtknpl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 71 ----VIHMRAGVKMGEASLQDTIILDGLTDAFYQyhMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIV 146
Cdd:PRK07851 139 faeaQARTAARAEGGAEAWHDPREDGLLPDVYIA--MGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 147 PVLVPSkkGPIeVKIDEHPRHGSNLEMMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSW 226
Cdd:PRK07851 217 PVTLPD--GTV-VSTDDGPRAGTTYEKVSQLKPVFRPDGT--VTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVST 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 227 AQTGIDPSIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRIL 306
Cdd:PRK07851 292 GVSGLSPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARIT 371
|
330 340 350
....*....|....*....|....*....|...
gi 704582759 307 VTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK07851 372 TTLLNNLQTHDKTFGLETMCVGGGQGMAMVLER 404
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
9-339 |
5.67e-91 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 276.85 E-value: 5.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 9 GQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvihMRAGVKMGEASlqdt 88
Cdd:PRK08947 65 GFNIARNAALLAGIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP----MNHGVDFHPGL---- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 89 iildGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-PIEVKIDEHPRH 167
Cdd:PRK08947 137 ----SKNVAKAAGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 168 GSNLEMMGKLKPCFlTDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIKKA 247
Cdd:PRK08947 213 ETTVEALAALRPAF-DPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 248 IDKAGWTLEQVDLFEINEAFASLSLAIAKELK---VNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAA 324
Cdd:PRK08947 292 LKRAGLSISDIDVFELNEAFAAQSLPCLKDLGlldKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLAT 371
|
330
....*....|....*
gi 704582759 325 LCIGGGMGIAMCVER 339
Cdd:PRK08947 372 MCIGLGQGIATVFER 386
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-210 |
9.48e-88 |
|
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: 264.16 E-value: 9.48e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 6 AGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHV--IHMRAGVKMGEA 83
Cdd:pfam00108 56 AGEGQNPARQAALKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYAlpTDARSGLKHGDE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 84 SLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEVKIDE 163
Cdd:pfam00108 136 KKHDLLIPDGLTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 704582759 164 HPRHGSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKS 210
Cdd:pfam00108 216 GIRPPTTAEPLAKLKPAF--DKEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
11-339 |
4.73e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 266.96 E-value: 4.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEASlqDTII 90
Cdd:PRK07801 65 NIARTSWLAAGLPEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGFTS--PFAE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 91 LDGLTDAF-----YQYHmgiTAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLvpskkgpiEVKIDEHP 165
Cdd:PRK07801 143 SKGWLHRYgdqevSQFR---GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG--------GVTVDEGP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 166 RHgSNLEMMGKLKPcfLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIK 245
Cdd:PRK07801 212 RE-TSLEKMAGLKP--LVEG-GRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 246 KAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAAL 325
Cdd:PRK07801 288 YALEKTGLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTM 367
|
330
....*....|....
gi 704582759 326 CIGGGMGIAMCVER 339
Cdd:PRK07801 368 CEGGGTANVTIIER 381
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
11-339 |
1.76e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 259.18 E-value: 1.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI------------------ 72
Cdd:PRK08170 65 NIARVVALRLGCGEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFsekmvrwlagwyaaksig 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 73 -HMRAGVKMGEASLQDTI-ILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFtKEIVPVLv 150
Cdd:PRK08170 145 qKLAALGKLRPSYLAPVIgLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPLF- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 151 pSKKGPIEVKiDEHPRHGSNLEMMGKLKPCFlTDGTGTVTAANASGMNDGAAAVILmkKSEAA--RRGLMPLARIVSWAQ 228
Cdd:PRK08170 223 -DRDGKFYDH-DDGVRPDSSMEKLAKLKPFF-DRPYGRVTAGNSSQITDGACWLLL--ASEEAvkKYGLPPLGRIVDSQW 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 229 TGIDPSIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELK-----------------VNLEKINVQGGA 291
Cdd:PRK08170 298 AALDPSQMGLGPVHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGA 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 704582759 292 IALGHPLGASGCRILVTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK08170 378 IALGHPVGASGARIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
4-338 |
4.58e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 251.85 E-value: 4.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVI--HMRAGVKM- 80
Cdd:PRK06366 57 IQAGVGQNPAGQAAYHAGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLpsDLRWGPKHl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 81 --GEASLQDTIILDGLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLvpskkgpiE 158
Cdd:PRK06366 137 lhKNYKIDDAMLVDGLIDAFYFEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------D 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 159 VKIDEHPRHgSNLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGV 238
Cdd:PRK06366 209 LDRDEGIRK-TTMEDLAKLPPAF--DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 239 GPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGG 318
Cdd:PRK06366 286 APIPATRKLLEKQNKSIDYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHM 365
|
330 340
....*....|....*....|
gi 704582759 319 KRGVAALCIGGGMGIAMCVE 338
Cdd:PRK06366 366 KTGLATLCHGGGGAHTLTLE 385
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
5-338 |
6.52e-80 |
|
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: 248.95 E-value: 6.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 5 PAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSkaphvihmragvkmgeas 84
Cdd:cd00826 55 GAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME------------------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 85 lqdtiildgltdafyqyhmgITAENVANQWQV--------SRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGP 156
Cdd:cd00826 117 --------------------TSAENNAKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 157 IEVKIDEHPRHGS--NLEMMGKLKPCFltDGTGTVTAANASGMNDGAAAVILMKKSEAA-------RRGLMPLARIVSWA 227
Cdd:cd00826 177 IHSDADEYIQFGDeaSLDEIAKLRPAF--DKEDFLTAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 228 QTGIDPS----IMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEK------------------I 285
Cdd:cd00826 255 STFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiI 334
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 704582759 286 NVQGGAIALGHPLGASGCRILVTLLHALERTGGKR-----GVAALCIGGGMGIAMCVE 338
Cdd:cd00826 335 NPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
9-339 |
2.35e-78 |
|
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: 244.47 E-value: 2.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 9 GQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvihMRAGVKMGEASLQDT 88
Cdd:TIGR02445 63 GFNIARNAALLAQIPHTSAAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP----MMHGVDFHPGMSLHV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 89 IILDGLtdafyqyhMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEV-KIDEHPRH 167
Cdd:TIGR02445 139 AKAAGM--------MGLTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQfDYDEVIRP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 168 GSNLEMMGKLKPCFLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIKKA 247
Cdd:TIGR02445 211 ETTVESLAALRPAFDPKN-GTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 248 IDKAGWTLEQVDLFEINEAFASLSLAIAKELKV---NLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAA 324
Cdd:TIGR02445 290 LKRAGLSISDIDVFELNEAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLAT 369
|
330
....*....|....*
gi 704582759 325 LCIGGGMGIAMCVER 339
Cdd:TIGR02445 370 MCIGLGQGIATVFER 384
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
11-339 |
1.23e-75 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 237.70 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGVKMGEASLQDTII 90
Cdd:PRK06504 65 NVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 91 LDGLTDAFYQYHMGitAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKGPIEV-KIDEHPRHGS 169
Cdd:PRK06504 145 EERYPGIQFSQFTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 170 NLEMMGKLKPcfLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIKKAID 249
Cdd:PRK06504 223 TLEGIAGVKL--IAEG-GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 250 KAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAALCIGG 329
Cdd:PRK06504 300 KAGMKIDDIDLYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGG 379
|
330
....*....|
gi 704582759 330 GMGIAMCVER 339
Cdd:PRK06504 380 GMANVTIVER 389
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
7-338 |
3.19e-74 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 233.12 E-value: 3.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 7 GAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAGvkmgeaslQ 86
Cdd:PRK06690 54 GPGGNVARLSALEAGLGLHIPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFS--------P 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 87 DTIildGLTDafyqyhMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPvlvpskkgpIEVKIDEHPR 166
Cdd:PRK06690 126 ETI---GDPD------MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILS---------FNGLLDESIK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 167 HGSNLE-MMGKLKPCFLTDGTgtVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPISAIK 245
Cdd:PRK06690 188 KEMNYErIIKRTKPAFLHNGT--VTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 246 KAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAAL 325
Cdd:PRK06690 266 KLLNEMNMKVEDIDYFEINEAFASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATL 345
|
330
....*....|...
gi 704582759 326 CIGGGMGIAMCVE 338
Cdd:PRK06690 346 GIGGGIGLALLFE 358
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
5-334 |
1.59e-72 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 229.66 E-value: 1.59e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 5 PAGA-GQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHvihmragvKMGEA 83
Cdd:PRK07108 59 PEGAtGANIARQIALRAGLPVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN--------EMNRH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 84 SLQDTIILDGLTDAFYQyhMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSKKG-------- 155
Cdd:PRK07108 131 MLREGWLVEHKPEIYWS--MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVAdkatgrlf 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 156 --PIEVKIDEHPRHGSNLEMMGKLKPCFltdGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDP 233
Cdd:PRK07108 209 tkEVTVSADEGIRPDTTLEGVSKIRSAL---PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 234 SIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHAL 313
Cdd:PRK07108 286 DEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEG 365
|
330 340
....*....|....*....|.
gi 704582759 314 ERTGGKRGVAALCIGGGMGIA 334
Cdd:PRK07108 366 KRRGAKYVVVTMCIGGGQGAA 386
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
14-339 |
6.66e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 228.89 E-value: 6.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 14 RQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMS--KAPHVIHMRAGVK---MGEASLQdt 88
Cdd:PRK06025 71 RMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytAAMAAEDMAAGKPplgMGSGNLR-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 89 iildgLTDAFYQYHMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVPSkkGPIEVKIDEHPRHG 168
Cdd:PRK06025 149 -----LRALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDD--GSVALDHEEFPRPQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 169 SNLEMMGKLKPCFLT------DGTGTVT------------------AANASGMNDGAAAVILMKKSEAARRGLMPLARIV 224
Cdd:PRK06025 222 TTAEGLAALKPAFTAiadyplDDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 225 SWAQTGIDPSIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCR 304
Cdd:PRK06025 302 AMANMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSI 381
|
330 340 350
....*....|....*....|....*....|....*
gi 704582759 305 ILVTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK06025 382 LIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
11-339 |
7.19e-71 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 225.37 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvihMRAGVKMGEASLQ-DTI 89
Cdd:PRK07850 65 NITRTAWLHAGLPYHVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP----LGANAGPGRGLPRpDSW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 90 ILDgLTDAFyqyhmgITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIVPVLVP---SKKGP----IEVKID 162
Cdd:PRK07850 141 DID-MPNQF------EAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldEEGQPtgetRLVTRD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 163 EHPRHgSNLEMMGKLKPcfLTDGtGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS 242
Cdd:PRK07850 214 QGLRD-TTMEGLAGLKP--VLEG-GIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 243 AIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGV 322
Cdd:PRK07850 290 ATAKVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTAL 369
|
330
....*....|....*..
gi 704582759 323 AALCIGGGMGIAMCVER 339
Cdd:PRK07850 370 ITMCAGGALSTGTIIER 386
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-339 |
4.95e-66 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 214.08 E-value: 4.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 4 VPAGAGQNPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPhvIHM-----RAGV 78
Cdd:PRK08963 60 VQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLP--IGVskklaRALV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 79 KMGEA-SLQDTI-ILDGLT--------DAFYQY----HMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKE 144
Cdd:PRK08963 138 DLNKArTLGQRLkLFSRLRlrdllpvpPAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 145 IVPVLVPSKKGPIEVkiDEHPRHGSNLEMMGKLKPCFLTDgTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIV 224
Cdd:PRK08963 218 VMTAHVPPYKQPLEE--DNNIRGDSTLEDYAKLRPAFDRK-HGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 225 SWAQTGIDP-SIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLA---------IAKEL--------KVNLEKIN 286
Cdd:PRK08963 295 SYAFAAIDVwQDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserFAREKlgrsqaigEVDMSKFN 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 704582759 287 VQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK08963 375 VLGGSIAYGHPFAATGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
217-339 |
5.07e-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: 193.63 E-value: 5.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 217 LMPLARIVSWAQTGIDPSIMGVGPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLEKINVQGGAIALGH 296
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 704582759 297 PLGASGCRILVTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
11-339 |
2.40e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 175.86 E-value: 2.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 11 NPVRQASVAAGIPYSVPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIH---MRAGVKMGEA-SLQ 86
Cdd:PRK09268 69 NLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNeglRKILLELNRAkTTG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 87 DTIIL--------------------DGLTdafyqyhMGITAENVANQWQVSRGEQDQLALQSQNRAEAAQKAGYFTKEIV 146
Cdd:PRK09268 149 DRLKAlgklrpkhlapeiprngeprTGLS-------MGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLIT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 147 PVLVPSKkgpievkiDEHPRHGSNLEMMGKLKPCFLTDGTGTVTAANASGMNDGAAAVILMKKSEAARRGLMPLARIVsW 226
Cdd:PRK09268 222 PFLGLTR--------DNNLRPDSSLEKLAKLKPVFGKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLV-D 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 227 AQT-------GIDPSIMGvgPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAK----------EL-------KVNL 282
Cdd:PRK09268 293 AETaavdfvhGKEGLLMA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLgldaplgSIDR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 704582759 283 EKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVAALCIGGGMGIAMCVER 339
Cdd:PRK09268 371 SKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
191-337 |
8.82e-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: 98.29 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 191 AANASGMNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGIDPS----IMGVGPISAIKKAIDKAGWTLEQVDLFEINEA 266
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 267 FASLSLAIAKEL---KVNLEKINVQGGAIALGHPLGASGCRILVTLLHALERTGGKR-------GVAALCIGGGMGIAMC 336
Cdd:cd00327 174 GTPIGDAVELALgldPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 704582759 337 V 337
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
195-332 |
7.08e-10 |
|
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: 59.58 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 195 SGMNDGAAAVILMKKsEAARRGLMPLARIVSWAQTGIDPSIMGVGPIS-------AIKKAIDKAGWTLEQVDLFEINEAF 267
Cdd:cd00829 202 CPVSDGAAAVVLASE-ERARELTDRPVWILGVGAASDTPSLSERDDFLsldaarlAARRAYKMAGITPDDIDVAELYDCF 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 268 ASLSLAIAKEL---------KVNLE---------KINVQGGAIALGHPLGASGCRILVTLLHALERTGGKRGVA----AL 325
Cdd:cd00829 281 TIAELLALEDLgfcekgeggKLVREgdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPgarvGL 360
|
....*..
gi 704582759 326 CIGGGMG 332
Cdd:cd00829 361 AHNIGGT 367
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
178-329 |
5.08e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 53.92 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 178 KPCFLTDGT------GTVTAANASGMNDGAAAVILMKKSEAAR-RGLMPLARIVSWA--------QTGIDPSIMG--VGP 240
Cdd:PRK06289 197 DEATNDDDAtnpvveGRLRRQDCSQVTDGGAGVVLASDAYLRDyADARPIPRIKGWGhrtaplglEQKLDRSAGDpyVLP 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 241 --ISAIKKAIDKAGWTLEQVDLFEINEAF-ASLSLAI--------AKELKVnLEK----------INVQGGAIALGHPLG 299
Cdd:PRK06289 277 hvRQAVLDAYRRAGVGLDDLDGFEVHDCFtPSEYLAIdhigltgpGESWKA-IENgeiaiggrlpINPSGGLIGGGHPVG 355
|
170 180 190
....*....|....*....|....*....|....*.
gi 704582759 300 ASGCRILVTLLHALERT------GGKRGVAALCIGG 329
Cdd:PRK06289 356 ASGVRMLLDAAKQVTGTagdyqvEGAKTFGTLNIGG 391
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
197-302 |
8.56e-08 |
|
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: 53.31 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 197 MNDGAAAVILMKKSEAARRGLMPLARIVSWAQTG-----IDPSIMGVGPISAIKKAIDKAGWTLEQVDLfeIN------- 264
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahgtstp 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 704582759 265 -------EAFASLSLAIAKELKVNLEKinvqgGAIalGHPLGASG 302
Cdd:cd00834 307 lndaaesKAIKRVFGEHAKKVPVSSTK-----SMT--GHLLGAAG 344
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
26-334 |
4.58e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 51.05 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 26 VPAWSCQMICGSGLKAVCLGAQSILTGDSSIVVAGGMESMSKAPHVIHMRAgvkMGEASlqdtiildgltDAFYQYHMGI 105
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEA---IARAG-----------DYEWEEFFGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 106 T----AENVANQWQVSRG-EQDQLALQSQNRAEAAQKAGY--FTKEI--------VPVLVPSKkgpievkidehprhgsn 170
Cdd:PRK06064 142 TfpglYALIARRYMHKYGtTEEDLALVAVKNHYNGSKNPYaqFQKEItveqvlnsPPVADPLK----------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 171 lemmgklkpcfLTDgtgtvtaanASGMNDGAAAVILMKKsEAARRGLMPLARIVSWAQ-------------TGIDPSIMg 237
Cdd:PRK06064 205 -----------LLD---------CSPITDGAAAVILASE-EKAKEYTDTPVWIKASGQasdtialhdrkdfTTLDAAVV- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 238 vgpisAIKKAIDKAGWTLEQVDLFE------INEAFASLSLAIAKE---LKVNLEK---------INVQGGAIALGHPLG 299
Cdd:PRK06064 263 -----AAEKAYKMAGIEPKDIDVAEvhdcftIAEILAYEDLGFAKKgegGKLAREGqtyiggdipVNPSGGLKAKGHPVG 337
|
330 340 350
....*....|....*....|....*....|....*..
gi 704582759 300 ASGCRILVTLLHAL--ERTGGKRGVaalcIGGGMGIA 334
Cdd:PRK06064 338 ATGVSQAVEIVWQLrgEAEKGRQQV----IGAGYGLT 370
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
192-302 |
3.04e-05 |
|
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: 45.47 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 192 ANASGMN--DGAAAVILMKKSEAARRGLMPLARIVSWA-------QTGIDPSimGVGPISAIKKAIDKAGWTLEQVDLfe 262
Cdd:COG0304 222 KDRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDIDY-- 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 704582759 263 IN------------EAfaslsLAIAKELKVNLEKINVQggAI--ALGHPLGASG 302
Cdd:COG0304 298 INahgtstplgdaaET-----KAIKRVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
199-314 |
2.07e-04 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 42.62 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 199 DGAAAVILMKKSEAARRGLMPLARIVSWAQTgIDPSIMGV------GPISAIKKAIDKAGWTLEQVDLFEINEafASLSL 272
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAAT-IDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAHG--TGTPI 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 704582759 273 AIAKELKVNLE-----KINVQGGAIALGHPLGASGCRILVTLLHALE 314
Cdd:cd00825 238 GDVKELKLLRSefgdkSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
200-259 |
2.36e-04 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 42.71 E-value: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 704582759 200 GAAAVILMKKSEAARRGLMPLARIVSWAQT-----GIDPSImgVGPISAIKKAIDKAGWTLEQVD 259
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDID 302
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
200-315 |
6.62e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 41.27 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 200 GAAAVILMKKSEAARRGLMPLARIVSWA--QTGIDPSIMGVGPI--SAIKKAIDKAGWTLEQVDLfeINEAFASLSLAIA 275
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTAstTDGAGRSVPAGGKGiaRAIRTALAKAGLSLDDLDV--ISAHGTSTPANDV 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 704582759 276 KELKVNLEKINVQGGAIAL-------GHPLGASGCRILVTLLHALER 315
Cdd:cd00828 310 AESRAIAEVAGALGAPLPVtaqkalfGHSKGAAGALQLIGALQSLEH 356
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
197-302 |
2.52e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.39 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 197 MNDGAAAVILMKKSEAARRGLMPLARIVSWAQTGiD------PSIMGVGPISAIKKAIDKAGWTLEQVD----------L 260
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTG-DayhmtaPAPDGEGAARAMKLALKDAGINPEDIDyinahgtstpA 308
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 704582759 261 FEINEAFA--SLSLAIAKELKVNLEKinvqggaIALGHPLGASG 302
Cdd:PRK07314 309 GDKAETQAikRVFGEHAYKVAVSSTK-------SMTGHLLGAAG 345
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
229-283 |
2.92e-03 |
|
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: 38.73 E-value: 2.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 704582759 229 TGIDPSIMGV-GPISAIKKAIDKAGWTLEQVDLFEINEAFASLSLAIAKELKVNLE 283
Cdd:cd24030 36 TGIKGTLQNVpGIIKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELGIPVE 91
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
195-320 |
3.13e-03 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 39.24 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 704582759 195 SGMNDGAAAVILMKKSEAARRGLMPLARI----------VSWAQTGIDPSIMGVGPISAiKKAIDKAGWT--LEQVDLFE 262
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVkalqlavsngWELQYNGWDGSYFPTTRIAA-RKAYREAGITdpREELSMAE 292
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 704582759 263 INEAFASLSLAIAKELKVNLE------------------KINVQGGAIALGHPLGASGCRILVTL-LHALERTGGKR 320
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRMLYEMyLQLLGRAGERQ 369
|
|
| |
