|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-380 |
1.48e-178 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 500.91 E-value: 1.48e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 1 MNFELTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKIN 80
Cdd:COG1960 1 MDFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 81 SSVGIAYSVcTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNG 160
Cdd:COG1960 81 ASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 161 PLADYYMVVALTNPELKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLD 240
Cdd:COG1960 160 PVADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 241 GGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAK 320
Cdd:COG1960 240 AGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 321 MVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-379 |
3.29e-178 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 499.87 E-value: 3.29e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 7 PQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGIA 86
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 87 YSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLADYY 166
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 167 MVVALTNPELKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIGV 246
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 247 AAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCTDA 326
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 496558494 327 AMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFR 379
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
7-373 |
1.41e-127 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 369.69 E-value: 1.41e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 7 PQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLpfpkeyggqggdylsyvlaleeiskinssvgia 86
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLLGAAL--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 87 ysvctslysgaLINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLADYY 166
Cdd:cd00567 48 -----------LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 167 MVVALTNPE-LKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIG 245
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 246 VAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKS-YSVPAAKAKMVCT 324
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFAT 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496558494 325 DAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVI 373
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
5-379 |
5.17e-121 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 354.80 E-value: 5.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 5 LTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVG 84
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 85 IAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLAD 164
Cdd:cd01156 82 LSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDAD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 165 YYMVVALTNPELKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRI 244
Cdd:cd01156 162 TLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCT 324
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 496558494 325 DAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFR 379
Cdd:cd01156 322 EKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
7-377 |
8.64e-113 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 333.70 E-value: 8.64e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 7 PQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSvGIA 86
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 87 YSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLADYY 166
Cdd:cd01160 80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 167 MVVALTNPELKTK-GLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIG 245
Cdd:cd01160 160 IVVARTGGEARGAgGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 246 VAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCTD 325
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 496558494 326 AAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNM 377
Cdd:cd01160 320 LQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
5-380 |
1.59e-111 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 330.56 E-value: 1.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 5 LTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVG 84
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 85 iAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLAD 164
Cdd:cd01162 81 -AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 165 YYMVVALTNPElKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRI 244
Cdd:cd01162 160 VYVVMARTGGE-GPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVP-AAKAKMVC 323
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKlCAMAKRFA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496558494 324 TDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:cd01162 319 TDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
32-380 |
4.59e-105 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 315.18 E-value: 4.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 32 DAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLaLEEISKINSSVGIAYSVCTSLYSGALINDGNEEQKKKYL 111
Cdd:cd01161 52 DQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYAR-LAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 112 PEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWN--GKEYILNGLKCFITNGPLADYYMVVALTNPELKT----KGLTAFI 185
Cdd:cd01161 131 PKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATgsvkDKITAFI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 186 VEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAFNYL 265
Cdd:cd01161 211 VERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 266 KEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAAT--DKQEGKSYSVPAAKAKMVCTDAAMHVATEAVQMLGGNGY 343
Cdd:cd01161 291 NNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGnmDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGF 370
|
330 340 350
....*....|....*....|....*....|....*..
gi 496558494 344 MKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:cd01161 371 MREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQH 407
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
5-372 |
3.23e-102 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 307.36 E-value: 3.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 5 LTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPfPKEYGGQGGDYLSYVLALEEISKINSSVG 84
Cdd:cd01151 13 LTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 85 IAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLAD 164
Cdd:cd01151 92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIAD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 165 YYMVVALTNPELKTKGltaFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLgEEGKGFAVAMKDLDGGRI 244
Cdd:cd01151 172 VFVVWARNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCT 324
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNC 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 496558494 325 DAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLV 372
Cdd:cd01151 328 GKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALI 375
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
5-380 |
1.46e-100 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 302.97 E-value: 1.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 5 LTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVG 84
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 85 IAYSVcTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLAD 164
Cdd:cd01157 81 TAIEA-NSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 165 YYMVVALTNPELKT---KGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDG 241
Cdd:cd01157 160 WYFLLARSDPDPKCpasKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 242 GRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKM 321
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 496558494 322 VCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
9-380 |
9.08e-93 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 283.69 E-value: 9.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 9 QKAVQQSARQFAQTVLQETVLEDDAAGRFPEEA--YKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGIA 86
Cdd:PLN02519 30 QLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 87 YSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLADYY 166
Cdd:PLN02519 110 YGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 167 MVVALTNPELKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIGV 246
Cdd:PLN02519 190 VVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 247 AAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCTDA 326
Cdd:PLN02519 270 AAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAER 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496558494 327 AMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:PLN02519 350 ATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
3-379 |
6.96e-79 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 248.31 E-value: 6.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 3 FELTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSS 82
Cdd:PTZ00461 35 YNPTPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 83 VGIAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKE-YILNGLKCFITNGP 161
Cdd:PTZ00461 115 FCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 162 LADYYMVVALTNPELktkglTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKDLDG 241
Cdd:PTZ00461 195 VADVFLIYAKVDGKI-----TAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLEL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 242 GRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKM 321
Cdd:PTZ00461 270 ERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496558494 322 VCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFR 379
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLK 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-368 |
2.82e-73 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 232.70 E-value: 2.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 1 MNFELTPQQKAVQQSARQF-AQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKI 79
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELiTRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 80 NssvGIAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGsFCL--TEPDAGSDAAGCKTTAIW-NGKEYiLNGLKCF 156
Cdd:PRK12341 81 G---APAFLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPA-YALalTEPGAGSDNNSATTTYTRkNGKVY-LNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 157 ITNGPLADYYMVVAL-TNPELKTKGLTAFIVEREWEGVSIGKIEdKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVA 235
Cdd:PRK12341 156 ITGAKEYPYMLVLARdPQPKDPKKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 236 MKDLDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVP 315
Cdd:PRK12341 235 MYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTS 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 496558494 316 AAKAKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEI 368
Cdd:PRK12341 315 AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
31-369 |
1.55e-66 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 216.10 E-value: 1.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 31 DDAAGRFP---EEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKinssvGIAYSVCTSLYSGA---LINDGNE 104
Cdd:cd01153 28 DDGRVVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSR-----GDAPLMYASGTQGAaatLLAHGTE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 105 EQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGK-EYILNGLKCFITNGP--LADYYMVVALTNPE---LKT 178
Cdd:cd01153 103 AQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEhdMSENIVHLVLARSEgapPGV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 179 KGLTAFIVER-----EWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPkenMLGEEGKGFAVAMKDLDGGRIGVAAQGLGI 253
Cdd:cd01153 183 KGLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 254 AKGAYDIAFNYLKEREQFGKPLYK------------NQYLAFKMAELETEIEMAQYML------YKAATDKQEGKSYS-- 313
Cdd:cd01153 260 AEAAYLNALAYAKERKQGGDLIKAapavtiihhpdvRRSLMTQKAYAEGSRALDLYTAtvqdlaERKATEGEDRKALSal 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 314 ----VPAAKAkmVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQ 369
Cdd:cd01153 340 adllTPVVKG--FGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQ 397
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-380 |
5.94e-60 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 198.13 E-value: 5.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 1 MNFELTPQQKAVQQSARQFAQTVLQETVL-EDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKI 79
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASENWEAYFaECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 80 NSSVGIAYSVCTSLysGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTT-AIWNGKEYiLNGLKCFIT 158
Cdd:PRK03354 81 GAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTyTRRNGKVY-LNGSKCFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 159 NGPLADYYMVVALTNPELKTKGLTAFIVEREWEGVSIGKIEdKCGIRCAQVSEVIFDNVRVPKENMLGEEGKGFAVAMKD 238
Cdd:PRK03354 158 SSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 239 LDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAK 318
Cdd:PRK03354 237 FDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAM 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558494 319 AKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:PRK03354 317 CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
5-372 |
5.10e-56 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 188.91 E-value: 5.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 5 LTPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFpKEYGGQGGDYLSYVLALEEISKINSSVG 84
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 85 IAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGKEYILNGLKCFITNGPLAD 164
Cdd:PLN02526 108 TFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFAD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 165 YYMVVALTNpelKTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLgEEGKGFAVAMKDLDGGRI 244
Cdd:PLN02526 188 VLVIFARNT---TTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYSVPAAKAKMVCT 324
Cdd:PLN02526 264 MVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWIT 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 496558494 325 DAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLV 372
Cdd:PLN02526 344 KKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALV 391
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-373 |
3.03e-54 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 183.32 E-value: 3.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 7 PQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAY-----KKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISK--- 78
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLPPELREESALGYREGREDrrrwqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAaga 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 79 --INSSVGIAYSVCTslysgaLINDGNEEQKKKYLPEVLSGKKMgsFCL--TEPDAGSDAAGCKTTAIWNGKEYILNGLK 154
Cdd:cd01152 81 pvPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPILSGEEI--WCQgfSEPGAGSDLAGLRTRAVRDGDDWVVNGQK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 155 CFITNGPLADYYMVVALTNPEL-KTKGLTAFIVEREWEGVSIGKIEDKCGirCAQVSEVIFDNVRVPKENMLGEEGKGFA 233
Cdd:cd01152 153 IWTSGAHYADWAWLLVRTDPEApKHRGISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 234 VAMKDLDGGRIGVAaqglGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEGKSYS 313
Cdd:cd01152 231 VAMTTLNFERVSIG----GSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496558494 314 VPAAKAKMVCTDAAMHVATEAVQMLG------GNGYMKEYH--VERMLRDAKITQIYEGTNEIQKLVI 373
Cdd:cd01152 307 AEASIAKLFGSELAQELAELALELLGtaallrDPAPGAELAgrWEADYLRSRATTIYGGTSEIQRNII 374
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
229-374 |
4.01e-51 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 167.82 E-value: 4.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 229 GKGFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQE 308
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496558494 309 GKSYSVPAAKAKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVIS 374
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
20-368 |
2.39e-43 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 154.86 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 20 AQTVLQETVLEDDAAGRFPEEAYKKMGEM----GFVGLPFPKEYGGQGGDYLSYVLALEEISKinSSVGIAYSVCTSLYS 95
Cdd:cd01155 21 AEQEFLEYYAEGGDRWWTPPPIIEKLKAKakaeGLWNLFLPEVSGLSGLTNLEYAYLAEETGR--SFFAPEVFNCQAPDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 96 G---ALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPD-AGSDAAGCKTTAIWNGKEYILNGLKCFITNG--PLADYYMVV 169
Cdd:cd01155 99 GnmeVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAgdPRCKIAIVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 170 ALTNPELKTKGL--TAFIVEREWEGVSIgkiedkcgIRCAQV----------SEVIFDNVRVPKENMLGEEGKGFAVAMK 237
Cdd:cd01155 179 GRTDPDGAPRHRqqSMILVPMDTPGVTI--------IRPLSVfgyddaphghAEITFDNVRVPASNLILGEGRGFEIAQG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 238 DLDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAA--TDKQEGKSYSVP 315
Cdd:cd01155 251 RLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAhmIDTVGNKAARKE 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 496558494 316 AAKAKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEI 368
Cdd:cd01155 331 IAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEV 383
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
96-371 |
2.78e-43 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 155.22 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 96 GALINDGNEEQKKKYLPEVLSGKKMGSFC---LTEPDAGSDAAGCKTTAIWN-GKEYILNGLKCFiTNGPLADYYMVVAl 171
Cdd:cd01154 121 YALRKYGPEELKQYLPGLLSDRYKTGLLGgtwMTEKQGGSDLGANETTAERSgGGVYRLNGHKWF-ASAPLADAALVLA- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 172 tNPE---LKTKGLTAFIVEREWE-----GVSIGKIEDKCGIRCAQVSEVIFDNVrvpKENMLGEEGKGFAVAMKDLDGGR 243
Cdd:cd01154 199 -RPEgapAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 244 IGVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAA-------TDKQEGKSYS--- 313
Cdd:cd01154 275 LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAArafdraaADKPVEAHMArla 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 496558494 314 VPAAKaKMVCTDAaMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKL 371
Cdd:cd01154 355 TPVAK-LIACKRA-APVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-118 |
3.12e-42 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 143.37 E-value: 3.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 6 TPQQKAVQQSARQFAQTVLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGI 85
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 496558494 86 AYSVCTSLYSGALINDGNEEQKKKYLPEVLSGK 118
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
39-371 |
1.51e-35 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 137.31 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 39 EEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGIaYSVCTSLYSGALINDGNEEQKKKYLPEVLSGK 118
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSM-YPGLSIGAANTLMAWGSEEQKEQYLTKLVSGE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 119 KMGSFCLTEPDAGSDAAGCKTTAIWNGK-EYILNGLKCFITNGP--LAD--YYMVVA-LTNPELKTKGLTAFIVEREW-- 190
Cdd:PTZ00456 181 WSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdLTEniVHIVLArLPNSLPTTKGLSLFLVPRHVvk 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 191 --------EGVSIGKIEDKCGIRCAQVSEVIFDNvrvPKENMLGEEGKGFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAF 262
Cdd:PTZ00456 261 pdgsletaKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNAL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 263 NYLKER------------EQFGKPLYKN----QYLAFKMAELE----TEIEMAQYM-LYKAATDKQEGKS------YSVP 315
Cdd:PTZ00456 338 RYARERrsmralsgtkepEKPADRIICHanvrQNILFAKAVAEggraLLLDVGRLLdIHAAAKDAATREAldheigFYTP 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496558494 316 AAKAKMvcTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKL 371
Cdd:PTZ00456 418 IAKGCL--TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQAL 471
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
122-215 |
2.37e-27 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 103.51 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 122 SFCLTEPDAGSDAAGCKTTAI-WNGKEYILNGLKCFITNGPLADYYMVVALTNPELKTKGLTAFIVEREWEGVSIGKIED 200
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAAdGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 496558494 201 KCGIRCAQVSEVIFD 215
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
79-366 |
6.12e-27 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 112.42 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 79 INSSVGIAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIW--NGKEYILN----- 151
Cdd:cd01150 94 YDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYdpLTQEFVINtpdft 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 152 GLKCFITN-GPLADYYMVVALTNPELKTKGLTAFIVE-REWE------GVSIGKIEDKCGIRCAQVSEVIFDNVRVPKEN 223
Cdd:cd01150 174 ATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPiRDPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPREN 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 224 MLG----------------EEGKGFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQFGKPL---------YKN 278
Cdd:cd01150 254 LLNrfgdvspdgtyvspfkDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPsdpevqildYQL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 279 Q------YLA---------FKMAELETEIEMAQYMlykaaTDKQEGKSYSVPAAKAKMVCTDAAMHVATEAVQMLGGNGY 343
Cdd:cd01150 334 QqyrlfpQLAaayafhfaaKSLVEMYHEIIKELLQ-----GNSELLAELHALSAGLKAVATWTAAQGIQECREACGGHGY 408
|
330 340
....*....|....*....|...
gi 496558494 344 MKEYHVERMLRDAKITQIYEGTN 366
Cdd:cd01150 409 LAMNRLPTLRDDNDPFCTYEGDN 431
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
23-357 |
1.91e-21 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 94.70 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 23 VLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGIAYSVcTSLYSGALINDG 102
Cdd:cd01163 9 RIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRA-HFGFVEALLLAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 103 NEEQKKKYLPEVLSGKKMGSfclTEPDAGSDAAGCKTTAIWNGKE-YILNGLKCFITNGPLADYYMVVALtNPELKtkgL 181
Cdd:cd01163 88 PEQFRKRWFGRVLNGWIFGN---AVSERGSVRPGTFLTATVRDGGgYVLNGKKFYSTGALFSDWVTVSAL-DEEGK---L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 182 TAFIVEREWEGVSIgkIEDKCGI--RCAQVSEVIFDNVRVPKENMLGEEGKGFAVAmkdLDGG--RIGVAAQGLGIAKGA 257
Cdd:cd01163 161 VFAAVPTDRPGITV--VDDWDGFgqRLTASGTVTFDNVRVEPDEVLPRPNAPDRGT---LLTAiyQLVLAAVLAGIARAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 258 YDIAFNYLKEReqfGKP-LYKNQ-------YLAFKMAELETEIEMAQYMLYKAA------------TDKQEGKSYSVPAA 317
Cdd:cd01163 236 LDDAVAYVRSR---TRPwIHSGAesarddpYVQQVVGDLAARLHAAEALVLQAAraldaaaaagtaLTAEARGEAALAVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 496558494 318 KAKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAK 357
Cdd:cd01163 313 AAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
65-380 |
3.26e-21 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 95.31 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 65 DYLSYVLALEEISKINSSVGIAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWN 144
Cdd:PLN02636 119 DPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 145 --GKEYILN-----GLKCFITN----GPLADYYMVVALTNPELK---TKGLTAFIVE-REWE------GVSIGKIEDKCG 203
Cdd:PLN02636 199 plTDEFVINtpndgAIKWWIGNaavhGKFATVFARLKLPTHDSKgvsDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 204 IRCAQVSEVIFDNVRVPKENMLGEEG----------------KGFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAFNYLKE 267
Cdd:PLN02636 279 LNGVDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 268 REQFGKPL--------YKNQY----------LAFKMAeleTEIEMAQYMLYKAATDKQ-EGKSYSVPAAKAKMVC--TDA 326
Cdd:PLN02636 359 RQQFGPPKqpeisildYQSQQhklmpmlastYAFHFA---TEYLVERYSEMKKTHDDQlVADVHALSAGLKAYITsyTAK 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496558494 327 AMHVATEAVqmlGGNGYMKEYHVERMLRDAKITQIYEGTNEIQKLVISGNMFRK 380
Cdd:PLN02636 436 ALSTCREAC---GGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQ 486
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
245-367 |
2.32e-20 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 85.86 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQ--FGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQE----GKSYSVP--- 315
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAaaaaGKPVTPAlra 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 496558494 316 -AAKAKMVCTDAAMHVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNE 367
Cdd:pfam08028 81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
98-368 |
6.80e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.40 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 98 LINDGNEEQKKKYLPEVLSGKKMGSFCLTEPD-AGSDAAGCKTTAIWNGKEYILNGLKCFiTNG---PLADYYMVVALTN 173
Cdd:PLN02876 529 LLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 174 PEL-KTKGLTAFIVEREWEGVSIGKIEDKCGIRCAQV--SEVIFDNVRVPKENMLGEEGKGFAVAMKDLDGGRIGVAAQG 250
Cdd:PLN02876 608 FNApKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAPHghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRL 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 251 LGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAELETEIEMAQYMLYKAA--TDKQEGKSYSVPAAKAKMVCTDAAM 328
Cdd:PLN02876 688 IGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAAdqLDRLGNKKARGIIAMAKVAAPNMAL 767
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 496558494 329 HVATEAVQMLGGNGYMKEYHVERMLRDAKITQIYEGTNEI 368
Cdd:PLN02876 768 KVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
38-344 |
1.64e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 90.40 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 38 PEEAYKKMGEMGFVGLPFPKEYGGQGgdYLSYvlALEEI-SKINS-SVGIAYSVCT--SLYSGALIND-GNEEQKKKYLP 112
Cdd:PRK13026 110 PPEVWDYLKKEGFFALIIPKEYGGKG--FSAY--ANSTIvSKIATrSVSAAVTVMVpnSLGPGELLTHyGTQEQKDYWLP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 113 EVLSGKKMGSFCLTEPDAGSDAAGCKTTAI-----WNGKEYI---LNGLKCFITNGPLADyymVVALT----NPE--LKT 178
Cdd:PRK13026 186 RLADGTEIPCFALTGPEAGSDAGAIPDTGIvcrgeFEGEEVLglrLTWDKRYITLAPVAT---VLGLAfklrDPDglLGD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 179 K---GLTAFIVEREWEGVSIGKIEDKCGIRcaqvseviFDN-------VRVPKENMLG---EEGKGFAVAMKDLDGGR-I 244
Cdd:PRK13026 263 KkelGITCALIPTDHPGVEIGRRHNPLGMA--------FMNgttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRgI 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 245 GVAAQGLGIAKGAYDIAFNYLKEREQFGKPLYKNQYLAFKMAeletEIEMAQYMLYKA----ATDKQEGKSYSVPAAKAK 320
Cdd:PRK13026 335 SLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALA----RIAGNTYLLEAArrltTTGLDLGVKPSVVTAIAK 410
|
330 340 350
....*....|....*....|....*....|....*..
gi 496558494 321 --------MVCTDAAMHVATEAVQMlG-----GNGYM 344
Cdd:PRK13026 411 yhmtelarDVVNDAMDIHAGKGIQL-GpknylGHAYM 446
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
38-342 |
1.34e-18 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 87.56 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 38 PEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVGIAYSVCTSLYSGALI-NDGNEEQKKKYLPEVLS 116
Cdd:PRK09463 111 PPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGELLlHYGTDEQKDHYLPRLAR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 117 GKKMGSFCLTEPDAGSDAAGCKTTAI-----WNGKEYI---LNGLKCFITNGPLAdyyMVVALT----NPE--LKTK--- 179
Cdd:PRK09463 191 GEEIPCFALTSPEAGSDAGSIPDTGVvckgeWQGEEVLgmrLTWNKRYITLAPIA---TVLGLAfklyDPDglLGDKedl 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 180 GLTAFIVEREWEGVSIGKIEDKCGIRcaqvseviFDN-------VRVPKENMLGEE---GKGFAVAMKDLDGGR-IGVAA 248
Cdd:PRK09463 268 GITCALIPTDTPGVEIGRRHFPLNVP--------FQNgptrgkdVFIPLDYIIGGPkmaGQGWRMLMECLSVGRgISLPS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 249 QGLGIAKGAYDIAFNYLKEREQFGKPLYK-------------NQYLAFKMAELETeiemaqymlykAATDKqeGKSYSVP 315
Cdd:PRK09463 340 NSTGGAKLAALATGAYARIRRQFKLPIGKfegieeplariagNAYLMDAARTLTT-----------AAVDL--GEKPSVL 406
|
330 340
....*....|....*....|....*..
gi 496558494 316 AAKAKMVCTDAAMHVATEAVQMLGGNG 342
Cdd:PRK09463 407 SAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
120-368 |
9.70e-15 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 75.56 E-value: 9.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 120 MGsfcLTEPDAGSDAAGCKTTA-IWNGKEYILNGLKCFITNgPLADYYMVVALTnpelkTKGLTAFIVER-----EWEGV 193
Cdd:PRK11561 182 MG---MTEKQGGSDVLSNTTRAeRLADGSYRLVGHKWFFSV-PQSDAHLVLAQA-----KGGLSCFFVPRflpdgQRNAI 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 194 SIGKIEDKCGIRCAQVSEVIFDNVrvpKENMLGEEGKGFAVAMKDldGG--RIGVAAQGLGIAKGAYDIAFNYLKEREQF 271
Cdd:PRK11561 253 RLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKM--GGmtRFDCALGSHGLMRRAFSVAIYHAHQRQVF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 272 GKPLYKN----QYLAfKMAeLETEIEMAQYMLYKAATDKQEGKSYSV------PAAKAKmVCTDAAMHVAtEAVQMLGGN 341
Cdd:PRK11561 328 GKPLIEQplmrQVLS-RMA-LQLEGQTALLFRLARAWDRRADAKEALwarlftPAAKFV-ICKRGIPFVA-EAMEVLGGI 403
|
250 260
....*....|....*....|....*..
gi 496558494 342 GYMKEYHVERMLRDAKITQIYEGTNEI 368
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
23-356 |
1.13e-13 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 71.61 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 23 VLQETVLEDDAAGRFPEEAYKKMGEMGFVGLPFPKEYGGQGGDYLSYVLALEEISKINSSVG-IAYSVCTSLYSGALIND 101
Cdd:cd01159 9 LIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwVASIVATHSRMLAAFPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 102 gnEEQKkkylpEVLSGkkmgsfcltEPD---AGSDAAGCKTTAIWNGkeYILNGLKCFITNGPLADYYMVVALTNPELKT 178
Cdd:cd01159 89 --EAQE-----EVWGD---------GPDtllAGSYAPGGRAERVDGG--YRVSGTWPFASGCDHADWILVGAIVEDDDGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 179 KGLTAFIVERewEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENMLgEEGKGFAV--AMKDLDGGRI--------GVAA 248
Cdd:cd01159 151 PLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTL-TAGDMMAGdgPGGSTPVYRMplrqvfplSFAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 249 QGLGIAKGAYDIAFNYLKEREQ---FGKPLYKNQYLAFKMAELETEIEMAQYMLYKAATDKQEG-KSYSVPAAKAKMVCT 324
Cdd:cd01159 228 VSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHaLAGGPIDVEERARIR 307
|
330 340 350
....*....|....*....|....*....|....*....
gi 496558494 325 DAAMHVAT---EAVQML----GGNGYMKEYHVERMLRDA 356
Cdd:cd01159 308 RDAAYAAKlsaEAVDRLfhaaGGSALYTASPLQRIWRDI 346
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
97-344 |
5.27e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 54.84 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 97 ALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGK--EYILN------------GLkcfitnGPL 162
Cdd:PLN02443 109 AIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKtdEFVIHsptltsskwwpgGL------GKV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 163 ADYYMVVALTNPELKTKGLTAFIVE-REWE------GVSIGKIEDKCGIRCAQVSE---VIFDNVRVPKENML------G 226
Cdd:PLN02443 183 STHAVVYARLITNGKDHGIHGFIVQlRSLDdhsplpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLmrlskvT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 227 EEGKGFAVAM-KDLDGG-----RIGVAAQGLGIAKGAYDIAFNYLKEREQFGK--------------------PLYKNQY 280
Cdd:PLN02443 263 REGKYVQSDVpRQLVYGtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGSqdggpetqvidyktqqsrlfPLLASAY 342
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558494 281 lAFKMaeleteieMAQYM--LYKAATDKQEGKSYS-VPAAKA-----KMVCTDAAMHVATEAVQMLGGNGYM 344
Cdd:PLN02443 343 -AFRF--------VGEWLkwLYTDVTQRLEANDFStLPEAHActaglKSLTTSATADGIEECRKLCGGHGYL 405
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
73-271 |
1.10e-06 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 50.54 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 73 LEEISKINSSVGIAYSVCTSLYSGALINDGNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGK--EYIL 150
Cdd:PLN02312 139 LEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKteEFVI 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 151 N-----GLKCFITNGPL-ADYYMVVALTNPELKTKGLTAFIVE-REWEG-----VSIGKIEDKCGIRCAQVSEVIFDNVR 218
Cdd:PLN02312 219 NtpcesAQKYWIGGAANhATHTIVFSQLHINGKNEGVHAFIAQiRDQDGnicpnIRIADCGHKIGLNGVDNGRIWFDNLR 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496558494 219 VPKENMLGE------EGK----------GFAVAMKDLDGGRIGVAAQGLGIAKGAYDIAFNYLKEREQF 271
Cdd:PLN02312 299 IPRENLLNSvadvspDGKyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
102-225 |
1.20e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.15 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558494 102 GNEEQKKKYLPEVLSGKKMGSFCLTEPDAGSDAAGCKTTAIWNGK--EYILNGLKCFITN------GPLADYYMVVALTN 173
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQtnEFVIHTPSVEAVKfwpgelGFLCNFALVYAKLI 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 496558494 174 PELKTKGLTAFIVE-------REWEGVSIGKIEDKCGIRCAQVSEVIFDNVRVPKENML 225
Cdd:PTZ00460 190 VNGKNKGVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLL 248
|
|
| |
