|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
15-402 |
9.20e-101 |
|
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: 304.28 E-value: 9.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 15 EDVLSIAKGLTDGEVEFLQQVDSLLESKYRENINQHWIDATVPEDYFKDLGELNYFNNPLlyKDRPNAKMPSqlfqffMS 94
Cdd:cd01151 4 EDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATI--KGYGCAGLSS------VA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 95 YLLA-----RFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDvAGGLETVAERQGDT 169
Cdd:cd01151 76 YGLIareveRVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSD-PGGMETRARKDGGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 170 WVINGEKKWIGGAHVSDVIPVFAVNKETGKPHCFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRLQNITS 249
Cdd:cd01151 155 YKLNGSKTWITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 250 FKDIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEY 329
Cdd:cd01151 235 LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKA 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584959699 330 DEVATSTAKMMNALRLRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINALVIGRALTGDSAF 402
Cdd:cd01151 315 TPEQISLLKRNNCGKALEIARTAREMLGGNGIS-DEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
24-401 |
1.03e-90 |
|
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: 278.26 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 24 LTDGEVEFLQQVDSLLESKYRENINQHWIDATVPEDYFKDLGELNYFNNPLlykdrpnakmP--------SQLFQFFMSY 95
Cdd:COG1960 5 LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTI----------PeeygglglSLVELALVLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 96 LLARFDISLATLLGVHQGLGHnTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGE 175
Cdd:COG1960 75 ELARADASLALPVGVHNGAAE-ALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAA-LRTTAVRDGDGYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 176 KKWIGGAHVSDVIPVFAVNKETGKPH---CFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRLQNI-TSFK 251
Cdd:COG1960 153 KTFITNAPVADVILVLARTDPAAGHRgisLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEgKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 252 DIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDE 331
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 332 VATSTAKMMNALRLRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINALVIGRALTGDSA 401
Cdd:COG1960 313 LEAAMAKLFATEAALEVADEALQIHGGYGYT-REYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
97-402 |
1.24e-84 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 264.02 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 97 LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDvAGGLETVAERQGDTWVINGEK 176
Cdd:PLN02526 99 VARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSD-ASSLNTTATKVEGGWILNGQK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 177 KWIGGAHVSDVIPVFAVNKETGKPHCFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRLQNITSFKDIAKI 256
Cdd:PLN02526 178 RWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 257 LYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLaQAMATCA-QLANMQAHGEYDEVATS 335
Cdd:PLN02526 258 LAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNI-QAMFLVGwRLCKLYESGKMTPGHAS 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584959699 336 TAKMMNALRLRETVAMGRGITGGNGILAdDYDIARFFSDAEAIYTYEGTHEINALVIGRALTGDSAF 402
Cdd:PLN02526 337 LGKAWITKKARETVALGRELLGGNGILA-DFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
114-394 |
5.34e-63 |
|
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: 205.21 E-value: 5.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 114 LGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGEKKWIGGAHVSDVIPVFAV 193
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAG-IRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 194 NKETGKPH----CFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRL-QNITSFKDIAKILYSTRAGVAYMA 268
Cdd:cd00567 122 TDEEGPGHrgisAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLgEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 269 TGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLAN-MQAHGEYDEVATSTAKMMNALRLRE 347
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWlLDQGPDEARLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 584959699 348 TVAMGRGITGGNGiLADDYDIARFFSDAEAIYTYEGTHEINALVIGR 394
Cdd:cd00567 282 VADLAMQIHGGRG-YSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
92-396 |
1.93e-59 |
|
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: 197.49 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 92 FMSYL-----LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDvAGGLETVAERQ 166
Cdd:cd01158 60 FLAYAiaieeLAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSD-AAALKTTAKKD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 167 GDTWVINGEKKWIGGAHVSDVIPVFAVNKETGKPH---CFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADR 243
Cdd:cd01158 139 GDDYVLNGSKMWITNGGEADFYIVFAVTDPSKGYRgitAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 244 LQNI-TSFKDIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLAN 322
Cdd:cd01158 219 LGEEgEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAAR 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584959699 323 MQAHGEYDEVATSTAKMMNALRLRETVAMGRGITGGNGILAdDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:cd01158 299 LKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTK-DYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
3-398 |
3.42e-50 |
|
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: 174.19 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 3 FEKETVLKTLFPEDvlsiaKGLTDGEVEFLQQVDSLLESKYRENINQHWIDAT--VPEDYFKDLGELNYFNnpllykdrp 80
Cdd:cd01161 7 FLGDIVTKQVFPYP-----SVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLekIPRKTLTQLKELGLFG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 81 nAKMPSQL----FQFFMSYLLAR---FDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGS 153
Cdd:cd01161 73 -LQVPEEYgglgLNNTQYARLAEivgMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 154 DvAGGLETVAERQ--GDTWVINGEKKWIGGAHVSDVIPVFA---VNKETG----KPHCFVVRPEQDGVDIEVIDNKIALR 224
Cdd:cd01161 152 D-AASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAkteVKDATGsvkdKITAFIVERSFGGVTNGPPEKKMGIK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 225 IVPNALIKLTNVKVDEADRLQNI-TSFKDIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKL 303
Cdd:cd01161 231 GSNTAEVYFEDVKIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 304 AMMQGNL--AQAMA-TCAQLANMQAHGEYdEVATSTAKMMNALRLRETVAMGRGITGGNGILAdDYDIARFFSDAEAIYT 380
Cdd:cd01161 311 ANMAILQyaTESMAyMTSGNMDRGLKAEY-QIEAAISKVFASEAAWLVVDEAIQIHGGMGFMR-EYGVERVLRDLRIFRI 388
|
410
....*....|....*...
gi 584959699 381 YEGTHEINALVIgrALTG 398
Cdd:cd01161 389 FEGTNEILRLFI--ALTG 404
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
23-396 |
1.20e-38 |
|
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: 142.55 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 23 GLTDGEVEFLQQVDSLLESK---YRENINQhwiDATVPEDYFKDLGELNYFNnpllykdrpnAKMPSQLFQFFMSYL--- 96
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEiapLAAKIDR---DNEFPRDLWRKMGKLGLLG----------ITAPEEYGGSGMGYLahv 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 97 -----LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWV 171
Cdd:cd01156 68 iimeeISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVS-MKLRAEKKGDRYV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 172 INGEKKWIGGAHVSDVIPVFAvnKETGKPH-----CFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRLQN 246
Cdd:cd01156 147 LNGSKMWITNGPDADTLVVYA--KTDPSAGahgitAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 247 ITSFKdiaKILYS----TRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLAN 322
Cdd:cd01156 225 ENKGV---YVLMSgldyERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAK 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584959699 323 MQAHGEYDEVATSTAKMMNALRLRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:cd01156 302 ACDRGNMDPKDAAGVILYAAEKATQVALDAIQILGGNGYI-NDYPTGRLLRDAKLYEIGAGTSEIRRMVIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
97-396 |
4.28e-35 |
|
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: 133.01 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 97 LARFDISLATLLgVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGEK 176
Cdd:cd01160 70 LARAGGSGPGLS-LHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQG-IRTTARKDGDHYVLNGSK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 177 KWIGGAHVSDVIPVFAVNKETGKPH----CFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRL-QNITSFK 251
Cdd:cd01160 148 TFITNGMLADVVIVVARTGGEARGAggisLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLgEENKGFY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 252 DIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDE 331
Cdd:cd01160 228 YLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDV 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584959699 332 VATSTAKMMNALRLRETVAMGRGITGGNGILAdDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:cd01160 308 AEASMAKYWATELQNRVAYECVQLHGGWGYMR-EYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
123-398 |
7.52e-31 |
|
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: 121.40 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDvAGGLETVAERQGDTWVINGEKKWIGGAHVSDVIPVFAVNKETGKP-- 200
Cdd:cd01162 97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSD-AAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKgi 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 201 HCFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRL-QNITSFKDIAKILYSTRAGVAYMATGGMAGALRAT 279
Cdd:cd01162 176 SCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLgGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 280 LDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDEVA-TSTAKMMNALRLRETVAMGRGITGG 358
Cdd:cd01162 256 RAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKlCAMAKRFATDECFDVANQALQLHGG 335
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 584959699 359 NGILAdDYDIARFFSDAEAIYTYEGTHEINALVIGRALTG 398
Cdd:cd01162 336 YGYLK-DYPVEQYVRDLRVHQILEGTNEIMRLIIARALLT 374
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
113-398 |
1.32e-29 |
|
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: 118.07 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 113 GLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGEKKWIGGAHVSDVIpvFA 192
Cdd:cd01157 87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAG-IKTKAEKKGDEYIINGQKMWITNGGKANWY--FL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 193 VNKETGKPHC--------FVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRL-QNITSFKDIAKILYSTRAG 263
Cdd:cd01157 164 LARSDPDPKCpaskaftgFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLiGEGAGFKIAMGAFDKTRPP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 264 VAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDEVATSTAKMMNAL 343
Cdd:cd01157 244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAAD 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 584959699 344 RLRETVAMGRGITGGNGiLADDYDIARFFSDAEAIYTYEGTHEINALVIGRALTG 398
Cdd:cd01157 324 IANQLATDAVQIFGGNG-FNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLG 377
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
97-396 |
5.66e-28 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 113.82 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 97 LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGEK 176
Cdd:PLN02519 99 ISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVS-MKCKAERVDGGYVLNGNK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 177 KWIGGAHVSDVIPVFAVNKETGKPH---CFVVRPEQDGVDIEVIDNKIALR-------IVPNALIKLTNVKVDEADRLQN 246
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDVAAGSKgitAFIIEKGMPGFSTAQKLDKLGMRgsdtcelVFENCFVPEENVLGQEGKGVYV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 247 ITSFKDIAKILYStrAGvaymATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAH 326
Cdd:PLN02519 258 MMSGLDLERLVLA--AG----PLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 327 GEYDEVATSTAKMMNALRLRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:PLN02519 332 GKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYI-NEYPTGRLLRDAKLYEIGAGTSEIRRMLIGREL 400
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
250-396 |
1.22e-26 |
|
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: 103.87 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 250 FKDIAKILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEY 329
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584959699 330 DEVATSTAKMMNALRLRETVAMGRGITGGNGiLADDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:pfam00441 84 DGAEASMAKLYASEAAVEVADLAMQLHGGYG-YLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
123-396 |
1.70e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 100.96 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPK-LQSHELRTCFALTEPEHGSDVAGGLETVAERQGDTWvINGEKKWIGGAHVSDVIPVFAVNKETGKPH 201
Cdd:PRK12341 100 GSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVY-LNGQKTFITGAKEYPYMLVLARDPQPKDPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 202 -CFV---VRPEQDGVDIEVIdNKIALRIVPNALIKLTNVKVDEADR--------LQNITSFkDIAKILYStrAGVAYMAT 269
Cdd:PRK12341 179 kAFTlwwVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDLvgeegmgfLNVMYNF-EMERLINA--ARSLGFAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 270 GGMAGALRatldYVTERKQFGKPISKYQLIQEKLAMMQ---GNLAQAMATCAQLANMqahGEYDEVATSTAKMMNALRLR 346
Cdd:PRK12341 255 CAFEDAAR----YANQRIQFGKPIGHNQLIQEKLTLMAikiENMRNMVYKVAWQADN---GQSLRTSAALAKLYCARTAM 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 584959699 347 ETVAMGRGITGGNGiLADDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:PRK12341 328 EVIDDAIQIMGGLG-YTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
130-396 |
1.85e-23 |
|
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: 101.29 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 130 KYVPKLQSHELRTCFA----LTEPEHGSDVaGGLETVAERQ-GDTWVINGEKkWIGGAHVSDVIPVFAvnKETGKPH--- 201
Cdd:cd01154 133 QYLPGLLSDRYKTGLLggtwMTEKQGGSDL-GANETTAERSgGGVYRLNGHK-WFASAPLADAALVLA--RPEGAPAgar 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 202 ---CFVV-RPEQDG----VDIEVIDNKIALRIVPNALIKLTNVkvdEADRL-QNITSFKDIAKILYSTRAGVAYMATGGM 272
Cdd:cd01154 209 glsLFLVpRLLEDGtrngYRIRRLKDKLGTRSVATGEVEFDDA---EAYLIgDEGKGIYYILEMLNISRLDNAVAALGIM 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 273 AGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATC---AQLANMQAHGEYDE-----VATSTAKMMNALR 344
Cdd:cd01154 286 RRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTfraARAFDRAAADKPVEahmarLATPVAKLIACKR 365
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 584959699 345 LRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINALVIGRAL 396
Cdd:cd01154 366 AAPVTSEAMEVFGGNGYL-EEWPVARLHREAQVTPIWEGTGNIQALDVLRVL 416
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
117-397 |
1.08e-22 |
|
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: 99.00 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 117 NTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVaGGLETVAERQGD-TWVINGEKKWI-GGAHVSD---VIPVF 191
Cdd:cd01153 94 ATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDL-GALRTKAVYQADgSWRINGVKRFIsAGEHDMSeniVHLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 192 AVNKETGK----------PHcFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKV----DEADRLqnitsfKDIAKIL 257
Cdd:cd01153 173 ARSEGAPPgvkglslflvPK-FLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGeligEEGMGL------AQMFAMM 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 258 YSTRAGVAYMATGGMAGALRATLDYVTERKQFGKP--------ISKYQLIQEKLAMM----QGNLAQAM--ATCAQLA-- 321
Cdd:cd01153 246 NGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikaapavtIIHHPDVRRSLMTQkayaEGSRALDLytATVQDLAer 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 322 ------NMQAHGEYDEVATSTAKMMNALRLRETVAMGRGITGGNGILaDDYDIARFFSDAEAIYTYEGTHEINAL-VIGR 394
Cdd:cd01153 326 kategeDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYT-REYPIEQYYRDARITTIYEGTTGIQALdLIGR 404
|
...
gi 584959699 395 ALT 397
Cdd:cd01153 405 KIV 407
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
115-395 |
1.32e-19 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 89.51 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 115 GHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVaGGLETVAERQGDTWVINGEKKWIGGAHVSDVIPVFAVN 194
Cdd:PRK03354 93 GFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDV-GSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 195 KETGKPHCF---VVRPEQDGVDIEVIDnKIALRIVPNALIKLTNVKVDEADRL-QNITSFKDIAKILYSTRAGVAYMATG 270
Cdd:PRK03354 172 GASPDKPVYtewFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFgREGNGFNRVKEEFDHERFLVALTNYG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 271 GMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDEVATSTAKMMNALRLRETVA 350
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVD 330
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 584959699 351 MGRGITGGNGIlADDYDIARFFSDAEAIYTYEGTHEINALVIGRA 395
Cdd:PRK03354 331 SAMQVLGGVGI-AGNHRISRFWRDLRVDRVSGGSDEMQILTLGRA 374
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
97-386 |
4.22e-19 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 88.46 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 97 LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGGLETVAERQGDTWVINGEK 176
Cdd:PTZ00461 108 LSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 177 KWIGGAHVSDVIPVFAvnKETGKPHCFVVRPEQDGVDIEVIDNKIALRIVPNALIKLTNVKVDEADRL-QNITSFKDIAK 255
Cdd:PTZ00461 188 IWITNGTVADVFLIYA--KVDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLgEEGKGMVGMMR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 256 ILYSTRAGVAYMATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDEVATS 335
Cdd:PTZ00461 266 NLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSD 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 584959699 336 TAKMMNALRLRETVAMGRGITGGNGiLADDYDIARFFSDAEAIYTYEGTHE 386
Cdd:PTZ00461 346 AAKLFATPIAKKVADSAIQVMGGMG-YSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
143-229 |
1.55e-18 |
|
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: 80.02 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 143 CFALTEPEHGSDVAGGLETVAERQGDTWVINGEKKWIGGAHVSDVIPVFAVNKETGKPH---CFVVRPEQDGVDIEVIDN 219
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGgisLFLVPKDAPGVSVRRIET 80
|
90
....*....|
gi 584959699 220 KIALRIVPNA 229
Cdd:pfam02770 81 KLGVRGLPTG 90
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
123-398 |
2.21e-18 |
|
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: 85.86 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGgLETVAERQGDTWVINGEKKWIGGAHVSDVIPVFAVNKETGKPH- 201
Cdd:cd01152 100 GTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAG-LRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHr 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 202 ---CFVVRPEQDGVDIEVIdNKIALRIVPNAlIKLTNVKVDEADRLQNITSFKDIAKilysTRAGVAYMATGGMA----G 274
Cdd:cd01152 179 gisILLVDMDSPGVTVRPI-RSINGGEFFNE-VFLDDVRVPDANRVGEVNDGWKVAM----TTLNFERVSIGGSAatffE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 275 ALRATLDYVTERkqfGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANMQAHGEYDEVATSTAKmMNALRLRETVAMGR- 353
Cdd:cd01152 253 LLLARLLLLTRD---GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAK-LFGSELAQELAELAl 328
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 584959699 354 GITGGNGILADDYDIARFFSDAEAIY-------TYEGTHEINALVIGRALTG 398
Cdd:cd01152 329 ELLGTAALLRDPAPGAELAGRWEADYlrsrattIYGGTSEIQRNIIAERLLG 380
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
79-303 |
2.43e-16 |
|
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: 80.84 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 79 RPNAKMPSQLFQFF-MSYLLARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAg 157
Cdd:cd01150 72 RMGELMADDPEKMLaLTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQ- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 158 GLETVA--ERQGDTWVIN-----GEKKWIGG-AHVSDVIPVFAVNKETGKP---HCFVVrPEQD--------GVDIEVID 218
Cdd:cd01150 151 GLETTAtyDPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNhglHAFIV-PIRDpkthqplpGVTVGDIG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 219 NKIALRIVPNALIKLTNVKVDE-------ADRL---QNITSFKDIAK-------ILYSTRAGVAYMATGGMAGALRATLD 281
Cdd:cd01150 230 PKMGLNGVDNGFLQFRNVRIPRenllnrfGDVSpdgTYVSPFKDPNKrygamlgTRSGGRVGLIYDAAMSLKKAATIAIR 309
|
250 260
....*....|....*....|....*....
gi 584959699 282 YVTERKQFGK-------PISKYQLIQEKL 303
Cdd:cd01150 310 YSAVRRQFGPkpsdpevQILDYQLQQYRL 338
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
123-395 |
1.31e-14 |
|
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: 74.73 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGGLETVAERQGDTWVINGEKKWIGGAhvsdvipvfavnketGKPHC 202
Cdd:cd01155 108 GSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVINGRKWWSSGA---------------GDPRC 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 203 ----FVVRPEQDGVDIEVIDNKIalrIVP-----------------------NALIKLTNVKVDEADRLQNITSFKDIAK 255
Cdd:cd01155 173 kiaiVMGRTDPDGAPRHRQQSMI---LVPmdtpgvtiirplsvfgyddaphgHAEITFDNVRVPASNLILGEGRGFEIAQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 256 ilysTRAGVAY----MATGGMAG-ALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMATCAQLANM------- 323
Cdd:cd01155 250 ----GRLGPGRihhcMRLIGAAErALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMidtvgnk 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584959699 324 QAHGEYDEVATSTAKMmnALRLretvaMGRGIT--GGNGIlADDYDIARFFSDAEAIYTYEGTHEINALVIGRA 395
Cdd:cd01155 326 AARKEIAMIKVAAPRM--ALKI-----IDRAIQvhGAAGV-SQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
101-372 |
2.48e-14 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 74.89 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 101 DISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAgGLETVA--ERQGDTWVIN----- 173
Cdd:PLN02636 134 DMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQ-GLQTTAtfDPLTDEFVINtpndg 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 174 GEKKWIGGAHV-SDVIPVFA----------VNKETGKpHCFVVrPEQD--------GVDIEVIDNKIALRIVPNALIKLT 234
Cdd:PLN02636 213 AIKWWIGNAAVhGKFATVFArlklpthdskGVSDMGV-HAFIV-PIRDmkthqvlpGVEIRDCGHKVGLNGVDNGALRFR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 235 NVKVDEaDRLQN-----------ITSFKDIAKILYST-------RAGVAYMATGGMAGALRATLDYVTERKQFGKP---- 292
Cdd:PLN02636 291 SVRIPR-DNLLNrfgdvsrdgkyTSSLPTINKRFAATlgelvggRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPkqpe 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 293 --ISKYQLIQEKL-AMMQGNLAQAMAT---CAQLANMQAHGEYDEVA-------------TS-TAKMMNAlrLRETVAmG 352
Cdd:PLN02636 370 isILDYQSQQHKLmPMLASTYAFHFATeylVERYSEMKKTHDDQLVAdvhalsaglkayiTSyTAKALST--CREACG-G 446
|
330 340
....*....|....*....|..
gi 584959699 353 RGITGGN--GILADDYDIARFF 372
Cdd:PLN02636 447 HGYAAVNrfGSLRNDHDIFQTF 468
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
75-280 |
1.52e-13 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 72.11 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 75 LYKDRPNAkmpsQLFQFFMSYLLARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSD 154
Cdd:PLN02312 124 LTETGPEA----ELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 155 VAgGLETVAERQGDT--WVIN-----GEKKWIGGA--HVSDVIpVFA---VNKETGKPHCFVVR-PEQDGV---DIEVID 218
Cdd:PLN02312 200 VR-GIETVTTYDPKTeeFVINtpcesAQKYWIGGAanHATHTI-VFSqlhINGKNEGVHAFIAQiRDQDGNicpNIRIAD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 219 --NKIALRIVPNALIKLTNVKVDEADRL----------QNITSFKD-------IAKILYSTRAGVA----YMATGGMAGA 275
Cdd:PLN02312 278 cgHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvspdgKYVSAIKDpdqrfgaFLAPLTSGRVTIAvsaiYSSKVGLAIA 357
|
....*
gi 584959699 276 LRATL 280
Cdd:PLN02312 358 IRYSL 362
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
123-182 |
1.07e-08 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 57.11 E-value: 1.07e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAGGLETVAERQGDTWVINGEKKWIGGA 182
Cdd:PLN02876 533 GNKEQQLEWLIPLLEGKIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGA 592
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
123-361 |
2.20e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 52.90 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAG----GLETVAERQGD-------TWvingEKKWIGGAHVSDVIPVf 191
Cdd:PRK09463 176 GTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSipdtGVVCKGEWQGEevlgmrlTW----NKRYITLAPIATVLGL- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 192 avnketgkphCFVVR-PEQ---DGVDIevidnKIALRIVPnaliklTNVK-VDEADR-------LQN-ITSFKDI----- 253
Cdd:PRK09463 251 ----------AFKLYdPDGllgDKEDL-----GITCALIP------TDTPgVEIGRRhfplnvpFQNgPTRGKDVfipld 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 254 AKILYSTRAGVAYM-----------------ATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGN--LAQAM 314
Cdd:PRK09463 310 YIIGGPKMAGQGWRmlmeclsvgrgislpsnSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNayLMDAA 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 584959699 315 ATCAQLANMQahGEYDEVATSTAKMMNALRLRETVAMGRGITGGNGI 361
Cdd:PRK09463 390 RTLTTAAVDL--GEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGI 434
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
58-303 |
2.29e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 52.93 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 58 EDYFKDLGELNYFNNPLLYKDRPNAKMPSQLFQFFMSY---LLARFDISLAT------LLGVHQGLGHNTFYFG------ 122
Cdd:PTZ00460 27 EQFETFLERQKFIDNEPMFKVHPDYYNWSRQDQILLNAektREAHKHLNLANpnyytpNLLCPQGTFISTVHFAmvipaf 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 ---GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAgGLETVA--ERQGDTWVIN-----GEKKWIGG-AHVSDVIPVF 191
Cdd:PTZ00460 107 qvlGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQ-NLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 192 A---VNKETGKPHCFVVR--------PEQdGVDIEVIDNKIALRIVPNALIKLTN------------VKVDEADRLQNIT 248
Cdd:PTZ00460 186 AkliVNGKNKGVHPFMVRirdkethkPLQ-GVEVGDIGPKMGYAVKDNGFLSFDHyripldsllaryIKVSEDGQVERQG 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584959699 249 SFK-DIAKILYStRAGVAYMATGGMAGALRATLDYVTERKQF----GKPIS--KYQLIQEKL 303
Cdd:PTZ00460 265 NPKvSYASMMYM-RNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQENSvlEYQTQQQKL 325
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
25-137 |
4.70e-07 |
|
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: 48.23 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 25 TDGEVEFLQQVDSLLESKYRENINQHWIDATVPEDYFKDLGELNYFNNPLlykdrpnakmPSQL----FQFFMSYL---- 96
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITI----------PEEYggagLDYLAYALvaee 70
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 584959699 97 LARFDISLATLLGVHQGLGHNTFYFGGSKEQIAKYVPKLQS 137
Cdd:pfam02771 71 LARADASVALALSVHSSLGAPPILRFGTEEQKERYLPKLAS 111
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
85-287 |
5.14e-07 |
|
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: 51.17 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 85 PSQLFQFFMSylLARFDISLATLLGVHQGLGHNTFYFGgsKEQIAKYVpkLQSHELRTCFALTEPEHGSDVAGGLETVAE 164
Cdd:cd01163 52 LPDLYEVVRE--LAAADSNIAQALRAHFGFVEALLLAG--PEQFRKRW--FGRVLNGWIFGNAVSERGSVRPGTFLTATV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 165 RQGDTWVINGEKKWIGGAHVSDVIPVFAVNkETGKPHCFVVRPEQDGvdIEVID--NKIALRIVPNALIKLTNVKVDE-- 240
Cdd:cd01163 126 RDGGGYVLNGKKFYSTGALFSDWVTVSALD-EEGKLVFAAVPTDRPG--ITVVDdwDGFGQRLTASGTVTFDNVRVEPde 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 584959699 241 ----ADRLQNITSFKDIAKILY-STRAGVAymatggmAGALRATLDYVTERK 287
Cdd:cd01163 203 vlprPNAPDRGTLLTAIYQLVLaAVLAGIA-------RAALDDAVAYVRSRT 247
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
123-361 |
1.85e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 49.96 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDvAGGL--ETVAERQgdtwVINGE----------KKWIGGAHVSDVIPV 190
Cdd:PRK13026 175 GTQEQKDYWLPRLADGTEIPCFALTGPEAGSD-AGAIpdTGIVCRG----EFEGEevlglrltwdKRYITLAPVATVLGL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 191 fAVNketgkphcfVVRPEQdgvdieVIDNKIALRIVpNALIKLTNVKVDEADR-------LQNITSF-KDI-----AKIL 257
Cdd:PRK13026 250 -AFK---------LRDPDG------LLGDKKELGIT-CALIPTDHPGVEIGRRhnplgmaFMNGTTRgKDVfipldWIIG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 258 YSTRAGVAY-----------------MATGGMAGALRATLDYVTERKQFGKPISKYQLIQEKLAMMQGNLAQAMA----T 316
Cdd:PRK13026 313 GPDYAGRGWrmlveclsagrgislpaLGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAarrlT 392
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 584959699 317 CAQLaNMqahGEYDEVATSTAKMMNALRLRETVAMGRGITGGNGI 361
Cdd:PRK13026 393 TTGL-DL---GVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
91-183 |
3.01e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 46.01 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 91 FFMSYLLARFDISLATLLGVHQGlGHNTFYFGGSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVaGGLETVAERQGD-T 169
Cdd:PTZ00456 133 FITRELMATANWGFSMYPGLSIG-AANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDL-GQVKTKAEPSADgS 210
|
90
....*....|....*
gi 584959699 170 WVINGEKKWI-GGAH 183
Cdd:PTZ00456 211 YKITGTKIFIsAGDH 225
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
123-290 |
1.64e-03 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 40.59 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 123 GSKEQIAKYVPKLQSHELRTCFALTEPEHGSDVAgGLETVA--ERQGDTWVIN-----GEKKWIGG-AHVSDVIPVFA-- 192
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQ-GLETTAtfDPKTDEFVIHsptltSSKWWPGGlGKVSTHAVVYArl 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 193 -VNKETGKPHCFVV--RPEQD-----GVDIEVIDNKI---ALRIVPNALIKLTNVKVDEAD---RLQNITS-----FKDI 253
Cdd:PLN02443 193 iTNGKDHGIHGFIVqlRSLDDhsplpGVTVGDIGMKFgngAYNTMDNGFLRFDHVRIPRDQmlmRLSKVTRegkyvQSDV 272
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 584959699 254 AK-ILYST----RAGVAYMATGGMAGALRATLDYVTERKQFG 290
Cdd:PLN02443 273 PRqLVYGTmvyvRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
271-386 |
3.76e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 37.33 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584959699 271 GMA-GALRATLDYVTERKQ--FGKPISKYQLIQEKLAMMQGNLAQAMATCAQlanmQAHGEYDEVATSTAKMMnALRLRE 347
Cdd:pfam08028 8 GAArAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLER----AAARIEAAAAAGKPVTP-ALRAEA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 584959699 348 TVAMGRG-------------ITGGNGiLADDYDIARFFSDAEAIYTYEGTHE 386
Cdd:pfam08028 83 RRAAAFAtelavaavdalfrAAGGSA-LFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| |
