|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-566 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 535.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 3 TYSAPLRDMRFVLHDVFNASGLWARLPALAerIDADTADAILEEASKVTGQLIAPLSRNGDEQG-VCFDAGQVTTPEGFR 81
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLGKTD--VTKELMDSLLEEASKLATQTLLPLYESSDSEGcVLLKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 82 EAWNTYREGGWVGLGGNPEYGGMGMPKMLGVLFEEMLYAADCSFSLYSALSAGSCLAIDAHASEALKATYLPPLYEGRWA 161
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 162 GTMCLTEPHAGTDLGLIRTRAEPQADGSVRISGSKIFITGGEQDLTENIVHLVLAKMPDAPAGAKGISLFLVPKFLVEAD 241
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 242 GRLGARNAVHCGSIEHKMGIKASATCVMNFDGAIGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANE 321
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 322 RLQSRAATGPQAHDKAADPIIHHGDVRRMLLTMRTLTEAGRAFAVYVGQQLDVARYAEDAGEREHAQRLVALLTPVAKAF 401
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 402 FTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALDLLGRKVLA-DGGQALASFASEVRAFSVDAP 480
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSlKGGNEVARFGKRVSKLVRAHL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 481 LHREALQASLARL-EATSSW------LRAQAGEDANLVSAVAVEYLQLFGLTAYAYMWARMAAVA---LAKRDEDDAFHG 550
Cdd:PTZ00456 503 FSRGALGQYARRLwLLQKQWrlattrVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAqkkVAAGQDADGFYQ 582
|
570
....*....|....*.
gi 499256869 551 AKLACAAFYFQRVLPR 566
Cdd:PTZ00456 583 CKVDTCQYVFQRILPR 598
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
43-457 |
1.43e-162 |
|
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: 469.95 E-value: 1.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 43 ILEEASKVTGQLIAPLSRNGDEQGVCFDAGQVTTPEGFREAWNTYREGGWVGLGGNPEYGGMGMPKMLGVLFEEMLYAAD 122
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 123 CSFSLYSALSAGSClAIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGSVRISGSKIFITGG 202
Cdd:cd01153 81 APLMYASGTQGAAA-TLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 203 EQDLTENIVHLVLAKMPDAPAGAKGISLFLVPKFLVEadgrlGARNAVHCGSIEHKMGIKASATCVMNFDGAIGYLVGEP 282
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 283 NKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQSRaatgPQAHDKAADPIIHHGDVRRMLLTMRTLTEAGR 362
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGG----DLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 363 AFAVYVGQQLDVARYAEDAGE-REHAQRLVALLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIY 441
Cdd:cd01153 311 ALDLYTATVQDLAERKATEGEdRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*.
gi 499256869 442 EGTNGIQALDLLGRKV 457
Cdd:cd01153 391 EGTTGIQALDLIGRKI 406
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-462 |
2.54e-109 |
|
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: 332.58 E-value: 2.54e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 38 DTADAILEEASKVTGQLIAPLSRNGDEQGvcfdagqvTTPegfREAWNTYREGGWVGLGGNPEYGGMGMPKMLGVLFEEM 117
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 118 LYAADCSFSLYSALSAGSCLAIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGsVRISGSKI 197
Cdd:COG1960 76 LARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 198 FITGGEQ-DlteniVHLVLAKMPDAPaGAKGISLFLVPKFlveADGrlgarnaVHCGSIEHKMGIKASATCVMNFDG--- 273
Cdd:COG1960 155 FITNAPVaD-----VILVLARTDPAA-GHRGISLFLVPKD---TPG-------VTVGRIEDKMGLRGSDTGELFFDDvrv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 274 AIGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDVRRMLLT 353
Cdd:COG1960 219 PAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 354 MRTLTEAGRAFAVYVGQQLDvaryaedagerehAQRLVALLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVR 433
Cdd:COG1960 287 MAAELEAARALVYRAAWLLD-------------AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 499256869 434 DVRIAQIYEGTNGIQALDlLGRKVLADGG 462
Cdd:COG1960 354 DARILTIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
138-453 |
1.71e-55 |
|
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: 190.57 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 138 AIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGsVRISGSKIFITGGeqdlTENIVHLVLAK 217
Cdd:cd00567 47 LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG----GDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 218 MPDAPAGAKGISLFLVPKflvEADGrlgarnaVHCGSIEHKMGIKASATCVMNFDGA---IGYLVGEPNKGLTAMFTMMN 294
Cdd:cd00567 122 TDEEGPGHRGISAFLVPA---DTPG-------VTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 295 YERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDVRRMLLTMRTLTEAGRAFAVYVGQQLDv 374
Cdd:cd00567 192 VGRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD- 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499256869 375 aryaedagereHAQRLVALLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALDLL 453
Cdd:cd00567 259 -----------QGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-450 |
8.85e-54 |
|
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: 187.48 E-value: 8.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 38 DTADAILEEASKVTGQLIAPLSRNGDEQGVcFDAGQVttpegfreawntyREGGWVGLGGNP---EYGGMGMPKMLGVLF 114
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGE-FPREVI-------------KEMAELGLMGIPipeEYGGAGLDFLAYAIA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 115 EEMLYAADCSFSLYSALSAGSCL-AIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGSVrIS 193
Cdd:cd01158 67 IEELAKVDASVAVIVSVHNSLGAnPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYV-LN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 194 GSKIFIT-GGEQDlteniVHLVLAkMPDAPAGAKGISLFLVPKflvEADGrlgarnaVHCGSIEHKMGIKASATCVMNFD 272
Cdd:cd01158 146 GSKMWITnGGEAD-----FYIVFA-VTDPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 273 GAI---GYLVGEPNKGL-TAMFTmMNYERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDVR 348
Cdd:cd01158 210 DVRvpkENILGEEGEGFkIAMQT-LDGGRIGIAAQALGIAQAALDAAVDYAKERKQ------------FGKPIADFQGIQ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 349 RMLLTMRTLTEAGRAFaVYVGQQLdvaryaEDAGE---REHAQrlvalltpvAKAFFTDNGLESCVLGQQVYGGHGYIRE 425
Cdd:cd01158 277 FKLADMATEIEAARLL-TYKAARL------KDNGEpfiKEAAM---------AKLFASEVAMRVTTDAVQIFGGYGYTKD 340
|
410 420
....*....|....*....|....*
gi 499256869 426 WGQEQRVRDVRIAQIYEGTNGIQAL 450
Cdd:cd01158 341 YPVERYYRDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
138-453 |
4.33e-46 |
|
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: 167.55 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 138 AIDAHASEALKaTYLPPL----YEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGSVRISGSKIFITGGEQDlteniVHL 213
Cdd:cd01154 122 ALRKYGPEELK-QYLPGLlsdrYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD-----AAL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 214 VLAKMPDAPAGAKGISLFLVPKFLveadgRLGARNAVHCGSIEHKMGIKASATCVMNFDGAIGYLVGEPNKGLTAMFTMM 293
Cdd:cd01154 196 VLARPEGAPAGARGLSLFLVPRLL-----EDGTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEML 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 294 NYERLSIGIQGIGCAEASYQSAARYANerlqSRAATGpqahdkaaDPIIHHGDVRRMLLTMRTLTEAGRAFAvyvgqqLD 373
Cdd:cd01154 271 NISRLDNAVAALGIMRRALSEAYHYAR----HRRAFG--------KPLIDHPLMRRDLAEMEVDVEAATALT------FR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 374 VARYAEDAGEREHAQRLVA-LLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALDL 452
Cdd:cd01154 333 AARAFDRAAADKPVEAHMArLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDV 412
|
.
gi 499256869 453 L 453
Cdd:cd01154 413 L 413
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
89-450 |
3.50e-43 |
|
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: 159.56 E-value: 3.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 89 EGGWVGLGGNPEYGGMGMPK-MLGVLFEEMLYAADCSFSLYSALSAGScLAIDAHASEALKATYLPPLYEGRWAGTMCLT 167
Cdd:cd01161 67 ELGLFGLQVPEEYGGLGLNNtQYARLAEIVGMDLGFSVTLGAHQSIGF-KGILLFGTEAQKEKYLPKLASGEWIAAFALT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 168 EPHAGTDLGLIRTRAEPQADGS-VRISGSKIFIT-GGEQDlteniVHLVLAKMP--DAPAGAK-GISLFLVPKflveadg 242
Cdd:cd01161 146 EPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITnGGIAD-----IFTVFAKTEvkDATGSVKdKITAFIVER------- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 243 rlgARNAVHCGSIEHKMGIKASATCVMNFDGA---IGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYA 319
Cdd:cd01161 214 ---SFGGVTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 320 NERLQsraatgpqahdkAADPIIHHGDVRRMLLTMRTLTEAGRAFAVYVGQQLD---VARYAEDAGerehaqrLVALLTP 396
Cdd:cd01161 291 NNRKQ------------FGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDrglKAEYQIEAA-------ISKVFAS 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499256869 397 VAKAFFTDNGLescvlgqQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQAL 450
Cdd:cd01161 352 EAAWLVVDEAI-------QIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
86-459 |
3.11e-40 |
|
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: 150.67 E-value: 3.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 86 TYREGGWVGLGG---NPEYGGMGMPKMLGVLFEEMLYAADCSFSLYSALSAGSCLAIDAHASEALKATYLPPLYEGRWAG 162
Cdd:cd01162 37 VLRKAAELGFGGiyiRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 163 TMCLTEPHAGTDLGLIRTRAEPQADGSVrISGSKIFITG-GEQDlteniVHLVLAKMpdAPAGAKGISLFLVPKflvEAD 241
Cdd:cd01162 117 SYCLTEPGSGSDAAALRTRAVREGDHYV-LNGSKAFISGaGDSD-----VYVVMART--GGEGPKGISCFVVEK---GTP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 242 G-RLGARnavhcgsiEHKMGIKASATCVMNFDGA---IGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAAR 317
Cdd:cd01162 186 GlSFGAN--------EKKMGWNAQPTRAVIFEDCrvpVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 318 YANERlqsRAATGPQAHDKAadpiihhgdVRRMLLTMRTLTEAGRAFAvyvgqqldvaRYAEDAGEREHAQRlvALLTPV 397
Cdd:cd01162 258 YLEER---KQFGKPLADFQA---------LQFKLADMATELVASRLMV----------RRAASALDRGDPDA--VKLCAM 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499256869 398 AKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALdLLGRKVLA 459
Cdd:cd01162 314 AKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIARALLT 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
81-458 |
1.28e-39 |
|
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: 148.80 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 81 REAWNTYREGGWVGLGGNPEYGGMGMP-KMLGVLFEEMLYAADCSFSLYSALSAGSClAIDAHASEALKATYLPPLYEGR 159
Cdd:cd01160 33 REVWRKAGEQGLLGVGFPEEYGGIGGDlLSAAVLWEELARAGGSGPGLSLHTDIVSP-YITRAGSPEQKERVLPQMVAGK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 160 WAGTMCLTEPHAGTDLGLIRTRAEPQADGSVrISGSKIFITGGeqdlTENIVHLVLAKMPDAPAGAKGISLFLVPKflvE 239
Cdd:cd01160 112 KIGAIAMTEPGAGSDLQGIRTTARKDGDHYV-LNGSKTFITNG----MLADVVIVVARTGGEARGAGGISLFLVER---G 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 240 ADGRLGARNAvhcgsieHKMGIKASATCVMNFDGA---IGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAA 316
Cdd:cd01160 184 TPGFSRGRKL-------KKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 317 RYANERlqsraatgpqahdKA-ADPIIHHGDVRRMLLTMRTLTEAGRAFavyvgqqldvaryAEDAGEREHAQRLVALLT 395
Cdd:cd01160 257 NYVKQR-------------KAfGKTLAQLQVVRHKIAELATKVAVTRAF-------------LDNCAWRHEQGRLDVAEA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499256869 396 PVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQaLDLLGRKVL 458
Cdd:cd01160 311 SMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
38-459 |
2.94e-34 |
|
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: 133.69 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 38 DTADAILEEASKVTGQLIAPLsrngdeqgvcfdAGQVTTPEGF-REAWNTYREGGWVGLGGNPEYGGMGMPKMLGVLFEE 116
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPL------------AAKIDRDNEFpRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIME 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 117 MLYAADCSFslysALSAG--SCLAIDA---HASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEPQADGSVr 191
Cdd:cd01156 72 EISRASGSV----ALSYGahSNLCINQiyrNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 192 ISGSKIFITGG-EQDlteniVHLVLAKMpDAPAGAKGISLFLVPKflveadgrlgARNAVHCGSIEHKMGIKASATCVMN 270
Cdd:cd01156 147 LNGSKMWITNGpDAD-----TLVVYAKT-DPSAGAHGITAFIVEK----------GMPGFSRAQKLDKLGMRGSNTCELV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 271 FDGAI---GYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDV 347
Cdd:cd01156 211 FEDCEvpeENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQ------------FGQPIGEFQLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 348 RRMLLTMRTLTEAGRAFAVYVGQQLDvaryaedAGEREHAQRLVALLTPVAKAffTDNGLESCvlgqQVYGGHGYIREWG 427
Cdd:cd01156 279 QGKLADMYTRLNASRSYLYTVAKACD-------RGNMDPKDAAGVILYAAEKA--TQVALDAI----QILGGNGYINDYP 345
|
410 420 430
....*....|....*....|....*....|..
gi 499256869 428 QEQRVRDVRIAQIYEGTNGIQALdLLGRKVLA 459
Cdd:cd01156 346 TGRLLRDAKLYEIGAGTSEIRRM-VIGRELFK 376
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
482-584 |
8.26e-26 |
|
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal region of many bacterial acetyl-CoA dehydrogenases.
Pssm-ID: 463716 Cd Length: 126 Bit Score: 102.63 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 482 HREALQASLARLEATSSWLRAQAGE-DANLVSAVAVEYLQLFGLTAYAYMWARMAAVALAKRDE---DDAFHGAKLACAA 557
Cdd:pfam12806 20 EAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAKLAAgakDAAFYEGKIATAR 99
|
90 100
....*....|....*....|....*..
gi 499256869 558 FYFQRVLPRGLGLEASIRAGSGSLYGL 584
Cdd:pfam12806 100 FFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
102-444 |
1.72e-25 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 108.87 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 102 GGMGMPKMLGVLFEEMLYAADCSFSLysALSAGSCLAIDA---HASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLI 178
Cdd:PTZ00461 92 GGAGMDAVAAVIIHHELSKYDPGFCL--AYLAHSMLFVNNfyySASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGM 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 179 RTRAEPQADGSVRISGSKIFITGGeqdlTENIVHLVLAKMPDApagakgISLFLVPKflveadgrlGARnAVHCGSIEHK 258
Cdd:PTZ00461 170 RTTAKKDSNGNYVLNGSKIWITNG----TVADVFLIYAKVDGK------ITAFVVER---------GTK-GFTQGPKIDK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 259 MGIKASATCVMNFDGAI---GYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERlqsraatgpQAHD 335
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVvpaENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER---------KAFG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 336 KaadPIIHHGDVRRMLLTMRTLTEAGRAFAVYVGQQL---DVARYAEDAGerehaqRLVAllTPVAKAfFTDNGLescvl 412
Cdd:PTZ00461 301 K---PISNFGQIQRYIAEGYADTEAAKALVYSVSHNVhpgNKNRLGSDAA------KLFA--TPIAKK-VADSAI----- 363
|
330 340 350
....*....|....*....|....*....|..
gi 499256869 413 gqQVYGGHGYIREWGQEQRVRDVRIAQIYEGT 444
Cdd:PTZ00461 364 --QVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
95-457 |
2.92e-24 |
|
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: 105.13 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 95 LGGNPE-YGGMGMPKM-LGVLFEEMlYAADCSF-SLYSALSAGSCLAIDAHASEALKATYLPPLYEGRWAGTMCLTEPHA 171
Cdd:cd01151 59 LGATIKgYGCAGLSSVaYGLIAREV-ERVDSGYrSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 172 GTDLGLIRTRAEPQADGsVRISGSKIFITGGeqDLTENIVhlVLAKMpdapAGAKGISLFLVPKflvEADGrLGARnavh 251
Cdd:cd01151 138 GSDPGGMETRARKDGGG-YKLNGSKTWITNS--PIADVFV--VWARN----DETGKIRGFILER---GMKG-LSAP---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 252 cgSIEHKMGIKASATCVMNFDGAigyLVGEPN-----KGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQSR 326
Cdd:cd01151 201 --KIQGKFSLRASITGEIVMDNV---FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 327 AatgpqahdkaadPIIHHGDVRRMLLTMRTLTEAGRAFAVYVGQQLDvaryaedagEREHAQRLVALLtpvaKAFFTDNG 406
Cdd:cd01151 276 R------------PLAAFQLVQKKLADMLTEIALGLLACLRVGRLKD---------QGKATPEQISLL----KRNNCGKA 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499256869 407 LESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALdLLGRKV 457
Cdd:cd01151 331 LEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL-ILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
37-461 |
1.98e-22 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 99.95 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 37 ADTADAILEEASKVTGQLIAPlsrngdeqgvcfDAGQVTTPEGFREAWNTYREGGWVGLGG---NPEYGGMGMPKMLGVL 113
Cdd:PLN02519 27 DDTQLQFKESVQQFAQENIAP------------HAAAIDATNSFPKDVNLWKLMGDFNLHGitaPEEYGGLGLGYLYHCI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 114 FEEMLYAADCSFSL-YSALSAGSCLAIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEpQADGSVRI 192
Cdd:PLN02519 95 AMEEISRASGSVGLsYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAE-RVDGGYVL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 193 SGSKIFITGGEQDLTenivhLVLAKMPDAPAGAKGISLFLVPKflveadGRLGARNAVHCgsieHKMGIKASATCVMNFD 272
Cdd:PLN02519 174 NGNKMWCTNGPVAQT-----LVVYAKTDVAAGSKGITAFIIEK------GMPGFSTAQKL----DKLGMRGSDTCELVFE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 273 GAI---GYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDVRR 349
Cdd:PLN02519 239 NCFvpeENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQ------------FGRPIGEFQFIQG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 350 MLLTMRTLTEAGRAFaVYvgqqlDVARYAeDAGEREHAQRLVALLtpvakaFFTDNGLESCVLGQQVYGGHGYIREWGQE 429
Cdd:PLN02519 307 KLADMYTSLQSSRSY-VY-----SVARDC-DNGKVDRKDCAGVIL------CAAERATQVALQAIQCLGGNGYINEYPTG 373
|
410 420 430
....*....|....*....|....*....|..
gi 499256869 430 QRVRDVRIAQIYEGTNGIQALdLLGRKVLADG 461
Cdd:PLN02519 374 RLLRDAKLYEIGAGTSEIRRM-LIGRELFKEE 404
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
58-460 |
5.74e-22 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 98.26 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 58 LSRNGDEQGV--CFDAGQVttPEGFREAwntYREGGWVGLGGNPEYGGMG---MPKMLgvLFEEM------LYAADCSFS 126
Cdd:PRK12341 20 ITRNFPEEYFrtCDENGTY--PREFMRA---LADNGISMLGVPEEFGGTPadyVTQML--VLEEVskcgapAFLITNGQC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 127 LYSALSAGSclaidahaSEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLIRTRAEpQADGSVRISGSKIFITGGEqdl 206
Cdd:PRK12341 93 IHSMRRFGS--------AEQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITGAK--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 207 tENIVHLVLAKMPDAPAGAKGISLFLVPKflvEADGRlgARNAVHcgsiehKMGIKASATCVMNFDGAI---GYLVGEPN 283
Cdd:PRK12341 161 -EYPYMLVLARDPQPKDPKKAFTLWWVDS---SKPGI--KINPLH------KIGWHMLSTCEVYLDNVEveeSDLVGEEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 284 KGLtaMFTMMNY--ERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqaHDKaadPIIHHGDVRRMLLTMRTLTEAG 361
Cdd:PRK12341 229 MGF--LNVMYNFemERLINAARSLGFAECAFEDAARYANQRIQ---------FGK---PIGHNQLIQEKLTLMAIKIENM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 362 RAFaVYvgqqldvaryaEDAGEREHAQRlVALLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIY 441
Cdd:PRK12341 295 RNM-VY-----------KVAWQADNGQS-LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIG 361
|
410
....*....|....*....
gi 499256869 442 EGTNGIQaLDLLGRKVLAD 460
Cdd:PRK12341 362 GGTDEIM-IYIAGRQILKD 379
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-453 |
3.34e-20 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 94.05 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 164 MCLTEPHAGTDLGLIRTRAEPQADGSVRISGSKIFITGGEQDlteniVHLVLAKMPdapagaKGISLFLVPKFLVEadgr 243
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQAK------GGLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 244 lGARNAVHCGSIEHKMGIKASATCVMNFDGAIGYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERl 323
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 324 qsraatgpQAHDKaadPIIHHGDVRRMLLTMRTLTEAGRAFAvyvgqqLDVARyAEDAGEREHAQRLVALLTPVAKAFFT 403
Cdd:PRK11561 325 --------QVFGK---PLIEQPLMRQVLSRMALQLEGQTALL------FRLAR-AWDRRADAKEALWARLFTPAAKFVIC 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499256869 404 DNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALDLL 453
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
99-458 |
1.47e-19 |
|
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: 90.72 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 99 PE-YGGMGMPKMLGVLFEEMLyAADCSfSLYSALSAGSC--LAIDAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDL 175
Cdd:cd01157 52 PEdCGGLGLGTFDTCLITEEL-AYGCT-GVQTAIEANSLgqMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 176 GLIRTRAEPQADGSVrISGSKIFITGGEQDLTenivHLVLAKM---PDAPAGaKGISlflvpKFLVEADgrlgaRNAVHC 252
Cdd:cd01157 130 AGIKTKAEKKGDEYI-INGQKMWITNGGKANW----YFLLARSdpdPKCPAS-KAFT-----GFIVEAD-----TPGIQP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 253 GSIEHKMGIKASATCVMNFDGAI----GYLVGEPNKGLTAMFTMmNYERLSIGIQGIGCAEASYQSAARYANERlqsraa 328
Cdd:cd01157 194 GRKELNMGQRCSDTRGITFEDVRvpkeNVLIGEGAGFKIAMGAF-DKTRPPVAAGAVGLAQRALDEATKYALER------ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 329 tgpqahDKAADPIIHHGDVRRMLLTMRTLTEAGRAfaVYVGQQLDVaryaeDAGEREhaqrlvALLTPVAKAFFTDNGLE 408
Cdd:cd01157 267 ------KTFGKLIAEHQAVSFMLADMAMKVELARL--AYQRAAWEV-----DSGRRN------TYYASIAKAFAADIANQ 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499256869 409 SCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALdLLGRKVL 458
Cdd:cd01157 328 LATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL-IISREHL 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-452 |
3.51e-19 |
|
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: 84.23 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 283 NKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQsraatgpqahdkAADPIIHHGDVRRMLLTMRTLTEAGR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKA------------FGRPLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 363 AfavyvgqqldvarYAEDAGEREHAQRLVALLTPVAKAFFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDVRIAQIYE 442
Cdd:pfam00441 69 L-------------LVYRAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|
gi 499256869 443 GTNGIQALDL 452
Cdd:pfam00441 136 GTSEIQRNII 145
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
89-458 |
4.72e-17 |
|
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: 83.17 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 89 EGGWVGLGGNPEYGGMGMPKMLGVLFEEMLYAADcsfSLYSALSAGSCLA---IDAHASEALKATYLPPLYEG--RWAgt 163
Cdd:cd01152 46 AAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG---APVPFNQIGIDLAgptILAYGTDEQKRRFLPPILSGeeIWC-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 164 MCLTEPHAGTDLGLIRTRAEPQADGSVrISGSKIFITGGEqdlTENIVHLVLAKMPDAPAgAKGISLFLVPkflVEADGr 243
Cdd:cd01152 121 QGFSEPGAGSDLAGLRTRAVRDGDDWV-VNGQKIWTSGAH---YADWAWLLVRTDPEAPK-HRGISILLVD---MDSPG- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 244 lgarnaVHCGSIEHKMGikASATCVMNFDG---AIGYLVGEPNKGLTAMFTMMNYERLSIGiqgigcaeASYQSAARYAN 320
Cdd:cd01152 192 ------VTVRPIRSING--GEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERVSIG--------GSAATFFELLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 321 ERLQSRAATGPQAHDkaaDPIIHHGDVRrmlLTMRtlteaGRAFAVYVGQqldvARYAEDAGEREHAQrlvallTPVAKA 400
Cdd:cd01152 256 ARLLLLTRDGRPLID---DPLVRQRLAR---LEAE-----AEALRLLVFR----LASALAAGKPPGAE------ASIAKL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499256869 401 FFTDNGLESCVLGQQVYGGHGYIREWGQEQRVRDV--------RIAQIYEGTNGIQaLDLLGRKVL 458
Cdd:cd01152 315 FGSELAQELAELALELLGTAALLRDPAPGAELAGRweadylrsRATTIYGGTSEIQ-RNIIAERLL 379
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
1.95e-15 |
|
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: 71.93 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 163 TMCLTEPHAGTDLGLIRTRAEPQADGSVRISGSKIFITGGeqdlTENIVHLVLAKmPDAPAGAKGISLFLVPKflveadg 242
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNA----GIADLFLVLAR-TGGDDRHGGISLFLVPK------- 68
|
90 100 110
....*....|....*....|....*....|
gi 499256869 243 rlgARNAVHCGSIEHKMGIKASATCVMNFD 272
Cdd:pfam02770 69 ---DAPGVSVRRIETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
38-158 |
8.15e-11 |
|
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: 59.40 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 38 DTADAILEEASKVTGQLIAPLSRNGDEQGvcfdagqvttpEGFREAWNTYREGGWVGLGGNPEYGGMGMPKMLGVLFEEM 117
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEG-----------EFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEE 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499256869 118 LYAADCSFSL-YSALSAGSCLAIDAHASEALKATYLPPLYEG 158
Cdd:pfam02771 71 LARADASVALaLSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
100-460 |
6.38e-09 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 58.30 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 100 EYGGMGMPKM-LGVLFEEMLYAADCSFSLYSaLSAGSCLAIdAHASEALKATYLPPLYEGRWAGTMCLTEPHAGTDLGLI 178
Cdd:PRK03354 59 EHGGLDAGFVtLAAVWMELGRLGAPTYVLYQ-LPGGFNTFL-REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 179 RTRAEpQADGSVRISGSKIFITGGEQdlTENIVhlVLAKmpDAPAGAKGIslflVPKFLVEAdgrlgARNAVHCGSIeHK 258
Cdd:PRK03354 137 KTTYT-RRNGKVYLNGSKCFITSSAY--TPYIV--VMAR--DGASPDKPV----YTEWFVDM-----SKPGIKVTKL-EK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 259 MGIKASATCVMNFDGAI---GYLVGEPNKGLTAMFTMMNYERLSIGIQGIGCAEASYQSAARYANERLQSRAATGPQA-- 333
Cdd:PRK03354 200 LGLRMDSCCEITFDDVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQli 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499256869 334 HDKAADPIIHHGDVRRMLLTmrtlteagrafavyvgqqldvARYAEDAGEREHAQrlvallTPVAKAFFTDNGLESCVLG 413
Cdd:PRK03354 280 QEKFAHMAIKLNSMKNMLYE---------------------AAWKADNGTITSGD------AAMCKYFCANAAFEVVDSA 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 499256869 414 QQVYGGHGYIREWGQEQRVRDVRIAQIYEGTNGIQALDlLGRKVLAD 460
Cdd:PRK03354 333 MQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILT-LGRAVLKQ 378
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-33 |
3.87e-07 |
|
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam02770, pfam00441, pfam02771. This family is one of the enzymes involved in AcylCoA interaction in beta-oxidation.
Pssm-ID: 463571 Cd Length: 32 Bit Score: 46.56 E-value: 3.87e-07
10 20 30
....*....|....*....|....*....|.
gi 499256869 3 TYSAPLRDMRFVLHDVFNASGlWARLPALAE 33
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEA-LAALPGFAD 30
|
|
| |
