|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-596 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 649.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 3 QYNAPLRDMQFVLHELLNVEEVFKELPpHADTNRELVDQVLEEGGKFASQVLFPLNHSGDREGCHYdRESKSVTTPKGFK 82
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLG-KTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVL-LKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 83 QAYQQYVQAGWAALSCDPEFGGQGLPLTINNSFYEMLNSSNQAWTMYPGLSHGAYECLHAHGSDEQKQLYLPKLVSGEWT 162
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 163 GTMCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFISAGENDVSDNIVHLVLARLPDAPEGSKGISLFLVPKFLPNAD 242
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 243 GSLGARNPIFCGAIEEKMGIHGNATCQMNLDGATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKD 322
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 323 RLQMRSLSGIKAADKPADPIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDKELTHPDEQVRKDAADIVALLTPVVKAF 402
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 403 LTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLDLLGRKILMDNGAK-LKKFGAQIQAFVEEHG 481
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGNeVARFGKRVSKLVRAHL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 482 TDE-SMSEFITPLADIGDKVTKLTMEIGMKSFANQDEAGAAAVPYLRVVGHLVFSYLFARMAKIALEKQDSG---DSFYT 557
Cdd:PTZ00456 503 FSRgALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGqdaDGFYQ 582
|
570 580 590
....*....|....*....|....*....|....*....
gi 2543670648 558 AKLATARFYFARLLPETAMLIRQARSGAgNLMALDAALF 596
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAGP-SIMASKEENW 620
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
42-458 |
0e+00 |
|
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: 524.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 42 VLEEGGKFASQVLFPLNHSGDREGCHYDreSKSVTTPKGFKQAYQQYVQAGWAALSCDPEFGGQGLPLTINNSFYEMLnS 121
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFD--DGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 122 SNQAWTMYPGLSHGAYECLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFIS 201
Cdd:cd01153 78 RGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 202 AGENDVSDNIVHLVLARLPDAPEGSKGISLFLVPKFLPNadgslGARNPIFCGAIEEKMGIHGNATCQMNLDGATGWLIG 281
Cdd:cd01153 158 AGEHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 282 QPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQMRSLSgikaADKPADPIIVHPDVRRMLLTAKAFAEG 361
Cdd:cd01153 233 EEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 362 GRAFTSYVALELDKELTHPDEQV-RKDAADIVALLTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINM 440
Cdd:cd01153 309 SRALDLYTATVQDLAERKATEGEdRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITT 388
|
410
....*....|....*...
gi 2543670648 441 IYEGTNTIQSLDLLGRKI 458
Cdd:cd01153 389 IYEGTTGIQALDLIGRKI 406
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
37-463 |
6.95e-115 |
|
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: 347.21 E-value: 6.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 37 ELVDQVLEEGGKFASQVLFPLNHSGDREGcHYDREsksvttpkgfkqAYQQYVQAGWAALSCDPEFGGQGLPLTINNSFY 116
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG-EFPRE------------LWRKLAELGLLGLTIPEEYGGLGLSLVELALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 117 EMLNSSNQAWTMYPGLSHGAYECLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGsYKITGN 196
Cdd:COG1960 74 EELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 197 KIFISAGenDVSDniVHLVLARLPDAPeGSKGISLFLVPKFLPNadgslgarnpIFCGAIEEKMGIHGNATCQMNLDG-- 274
Cdd:COG1960 153 KTFITNA--PVAD--VILVLARTDPAA-GHRGISLFLVPKDTPG----------VTVGRIEDKMGLRGSDTGELFFDDvr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 275 -ATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQmrslsgikaadkPADPIIVHPDVRRMLL 353
Cdd:COG1960 218 vPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 354 TAKAFAEGGRAFTSYVALeldkelthpdeqvRKDAADIVALLTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYV 433
Cdd:COG1960 286 DMAAELEAARALVYRAAW-------------LLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLY 352
|
410 420 430
....*....|....*....|....*....|
gi 2543670648 434 RDARINMIYEGTNTIQSLDlLGRKILMDNG 463
Cdd:COG1960 353 RDARILTIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
140-454 |
1.14e-65 |
|
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: 217.54 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 140 LHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGsYKITGNKIFISAGenDVSDniVHLVLARL 219
Cdd:cd00567 48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG--GDAD--LFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 220 PDAPEGSKGISLFLVPKflpNADGslgarnpIFCGAIEEKMGIHGNATCQMNLDGA---TGWLIGQPHKGLQAMFVFMNA 296
Cdd:cd00567 123 DEEGPGHRGISAFLVPA---DTPG-------VTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 297 ARLGVGMQGLGLTEVAYQNALVYAKDRLQmrslsgikaadkPADPIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDKE 376
Cdd:cd00567 193 GRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQG 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543670648 377 lthpDEQVRKDAAdivalltpVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLDLL 454
Cdd:cd00567 261 ----PDEARLEAA--------MAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
140-454 |
5.17e-54 |
|
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: 189.50 E-value: 5.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 140 LHAHGSDEQKQLYLPKLVSGE---WTGTMCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFISAGENDVsdnivHLVL 216
Cdd:cd01154 123 LRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADA-----ALVL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 217 ARLPDAPEGSKGISLFLVPKFLPNadgslGARNPIFCGAIEEKMGIHGNATCQMNLDGATGWLIGQPHKGLQAMFVFMNA 296
Cdd:cd01154 198 ARPEGAPAGARGLSLFLVPRLLED-----GTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 297 ARLGVGMQGLGLTEVAYQNALVYAKDRlqmrslsgiKAADKPadpIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDKE 376
Cdd:cd01154 273 SRLDNAVAALGIMRRALSEAYHYARHR---------RAFGKP---LIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRA 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543670648 377 lthpdEQVRKDAADIVALLTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLDLL 454
Cdd:cd01154 341 -----AADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVL 413
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
48-451 |
2.59e-51 |
|
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: 180.93 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 48 KFASQVLFPLNHSGDREGcHYDRESksvttpkgFKQAYQQyvqaGWAALSCDPEFGGQGLP------------------- 108
Cdd:cd01158 12 DFAEKEIAPLAAEMDEKG-EFPREV--------IKEMAEL----GLMGIPIPEEYGGAGLDflayaiaieelakvdasva 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 109 --LTINNSFYEMLnssnqawtmypglshgayecLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQ 186
Cdd:cd01158 79 viVSVHNSLGANP--------------------IIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 187 ADgSYKITGNKIFISAGenDVSDniVHLVLARLpDAPEGSKGISLFLVPKflpNADGslgarnpIFCGAIEEKMGIHGNA 266
Cdd:cd01158 139 GD-DYVLNGSKMWITNG--GEAD--FYIVFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 267 TCQMNLDGA---TGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQMrslsgikaadkpADPII 343
Cdd:cd01158 203 TTELIFEDVrvpKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQF------------GKPIA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 344 VHPDVRRMLLTAKAFAEGGRAFTsYVALELdKELTHPdeqVRKDAAdivalltpVVKAFLTDNAWMATSECLQVYGGHGY 423
Cdd:cd01158 271 DFQGIQFKLADMATEIEAARLLT-YKAARL-KDNGEP---FIKEAA--------MAKLFASEVAMRVTTDAVQIFGGYGY 337
|
410 420
....*....|....*....|....*...
gi 2543670648 424 IAEWGMEQYVRDARINMIYEGTNTIQSL 451
Cdd:cd01158 338 TKDYPVERYYRDAKITEIYEGTSEIQRL 365
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
90-459 |
1.01e-39 |
|
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: 149.13 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 90 QAGWAALSCDPEFGGQGLPLTINNSFYEMLNSSNQAWTMYPGLSHGAYECLHAHGSDEQKQLYLPKLVSGEWTGTMCLTE 169
Cdd:cd01162 43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 170 AHCGTDLGLLRSKAEPQADgSYKITGNKIFIS-AGENDVsdnivHLVLARlpDAPEGSKGISLFLVPKFLPNadgslgar 248
Cdd:cd01162 123 PGSGSDAAALRTRAVREGD-HYVLNGSKAFISgAGDSDV-----YVVMAR--TGGEGPKGISCFVVEKGTPG-------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 249 npIFCGAIEEKMGIHGNATCQMNLDGA---TGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGltevAYQNALVYAKDRLQ 325
Cdd:cd01162 187 --LSFGANEKKMGWNAQPTRAVIFEDCrvpVENRLGGEGQGFGIAMAGLNGGRLNIASCSLG----AAQAALDLARAYLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 326 MRSLSGIKAADKPAdpiivhpdVRRMLLTAKAFAEGGRAFTSYVALELDKElthpdeqvRKDAADIVALltpvVKAFLTD 405
Cdd:cd01162 261 ERKQFGKPLADFQA--------LQFKLADMATELVASRLMVRRAASALDRG--------DPDAVKLCAM----AKRFATD 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2543670648 406 NAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLdLLGRKIL 459
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIARALL 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
86-451 |
7.87e-39 |
|
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: 147.61 E-value: 7.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 86 QQYVQAGWAALSCDPEFGGQGLpltiNNSFYEMLnssnqawTMYPGLSHGAYECLHAH-----------GSDEQKQLYLP 154
Cdd:cd01161 63 TQLKELGLFGLQVPEEYGGLGL----NNTQYARL-------AEIVGMDLGFSVTLGAHqsigfkgillfGTEAQKEKYLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 155 KLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGS-YKITGNKIFISAGenDVSDniVHLVLARLPDA-PEGSK--GIS 230
Cdd:cd01161 132 KLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEVKdATGSVkdKIT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 231 LFLVPKflpnadgSLGArnpIFCGAIEEKMGIHGNATCQMNLDGA---TGWLIGQPHKGLQAMFVFMNAARLGVGMQGLG 307
Cdd:cd01161 208 AFIVER-------SFGG---VTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 308 LTEVAYQNALVYAKDRLQMrslsgikaADKPADPIIVHPDVRRMLLTAKAfAEggrAFTSYVALELDKELThPDEQVrkD 387
Cdd:cd01161 278 TMKRCIEKAVDYANNRKQF--------GKKIHEFGLIQEKLANMAILQYA-TE---SMAYMTSGNMDRGLK-AEYQI--E 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543670648 388 AAdivalltpVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSL 451
Cdd:cd01161 343 AA--------ISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
471-591 |
1.05e-36 |
|
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: 133.06 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 471 AQIQAFVEEHGTDESMSEFITPLADIGDKVTKLTMEIGMKSFA-NQDEAGAAAVPYLRVVGHLVFSYLFARMAKIALEKQ 549
Cdd:pfam12806 2 AEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAKL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2543670648 550 DSGDS---FYTAKLATARFYFARLLPETAMLIRQARSGAGNLMAL 591
Cdd:pfam12806 82 AAGAKdaaFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
92-458 |
1.05e-31 |
|
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: 126.37 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 92 GWAALSCDPEFGGQGLPLTINNSFYEMLNSSNQAWtmypGLSHGAYE--C---LHAHGSDEQKQLYLPKLVSGEWTGTMC 166
Cdd:cd01156 46 GLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV----ALSYGAHSnlCinqIYRNGSAAQKEKYLPKLISGEHIGALA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 167 LTEAHCGTDLGLLRSKAEPQaDGSYKITGNKIFISAGendvSDNIVHLVLARlPDAPEGSKGISLFLVPKFLPNadgslg 246
Cdd:cd01156 122 MSEPNAGSDVVSMKLRAEKK-GDRYVLNGSKMWITNG----PDADTLVVYAK-TDPSAGAHGITAFIVEKGMPG------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 247 arnpiFCGAIE-EKMGIHGNATCQM---NLDGATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKD 322
Cdd:cd01156 190 -----FSRAQKlDKLGMRGSNTCELvfeDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 323 RLQMrslsGIKAAD------KPADpiivhpdvrrMLLTAKAfaegGRAFTSYVALELDKelthpDEQVRKDAADIVallt 396
Cdd:cd01156 265 RKQF----GQPIGEfqlvqgKLAD----------MYTRLNA----SRSYLYTVAKACDR-----GNMDPKDAAGVI---- 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2543670648 397 pvvkAFLTDNA-WMATsECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLdLLGRKI 458
Cdd:cd01156 318 ----LYAAEKAtQVAL-DAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM-VIGREL 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
143-459 |
1.37e-31 |
|
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: 126.08 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 143 HGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAepQADGS-YKITGNKIFISAGEndVSDniVHLVLARLPD 221
Cdd:cd01160 94 AGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTA--RKDGDhYVLNGSKTFITNGM--LAD--VVIVVARTGG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 222 APEGSKGISLFLVPKflpNADGSLGARNPifcgaieEKMGIHGNATCQMNLDGA---TGWLIGQPHKGLQAMFVFMNAAR 298
Cdd:cd01160 168 EARGAGGISLFLVER---GTPGFSRGRKL-------KKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQER 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 299 LGVGMQGLGLTEVAYQNALVYAKDRlqmrslsgiKAADKPadpIIVHPDVRRMLLTAKAFAEGGRAFtsyvaleLDKELT 378
Cdd:cd01160 238 LLIAAGALAAAEFMLEETRNYVKQR---------KAFGKT---LAQLQVVRHKIAELATKVAVTRAF-------LDNCAW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 379 HpDEQVRKDAADIValltpVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQsLDLLGRKI 458
Cdd:cd01160 299 R-HEQGRLDVAEAS-----MAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQM 371
|
.
gi 2543670648 459 L 459
Cdd:cd01160 372 V 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
101-461 |
1.14e-23 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 103.42 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 101 EFGGQGLPLTINNSFYEMLNSSNQAwtmyPGLSHGAYE--CLHA---HGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTD 175
Cdd:PLN02519 81 EYGGLGLGYLYHCIAMEEISRASGS----VGLSYGAHSnlCINQlvrNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 176 LGLLRSKAEpQADGSYKITGNKIFISAGEndVSDNIVhlVLARlPDAPEGSKGISLFLVPKFLPNadgslgarnpiFCGA 255
Cdd:PLN02519 157 VVSMKCKAE-RVDGGYVLNGNKMWCTNGP--VAQTLV--VYAK-TDVAAGSKGITAFIIEKGMPG-----------FSTA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 256 IE-EKMGIHGNATCQM---NLDGATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQMrslsg 331
Cdd:PLN02519 220 QKlDKLGMRGSDTCELvfeNCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQF----- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 332 ikaadkpADPIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDKelTHPDeqvRKDAADIValltpvvkAFLTDNAWMAT 411
Cdd:PLN02519 295 -------GRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN--GKVD---RKDCAGVI--------LCAAERATQVA 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2543670648 412 SECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLdLLGRKILMD 461
Cdd:PLN02519 355 LQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGRELFKE 403
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
127-458 |
2.25e-23 |
|
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: 102.44 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 127 TMYPglshgayecLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGsYKITGNKIFIsaGEND 206
Cdd:cd01151 101 VMLP---------IYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKTWI--TNSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 207 VSDNIVhlVLARLpdapEGSKGISLFLVPKflpnadGSLGARNPifcgAIEEKMGIHGNATCQMNLDGAtgwLIGQ---- 282
Cdd:cd01151 169 IADVFV--VWARN----DETGKIRGFILER------GMKGLSAP----KIQGKFSLRASITGEIVMDNV---FVPEenll 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 283 PH-KGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQM-RSLSGIK-AADKPADPIIvhpDVRRMLLTA---- 355
Cdd:cd01151 230 PGaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFgRPLAAFQlVQKKLADMLT---EIALGLLAClrvg 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 356 KAFAEGgraftsyvaleldkelthpdeqvrKDAADIVALLtpvvKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRD 435
Cdd:cd01151 307 RLKDQG------------------------KATPEQISLL----KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVN 358
|
330 340
....*....|....*....|...
gi 2543670648 436 ARINMIYEGTNTIQSLdLLGRKI 458
Cdd:cd01151 359 LESVNTYEGTHDIHAL-ILGRAI 380
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
165-454 |
5.97e-23 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 102.91 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 165 MCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFISAGENDVsdnivHLVLARLPdapegsKGISLFLVPKFLPNadgs 244
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDA-----HLVLAQAK------GGLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 245 lGARNPIFCGAIEEKMGIHGNATCQMNLDGATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRL 324
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 325 QMrslsgikaadkpADPIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDKElTHPDEQVRkdaadiVALLTPVVKAFLT 404
Cdd:PRK11561 326 VF------------GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRR-ADAKEALW------ARLFTPAAKFVIC 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2543670648 405 DNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLDLL 454
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
284-458 |
5.48e-21 |
|
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: 89.62 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 284 HKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRlqmrslsgiKAADKPadpIIVHPDVRRMLLTAKAFAEGGR 363
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRR---------KAFGRP---LIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 364 AFTSYVALELDKELTHPDEqvrkdaadivallTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYE 443
Cdd:pfam00441 69 LLVYRAAEALDAGGPDGAE-------------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|....*
gi 2543670648 444 GTNTIQsLDLLGRKI 458
Cdd:pfam00441 136 GTSEIQ-RNIIARRL 149
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
145-445 |
3.43e-20 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 93.08 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 145 SDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFISAGEndVSDniVHLVLARLpdapE 224
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGT--VAD--VFLIYAKV----D 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 225 GSkgISLFLVPKFLPNadgslgarnpIFCGAIEEKMGIHGNATCQMNLD----GATGwLIGQPHKGLQAMFVFMNAARLG 300
Cdd:PTZ00461 207 GK--ITAFVVERGTKG----------FTQGPKIDKCGMRASHMCQLFFEdvvvPAEN-LLGEEGKGMVGMMRNLELERVT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 301 VGMQGLGLTEVAYQNALVYAKDRlqmrslsgiKAADKpadPIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELdkeltHP 380
Cdd:PTZ00461 274 LAAMAVGIAERSVELMTSYASER---------KAFGK---PISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-----HP 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2543670648 381 DEQVR--KDAADIVAllTPVVKAfLTDNAwmatsecLQVYGGHGYIAEWGMEQYVRDARINMIYEGT 445
Cdd:PTZ00461 337 GNKNRlgSDAAKLFA--TPIAKK-VADSA-------IQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
144-451 |
2.03e-17 |
|
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: 84.17 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 144 GSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEPQADgSYKITGNKIFISAGendvSDNIVHLVLARL---P 220
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNG----GKANWYFLLARSdpdP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 221 DAPeGSKGISLFLVPKFLPNadgslgarnpIFCGAIEEKMGIHGNATCQMNLDG----ATGWLIGqPHKGLQ-AMFVFmN 295
Cdd:cd01157 172 KCP-ASKAFTGFIVEADTPG----------IQPGRKELNMGQRCSDTRGITFEDvrvpKENVLIG-EGAGFKiAMGAF-D 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 296 AARLGVGMQGLGLTEVAYQNALVYAKDRlqmrslsgiKAADKPadpIIVHPDVRRMLLTAKAFAEGGRAFTSYVALELDk 375
Cdd:cd01157 239 KTRPPVAAGAVGLAQRALDEATKYALER---------KTFGKL---IAEHQAVSFMLADMAMKVELARLAYQRAAWEVD- 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2543670648 376 elthpdeQVRKDAadivaLLTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSL 451
Cdd:cd01157 306 -------SGRRNT-----YYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
78-461 |
6.50e-16 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 79.77 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 78 PKGFKQAYqqyVQAGWAALSCDPEFGGQGLPLTInnsfyEMLNSSNQAWTMYPGLSHGAYECLH---AHGSDEQ-KQLYL 153
Cdd:PRK12341 39 PREFMRAL---ADNGISMLGVPEEFGGTPADYVT-----QMLVLEEVSKCGAPAFLITNGQCIHsmrRFGSAEQlRKTAE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 154 PKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEpQADGSYKITGNKIFIS-AGENDVSdnivhLVLARLPDAPEGSKGISLF 232
Cdd:PRK12341 111 STLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITgAKEYPYM-----LVLARDPQPKDPKKAFTLW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 233 LVPkflPNADGSlgARNPIfcgaieEKMGIHGNATCQMNLDGAT---GWLIGQPHKG-LQAMFVFmNAARLGVGMQGLGL 308
Cdd:PRK12341 185 WVD---SSKPGI--KINPL------HKIGWHMLSTCEVYLDNVEveeSDLVGEEGMGfLNVMYNF-EMERLINAARSLGF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 309 TEVAYQNALVYAKDRLQMrslsgikaaDKPadpiIVHPDVRRMLLTAKAFA-EGGRAFTSYVALELDKELThpdeqVRKD 387
Cdd:PRK12341 253 AECAFEDAARYANQRIQF---------GKP----IGHNQLIQEKLTLMAIKiENMRNMVYKVAWQADNGQS-----LRTS 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2543670648 388 AAdivalltpVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQsLDLLGRKILMD 461
Cdd:PRK12341 315 AA--------LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRQILKD 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
91-459 |
3.44e-14 |
|
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: 74.31 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 91 AGWAALSCDPEFGGQGLPLT----INNSFYE--MLNSSNQAWTMYPGLShgayecLHAHGSDEQKQLYLPKLVSGE--Wt 162
Cdd:cd01152 47 AGWAAPGWPKEYGGRGASLMeqliFREEMAAagAPVPFNQIGIDLAGPT------ILAYGTDEQKRRFLPPILSGEeiW- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 163 gtmCL--TEAHCGTDLGLLRSKAEPQADGsYKITGNKIFISAGEndVSDNivHLVLARL-PDAPEgSKGISLFLVPKflp 239
Cdd:cd01152 120 ---CQgfSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH--YADW--AWLLVRTdPEAPK-HRGISILLVDM--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 240 NADGSlgARNPifcgaIEEKMGIHGnaTCQMNLD----------GAT--GWLIGQPHKGLQAMFVFMNAARLGVGMQGLG 307
Cdd:cd01152 188 DSPGV--TVRP-----IRSINGGEF--FNEVFLDdvrvpdanrvGEVndGWKVAMTTLNFERVSIGGSAATFFELLLARL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 308 LTEVAYQNALVyaKDRLQMRSLSGIkAADKPADPIIVHPDVRRMLLTAKAFAEGgrAFTSYVALELDKELthpdeqvrkd 387
Cdd:cd01152 259 LLLTRDGRPLI--DDPLVRQRLARL-EAEAEALRLLVFRLASALAAGKPPGAEA--SIAKLFGSELAQEL---------- 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2543670648 388 AADIVALLTPvvKAFLTDNAWMATSEclqvygghgyiAEWgmEQYVRDARINMIYEGTNTIQsLDLLGRKIL 459
Cdd:cd01152 324 AELALELLGT--AALLRDPAPGAELA-----------GRW--EADYLRSRATTIYGGTSEIQ-RNIIAERLL 379
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
164-273 |
8.96e-14 |
|
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: 67.31 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 164 TMCLTEAHCGTDLGLLRSKAEPQADGSYKITGNKIFIS-AGENDvsdniVHLVLARlPDAPEGSKGISLFLVPKFLPNad 242
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIAD-----LFLVLAR-TGGDDRHGGISLFLVPKDAPG-- 72
|
90 100 110
....*....|....*....|....*....|.
gi 2543670648 243 gslgarnpIFCGAIEEKMGIHGNATCQMNLD 273
Cdd:pfam02770 73 --------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
139-476 |
9.01e-11 |
|
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: 64.66 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 139 CLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKA--EPQAD----GSYKITGNKIFIsaGENDVSDNIV 212
Cdd:cd01150 112 AIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQefviNTPDFTATKWWP--GNLGKTATHA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 213 hLVLARL--PDAPEGSKGislFLVPKFLPNADGSLGArnpIFCGAIEEKMGIHG-------------------NATCQMN 271
Cdd:cd01150 190 -VVFAQLitPGKNHGLHA---FIVPIRDPKTHQPLPG---VTVGDIGPKMGLNGvdngflqfrnvriprenllNRFGDVS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 272 LDGATGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQmrslSGIKAADkPADPIIVHPDVRRM 351
Cdd:cd01150 263 PDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ----FGPKPSD-PEVQILDYQLQQYR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 352 LLTAKAFAEGGRAFTSYVA---LELDKELTHPDEQVrkdAADIVALlTPVVKAFLTDNAWMATSECLQVYGGHGYIAEWG 428
Cdd:cd01150 338 LFPQLAAAYAFHFAAKSLVemyHEIIKELLQGNSEL---LAELHAL-SAGLKAVATWTAAQGIQECREACGGHGYLAMNR 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2543670648 429 MEQYVRDARINMIYEGTNTIqsLDLLGRKILMDNGAKLKKFGAQIQAF 476
Cdd:cd01150 414 LPTLRDDNDPFCTYEGDNTV--LLQQTANYLLKKYAQAFSLADYLEAY 459
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-35 |
1.41e-09 |
|
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: 53.50 E-value: 1.41e-09
10 20 30
....*....|....*....|....*....|...
gi 2543670648 3 QYNAPLRDMQFVLHELLNVEEVFKeLPPHADTN 35
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEALAA-LPGFADAD 32
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
36-160 |
3.19e-09 |
|
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: 54.78 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 36 RELVDQVLEeggkFASQVLFPLNHSGDREGcHYDREsksvttpkgfkqAYQQYVQAGWAALSCDPEFGGQGLPLTINNSF 115
Cdd:pfam02771 5 EALRDTVRE----FAEEEIAPHAAEWDEEG-EFPRE------------LWKKLGELGLLGITIPEEYGGAGLDYLAYALV 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2543670648 116 YEMLNSSNQAWTMYPGLSHGAY-ECLHAHGSDEQKQLYLPKLVSGE 160
Cdd:pfam02771 68 AEELARADASVALALSVHSSLGaPPILRFGTEEQKERYLPKLASGE 113
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
101-461 |
1.81e-07 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 53.68 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 101 EFGGQGLPLTINNSFYEMLNSSNQAWTMYPGLSHGaYECLHAHGSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLR 180
Cdd:PRK03354 59 EHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG-FNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 181 SKAEpQADGSYKITGNKIFISAGENdvSDNIVhlVLARLPDAPEgsKGI-SLFLVPKFLPNAdgslgARNPIfcgaieEK 259
Cdd:PRK03354 138 TTYT-RRNGKVYLNGSKCFITSSAY--TPYIV--VMARDGASPD--KPVyTEWFVDMSKPGI-----KVTKL------EK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 260 MGIHGNATCQMNLDGA---TGWLIGQPHKGLQAMFVFMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQMRSLSGIKA-- 334
Cdd:PRK03354 200 LGLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQli 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 335 ADKPADPIIVHPDVRRMLLTAKAFAEGGraftsyvaleldkELThpdeqvRKDAAdivalltpVVKAFLTDNAWMATSEC 414
Cdd:PRK03354 280 QEKFAHMAIKLNSMKNMLYEAAWKADNG-------------TIT------SGDAA--------MCKYFCANAAFEVVDSA 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2543670648 415 LQVYGGHGYIAEWGMEQYVRDARINMIYEGTNTIQSLDlLGRKILMD 461
Cdd:PRK03354 333 MQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILT-LGRAVLKQ 378
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
144-325 |
9.47e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 41.76 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 144 GSDEQKQLYLPKLVSGEWTGTMCLTEAHCGTDLGLLRSKAEpQADGSYKITGNKIFIsaGENDVSDniVHLVLARLPDap 223
Cdd:PLN02526 125 GSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI--GNSTFAD--VLVIFARNTT-- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 224 egSKGISLFLVPKflpnadGSLGARnpifCGAIEEKMGIH--GNATCQMN---------LDGATGWligqphkglQAMFV 292
Cdd:PLN02526 198 --TNQINGFIVKK------GAPGLK----ATKIENKIGLRmvQNGDIVLKdvfvpdedrLPGVNSF---------QDTNK 256
|
170 180 190
....*....|....*....|....*....|...
gi 2543670648 293 FMNAARLGVGMQGLGLTEVAYQNALVYAKDRLQ 325
Cdd:PLN02526 257 VLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQ 289
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
300-446 |
1.41e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 39.25 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 300 GVGMQGLGLTEVAYQNALVYAKDRLQMRSlsGIKAADKPAdpiiVHPDVRRM---LLTAKAFAEggRAFTSYVALELDKe 376
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRAYF--GVPLAEDPA----TQLALAEAaarIDAARLLLE--RAAARIEAAAAAG- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543670648 377 lTHPDEQVRKDAAdivalltpVVKAFLTDNAWMATSECLQVYGGHGYIAEWGMEQYVRDARINMIYEGTN 446
Cdd:pfam08028 72 -KPVTPALRAEAR--------RAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| |
