|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
6-402 |
0e+00 |
|
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: 610.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 6 ARAKDYIERTKAFIAQEIEPIEAEFwvevHELNQGGDWTKWQWPSQLEQLKAKAKAAGLWNMFLPCPELGQGLSVQEYAH 85
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEF----LEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 86 IAELSGRSLIAPTVFNCNAPDSGNMEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAVASSDATNMQATAVIDGDEIV 165
Cdd:cd01155 77 LAEETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 166 LNGRKWWSSGLGDPNAKIIIFMAHTPDESKDRHHQHSMVLVPVDTAGVKIERMLPVFGDYDAPHGHGEVSFDNVRVPVAN 245
Cdd:cd01155 157 INGRKWWSSGAGDPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHGHAEITFDNVRVPASN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 246 FIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAA 325
Cdd:cd01155 237 LILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2184264920 326 YKMDTLGNMAALTEISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAKLEL 402
Cdd:cd01155 317 HMIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMEL 393
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
2-402 |
7.17e-161 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 473.13 E-value: 7.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 2 FELSARAKDYIERTKAFIAQEIEPIEAEFWVEVHELNqggdwtKWQWPSQLEQLKAKAKAAGLWNMFLPCPE-------- 73
Cdd:PLN02876 400 FVPSEKVLELRKKLIKFMEDHIYPMENEFYKLAQSSS------RWTVHPEEERLKELAKKEGLWNLWIPLDSaararkll 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 74 ----------------LGQGLSVQEYAHIAELSGRSLIAPTVFNCNAPDSGNMEVLWRYGSEAQKQEWLTPLLEGKIRSV 137
Cdd:PLN02876 474 fednkhmvsgdsadqlLGAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSG 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 138 FCMTEPAVASSDATNMQATAVIDGDEIVLNGRKWWSSGLGDPNAKIIIFMAHTpDESKDRHHQHSMVLVPVDTAGVKIER 217
Cdd:PLN02876 554 FAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKT-DFNAPKHKQQSMILVDIQTPGVQIKR 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 218 MLPVFGDYDAPHGHGEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEI 297
Cdd:PLN02876 633 PLLVFGFDDAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLI 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 298 LKLGGNLERVAEARVAIDQARLLTLYAAYKMDTLGNMAALTEISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFF 377
Cdd:PLN02876 713 AQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLW 792
|
410 420
....*....|....*....|....*
gi 2184264920 378 AQARSLRLADGPDEVHKGMIAKLEL 402
Cdd:PLN02876 793 ATARTLRIADGPDEVHLGTIAKLEL 817
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
2-406 |
3.30e-108 |
|
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: 323.72 E-value: 3.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 2 FELSARAKDYIERTKAFIAQEIEPIEAEFWvevhelnQGGDWTKwqwpsqleQLKAKAKAAGLWNMFLPcPEL-GQGLSV 80
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWD-------REGEFPR--------ELWRKLAELGLLGLTIP-EEYgGLGLSL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 81 QEYAHIAELSGRSLiAPTVFNCNAPDsGNMEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVID 160
Cdd:COG1960 67 VELALVLEELARAD-ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 161 GDEIVLNGRKWWSSGLgdPNAKIIIFMAHTPDEskDRHHQHSMVLVPVDTAGVKIERMLPVFGDYdaPHGHGEVSFDNVR 240
Cdd:COG1960 144 GDGYVLNGQKTFITNA--PVADVILVLARTDPA--AGHRGISLFLVPKDTPGVTVGRIEDKMGLR--GSDTGELFFDDVR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 241 VPVANFIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLL 320
Cdd:COG1960 218 VPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 321 TLYAAYKMDTlgNMAALTEISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAKL 400
Cdd:COG1960 298 VYRAAWLLDA--GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARR 375
|
....*.
gi 2184264920 401 ELAKRG 406
Cdd:COG1960 376 LLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
108-399 |
3.75e-89 |
|
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: 273.01 E-value: 3.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 108 GNMEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSGLGDpnAKIIIFM 187
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD--ADLFIVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 188 AHTpDESKDRHHQHSMVLVPVDTAGVKIERMLPVFGDydAPHGHGEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIH 267
Cdd:cd00567 120 ART-DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGM--RGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 268 HCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTlGNMAALTEISAIKVVA 347
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2184264920 348 PSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:cd00567 276 TEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
113-399 |
9.77e-49 |
|
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: 169.76 E-value: 9.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 113 LWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSGLGDpnAKIIIFMAHTpD 192
Cdd:cd01158 92 IIKFGTEEQKKKYLPPLATGEKIGAFALSEPG-AGSDAAALKTTAKKDGDDYVLNGSKMWITNGGE--ADFYIVFAVT-D 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 193 ESKdRHHQHSMVLVPVDTAGVKIERMLPVFGDYDAPHGhgEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMRC 272
Cdd:cd01158 168 PSK-GYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTT--ELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 273 IGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDtlgNMAALTEISAI-KVVAPSVL 351
Cdd:cd01158 245 LGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKD---NGEPFIKEAAMaKLFASEVA 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2184264920 352 EKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:cd01158 322 MRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK 369
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
58-406 |
2.06e-40 |
|
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: 148.39 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 58 KAKAAGLWNMFLPcPEL-GQGLSVQEYAHIAELSGRSLIAPTVFNCNApDSGNMEVLWrYGSEAQKQEWLTPLLEGKIRS 136
Cdd:cd01161 64 QLKELGLFGLQVP-EEYgGLGLNNTQYARLAEIVGMDLGFSVTLGAHQ-SIGFKGILL-FGTEAQKEKYLPKLASGEWIA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 137 VFCMTEPAvASSDATNMQATAVI--DGDEIVLNGRKWWSSGLGdpNAKIIIFMAHTP--DESKDRHHQHSMVLVPVDTAG 212
Cdd:cd01161 141 AFALTEPS-SGSDAASIRTTAVLseDGKHYVLNGSKIWITNGG--IADIFTVFAKTEvkDATGSVKDKITAFIVERSFGG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 213 VKI---ERMLPVFGDYDAphghgEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMS 289
Cdd:cd01161 218 VTNgppEKKMGIKGSNTA-----EVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 290 RTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTLGNMAALTEISAIKVVAPSVLEKVVDMAMQIHGGAGVSR 369
Cdd:cd01161 293 RKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMR 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 2184264920 370 DTPLTGFFAQARSLRLADGPDEVHKGMIAKLELAKRG 406
Cdd:cd01161 373 EYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
115-404 |
2.27e-37 |
|
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: 139.50 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 115 RYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSGLGDPNakIIIFMAHTPDES 194
Cdd:cd01162 95 SFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD--VYVVMARTGGEG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 195 KdrhHQHSMVLVPVDTAGVKiermlpvFGDYDAPHG-HGE----VSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHC 269
Cdd:cd01162 172 P---KGISCFVVEKGTPGLS-------FGANEKKMGwNAQptraVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 270 MRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTlGNMAALTEISAIKVVAPS 349
Cdd:cd01162 242 SCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATD 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2184264920 350 VLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAKLELAK 404
Cdd:cd01162 321 ECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
110-399 |
1.46e-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: 134.55 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 110 MEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWW-SSGLgdpNAKIIIFMA 188
Cdd:cd01160 88 SPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFiTNGM---LADVVIVVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 189 HTPDESKDrHHQHSMVLVPVDTAGVKIERMLPVFGDYdaPHGHGEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHH 268
Cdd:cd01160 164 RTGGEARG-AGGISLFLVERGTPGFSRGRKLKKMGWK--AQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 269 CMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAE--ARVAIDQA---RLLTLYAAYKMDTlgnmaalTEISAI 343
Cdd:cd01160 241 AAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAElaTKVAVTRAfldNCAWRHEQGRLDV-------AEASMA 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2184264920 344 KVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:cd01160 314 KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
251-399 |
1.56e-34 |
|
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: 125.44 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 251 GQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDT 330
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2184264920 331 LGNMAAltEISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:pfam00441 81 GGPDGA--EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
48-399 |
4.02e-32 |
|
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: 125.15 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 48 WPSQLEQLK---AKAKAAGLWNMFLPCPELGQGLSVQEYAHIAELSGRSLiAPTVFNCNAPDS-GNmeVLWRYGSEAQKQ 123
Cdd:cd01152 30 YREGREDRRrwqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG-APVPFNQIGIDLaGP--TILAYGTDEQKR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 124 EWLTPLLEGKIRsvFCM--TEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSGLgdPNAKIIIFMAHTPDESKdRHHQH 201
Cdd:cd01152 107 RFLPPILSGEEI--WCQgfSEPG-AGSDLAGLRTRAVRDGDDWVVNGQKIWTSGA--HYADWAWLLVRTDPEAP-KHRGI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 202 SMVLVPVDTAGVKIERMLPVfgdyDAPHGHGEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHcmrcIGAAEKSLE 281
Cdd:cd01152 181 SILLVDMDSPGVTVRPIRSI----NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSI----GGSAATFFE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 282 LMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTLGNMAAltEISAIKVVAPSVLEKVVDMAMQI 361
Cdd:cd01152 253 LLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGA--EASIAKLFGSELAQELAELALEL 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2184264920 362 HGGAGVSRDTPLTGFFA--------QARSLRLADGPDEVHKGMIAK 399
Cdd:cd01152 331 LGTAALLRDPAPGAELAgrweadylRSRATTIYGGTSEIQRNIIAE 376
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
4-404 |
1.13e-26 |
|
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: 109.98 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 4 LSARAKDYIERTKAFIAQEIEPIEAEFwvevhelNQGGDWTkwqWPsqleqLKAKAKAAGLWNMFLPCPELGQGLSVQEY 83
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEY-------DKSGEYP---WP-----LIKRAWELGLMNTHIPEDCGGLGLGTFDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 84 AHIAElsgrsliaPTVFNCN-------APDSGNMEVLWRyGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQAT 156
Cdd:cd01157 66 CLITE--------ELAYGCTgvqtaieANSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 157 AVIDGDEIVLNGRKWWSSGLGdpNAKIIIFMAHT-PDESKDRHHQHSMVLVPVDTAGVKIERMLPVFGDyDAPHGHGeVS 235
Cdd:cd01157 136 AEKKGDEYIINGQKMWITNGG--KANWYFLLARSdPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQ-RCSDTRG-IT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 236 FDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAID 315
Cdd:cd01157 212 FEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 316 QARLLTLYAAYKMDTLGNMAALTEISaiKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKG 395
Cdd:cd01157 292 LARLAYQRAAWEVDSGRRNTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
....*....
gi 2184264920 396 MIAKLELAK 404
Cdd:cd01157 370 IISREHLGK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
118-399 |
6.51e-25 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 105.40 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 118 SEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDE-IVLNGRKWWSSG---------LGDPNAKIIIFM 187
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNGnYVLNGSKIWITNgtvadvfliYAKVDGKITAFV 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 188 AhtpdeskDRHHQHSMVLVPVDTAGVKIERMLPVFgdydaphghgevsFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIH 267
Cdd:PTZ00461 214 V-------ERGTKGFTQGPKIDKCGMRASHMCQLF-------------FEDVVVPAENLLGEEGKGMVGMMRNLELERVT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 268 HCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTlYAAYKMDTLGNMAALTEiSAIKVVA 347
Cdd:PTZ00461 274 LAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALV-YSVSHNVHPGNKNRLGS-DAAKLFA 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2184264920 348 PSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:PTZ00461 352 TPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
113-399 |
5.13e-24 |
|
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: 102.49 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 113 LWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWW-SSGlgdPNAKIIIFMAHTp 191
Cdd:cd01156 95 IYRNGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKMWiTNG---PDADTLVVYAKT- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 192 dESKDRHHQHSMVLVPVDTAGVKIERMLPVFGDYDAPhgHGEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMR 271
Cdd:cd01156 170 -DPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSN--TCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 272 CIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTlGNMAALTEISAIKVVAPSVl 351
Cdd:cd01156 247 PIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR-GNMDPKDAAGVILYAAEKA- 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2184264920 352 EKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAK 399
Cdd:cd01156 325 TQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGR 372
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
115-397 |
1.78e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 100.96 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 115 RYGSEAQKQEWLTPLLE-GKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSGLGdpNAKIIIFMAHTPdE 193
Cdd:PRK12341 98 RFGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTYTRKNGKVYLNGQKTFITGAK--EYPYMLVLARDP-Q 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 194 SKDRHHQHSMVLVPVDTAGVKIE-------RMLPVFgdydaphghgEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRI 266
Cdd:PRK12341 174 PKDPKKAFTLWWVDSSKPGIKINplhkigwHMLSTC----------EVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 267 HHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMD---TLGNMAALTEIsai 343
Cdd:PRK12341 244 INAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADngqSLRTSAALAKL--- 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2184264920 344 kVVAPSVLEkVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVhkgMI 397
Cdd:PRK12341 321 -YCARTAME-VIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI---MI 369
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
110-393 |
8.66e-22 |
|
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: 96.27 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 110 MEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSglGDPNAKIIIFMAH 189
Cdd:cd01151 102 MLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRARKDGGGYKLNGSKTWIT--NSPIADVFVVWAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 190 TPDESKDRHhqhsmVLVPVDTAGVKIERMLPVFGDYDAPHGHgeVSFDNVRVPVANFIGGAgQGFEIAQGRLGPGRIHHC 269
Cdd:cd01151 179 NDETGKIRG-----FILERGMKGLSAPKIQGKFSLRASITGE--IVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 270 MRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTlGNMAAlTEISAIKVVAPS 349
Cdd:cd01151 251 WGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQ-GKATP-EQISLLKRNNCG 328
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2184264920 350 VLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVH 393
Cdd:cd01151 329 KALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH 372
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
138-237 |
6.00e-21 |
|
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: 86.57 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 138 FCMTEPAvASSDATNMQATAVI-DGDEIVLNGRKWWSSGLGDPNAKIIIFMAHTPdeskDRHHQHSMVLVPVDTAGVKIE 216
Cdd:pfam02770 2 FALTEPG-AGSDVASLKTTAADgDGGGWVLNGTKWWITNAGIADLFLVLARTGGD----DRHGGISLFLVPKDAPGVSVR 76
|
90 100
....*....|....*....|.
gi 2184264920 217 RMLPVFGdYDApHGHGEVSFD 237
Cdd:pfam02770 77 RIETKLG-VRG-LPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
63-392 |
1.88e-16 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 80.26 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 63 GLWNMFLPCPELGQGLSVQEYAHIAELSGRsLIAPTVFNCNAPdsGNMEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTE 142
Cdd:PRK03354 50 GIDSLLIPEEHGGLDAGFVTLAAVWMELGR-LGAPTYVLYQLP--GGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 143 PAvASSDATNMQATAVIDGDEIVLNGRKWW-SSGLGDPnakIIIFMAHtpDESKDRHHQHSMVLVPVDTAGVKIERmLPV 221
Cdd:PRK03354 127 PG-AGSDVGSLKTTYTRRNGKVYLNGSKCFiTSSAYTP---YIVVMAR--DGASPDKPVYTEWFVDMSKPGIKVTK-LEK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 222 FG---DYDAphghgEVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEIL 298
Cdd:PRK03354 200 LGlrmDSCC-----EITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 299 KLGGNLERVAEARVAIDQARLLTLYAAYKMDTlGNMAAlTEISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFA 378
Cdd:PRK03354 275 RFQLIQEKFAHMAIKLNSMKNMLYEAAWKADN-GTITS-GDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWR 352
|
330
....*....|....
gi 2184264920 379 QARSLRLADGPDEV 392
Cdd:PRK03354 353 DLRVDRVSGGSDEM 366
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
113-392 |
1.77e-14 |
|
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: 74.71 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 113 LWRYGSEAQKQeWLTPLLEGKIR----SVFCMTEPAVASSDATNMQATAVIDGDEIVLNGRKWWSSGlgdPNAKIIIFMA 188
Cdd:cd01154 123 LRKYGPEELKQ-YLPGLLSDRYKtgllGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASA---PLADAALVLA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 189 HTPDeSKDRHHQHSMVLVP-VDTAG----VKIERMLPVFGDYDAPHGhgEVSFDNVrvpVANFIGGAGQGFEIAQGRLGP 263
Cdd:cd01154 199 RPEG-APAGARGLSLFLVPrLLEDGtrngYRIRRLKDKLGTRSVATG--EVEFDDA---EAYLIGDEGKGIYYILEMLNI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 264 GRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAykmDTLGNMAALTEISA- 342
Cdd:cd01154 273 SRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAA---RAFDRAAADKPVEAh 349
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2184264920 343 --------IKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEV 392
Cdd:cd01154 350 marlatpvAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
49-388 |
2.12e-14 |
|
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: 74.35 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 49 PSQLEQLKAKAKAaGLWNMFLPCPELGQGLSVQEYAHIAELSGRSlIAPTVFNCNApdSGNMEVLWRYGSEAQKQEWLTP 128
Cdd:cd01153 36 PPFKEALDAFAEA-GWMALGVPEEYGGQGLPITVYSALAEIFSRG-DAPLMYASGT--QGAAATLLAHGTEAQREKWIPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 129 LLEGKIRSVFCMTEPAvASSDATNMQATAVIDGD-EIVLNGRKWW-SSGLGDPNAKII-IFMAHTPDESKDRHHQhSMVL 205
Cdd:cd01153 112 LAEGEWTGTMCLTEPD-AGSDLGALRTKAVYQADgSWRINGVKRFiSAGEHDMSENIVhLVLARSEGAPPGVKGL-SLFL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 206 VP-----VDTAGVKIERMLPVFGDYDAPhgHGEVSFDNVRVPVanfIGGAGQG----FEIAQG-RLGPGrihhcMRCIGA 275
Cdd:cd01153 190 VPkflddGERNGVTVARIEEKMGLHGSP--TCELVFDNAKGEL---IGEEGMGlaqmFAMMNGaRLGVG-----TQGTGL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 276 AEKSLELMIDRGMSRTAFGK--------EILKLGGNLERVAEARVAIDQARLLTLYAAYKMDtLGNMAALTEISA----- 342
Cdd:cd01153 260 AEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQD-LAERKATEGEDRkalsa 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2184264920 343 --------IKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADG 388
Cdd:cd01153 339 ladlltpvVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
60-369 |
4.97e-13 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 71.00 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 60 KAAGLWNMFLPcPELGqGLSVQEYAH---IAELSGRSLI-APTVFncnAPDS-GNMEVLWRYGSEAQKQEWLTPLLEGKI 134
Cdd:PRK09463 119 KEHGFFGMIIP-KEYG-GLEFSAYAHsrvLQKLASRSGTlAVTVM---VPNSlGPGELLLHYGTDEQKDHYLPRLARGEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 135 RSVFCMTEPAvASSDATNMQATAVI-----DGDEIV---LNGRKWWSSgLGdPNAKII--IFMAHTPDE--SKDRHHQHS 202
Cdd:PRK09463 194 IPCFALTSPE-AGSDAGSIPDTGVVckgewQGEEVLgmrLTWNKRYIT-LA-PIATVLglAFKLYDPDGllGDKEDLGIT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 203 MVLVPVDTAGVKI-ERMLPVFgdydAPHGHGEVSFDNVRVPVANFIGG---AGQGFE-----IAQGR------LGPGRIH 267
Cdd:PRK09463 271 CALIPTDTPGVEIgRRHFPLN----VPFQNGPTRGKDVFIPLDYIIGGpkmAGQGWRmlmecLSVGRgislpsNSTGGAK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 268 HCMRCIGAaekslelmidRGMSRTAFGKEIlklgGNLERVAE--ARVA-----IDQARLLTLYAaykMDtLGNMAALteI 340
Cdd:PRK09463 347 LAALATGA----------YARIRRQFKLPI----GKFEGIEEplARIAgnaylMDAARTLTTAA---VD-LGEKPSV--L 406
|
330 340 350
....*....|....*....|....*....|
gi 2184264920 341 SAI-KVVAPSVLEKVVDMAMQIHGGAGVSR 369
Cdd:PRK09463 407 SAIaKYHLTERGRQVINDAMDIHGGKGICL 436
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
60-367 |
2.27e-11 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 65.75 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 60 KAAGLWNMFLPcPELGqGLSVQEYAH---IAELSGRSL-IAPTVFncnAPDS-GNMEVLWRYGSEAQKQEWLTPLLEGKI 134
Cdd:PRK13026 118 KKEGFFALIIP-KEYG-GKGFSAYANstiVSKIATRSVsAAVTVM---VPNSlGPGELLTHYGTQEQKDYWLPRLADGTE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 135 RSVFCMTEPAvASSDATNMQATAVI-----DGDEIV---LNGRKWWSSgLGdPNAKII--IFMAHTPDE--SKDRHHQHS 202
Cdd:PRK13026 193 IPCFALTGPE-AGSDAGAIPDTGIVcrgefEGEEVLglrLTWDKRYIT-LA-PVATVLglAFKLRDPDGllGDKKELGIT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 203 MVLVPVDTAGVKI-ERMLPVfgdyDAPHGHGEVSFDNVRVPVANFIGG---AGQGFE-----IAQGR------LGPGRIH 267
Cdd:PRK13026 270 CALIPTDHPGVEIgRRHNPL----GMAFMNGTTRGKDVFIPLDWIIGGpdyAGRGWRmlvecLSAGRgislpaLGTASGH 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 268 HCMRCIGAAekslelmidrGMSRTAFGKEIlklgGNLERVAE--ARVA-----IDQARLLTLYAaykmdtLGNMAALTEI 340
Cdd:PRK13026 346 MATRTTGAY----------AYVRRQFGMPI----GQFEGVQEalARIAgntylLEAARRLTTTG------LDLGVKPSVV 405
|
330 340
....*....|....*....|....*...
gi 2184264920 341 SAI-KVVAPSVLEKVVDMAMQIHGGAGV 367
Cdd:PRK13026 406 TAIaKYHMTELARDVVNDAMDIHAGKGI 433
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
13-133 |
2.90e-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: 54.39 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 13 ERTKAFIAQEIEPIEAEfWVEVHELnqggDWTKWQwpsqleqlkaKAKAAGLWNMFLPcPELG-QGLSVQEYAHIAELSG 91
Cdd:pfam02771 9 DTVREFAEEEIAPHAAE-WDEEGEF----PRELWK----------KLGELGLLGITIP-EEYGgAGLDYLAYALVAEELA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2184264920 92 RSLiAPTVFNCNAPDSGNMEVLWRYGSEAQKQEWLTPLLEGK 133
Cdd:pfam02771 73 RAD-ASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
268-384 |
3.22e-08 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 51.96 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 268 HCMRCIGAAEKSLELMIDR--GMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAY------KMDTLGNMAALTE 339
Cdd:pfam08028 2 IAAAALGAARAALAEFTERarGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAArieaaaAAGKPVTPALRAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2184264920 340 ISAIKVVAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLR 384
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAA 126
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
113-406 |
4.87e-08 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 54.50 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 113 LWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGDEIVLNGRKWWSSglGDPNAKIIIFMAHTPD 192
Cdd:PLN02519 121 LVRNGTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWCT--NGPVAQTLVVYAKTDV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 193 ESkdrhHQHSMvlvpvdTAGVkIERMLPVFGDYDAPHGHG-------EVSFDNVRVPVANFIGGAGQGFEIAQGRLGPGR 265
Cdd:PLN02519 198 AA----GSKGI------TAFI-IEKGMPGFSTAQKLDKLGmrgsdtcELVFENCFVPEENVLGQEGKGVYVMMSGLDLER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 266 IHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEARVAIDQARLLTLYAAYKMDTlgNMAALTEISAIKV 345
Cdd:PLN02519 267 LVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN--GKVDRKDCAGVIL 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2184264920 346 VAPSVLEKVVDMAMQIHGGAGVSRDTPLTGFFAQARSLRLADGPDEVHKGMIAKlELAKRG 406
Cdd:PLN02519 345 CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR-ELFKEE 404
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
4-328 |
3.80e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 48.70 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 4 LSARAKDYIERTKAFIAQEIEPIEAEFWvevhelnqggdwTKWQWPSQLEQLKAKAKAAGLWNMFLPCPelgqGLSVQEY 83
Cdd:PLN02526 29 LTPEEQALRKRVRECMEKEVAPIMTEYW------------EKAEFPFHIIPKLGSLGIAGGTIKGYGCP----GLSITAS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 84 A-HIAELSgRSLIAPTVFnCNAPDSGNMEVLWRYGSEAQKQEWLtPLLeGKIRSVFC--MTEPAVAsSDATNMQATAVID 160
Cdd:PLN02526 93 AiATAEVA-RVDASCSTF-ILVHSSLAMLTIALCGSEAQKQKYL-PSL-AQLDTVACwaLTEPDYG-SDASSLNTTATKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 161 GDEIVLNGRKWW--SSGLGDpnaKIIIFMAHTPDEskdrhhQHSMVLVPVDTAGV---KIE-----RMLPvfgdydaphg 230
Cdd:PLN02526 168 EGGWILNGQKRWigNSTFAD---VLVIFARNTTTN------QINGFIVKKGAPGLkatKIEnkiglRMVQ---------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 231 HGEVSFDNVRVPVANFIGGAgQGFEIAQGRLGPGRIHHCMRCIGAAEKSLELMIDRGMSRTAFGKEILKLGGNLERVAEA 310
Cdd:PLN02526 229 NGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRM 307
|
330 340
....*....|....*....|....
gi 2184264920 311 RVAIdQA------RLLTLYAAYKM 328
Cdd:PLN02526 308 LGNI-QAmflvgwRLCKLYESGKM 330
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
117-245 |
1.30e-05 |
|
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: 47.32 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 117 GSEAQKQEWLTPLLEGKIRSVFCMTEpavaSSDATNMQA---TAVID--GDEIVLN-----GRKWWSSGLGDpNAKIIIF 186
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTE----LGHGSNLQGletTATYDplTQEFVINtpdftATKWWPGNLGK-TATHAVV 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2184264920 187 MA--HTPDEskdRHHQHSMVlVPV---DT----AGVKIERMLPVFG----DydaphgHGEVSFDNVRVPVAN 245
Cdd:cd01150 192 FAqlITPGK---NHGLHAFI-VPIrdpKThqplPGVTVGDIGPKMGlngvD------NGFLQFRNVRIPREN 253
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
108-207 |
3.78e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 42.55 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 108 GNMEVLWRYGSEAQKQEWLTPLLEGKIRSVFCMTEPAvASSDATNMQATAVIDGD-EIVLNGRK-WWSSGLGDPNAKII- 184
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPSADgSYKITGTKiFISAGDHDLTENIVh 233
|
90 100
....*....|....*....|...
gi 2184264920 185 IFMAHTPDeSKDRHHQHSMVLVP 207
Cdd:PTZ00456 234 IVLARLPN-SLPTTKGLSLFLVP 255
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
60-242 |
5.12e-03 |
|
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: 38.84 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 60 KAAGLWNMFLPCPELGQGLSVQEYAH-IAELSgrsliaptvfncnAPDS----------GNMEVLWRYGSEAQKQEWLTP 128
Cdd:cd01163 32 RQSGLGTLRVPKEYGGLGASLPDLYEvVRELA-------------AADSniaqalrahfGFVEALLLAGPEQFRKRWFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264920 129 LLEGKIrsvFCMTEPAVASSDATNMQATAVIDGDEIVLNGRKWWSSGLGDpnAKIIIFMAHtpdeskDRHHQHSMVLVPV 208
Cdd:cd01163 99 VLNGWI---FGNAVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALF--SDWVTVSAL------DEEGKLVFAAVPT 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 2184264920 209 DTAGVKiermlpVFGDYDA----PHGHGEVSFDNVRVP 242
Cdd:cd01163 168 DRPGIT------VVDDWDGfgqrLTASGTVTFDNVRVE 199
|
|
| |
