|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
6-364 |
4.68e-61 |
|
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: 200.84 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 6 AERAELAAAVRELLQNECTEqdVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLP-A 84
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAP--EAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASlA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 85 PFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWAkeGVAVKATERADGHTLNGNAHYVLSGQIA 162
Cdd:COG1960 85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTepGAGSDAA--ALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 163 DVLLVVARTGGDDVGGV-GIFEVTPDATGLTRAAA-TVFDP-SVRLSTFTFTDT---PARRIGTA--GWDAVSHALDLAV 234
Cdd:COG1960 163 DVILVLARTDPAAGHRGiSLFLVPKDTPGVTVGRIeDKMGLrGSDTGELFFDDVrvpAENLLGEEgkGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 235 IALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGSDDAAGAIALAGFF 314
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARA-LVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 500047279 315 CAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRER 364
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLI 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
92-364 |
1.06e-36 |
|
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: 135.49 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 92 LATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWAkeGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVA 169
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTepGAGSDLA--GIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 170 RTGGDDVGGVGI--FEVTPDATGLT--RAAATVFDPSVRLSTFTFTDTP---ARRIGT--AGWDAVSHALDLAVIALAGE 240
Cdd:cd00567 121 RTDEEGPGHRGIsaFLVPADTPGVTvgRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEegGGFELAMKGLNVGRLLLAAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 241 QVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDAAGAIALAGFFCAEAYN 320
Cdd:cd00567 201 ALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 500047279 321 TTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRER 364
Cdd:cd00567 281 EVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLI 324
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
222-363 |
6.13e-20 |
|
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: 85.38 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 222 GWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGS 301
Cdd:pfam00441 3 GFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARL-LVYRAAEALDAG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500047279 302 DDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRE 363
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRN 143
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
39-349 |
6.57e-17 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 81.46 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 39 DPQLWRKLAAQGVTGLLIDPEYGGVGLGALE----LEAVAEETGAALLPapFIGSAVLATALIEAAGTAEDKQRLLPGLA 114
Cdd:PLN02519 61 DVNLWKLMGDFNLHGITAPEEYGGLGLGYLYhciaMEEISRASGSVGLS--YGAHSNLCINQLVRNGTPAQKEKYLPKLI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 115 EGTSIATVAVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVART-GGDDVGGVGIFEVTPDATGLTr 193
Cdd:PLN02519 139 SGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTdVAAGSKGITAFIIEKGMPGFS- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 194 AAATVFDPSVRLS-----TFTFTDTPARRI-GTAGWDA--VSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRA 265
Cdd:PLN02519 218 TAQKLDKLGMRGSdtcelVFENCFVPEENVlGQEGKGVyvMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 266 IGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGSDDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFV 345
Cdd:PLN02519 298 IGEFQFIQGKLADMYTSLQSSRS-YVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLL 376
|
....
gi 500047279 346 RRAR 349
Cdd:PLN02519 377 RDAK 380
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
6-364 |
4.68e-61 |
|
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: 200.84 E-value: 4.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 6 AERAELAAAVRELLQNECTEqdVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLP-A 84
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAP--EAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASlA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 85 PFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWAkeGVAVKATERADGHTLNGNAHYVLSGQIA 162
Cdd:COG1960 85 LPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTepGAGSDAA--ALRTTAVRDGDGYVLNGQKTFITNAPVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 163 DVLLVVARTGGDDVGGV-GIFEVTPDATGLTRAAA-TVFDP-SVRLSTFTFTDT---PARRIGTA--GWDAVSHALDLAV 234
Cdd:COG1960 163 DVILVLARTDPAAGHRGiSLFLVPKDTPGVTVGRIeDKMGLrGSDTGELFFDDVrvpAENLLGEEgkGFKIAMSTLNAGR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 235 IALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGSDDAAGAIALAGFF 314
Cdd:COG1960 243 LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARA-LVYRAAWLLDAGEDAALEAAMAKLF 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 500047279 315 CAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRER 364
Cdd:COG1960 322 ATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLI 371
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
92-364 |
1.06e-36 |
|
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: 135.49 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 92 LATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWAkeGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVA 169
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTepGAGSDLA--GIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 170 RTGGDDVGGVGI--FEVTPDATGLT--RAAATVFDPSVRLSTFTFTDTP---ARRIGT--AGWDAVSHALDLAVIALAGE 240
Cdd:cd00567 121 RTDEEGPGHRGIsaFLVPADTPGVTvgRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEegGGFELAMKGLNVGRLLLAAV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 241 QVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDAAGAIALAGFFCAEAYN 320
Cdd:cd00567 201 ALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAR 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 500047279 321 TTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRER 364
Cdd:cd00567 281 EVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLI 324
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
41-349 |
2.89e-32 |
|
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: 124.53 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 41 QLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLPAP-FIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSI 119
Cdd:cd01160 34 EVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPgLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 120 ATVAVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVARTGGDDVGGVGI--FEVTPDATGLTRA--- 194
Cdd:cd01160 114 GAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAGGIslFLVERGTPGFSRGrkl 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 195 ---------AATVFDPSVRLstftftdtPARR-IG--TAGWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQF 262
Cdd:cd01160 194 kkmgwkaqdTAELFFDDCRV--------PAENlLGeeNKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 263 GRAIGSFQALKHMAADLLVQVEsSTSAAQHAAAEKAAGSDDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAH 342
Cdd:cd01160 266 GKTLAQLQVVRHKIAELATKVA-VTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIA 344
|
....*..
gi 500047279 343 LFVRRAR 349
Cdd:cd01160 345 RAYRDAR 351
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
7-349 |
2.78e-30 |
|
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: 119.05 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 7 ERAELAAAVRELLQNECteQDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALElEAVAEETgaallpapf 86
Cdd:cd01156 5 EIEMLRQSVREFAQKEI--APLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLA-HVIIMEE--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 87 IGSAVLATALIEAA------------GTAEDKQRLLPGLAEGTSIATVAVTGARGTWAKEGVAVKATERADGHTLNGNAH 154
Cdd:cd01156 73 ISRASGSVALSYGAhsnlcinqiyrnGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 155 YVLSGQIADVLLVVARTGGDDVGG-VGIFEVTPDATGLTRAAAtvFDP-SVRLS---TFTFTD--TPARRIGTA---GWD 224
Cdd:cd01156 153 WITNGPDADTLVVYAKTDPSAGAHgITAFIVEKGMPGFSRAQK--LDKlGMRGSntcELVFEDceVPEENILGGenkGVY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 225 AVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDA 304
Cdd:cd01156 231 VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDP 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 500047279 305 AGAiALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:cd01156 311 KDA-AGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAK 354
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
7-351 |
3.04e-29 |
|
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: 116.21 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 7 ERAELAAAVRELLQNECteQDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLPAPF 86
Cdd:cd01158 2 EHQMIRKTVRDFAEKEI--APLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 87 IGSA--VLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GArGTWAKeGVAVKATERADGHTLNGNAHYVLSGQIA 162
Cdd:cd01158 80 IVSVhnSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSepGA-GSDAA-ALKTTAKKDGDDYVLNGSKMWITNGGEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 163 DVLLVVARTGGDDVGG-VGIFEVTPDATGLT----------RAAATvfdpsvrlSTFTFTD--TPA-RRIGTAGwDAVSH 228
Cdd:cd01158 158 DFYIVFAVTDPSKGYRgITAFIVERDTPGLSvgkkedklgiRGSST--------TELIFEDvrVPKeNILGEEG-EGFKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 229 A---LDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDAA 305
Cdd:cd01158 229 AmqtLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIK 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 500047279 306 GAiALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTG 351
Cdd:cd01158 309 EA-AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKIT 353
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
44-349 |
1.72e-24 |
|
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: 102.91 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 44 RKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLP-APFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATV 122
Cdd:cd01162 39 RKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVStAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 123 AVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVARTGGDDVGGVGIFEVTPDATGLT---------- 192
Cdd:cd01162 119 CLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKGISCFVVEKGTPGLSfganekkmgw 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 193 RAAATvfdpsvRLSTFTFTDTPAR-RIGT--AGWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSF 269
Cdd:cd01162 199 NAQPT------RAVIFEDCRVPVEnRLGGegQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 270 QALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:cd01162 273 QALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLR 352
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
222-363 |
6.13e-20 |
|
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: 85.38 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 222 GWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGS 301
Cdd:pfam00441 3 GFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARL-LVYRAAEALDAG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500047279 302 DDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTGLQLFGSSAQHRE 363
Cdd:pfam00441 82 GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRN 143
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
6-116 |
9.41e-18 |
|
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: 77.89 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 6 AERAELAAAVRELLQNECTeqDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLPAP 85
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIA--PHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVA 79
|
90 100 110
....*....|....*....|....*....|...
gi 500047279 86 FIGSA--VLATALIEAAGTAEDKQRLLPGLAEG 116
Cdd:pfam02771 80 LALSVhsSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
39-349 |
6.57e-17 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 81.46 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 39 DPQLWRKLAAQGVTGLLIDPEYGGVGLGALE----LEAVAEETGAALLPapFIGSAVLATALIEAAGTAEDKQRLLPGLA 114
Cdd:PLN02519 61 DVNLWKLMGDFNLHGITAPEEYGGLGLGYLYhciaMEEISRASGSVGLS--YGAHSNLCINQLVRNGTPAQKEKYLPKLI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 115 EGTSIATVAVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVART-GGDDVGGVGIFEVTPDATGLTr 193
Cdd:PLN02519 139 SGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTdVAAGSKGITAFIIEKGMPGFS- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 194 AAATVFDPSVRLS-----TFTFTDTPARRI-GTAGWDA--VSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRA 265
Cdd:PLN02519 218 TAQKLDKLGMRGSdtcelVFENCFVPEENVlGQEGKGVyvMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 266 IGSFQALKHMAADLLVQVESSTSaAQHAAAEKAAGSDDAAGAIALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFV 345
Cdd:PLN02519 298 IGEFQFIQGKLADMYTSLQSSRS-YVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLL 376
|
....
gi 500047279 346 RRAR 349
Cdd:PLN02519 377 RDAK 380
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
24-349 |
5.52e-16 |
|
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: 78.66 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 24 TEQDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLPAPFIGSAV-LATALIEAAGT 102
Cdd:cd01161 43 EEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGMDLGFSVTLGAHQsIGFKGILLFGT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 103 AEDKQRLLPGLAEGTSIATVAVTG-ARGTWAKeGVAVKATERADG--HTLNGNAHYVLSGQIADVLLVVARTGGDDVGGV 179
Cdd:cd01161 123 EAQKEKYLPKLASGEWIAAFALTEpSSGSDAA-SIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDATGS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 180 G-----IFEVTPDATGLT----------RAAATvfdpsvrlSTFTFTDT--PARRI-GTA--GWDAVSHALDLAVIALAG 239
Cdd:cd01161 202 VkdkitAFIVERSFGGVTngppekkmgiKGSNT--------AEVYFEDVkiPVENVlGEVgdGFKVAMNILNNGRFGMGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 240 EQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLV-QVESSTSAAQHAAAEKAAGSDDAAGAIALAGFFCAEA 318
Cdd:cd01161 274 ALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAIlQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEA 353
|
330 340 350
....*....|....*....|....*....|.
gi 500047279 319 YNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:cd01161 354 AWLVVDEAIQIHGGMGFMREYGVERVLRDLR 384
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
1-349 |
5.62e-16 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 78.62 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 1 MTISVAERAEL-AAAVRELLQNECTEQDVRQTisSDEGYDPQ-LWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETG 78
Cdd:PRK12341 1 MDFSLTEEQELlLASIRELITRNFPEEYFRTC--DENGTYPReFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 79 AALLPAPFIGSAVLATALIEaAGTAED-KQRLLPGLAEGTSIATVAVTGARGTWAKEGVAVKATERADGHTLNGNAHYVL 157
Cdd:PRK12341 79 KCGAPAFLITNGQCIHSMRR-FGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 158 SGQIADVLLVVARTGGDDVGGVGI--FEVTPDATGLTRAA-----------ATVFDPSVRLSTftftdtpARRIGTAGWD 224
Cdd:PRK12341 158 GAKEYPYMLVLARDPQPKDPKKAFtlWWVDSSKPGIKINPlhkigwhmlstCEVYLDNVEVEE-------SDLVGEEGMG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 225 --AVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSD 302
Cdd:PRK12341 231 flNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 500047279 303 DAAGAiALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:PRK12341 311 LRTSA-ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVR 356
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
35-283 |
4.40e-15 |
|
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: 75.86 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 35 DEGYDPQLWRKLAAQGVTGLLIDpEYGGVGLGALELEAVAEE---TGAALLPAPFIGSAvLATALIEAAGTAEDKQRLLP 111
Cdd:cd01151 42 EEKFDRKIIEEMGELGLLGATIK-GYGCAGLSSVAYGLIAREverVDSGYRSFMSVQSS-LVMLPIYDFGSEEQKQKYLP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 112 GLAEGTSIATVAVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVARTGGDDVGGVGIFEvtPDATGL 191
Cdd:cd01151 120 KLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETGKIRGFILE--RGMKGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 192 T----------RAAAT-------VFDPSVRLstftftdTParriGTAGWDAVSHALDLAVIALAGEQVGGTRRIFDITID 254
Cdd:cd01151 198 SapkiqgkfslRASITgeivmdnVFVPEENL-------LP----GAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQ 266
|
250 260
....*....|....*....|....*....
gi 500047279 255 YLKTRIQFGRAIGSFQALKHMAADLLVQV 283
Cdd:cd01151 267 YVLDRKQFGRPLAAFQLVQKKLADMLTEI 295
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
56-360 |
8.98e-14 |
|
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: 71.85 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 56 IDPEYGGVGLGALELEAVAEE-----TGAALLpapfIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVTGARGT 130
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEElaygcTGVQTA----IEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 131 WAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVART----GGDDVGGVGIFEVTPDATGLT----------RAAA 196
Cdd:cd01157 127 SDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSdpdpKCPASKAFTGFIVEADTPGIQpgrkelnmgqRCSD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 197 TvfdpsvRLSTFTFTDTPARRIGT---AGWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALK 273
Cdd:cd01157 207 T------RGITFEDVRVPKENVLIgegAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 274 HMAADLLVQVE-SSTSAAQHAAAEKAAGSDDAAGAIALAgfFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRARTgL 352
Cdd:cd01157 281 FMLADMAMKVElARLAYQRAAWEVDSGRRNTYYASIAKA--FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKI-Y 357
|
....*...
gi 500047279 353 QLFGSSAQ 360
Cdd:cd01157 358 QIYEGTSQ 365
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
41-349 |
1.36e-11 |
|
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: 65.49 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 41 QLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLPAPFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIA 120
Cdd:cd01153 40 EALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 121 TVAVTGARGTWAKEGVAVKATERADG-HTLNGNAHYVLSGQIAD----VLLVVARTGgddvggvgifEVTPDATGL---- 191
Cdd:cd01153 120 TMCLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAGEHDMseniVHLVLARSE----------GAPPGVKGLslfl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 192 --------TRAAATVfdpsVRLS-----------TFTFTDTPARRIGTA--GWDAVSHALDLAVIALAGEQVGGTRRIFD 250
Cdd:cd01153 190 vpkflddgERNGVTV----ARIEekmglhgsptcELVFDNAKGELIGEEgmGLAQMFAMMNGARLGVGTQGTGLAEAAYL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 251 ITIDYLKTRIQFGRAIGSFQALKHM-----AADLLVQ---VESS------TSAAQHAAAEKAAGSDDAAGAIALAG---- 312
Cdd:cd01153 266 NALAYAKERKQGGDLIKAAPAVTIIhhpdvRRSLMTQkayAEGSraldlyTATVQDLAERKATEGEDRKALSALADlltp 345
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 500047279 313 ---FFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:cd01153 346 vvkGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDAR 385
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
1-349 |
1.39e-11 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 65.24 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 1 MTISVAERAEL-AAAVRELLQNECTEQDVRQTISSDEgYdPQLWRK-LAAQGVTGLLIDPEYGGVGLGALELEAVAEETG 78
Cdd:PRK03354 1 MDFNLNDEQELfVAGIRELMASENWEAYFAECDRDSV-Y-PERFVKaLADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 79 AALLPAPFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWakeGVAVKATERADGHT-LNGNAHY 155
Cdd:PRK03354 79 RLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITepGAGSDV---GSLKTTYTRRNGKVyLNGSKCF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 156 VLSGQIADVLLVVARTGGddvggvgifevTPDATGLTRAAATVFDPSVRLSTFT-------------FTDTPARR---IG 219
Cdd:PRK03354 156 ITSSAYTPYIVVMARDGA-----------SPDKPVYTEWFVDMSKPGIKVTKLEklglrmdscceitFDDVELDEkdmFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 220 TAG--WDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEK 297
Cdd:PRK03354 225 REGngFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKA 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 500047279 298 AAGSDDAAGAiALAGFFCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:PRK03354 305 DNGTITSGDA-AMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLR 355
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
8-349 |
2.93e-09 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 58.03 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 8 RAELAAAVRELLQNECTEQDVrqtissDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEET-----GAALl 82
Cdd:PTZ00461 45 RETVAKFSREVVDKHAREDDI------NMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELskydpGFCL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 83 paPFIGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVTGARGTWAKEGVAVKATERADG-HTLNGNAHYVLSGQI 161
Cdd:PTZ00461 118 --AYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 162 ADVLLVVARTGGDDVGgvgiFEVTPDATGLTRaAATVFDPSVRLST-----FTFTDTPARRI-GTAGWDAVS--HALDLA 233
Cdd:PTZ00461 196 ADVFLIYAKVDGKITA----FVVERGTKGFTQ-GPKIDKCGMRASHmcqlfFEDVVVPAENLlGEEGKGMVGmmRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 234 VIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQALKHMAADLLVQVESSTSAAQHAAAEKAAGSDDAAGAIAlAGF 313
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDA-AKL 349
|
330 340 350
....*....|....*....|....*....|....*.
gi 500047279 314 FCAEAYNTTAMQAVQMHGGIGFTWEHPAHLFVRRAR 349
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAK 385
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
45-270 |
6.17e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 57.17 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 45 KLAAQGVTGLLIDpEYGGVGLGALELE-AVAEETGAALLPAPFI-GSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATV 122
Cdd:PLN02526 68 KLGSLGIAGGTIK-GYGCPGLSITASAiATAEVARVDASCSTFIlVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACW 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 123 AVTGARGTWAKEGVAVKATERADGHTLNGNAHYVLSGQIADVLLVVARTGGDDVGGVGIfeVTPDATGLTraaATVFDPS 202
Cdd:PLN02526 147 ALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFI--VKKGAPGLK---ATKIENK 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500047279 203 VRLSTF---------TFTDTPARRIGTAGWDAVSHALDLAVIALAGEQVGGTRRIFDITIDYLKTRIQFGRAIGSFQ 270
Cdd:PLN02526 222 IGLRMVqngdivlkdVFVPDEDRLPGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQ 298
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
7-275 |
5.59e-07 |
|
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: 50.81 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 7 ERAELAAAVRELLQNECT---EQDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGVGLGALELEAVAEETGAALLP 83
Cdd:cd01152 2 SEEAFRAEVRAWLAAHLPpelREESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 84 APFIGSAV-LATALIEAAGTAEDKQRLLPGLAEGTSIATVAVT--GARGTWAkeGVAVKATERADGHTLNGNAHYVLSGQ 160
Cdd:cd01152 82 VPFNQIGIdLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSepGAGSDLA--GLRTRAVRDGDDWVVNGQKIWTSGAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 161 IADVLLVVARTGGDDVGGVGI--FEVTPDATGLTRAAATVFDPSVRLSTFTFTD--TP-ARRIGT--AGWDAVSHALD-- 231
Cdd:cd01152 160 YADWAWLLVRTDPEAPKHRGIsiLLVDMDSPGVTVRPIRSINGGEFFNEVFLDDvrVPdANRVGEvnDGWKVAMTTLNfe 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 500047279 232 ----LAVIALAGEQVGG-----TRRIFDITIDYLkTRIQFGRAIGSFQALKHM 275
Cdd:cd01152 240 rvsiGGSAATFFELLLArllllTRDGRPLIDDPL-VRQRLARLEAEAEALRLL 291
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
9-165 |
6.59e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 41.87 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 9 AELAAAVRELLQNE----CTEQDVRQTISSDEGYDPQLWRKLAAQGVTGLLIDPEYGGvglgaLELEAVAEETGAALLPA 84
Cdd:PRK13026 76 PTLTAEEQAFIDNEvetlLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGG-----KGFSAYANSTIVSKIAT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 85 PFIGSAVLATA--------LIEAAGTAEDKQRLLPGLAEGTSIATVAVTGAR-----GTWAKEGVAVKAT---ERADGHT 148
Cdd:PRK13026 151 RSVSAAVTVMVpnslgpgeLLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEagsdaGAIPDTGIVCRGEfegEEVLGLR 230
|
170
....*....|....*..
gi 500047279 149 LNGNAHYVLSGQIADVL 165
Cdd:PRK13026 231 LTWDKRYITLAPVATVL 247
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
53-216 |
2.40e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 39.86 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 53 GLLIDPEYGGVGLGALELEAVAEETGAALLPAPF--IGSAVLATALIEAAGTAEDKQRLLPGLAEGTSIATVAVtgargt 130
Cdd:PTZ00457 67 GARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLstIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWAT------ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500047279 131 waKEGVAVKATERADGHTLNGNAHYVLSGQI-------ADVLLVVARTGGDDVGGV--------GIFEVTPDATGLtraa 195
Cdd:PTZ00457 141 --EEGCGSDISMNTTKASLTDDGSYVLTGQKrcefaasATHFLVLAKTLTQTAAEEgatevsrnSFFICAKDAKGV---- 214
|
170 180
....*....|....*....|.
gi 500047279 196 atvfdpSVRLSTFTFTDTPAR 216
Cdd:PTZ00457 215 ------SVNGDSVVFENTPAA 229
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
117-193 |
5.44e-03 |
|
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: 35.72 E-value: 5.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500047279 117 TSIATVAVTGARGTWakegvavkateradghTLNGNAHYVLSGQIADVLLVVARTGGDDVGGV-GIFEVTPDATGLTR 193
Cdd:pfam02770 14 ASLKTTAADGDGGGW----------------VLNGTKWWITNAGIADLFLVLARTGGDDRHGGiSLFLVPKDAPGVSV 75
|
|
| |
