|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
40-454 |
4.88e-161 |
|
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: 466.10 E-value: 4.88e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 40 VLEEAGKFATDVLAPLNKVGDEHGIKLSDGKVTTAPGWPDAYKRWTEGGWNAVSGPEDFGGQGLPIAINAACTEIWSAsN 119
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSR-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 120 LAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADGTYRIKGTKIFITYG 199
Cdd:cd01153 80 DAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 200 EHDMTDNIVHFVLARLPDAPAGTKGISLFLVPKFMVNadgslGQRNDIYASGVEHKLGMHASPTCTMTMGDHGgaiGFLI 279
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAK---GELI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 280 GEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQGRAvGSKSDGSDAIFVHPDVKRMLMRMRAQTAAAR 359
Cdd:cd01153 232 GEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGD-LIKAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 360 TICYATAVAIDVSTRARDPKVRADAAAR-AALLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIY 438
Cdd:cd01153 311 ALDLYTATVQDLAERKATEGEDRKALSAlADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*.
gi 654685427 439 EGTNGIQAIDLVTRKL 454
Cdd:cd01153 391 EGTTGIQALDLIGRKI 406
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
1-506 |
5.24e-149 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 443.16 E-value: 5.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 1 MTYRAPISDMLLSLNHGAGLKAAVEAGHYGDFDADIAAAVLEEAGKFATDVLAPLNKVGDEHGIK-LSDGKVTTAPGWPD 79
Cdd:PTZ00456 24 LQYQPRIRDVQFLVEEVFNMYDHYEKLGKTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVlLKDGNVTTPKGFKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 80 AYKRWTEGGWNAVSGPEDFGGQGLPIAINAACTEIWSASNLAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSGEWTG 159
Cdd:PTZ00456 104 AYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 160 TMQLTEPQAGSDVGALRTRAEKQADGTYRIKGTKIFITYGEHDMTDNIVHFVLARLPDAPAGTKGISLFLVPKFMVNADG 239
Cdd:PTZ00456 184 TMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPDG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 240 SLGQRNDIYASGVEHKLGMHASPTCTMTMGDhggAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYA 319
Cdd:PTZ00456 264 SLETAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 320 QERKQGRAVGSKSD---GSDAIFVHPDVKRMLMRMRAQTAAARTICYATAVAIDVSTRARDPKVRADAAARAALLTPMAK 396
Cdd:PTZ00456 341 RERRSMRALSGTKEpekPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 397 GYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAIDLVTRK-LAANGGaavwallDELAATVKK 475
Cdd:PTZ00456 421 GCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKvLSLKGG-------NEVARFGKR 493
|
490 500 510
....*....|....*....|....*....|.
gi 654685427 476 VEASNDPAFGTTGVKLREALEALTRTSKWLL 506
Cdd:PTZ00456 494 VSKLVRAHLFSRGALGQYARRLWLLQKQWRL 524
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
31-458 |
9.26e-117 |
|
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: 351.84 E-value: 9.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 31 DFD-ADIAAAVLEEAGKFATDVLAPLNKVGDEHGiklsdgkvttapGWP-DAYKRWTEGGWNAVSGPEDFGGQGLPIAIN 108
Cdd:COG1960 2 DFElTEEQRALRDEVREFAEEEIAPEAREWDREG------------EFPrELWRKLAELGLLGLTIPEEYGGLGLSLVEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 109 AACTEIWSASNLAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADGtYR 188
Cdd:COG1960 70 ALVLEELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 189 IKGTKIFITYGE-HDmtdniVHFVLARLPDAPaGTKGISLFLVPKFMVnadgslgqrnDIYASGVEHKLGMHASPTCTMT 267
Cdd:COG1960 149 LNGQKTFITNAPvAD-----VILVLARTDPAA-GHRGISLFLVPKDTP----------GVTVGRIEDKMGLRGSDTGELF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 268 MGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaifvHPDVKR 346
Cdd:COG1960 213 FDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQfGRPIAD----------FQAVQH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 347 MLMRMRAQTAAARTICYATAVAIDVSTRARdpkvradaaaraaLLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAA 426
Cdd:COG1960 283 RLADMAAELEAARALVYRAAWLLDAGEDAA-------------LEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLE 349
|
410 420 430
....*....|....*....|....*....|..
gi 654685427 427 QHYRDARITAIYEGTNGIQAIDLVTRKLAANG 458
Cdd:COG1960 350 RLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
131-449 |
1.82e-64 |
|
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: 214.46 E-value: 1.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 131 SAMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADGtYRIKGTKIFITYGehDMTDniVHF 210
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG--GDAD--LFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 211 VLARLPDAPAGTKGISLFLVPKfmvNADGslgqrndIYASGVEHKLGMHASPTCTMTMGD-HGGAIGfLIGEENQGMRCM 289
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPA---DTPG-------VTVGRIWDKMGMRGSGTGELVFDDvRVPEDN-LLGEEGGGFELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 290 FTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaifvHPDVKRMLMRMRAQTAAARTICYATAVA 368
Cdd:cd00567 187 MKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQfGKPLAE----------FQAVQFKLADMAAELEAARLLLYRAAWL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 369 IDVSTRARdpkvradaaaraALLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAID 448
Cdd:cd00567 257 LDQGPDEA------------RLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLI 324
|
.
gi 654685427 449 L 449
Cdd:cd00567 325 I 325
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
32-452 |
3.99e-61 |
|
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: 208.38 E-value: 3.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 32 FDADIAAAVLEEAGKFAT----------DVLAPLNKVGDEHGIKLSdgKVTTAPGWPDAYKR-WTEGGWNAVSGPEDFGG 100
Cdd:cd01154 14 FGDPEEEPDLSRLGELAGgelyelarlaDRNPPVLEMWDRWGRRVD--RVWVHPAWHALMRRlIEEGVINIEDGPAGEGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 101 qglPIAINAACTEIWSAsnlAFG-LCPL-LTASAMEALDAHGSSELKKIYLEKLVSGE---WTGTMQLTEPQAGSDVGAL 175
Cdd:cd01154 92 ---RHVHFAAGYLLSDA---AAGlLCPLtMTDAAVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGAN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 176 RTRAEKQADGTYRIKGTKIFITYGEHDmtdniVHFVLARLPDAPAGTKGISLFLVPKFmvNADGSlgqRNDIYASGVEHK 255
Cdd:cd01154 166 ETTAERSGGGVYRLNGHKWFASAPLAD-----AALVLARPEGAPAGARGLSLFLVPRL--LEDGT---RNGYRIRRLKDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 256 LGMHASPTCTMTMGDhggAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERkqgRAVGSksdgs 335
Cdd:cd01154 236 LGTRSVATGEVEFDD---AEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHR---RAFGK----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 336 dAIFVHPDVKRMLMRMRAQTAAARTICYATAVAIDVSTRARdpkvrADAAARAALLTPMAKGYSTDIGNEVAYLGVQVHG 415
Cdd:cd01154 305 -PLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADK-----PVEAHMARLATPVAKLIACKRAAPVTSEAMEVFG 378
|
410 420 430
....*....|....*....|....*....|....*..
gi 654685427 416 GMGFIEETGAAQHYRDARITAIYEGTNGIQAIDLVTR 452
Cdd:cd01154 379 GNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLRV 415
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
35-445 |
8.31e-59 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 200.96 E-value: 8.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 35 DIAAAVLEEAGKFATDVLAPLNKVGDEHGIklsdgkvttAPgwPDAYKRWTEGGWNAVSGPEDFGGQGLPIAINAACTEI 114
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGE---------FP--REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 115 WSASNLAFGLCPLLTAS-AMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADgTYRIKGTK 193
Cdd:cd01158 70 LAKVDASVAVIVSVHNSlGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 194 IFITYGEHdmTDNIVhfVLARLpDAPAGTKGISLFLVPKfmvNADGslgqrndIYASGVEHKLGMHASPTCTMTMGDHGG 273
Cdd:cd01158 149 MWITNGGE--ADFYI--VFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFEDVRV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 274 AIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaifvHPDVKRMLMRMR 352
Cdd:cd01158 214 PKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQfGKPIAD----------FQGIQFKLADMA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 353 AQTAAARTICYATAvaidvstRARDPKVRADAAARaalltpMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDA 432
Cdd:cd01158 284 TEIEAARLLTYKAA-------RLKDNGEPFIKEAA------MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDA 350
|
410
....*....|...
gi 654685427 433 RITAIYEGTNGIQ 445
Cdd:cd01158 351 KITEIYEGTSEIQ 363
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
81-454 |
6.46e-40 |
|
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: 149.57 E-value: 6.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 81 YKRWTEGGWNAVSGPEDFGGQGLPIAINAACTEIWSASNlAFGLCPLL-TASAMEALDAHGSSELKKIYLEKLVSGEWTG 159
Cdd:cd01160 36 WRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG-GSGPGLSLhTDIVSPYITRAGSPEQKERVLPQMVAGKKIG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 160 TMQLTEPQAGSDVGALRTRAEKQADgTYRIKGTKIFITYGEHdmTDniVHFVLARLPDAPAGTKGISLFLVPKFMvnaDG 239
Cdd:cd01160 115 AIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML--AD--VVIVVARTGGEARGAGGISLFLVERGT---PG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 240 SLGQRNdiyasgvEHKLGMHASPTCTMTMGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYA 319
Cdd:cd01160 187 FSRGRK-------LKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 320 QERKQ-GRAVGSksdgsdaifvHPDVKRMLMRMRAQTAAARTICYATAV-----AIDVSTRArdpkvradaaaraalltp 393
Cdd:cd01160 260 KQRKAfGKTLAQ----------LQVVRHKIAELATKVAVTRAFLDNCAWrheqgRLDVAEAS------------------ 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654685427 394 MAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAiDLVTRKL 454
Cdd:cd01160 312 MAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMK-ELISRQM 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
39-456 |
1.14e-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: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 39 AVLEEAGKFATDVLAPLNKVGDEHGIklsdgkvttapgWP-DAYKRWTEGGWNAVSGPEDFGGQGLPiAINAACteIWSA 117
Cdd:cd01162 7 AIQEVARAFAAKEMAPHAADWDQKKH------------FPvDVLRKAAELGFGGIYIRDDVGGSGLS-RLDASI--IFEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 118 snLAFGlCPLLTA----SAMEA--LDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADgTYRIKG 191
Cdd:cd01162 72 --LSTG-CVSTAAyisiHNMCAwmIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 192 TKIFITYGehdmTDNIVHFVLARlpDAPAGTKGISLFLVPKfmvNADG-SLGQRndiyasgvEHKLGMHASPTCTMTMGD 270
Cdd:cd01162 148 SKAFISGA----GDSDVYVVMAR--TGGEGPKGISCFVVEK---GTPGlSFGAN--------EKKMGWNAQPTRAVIFED 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 271 HGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaifvHPDVKRMLM 349
Cdd:cd01162 211 CRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQfGKPLAD----------FQALQFKLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 350 RMRAQTAAARTICYATAVAIDvstrARDPKvradaaarAALLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHY 429
Cdd:cd01162 281 DMATELVASRLMVRRAASALD----RGDPD--------AVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYV 348
|
410 420
....*....|....*....|....*..
gi 654685427 430 RDARITAIYEGTNGIQAIdLVTRKLAA 456
Cdd:cd01162 349 RDLRVHQILEGTNEIMRL-IIARALLT 374
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
42-454 |
6.36e-39 |
|
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: 146.79 E-value: 6.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 42 EEAGKFATDVLAPLNKvgdehgiklsdgKVTTAPGWP-DAYKRWTEGGWNAVSGPEDFGGQGLP-IAINAACTEIWSAS- 118
Cdd:cd01156 11 QSVREFAQKEIAPLAA------------KIDRDNEFPrDLWRKMGKLGLLGITAPEEYGGSGMGyLAHVIIMEEISRASg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 119 --NLAFG----LCplltasaMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQaDGTYRIKGT 192
Cdd:cd01156 79 svALSYGahsnLC-------INQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK-GDRYVLNGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 193 KIFITYGehdmTDNIVHFVLARlPDAPAGTKGISLFLVPKFMVNAdgSLGQRNDiyasgvehKLGMHASPTCTMTMGDHG 272
Cdd:cd01156 151 KMWITNG----PDADTLVVYAK-TDPSAGAHGITAFIVEKGMPGF--SRAQKLD--------KLGMRGSNTCELVFEDCE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 273 GAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGsksdgsDAIFVHPDVKRMLMRM 351
Cdd:cd01156 216 VPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQfGQPIG------EFQLVQGKLADMYTRL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 352 RaqtaAARTicYATAVAIDVSTRARDPKvradaAARAALLtpmakgYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRD 431
Cdd:cd01156 290 N----ASRS--YLYTVAKACDRGNMDPK-----DAAGVIL------YAAEKATQVALDAIQILGGNGYINDYPTGRLLRD 352
|
410 420
....*....|....*....|...
gi 654685427 432 ARITAIYEGTNGIQAIdLVTRKL 454
Cdd:cd01156 353 AKLYEIGAGTSEIRRM-VIGREL 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
95-444 |
6.17e-37 |
|
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: 142.22 E-value: 6.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 95 PEDFGGQGLPIAINAACTEIWSAsNLAFGLcplltasameALDAH-----------GSSELKKIYLEKLVSGEWTGTMQL 163
Cdd:cd01161 76 PEEYGGLGLNNTQYARLAEIVGM-DLGFSV----------TLGAHqsigfkgillfGTEAQKEKYLPKLASGEWIAAFAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 164 TEPQAGSDVGALRTRAEKQADGT-YRIKGTKIFITYGehDMTDNIVHFVLARLPDAPAGTK-GISLFLVPKfmvnadgSL 241
Cdd:cd01161 145 TEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIADIFTVFAKTEVKDATGSVKdKITAFIVER-------SF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 242 GqrndiyasGV-----EHKLGMHASPTCTMTMGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQAL 316
Cdd:cd01161 216 G--------GVtngppEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 317 SYAQERKQgraVGSKsdgsdaIFVHPDVKRMLMRMRAQTAAARTICYATAVAIDVSTRARdpkvradaaarAALLTPMAK 396
Cdd:cd01161 288 DYANNRKQ---FGKK------IHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAE-----------YQIEAAISK 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 654685427 397 GYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGI 444
Cdd:cd01161 348 VFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEI 395
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
42-454 |
3.04e-31 |
|
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: 125.39 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 42 EEAGKFATDVLAPLNKVGDEHGiklsdgkvtTAPgWPDAYKRWTEGGWNAvSGPEDFGGQGLPIAINAACTEiwsasNLA 121
Cdd:cd01157 10 ETARKFAREEIIPVAAEYDKSG---------EYP-WPLIKRAWELGLMNT-HIPEDCGGLGLGTFDTCLITE-----ELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 122 FGLCPLLTASAMEALDA-----HGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQADgTYRIKGTKIFI 196
Cdd:cd01157 74 YGCTGVQTAIEANSLGQmpviiSGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 197 TYGEHDMTdnivHFVLARL---PDAPAGtKGISlflvpKFMVNADGSLGQRNDiyasgVEHKLGMHASPTCTMTMGDHGG 273
Cdd:cd01157 153 TNGGKANW----YFLLARSdpdPKCPAS-KAFT-----GFIVEADTPGIQPGR-----KELNMGQRCSDTRGITFEDVRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 274 AIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKqgrAVGSksdgsdAIFVHPDVKRMLMRMRA 353
Cdd:cd01157 218 PKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERK---TFGK------LIAEHQAVSFMLADMAM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 354 QTAAARTICYATAVAIDVSTRArdpkvradaaaraALLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDAR 433
Cdd:cd01157 289 KVELARLAYQRAAWEVDSGRRN-------------TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAK 355
|
410 420
....*....|....*....|.
gi 654685427 434 ITAIYEGTNGIQAIdLVTRKL 454
Cdd:cd01157 356 IYQIYEGTSQIQRL-IISREH 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
39-447 |
3.09e-28 |
|
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: 116.69 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 39 AVLEEAGKFATDVLAPLNKVGDEHGiklsdgkvtTAPgwPDAYKRWTEGGWNAVSgPEDFGGQGLPIAINA-ACTEIWSA 117
Cdd:cd01151 19 AIRDTAREFCQEELAPRVLEAYREE---------KFD--RKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGlIAREVERV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 118 SNLAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAeKQADGTYRIKGTKIFIT 197
Cdd:cd01151 87 DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA-RKDGGGYKLNGSKTWIT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 198 ygEHDMTDNIVhfVLARLpdapAGTKGISLFLVPKfmvNADGslgqrndIYASGVEHKLGMHASPTCTMTMGDhggaigF 277
Cdd:cd01151 166 --NSPIADVFV--VWARN----DETGKIRGFILER---GMKG-------LSAPKIQGKFSLRASITGEIVMDN------V 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 278 LIGEEN-----QGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQgravgsksdgsdaiFVHPDVKRMLMRMR 352
Cdd:cd01151 222 FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQ--------------FGRPLAAFQLVQKK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 353 AQTAAARtICYATAVAIDVStRARDpkvradaaarAALLTP----MAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQH 428
Cdd:cd01151 288 LADMLTE-IALGLLACLRVG-RLKD----------QGKATPeqisLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRH 355
|
410
....*....|....*....
gi 654685427 429 YRDARITAIYEGTNGIQAI 447
Cdd:cd01151 356 MVNLESVNTYEGTHDIHAL 374
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-445 |
8.35e-26 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 103.49 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 283 NQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaifvHPDVKRMLMRMRAQTAAARTI 361
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAfGRPLID----------FQLVRHKLAEMAAEIEAARLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 362 CYATAVAIDVSTRARdpkvradaaaraaLLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGT 441
Cdd:pfam00441 71 VYRAAEALDAGGPDG-------------AEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGT 137
|
....
gi 654685427 442 NGIQ 445
Cdd:pfam00441 138 SEIQ 141
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
34-454 |
3.38e-25 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 108.04 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 34 ADIAAAVLEEAGKFATDVLAPlnkvgdeHGIKLSdgKVTTAPGWPDAYKRWTEGGWNAVSGPEDFGGQGLPIAINA-ACT 112
Cdd:PLN02519 27 DDTQLQFKESVQQFAQENIAP-------HAAAID--ATNSFPKDVNLWKLMGDFNLHGITAPEEYGGLGLGYLYHCiAME 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 113 EIWSASN---LAFG----LCplltasaMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKqADG 185
Cdd:PLN02519 98 EISRASGsvgLSYGahsnLC-------INQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAER-VDG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 186 TYRIKGTKIFITYGEHDMTdnivhFVLARLPDAPAGTKGISLFLVPKFMVNAdgSLGQRNDiyasgvehKLGMHASPTCT 265
Cdd:PLN02519 170 GYVLNGNKMWCTNGPVAQT-----LVVYAKTDVAAGSKGITAFIIEKGMPGF--STAQKLD--------KLGMRGSDTCE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 266 MTMGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSKSdgsdaiFVHPDV 344
Cdd:PLN02519 235 LVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQfGRPIGEFQ------FIQGKL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 345 KRMLMRMRAQTAaarticYATAVAIDVSTRARDPKvradaAARAALLtpmakgYSTDIGNEVAYLGVQVHGGMGFIEETG 424
Cdd:PLN02519 309 ADMYTSLQSSRS------YVYSVARDCDNGKVDRK-----DCAGVIL------CAAERATQVALQAIQCLGGNGYINEYP 371
|
410 420 430
....*....|....*....|....*....|
gi 654685427 425 AAQHYRDARITAIYEGTNGIQAIdLVTRKL 454
Cdd:PLN02519 372 TGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
161-500 |
9.24e-25 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 108.30 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 161 MQLTEPQAGSDVGALRTRAEKQADGTYRIKGTKIFITYGEHDmtdniVHFVLARlpdapaGTKGISLFLVPKFMVNadgs 240
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQ------AKGGLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 241 lGQRNDIYASGVEHKLGMHASPTCTMTMGDhggAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQALSYAQ 320
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQD---AIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAH 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 321 ERKqgrAVGSksdgsdAIFVHPDVKRMLMRMRAQTAAARTICYATAVAIDvstRARDPKvradAAARAALLTPMAKGYST 400
Cdd:PRK11561 323 QRQ---VFGK------PLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD---RRADAK----EALWARLFTPAAKFVIC 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 401 DIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAIDlVTRKLAANGGaaVWALLDELAATVKKVEASN 480
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLD-VLRVLNKQPG--VYDLLSEAFVEVKGQDRHF 463
|
330 340
....*....|....*....|
gi 654685427 481 DPAFGTTGVKLREALEALTR 500
Cdd:PRK11561 464 DRAVRQLQQRLRKPAEEQGR 483
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
79-441 |
3.23e-23 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 102.32 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 79 DAYKRWTEGGWNAVSGPEDFGGQGLPIAinAACTEIWSASNLAFGLCPLLTASAMEALDA---HGSSELKKIYLEKLVSG 155
Cdd:PTZ00461 72 DLFKQLGDLGVMGVTVPEADGGAGMDAV--AAVIIHHELSKYDPGFCLAYLAHSMLFVNNfyySASPAQRARWLPKVLTG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 156 EWTGTMQLTEPQAGSDVGALRTRAEKQADGTYRIKGTKIFITYGehdmTDNIVHFVLARLPDApagtkgISLFLVPKFMv 235
Cdd:PTZ00461 150 EHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNG----TVADVFLIYAKVDGK------ITAFVVERGT- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 236 nADGSLGQRNDiyasgvehKLGMHASPTCTMTMGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAYQQA 315
Cdd:PTZ00461 219 -KGFTQGPKID--------KCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 316 LSYAQERKqgrAVGSKsdgsdaIFVHPDVKRMLMRMRAQTAAARTICYATAVAIDVSTRARdpkvradaaaraaLLTPMA 395
Cdd:PTZ00461 290 TSYASERK---AFGKP------ISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNR-------------LGSDAA 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 654685427 396 KGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGT 441
Cdd:PTZ00461 348 KLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
140-444 |
6.13e-22 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 97.88 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 140 GSSE-LKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALRTRAEKQaDGTYRIKGTKIFITYGehdmTDNIVHFVLARLPDA 218
Cdd:PRK12341 100 GSAEqLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRK-NGKVYLNGQKTFITGA----KEYPYMLVLARDPQP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 219 PAGTKGISLFLVPKfmvNADGSlgQRNDIyasgveHKLGMHASPTCTMTMGDHGGAIGFLIGEENQG-MRCM--FTMmnq 295
Cdd:PRK12341 175 KDPKKAFTLWWVDS---SKPGI--KINPL------HKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGfLNVMynFEM--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 296 ARLGVGLEGVGVADRAYQQALSYAQERKQ-GRAVGSksdgsdaiFVHPDVKRMLMRMRAQTAaaRTICYATAVAID--VS 372
Cdd:PRK12341 241 ERLINAARSLGFAECAFEDAARYANQRIQfGKPIGH--------NQLIQEKLTLMAIKIENM--RNMVYKVAWQADngQS 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654685427 373 TRardpkvradaaaraaLLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGI 444
Cdd:PRK12341 311 LR---------------TSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
466-585 |
3.10e-21 |
|
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: 89.53 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 466 LDELAATVKkvEASNDPAFGTTGVKLREALEALTRTSKWLLERVTSA-PNEALAGATPYLQQFGSTLGGCLLASEALAAK 544
Cdd:pfam12806 1 LAEIRAFIA--AAAGDPALAAEAAALAAALAALQEATAWLLARAAKGdPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 654685427 545 ---ADGNTDAARY---VSLARFFAENISVQAGALERTVTESAESVAA 585
Cdd:pfam12806 79 aklAAGAKDAAFYegkIATARFFAERVLPRTAALAAAIEAGDDSLMA 125
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
80-445 |
1.43e-18 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 87.79 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 80 AYKRWT----EGGWNAVSGPEDFGGQGLPIAINAACTEIWSASNLAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSG 155
Cdd:cd01152 36 DRRRWQralaAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 156 EWTGTMQLTEPQAGSDVGALRTRAEKQADGtYRIKGTKIFITYGEH-DMtdnivHFVLARLPDAPAGTKGISLFLVpkfm 234
Cdd:cd01152 116 EEIWCQGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAHYaDW-----AWLLVRTDPEAPKHRGISILLV---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 235 vnadgslgqrnDIYASGVE---HKLGMHASPTCTMTMGDHGGAIGFLIGEENQGMR-CMFTMMNQaRLGVGlegvGVADR 310
Cdd:cd01152 186 -----------DMDSPGVTvrpIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKvAMTTLNFE-RVSIG----GSAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 311 AYQQALSYAQERKQGRAVGSKSdgsdaifvhPDVKRMLMRMRAQTAAARTICYaTAVAIDVSTRARDPKvradaaaraal 390
Cdd:cd01152 250 FFELLLARLLLLTRDGRPLIDD---------PLVRQRLARLEAEAEALRLLVF-RLASALAAGKPPGAE----------- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654685427 391 lTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQ--------HYRDARITAIYEGTNGIQ 445
Cdd:cd01152 309 -ASIAKLFGSELAQELAELALELLGTAALLRDPAPGAelagrweaDYLRSRATTIYGGTSEIQ 370
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
160-268 |
6.67e-15 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 70.39 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 160 TMQLTEPQAGSDVGALRTRAEKQADGTYRIKGTKIFITYGehdmTDNIVHFVLARlPDAPAGTKGISLFLVPKfmvNADG 239
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNA----GIADLFLVLAR-TGGDDRHGGISLFLVPK---DAPG 72
|
90 100
....*....|....*....|....*....
gi 654685427 240 slgqrndIYASGVEHKLGMHASPTCTMTM 268
Cdd:pfam02770 73 -------VSVRRIETKLGVRGLPTGELVF 94
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
83-449 |
1.42e-12 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 69.48 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 83 RWTEG----GWNAVSGPEDFGGQGLPIAINAActeIWSASNLAFGLCPLL--TASAMEALDAHGSSELKKIYLEKLVSGE 156
Cdd:PRK03354 41 RFVKAladmGIDSLLIPEEHGGLDAGFVTLAA---VWMELGRLGAPTYVLyqLPGGFNTFLREGTQEQIDKIMAFRGTGK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 157 WTGTMQLTEPQAGSDVGALRTrAEKQADGTYRIKGTKIFITYGEHdmTDNIVhfVLARlpDAPAGTKGIslflVPKFMVn 236
Cdd:PRK03354 118 QMWNSAITEPGAGSDVGSLKT-TYTRRNGKVYLNGSKCFITSSAY--TPYIV--VMAR--DGASPDKPV----YTEWFV- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 237 adgslgqrnDIYASGVE----HKLGMHASPTCTMTMGDHGGAIGFLIGEENQGMRCMFTMMNQARLGVGLEGVGVADRAY 312
Cdd:PRK03354 186 ---------DMSKPGIKvtklEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 313 QQALSYAQERKQ-GRAVGSKSDGSDAiFVHPDVKRMLMrmraqtaaaRTICYATAVAIDVSTRARDPkvradaaaraall 391
Cdd:PRK03354 257 EDAARYANQRVQfGEAIGRFQLIQEK-FAHMAIKLNSM---------KNMLYEAAWKADNGTITSGD------------- 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 654685427 392 TPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAIDL 449
Cdd:PRK03354 314 AAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL 371
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
39-156 |
3.42e-08 |
|
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: 51.70 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 39 AVLEEAGKFATDVLAPLNKVGDEHGIklsdgkvttapGWPDAYKRWTEGGWNAVSGPEDFGGQGLPIAINAACTEIWSAS 118
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDEEGE-----------FPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARA 74
|
90 100 110
....*....|....*....|....*....|....*....
gi 654685427 119 NLAFGLCPLLTAS-AMEALDAHGSSELKKIYLEKLVSGE 156
Cdd:pfam02771 75 DASVALALSVHSSlGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
98-451 |
2.44e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 53.32 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 98 FGGQGLPIAINAACT-EIWSASNLAFGLCPLLTASAMEALDAHGSSELKKIYLEKLVSGEWTGTMQLTEPQAGSDVGALR 176
Cdd:PLN02526 82 YGCPGLSITASAIATaEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 177 TRAEKqADGTYRIKGTKIFItyGEHDMTDNIVhfVLARlpdaPAGTKGISLFLVPKfmvnadGSLGQRndiyASGVEHKL 256
Cdd:PLN02526 162 TTATK-VEGGWILNGQKRWI--GNSTFADVLV--IFAR----NTTTNQINGFIVKK------GAPGLK----ATKIENKI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 257 GMHASPTCTMTMGDhggaiGFLIGEENQGMRCMFTMMNQ----ARLGVGLEGVGVADRAYQQALSYAQERKQGRAVGSKS 332
Cdd:PLN02526 223 GLRMVQNGDIVLKD-----VFVPDEDRLPGVNSFQDTNKvlavSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 333 DGSDAIFVhpdvkRMLMRMRAQTAAARTIC--YATAVaidvstrardpkvradaaaraalLTP----MAKGYSTDIGNEV 406
Cdd:PLN02526 298 QINQEKLV-----RMLGNIQAMFLVGWRLCklYESGK-----------------------MTPghasLGKAWITKKARET 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 654685427 407 AYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTNGIQAidLVT 451
Cdd:PLN02526 350 VALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINA--LVT 392
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
299-442 |
8.67e-04 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 39.64 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654685427 299 GVGLEGVGVADRAYQQALSYAQERKQGRAVGSKSDGSDAIFvhpdvkrMLMRMRAQTAAARTICYATAVAIDVSTRARDP 378
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQL-------ALAEAAARIDAARLLLERAAARIEAAAAAGKP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654685427 379 kvradAAARAALLTPMAKGYSTDIGNEVAYLGVQVHGGMGFIEETGAAQHYRDARITAIYEGTN 442
Cdd:pfam08028 74 -----VTPALRAEARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| |
