|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-591 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 566.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 3 EYKAPLREMNFLLHEVFEADKLWARLPALADTadRETADAILEEMAKLAANTLDPINRTGDEEGCHW-NDGVVSTPKGFP 81
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLGKTDVT--KELMDSLLEEASKLATQTLLPLYESSDSEGCVLlKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 82 EAYATYCEGGWGALVGNPEFGGMGMPKMLGAQVEEMICSANISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWA 161
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 162 GAMDLTEPHAGTDLGIIRTKAEPQEDGSYSITGSKIFITGGDHDLSENIIHLVLAKLPDAPKGPKGISLFLVPKIMVNED 241
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 242 GSLGERNAVSCGSIEHKMGIKASSTCAMNFDGAKGWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARD 321
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 322 RVQSRSPEGAKLPEKAADPIIVHPDVRRMLLTQKALIGGARALSTYVAKWLDL-AKFGEGEEKKHAEALVALLTPVAKAF 400
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIhAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 401 FTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDLIGRKTVA-NSGAFFELFAADVQAFIDAN- 478
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSlKGGNEVARFGKRVSKLVRAHl 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 479 GDNEALAEFIQPLGAELQRLKEVTAAVIEASKTDPNAPGAASVEYLHLFGYVAYAYMWAKVVSVA----APQADADDFYR 554
Cdd:PTZ00456 503 FSRGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAqkkvAAGQDADGFYQ 582
|
570 580 590
....*....|....*....|....*....|....*..
gi 1151112981 555 TQVKTARFYFARLLPQAAALSSSVLAGSETLMDLEEA 591
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAGPSIMASKEEN 619
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
43-457 |
1.07e-172 |
|
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: 495.76 E-value: 1.07e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 43 ILEEMAKLAANTLDPINRTGDEEGCHWNDGVVSTPKGFPEAYATYCEGGWGALVGNPEFGGMGMPKMLGAQVEEMIcSAN 122
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 123 ISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDGSYSITGSKIFITGG 202
Cdd:cd01153 80 DAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 203 DHDLSENIIHLVLAKLPDAPKGPKGISLFLVPKIMVNedgslGERNAVSCGSIEHKMGIKASSTCAMNFDGAKGWLVGEL 282
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 283 NKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQSRSPegakLPEKAADPIIVHPDVRRMLLTQKALIGGAR 362
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDL----IKAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 363 ALSTYVAKWLDLAKFG--EGEEKKHAEALVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIY 440
Cdd:cd01153 311 ALDLYTATVQDLAERKatEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*..
gi 1151112981 441 EGTNGIQALDLIGRKTV 457
Cdd:cd01153 391 EGTTGIQALDLIGRKIV 407
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-461 |
2.05e-116 |
|
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: 351.06 E-value: 2.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 38 ETADAILEEMAKLAANTLDPINRTGDEEGchwndgvvstpkGFP-EAYATYCEGGWGALVGNPEFGGMGMPKMLGAQVEE 116
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG------------EFPrELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 117 MICSANISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDGsYSITGSK 196
Cdd:COG1960 75 ELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 197 IFITGGD-HDlseniIHLVLAKLPDAPkGPKGISLFLVPKimvNEDGslgernaVSCGSIEHKMGIKASSTCAMNFDG-- 273
Cdd:COG1960 154 TFITNAPvAD-----VILVLARTDPAA-GHRGISLFLVPK---DTPG-------VTVGRIEDKMGLRGSDTGELFFDDvr 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 274 -AKGWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQsrspegaklpekAADPIIVHPDVRRMLL 352
Cdd:COG1960 218 vPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 353 TQKALIGGARALSTYVAKWLDlakfgegeekkhAEALVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVR 432
Cdd:COG1960 286 DMAAELEAARALVYRAAWLLD------------AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 1151112981 433 DVRITQIYEGTNGIQALDlIGRKTVANSG 461
Cdd:COG1960 354 DARILTIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
138-451 |
8.50e-60 |
|
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: 202.13 E-value: 8.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 138 AIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDGsYSITGSKIFITGGDH-DLseniiHLVLA 216
Cdd:cd00567 47 LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGDaDL-----FIVLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 217 KLPDAPKGPKGISLFLVPKimvnedgslgERNAVSCGSIEHKMGIKASSTCAMNFDGAK---GWLVGELNKGLAAMFTMM 293
Cdd:cd00567 121 RTDEEGPGHRGISAFLVPA----------DTPGVTVGRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEEGGGFELAMKGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 294 NYERLGVGIQGLGASERSYQSAIEYARDRVQsrspegaklpekAADPIIVHPDVRRMLLTQKALIGGARALsTYVAKWLd 373
Cdd:cd00567 191 NVGRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLL-LYRAAWL- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151112981 374 lakfgegeeKKHAEALVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDL 451
Cdd:cd00567 257 ---------LDQGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-449 |
4.87e-57 |
|
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: 195.95 E-value: 4.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 38 ETADAILEEMAKLAANTLDPINRTGDEEGchwndgvvstpkGFP-EAYATYCEGGWGALVGNPEFGGMGMPKMLGAQVEE 116
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKG------------EFPrEVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 117 MICSANISFALYPVLTNGACL-AIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDgSYSITGS 195
Cdd:cd01158 69 ELAKVDASVAVIVSVHNSLGAnPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 196 KIFITGGDHdlseNIIHLVLAKLpDAPKGPKGISLFLVPKimvNEDGslgernaVSCGSIEHKMGIKASSTCAMNFDGA- 274
Cdd:cd01158 148 KMWITNGGE----ADFYIVFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFEDVr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 275 --KGWLVGELNKGLA-AMFTMmNYERLGVGIQGLGASERSYQSAIEYARDRVQsrspegaklpekAADPIIVHPDVRRML 351
Cdd:cd01158 213 vpKENILGEEGEGFKiAMQTL-DGGRIGIAAQALGIAQAALDAAVDYAKERKQ------------FGKPIADFQGIQFKL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 352 LTQKALIGGARALsTYVAKWLDLAkfGEGEEKKHAealvalltpVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLV 431
Cdd:cd01158 280 ADMATEIEAARLL-TYKAARLKDN--GEPFIKEAA---------MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYY 347
|
410
....*....|....*...
gi 1151112981 432 RDVRITQIYEGTNGIQAL 449
Cdd:cd01158 348 RDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
131-450 |
6.46e-53 |
|
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: 186.42 E-value: 6.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 131 LTNGACLAIDAHASEELKQKYLP---NMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDGSYSITGSKIFITGGDHDls 207
Cdd:cd01154 115 MTDAAVYALRKYGPEELKQYLPGllsDRYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 208 eniIHLVLAKLPDAPKGPKGISLFLVPKimVNEDGSlgeRNAVSCGSIEHKMGIKASSTCAMNFDGAKGWLVGELNKGLA 287
Cdd:cd01154 193 ---AALVLARPEGAPAGARGLSLFLVPR--LLEDGT---RNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIY 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 288 AMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVqsrspegaklpeKAADPIIVHPDVRRMLLTQKALIGGARALSTY 367
Cdd:cd01154 265 YILEMLNISRLDNAVAALGIMRRALSEAYHYARHRR------------AFGKPLIDHPLMRRDLAEMEVDVEAATALTFR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 368 VAKWLDLAKFGEGEEKKHAEalvaLLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQ 447
Cdd:cd01154 333 AARAFDRAAADKPVEAHMAR----LATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
...
gi 1151112981 448 ALD 450
Cdd:cd01154 409 ALD 411
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
90-462 |
9.11e-43 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 158.40 E-value: 9.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 90 GGWGALVgNPEFGGMGMPKMLGAQVEEmICSANISFALypvltngaclAIDAHAS-----------EELKQKYLPNMYAG 158
Cdd:cd01161 69 GLFGLQV-PEEYGGLGLNNTQYARLAE-IVGMDLGFSV----------TLGAHQSigfkgillfgtEAQKEKYLPKLASG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 159 TWAGAMDLTEPHAGTDLGIIRTKAEPQEDGS-YSITGSKIFITGGdhDLSEniIHLVLAKLP--DAPKGPK-GISLFLVP 234
Cdd:cd01161 137 EWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEvkDATGSVKdKITAFIVE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 235 KimvnedgSLGernAVSCGSIEHKMGIKASSTCAMNFDGAK---GWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERS 311
Cdd:cd01161 213 R-------SFG---GVTNGPPEKKMGIKGSNTAEVYFEDVKipvENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 312 YQSAIEYARDRVQSRSP--EGAKLPEKAAdpiivhpdvrRMLLTQKAliggARALSTYVAKWLDLakfGEGEEKKHAEAL 389
Cdd:cd01161 283 IEKAVDYANNRKQFGKKihEFGLIQEKLA----------NMAILQYA----TESMAYMTSGNMDR---GLKAEYQIEAAI 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151112981 390 VALLTPVAKAFFTDKGLectvlgqQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQaldligRKTVANSGA 462
Cdd:cd01161 346 SKVFASEAAWLVVDEAI-------QIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL------RLFIALTGL 405
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
89-454 |
2.16e-40 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 151.06 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 89 EGGWGALVGNPEFGGMGMPKMLGAQVEEMICSANISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTE 168
Cdd:cd01162 43 ELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 169 PHAGTDLGIIRTKAEpQEDGSYSITGSKIFITG-GDHDlseniIHLVLAKlpDAPKGPKGISLFLVPKimvnedGSLGer 247
Cdd:cd01162 123 PGSGSDAAALRTRAV-REGDHYVLNGSKAFISGaGDSD-----VYVVMAR--TGGEGPKGISCFVVEK------GTPG-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 248 naVSCGSIEHKMGIKASSTCAMNFDGAK---GWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQ 324
Cdd:cd01162 187 --LSFGANEKKMGWNAQPTRAVIFEDCRvpvENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 325 SRSPEGA------KLPEKAADPIIVHPDVRRmlltqkaligGARALstyvakwldlakfgegeEKKHAEAlvALLTPVAK 398
Cdd:cd01162 265 FGKPLADfqalqfKLADMATELVASRLMVRR----------AASAL-----------------DRGDPDA--VKLCAMAK 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151112981 399 AFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALdLIGR 454
Cdd:cd01162 316 RFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIAR 370
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
100-457 |
1.49e-38 |
|
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: 145.72 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 100 EFGGMGMPKMLGAQVEEMICSANISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIR 179
Cdd:cd01160 52 EYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 180 TKAepQEDGS-YSITGSKIFITGGDHdlseNIIHLVLAKLPDAPKGPKGISLFLVpkimvnEDGSLGernaVSCGSIEHK 258
Cdd:cd01160 132 TTA--RKDGDhYVLNGSKTFITNGML----ADVVIVVARTGGEARGAGGISLFLV------ERGTPG----FSRGRKLKK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 259 MGIKASSTCAMNFDGA---KGWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERsyqsAIEYARDRVQSRSPEGAKLPE 335
Cdd:cd01160 196 MGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEF----MLEETRNYVKQRKAFGKTLAQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 336 KAAdpiivhpdVRRMLLTQKALIGGARALsTYVAKWLDlakfgegEEKKHAEALVALltpvAKAFFTDKGLECTVLGQQV 415
Cdd:cd01160 272 LQV--------VRHKIAELATKVAVTRAF-LDNCAWRH-------EQGRLDVAEASM----AKYWATELQNRVAYECVQL 331
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1151112981 416 FGGHGYIREWGQEQLVRDVRITQIYEGTNGIQaLDLIGRKTV 457
Cdd:cd01160 332 HGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
468-588 |
2.54e-37 |
|
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: 134.60 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 468 AADVQAFIDANGDNEALAEFIQPLGAELQRLKEVTAAVIE-ASKTDPNAPGAASVEYLHLFGYVAYAYMWAKVVSVAAPQ 546
Cdd:pfam12806 1 LAEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLArAAKGDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1151112981 547 ADA----DDFYRTQVKTARFYFARLLPQAAALSSSVLAGSETLMDL 588
Cdd:pfam12806 81 LAAgakdAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
99-458 |
1.64e-35 |
|
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: 137.54 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 99 PEFGGMGMPKMLGAQVEEMICSANISFAL-YPVLTNgACL-AIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLG 176
Cdd:cd01156 54 EEYGGSGMGYLAHVIIMEEISRASGSVALsYGAHSN-LCInQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 177 IIRTKAEpQEDGSYSITGSKIFITGG-DHDlseniIHLVLAKlPDAPKGPKGISLFLVPKIMvnedgslgerNAVSCGSI 255
Cdd:cd01156 133 SMKLRAE-KKGDRYVLNGSKMWITNGpDAD-----TLVVYAK-TDPSAGAHGITAFIVEKGM----------PGFSRAQK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 256 EHKMGIKASSTCAMNFDGAK---GWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQSRSPEG-- 330
Cdd:cd01156 196 LDKLGMRGSNTCELVFEDCEvpeENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGef 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 331 AKLPEKAADpiivhpdvrrMLLTQKAliggARALSTYVAKWLDlakFGEGEEKkhaEALVALLTPVAKAffTDKGLEctv 410
Cdd:cd01156 276 QLVQGKLAD----------MYTRLNA----SRSYLYTVAKACD---RGNMDPK---DAAGVILYAAEKA--TQVALD--- 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1151112981 411 lGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALdLIGRKTVA 458
Cdd:cd01156 331 -AIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM-VIGRELFK 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
99-454 |
4.68e-32 |
|
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: 127.86 E-value: 4.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 99 PEFGGMGMpkmLGAQVEEMICS--ANISFAL---------------YPVLTNGACLAIDAHASEELKQKYLPNMYAGTWA 161
Cdd:cd01151 51 EEMGELGL---LGATIKGYGCAglSSVAYGLiarevervdsgyrsfMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 162 GAMDLTEPHAGTDLGIIRTKAEPQEDGsYSITGSKIFITGGdhDLSENIIhlVLAKLPDAPKgpkgISLFLVPKIMvneD 241
Cdd:cd01151 128 GCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKTWITNS--PIADVFV--VWARNDETGK----IRGFILERGM---K 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 242 GslgernaVSCGSIEHKMGIKASSTCAMNFDGAKgwlVGELN-----KGLAAMFTMMNYERLGVGIQGLGASERSYQSAI 316
Cdd:cd01151 196 G-------LSAPKIQGKFSLRASITGEIVMDNVF---VPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTAR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 317 EYARDRVQSRSPEGAK--LPEKAADPIIvhpDVRRMLLtqkaliggaraLSTYVAKWLDlakfgegeEKKHAEALVALLt 394
Cdd:cd01151 266 QYVLDRKQFGRPLAAFqlVQKKLADMLT---EIALGLL-----------ACLRVGRLKD--------QGKATPEQISLL- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 395 pvaKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALdLIGR 454
Cdd:cd01151 323 ---KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL-ILGR 378
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
109-500 |
9.81e-25 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 108.30 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 109 MLGAQVEE-MICSANISFALYPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGA----MDLTEPHAGTDLGIIRTKAE 183
Cdd:PRK11561 122 MLHAQVEAgTLCPITMTFAATPLLLQMLPAPFQDWLTPLLSDRYDSHLLPGGQKRGlligMGMTEKQGGSDVLSNTTRAE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 184 PQEDGSYSITGSKIFITGGDHDlseniIHLVLAKlpdapkGPKGISLFLVPKIMVNedgslGERNAVSCGSIEHKMGIKA 263
Cdd:PRK11561 202 RLADGSYRLVGHKWFFSVPQSD-----AHLVLAQ------AKGGLSCFFVPRFLPD-----GQRNAIRLERLKDKLGNRS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 264 SSTCAMNFDGAKGWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRvqsrspegaklpEKAADPIIV 343
Cdd:PRK11561 266 NASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR------------QVFGKPLIE 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 344 HPdVRRMLLTQKALiggarALSTYVAKWLDLAKFGEGEEKKHAEALVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIR 423
Cdd:PRK11561 334 QP-LMRQVLSRMAL-----QLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCE 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151112981 424 EWGQEQLVRDVRITQIYEGTNGIQALDLIgrKTVANSGAFFELFAadvQAFIDANGDNEALAEFIQPLGAELQRLKE 500
Cdd:PRK11561 408 ESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLNKQPGVYDLLS---EAFVEVKGQDRHFDRAVRQLQQRLRKPAE 479
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-454 |
2.74e-23 |
|
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: 96.17 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 283 NKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQsrspegaklpekAADPIIVHPDVRRMLLTQKALIGGAR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKA------------FGRPLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 363 ALSTYVAKWLDlakfgegeekkhAEALVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEG 442
Cdd:pfam00441 69 LLVYRAAEALD------------AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEG 136
|
170
....*....|..
gi 1151112981 443 TNGIQaLDLIGR 454
Cdd:pfam00441 137 TSEIQ-RNIIAR 147
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
99-454 |
4.87e-23 |
|
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: 101.12 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 99 PE-FGGMGMPKMLGAQVEEMI---CS-------ANiSFALYPVLTNGaclaidahaSEELKQKYLPNMYAGTWAGAMDLT 167
Cdd:cd01157 52 PEdCGGLGLGTFDTCLITEELaygCTgvqtaieAN-SLGQMPVIISG---------NDEQKKKYLGRMTEEPLMCAYCVT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 168 EPHAGTDLGIIRTKAEPQEDgSYSITGSKIFITGGDHdlseNIIHLVLAKLPDAPKGP--KGISLFLVPkimvnedgslG 245
Cdd:cd01157 122 EPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGK----ANWYFLLARSDPDPKCPasKAFTGFIVE----------A 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 246 ERNAVSCGSIEHKMGIKASSTCAMNFDG----AKGWLVGElNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARD 321
Cdd:cd01157 187 DTPGIQPGRKELNMGQRCSDTRGITFEDvrvpKENVLIGE-GAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 322 RvqsrspegaklpEKAADPIIVHPDVRRMLLTQKALIGGARaLSTYVAKWldlakfgEGEEKKHAEALVAlltpVAKAFF 401
Cdd:cd01157 266 R------------KTFGKLIAEHQAVSFMLADMAMKVELAR-LAYQRAAW-------EVDSGRRNTYYAS----IAKAFA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1151112981 402 TDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALdLIGR 454
Cdd:cd01157 322 ADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL-IISR 373
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
100-455 |
6.95e-23 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 101.11 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 100 EFGGMGMPKMLGAQVEEMICSANISFAL-YPVLTNGACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGII 178
Cdd:PLN02519 81 EYGGLGLGYLYHCIAMEEISRASGSVGLsYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 179 RTKAEpQEDGSYSITGSKIFITGGDhdlSENIIhLVLAKlPDAPKGPKGISLFLVPKIMvnedgslgerNAVSCGSIEHK 258
Cdd:PLN02519 161 KCKAE-RVDGGYVLNGNKMWCTNGP---VAQTL-VVYAK-TDVAAGSKGITAFIIEKGM----------PGFSTAQKLDK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 259 MGIKASSTCAMNFDGA---KGWLVGELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRVQSRSPEG--AKL 333
Cdd:PLN02519 225 LGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGefQFI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 334 PEKAADpiivhpdvrrMLLTQKAliggARALSTYVAKWLDLakfGEGEEKKHAEALValltpvakaFFTDKGLECTVLGQ 413
Cdd:PLN02519 305 QGKLAD----------MYTSLQS----SRSYVYSVARDCDN---GKVDRKDCAGVIL---------CAAERATQVALQAI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1151112981 414 QVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALdLIGRK 455
Cdd:PLN02519 359 QCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGRE 399
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
134-443 |
9.46e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 97.70 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 134 GACLAIDAH-----------ASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEDGSYSITGSKIFITGG 202
Cdd:PTZ00461 114 GFCLAYLAHsmlfvnnfyysASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 203 dhdlSENIIHLVLAKLPDApkgpkgISLFLVpkimvnEDGSLGernaVSCGSIEHKMGIKASSTCAMNFDGA---KGWLV 279
Cdd:PTZ00461 194 ----TVADVFLIYAKVDGK------ITAFVV------ERGTKG----FTQGPKIDKCGMRASHMCQLFFEDVvvpAENLL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 280 GELNKGLAAMFTMMNYERLGVGIQGLGASERSYQSAIEYARDRvqsrspegaklpEKAADPIIVHPDVRRMLLTQKALIG 359
Cdd:PTZ00461 254 GEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER------------KAFGKPISNFGQIQRYIAEGYADTE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 360 GARALSTYVAKwlDLAKFGEGEEKKHAEALVAllTPVAKAfFTDKGLectvlgqQVFGGHGYIREWGQEQLVRDVRITQI 439
Cdd:PTZ00461 322 AAKALVYSVSH--NVHPGNKNRLGSDAAKLFA--TPIAKK-VADSAI-------QVMGGMGYSRDMPVERLWRDAKLLEI 389
|
....
gi 1151112981 440 YEGT 443
Cdd:PTZ00461 390 GGGT 393
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
80-446 |
1.87e-21 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 96.72 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 80 FPEAYATYC-EGG------WGALVGNPeFGGMGMPKMLGAQ----VEEMICSANIS--FALYPVLTNGACLAIDAH--AS 144
Cdd:PRK12341 24 FPEEYFRTCdENGtyprefMRALADNG-ISMLGVPEEFGGTpadyVTQMLVLEEVSkcGAPAFLITNGQCIHSMRRfgSA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 145 EELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEpQEDGSYSITGSKIFITGGdhdlSENIIHLVLAKLPDAPKG 224
Cdd:PRK12341 103 EQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITGA----KEYPYMLVLARDPQPKDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 225 PKGISLFLVPKimvNEDGSlgERNAVscgsieHKMGIKASSTCAMNFDGA---KGWLVGElnKGLAAMFTMMNY--ERLG 299
Cdd:PRK12341 178 KKAFTLWWVDS---SKPGI--KINPL------HKIGWHMLSTCEVYLDNVeveESDLVGE--EGMGFLNVMYNFemERLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 300 VGIQGLGASERSYQSAIEYARDRVQSRSPEGAK--LPEKAADPIIVHPDVRRMLltqkaliggaralstYVAKWldlakf 377
Cdd:PRK12341 245 NAARSLGFAECAFEDAARYANQRIQFGKPIGHNqlIQEKLTLMAIKIENMRNMV---------------YKVAW------ 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151112981 378 gegeEKKHAEAlVALLTPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGI 446
Cdd:PRK12341 304 ----QADNGQS-LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
89-454 |
5.81e-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: 85.86 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 89 EGGWGALVGNPEFGGMGMPKMLGAQVEEMICSANisfALYPVLTNGACLA---IDAHASEELKQKYLPNMYAGTWAGAMD 165
Cdd:cd01152 46 AAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG---APVPFNQIGIDLAgptILAYGTDEQKRRFLPPILSGEEIWCQG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 166 LTEPHAGTDLGIIRTKAEpQEDGSYSITGSKIFITGG---DHdlseniiHLVLAKL-PDAPKgPKGISLFLVPkimVNED 241
Cdd:cd01152 123 FSEPGAGSDLAGLRTRAV-RDGDDWVVNGQKIWTSGAhyaDW-------AWLLVRTdPEAPK-HRGISILLVD---MDSP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 242 GslgernaVSCGSIEHKMGikASSTCAMNFDGAK---GWLVGELNKGLAAMFTMMNYERLGVGiqglgaseRSYQSAIEY 318
Cdd:cd01152 191 G-------VTVRPIRSING--GEFFNEVFLDDVRvpdANRVGEVNDGWKVAMTTLNFERVSIG--------GSAATFFEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 319 ARDRVQSRSPEGAKLpekAADpiivhPDVRRMLLtqkALIGGARALStyvAKWLDLAKFGEGEEKKHAEAlvalltPVAK 398
Cdd:cd01152 254 LLARLLLLTRDGRPL---IDD-----PLVRQRLA---RLEAEAEALR---LLVFRLASALAAGKPPGAEA------SIAK 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151112981 399 AFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDV--------RITQIYEGTNGIQaLDLIGR 454
Cdd:cd01152 314 LFGSELAQELAELALELLGTAALLRDPAPGAELAGRweadylrsRATTIYGGTSEIQ-RNIIAE 376
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
2.45e-17 |
|
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: 77.32 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 163 AMDLTEPHAGTDLGIIRTKAEPQEDGSYSITGSKIFITGGDHdlSEniIHLVLAKlPDAPKGPKGISLFLVPKIMVNedg 242
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGI--AD--LFLVLAR-TGGDDRHGGISLFLVPKDAPG--- 72
|
90 100 110
....*....|....*....|....*....|
gi 1151112981 243 slgernaVSCGSIEHKMGIKASSTCAMNFD 272
Cdd:pfam02770 73 -------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
80-456 |
2.81e-13 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 71.79 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 80 FPEAY-ATYCEGGWGALVGNPEFGGMGMPKM-LGAQVEEMICSANISFALYPVltNGACLAIDAHASEELKQKYLPnmYA 157
Cdd:PRK03354 38 YPERFvKALADMGIDSLLIPEEHGGLDAGFVtLAAVWMELGRLGAPTYVLYQL--PGGFNTFLREGTQEQIDKIMA--FR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 158 GT----WAGAMdlTEPHAGTDLGIIRTKAEpQEDGSYSITGSKIFITGgdhdlSENIIHLV-LAKLPDAPKGPKGISLFL 232
Cdd:PRK03354 114 GTgkqmWNSAI--TEPGAGSDVGSLKTTYT-RRNGKVYLNGSKCFITS-----SAYTPYIVvMARDGASPDKPVYTEWFV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 233 ---VPKIMVNEdgslgernavscgsiEHKMGIKASSTCAMNFDGAK---GWLVGELNKGLAAMFTMMNYERLGVGIQGLG 306
Cdd:PRK03354 186 dmsKPGIKVTK---------------LEKLGLRMDSCCEITFDDVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 307 ASERSYQSAIEYARDRVQSRSPEGAK--LPEKAADPIIVHPDVRRMLltqkaliggaralstYVAKWldlaKFGEGEEKK 384
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFqlIQEKFAHMAIKLNSMKNML---------------YEAAW----KADNGTITS 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151112981 385 HAEALvalltpvAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTNGIQALDLiGRKT 456
Cdd:PRK03354 312 GDAAM-------CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL-GRAV 375
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
38-158 |
6.44e-10 |
|
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: 56.70 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 38 ETADAILEEMAKLAANTLDPINRTGDEEGchwndgvvstpkGFP-EAYATYCEGGWGALVGNPEFGGMGMPKMLGAQVEE 116
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEG------------EFPrELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1151112981 117 MICSANISFALYPVLTNG-ACLAIDAHASEELKQKYLPNMYAG 158
Cdd:pfam02771 70 ELARADASVALALSVHSSlGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
135-455 |
4.55e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 55.63 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 135 ACLAIDAHASEELKQKYLPNMYAGTWAGAMDLTEPHAGTDLGIIRTKAEPQEdGSYSITGSKIFItgGDHDLSENIIhlV 214
Cdd:PLN02526 117 AMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVE-GGWILNGQKRWI--GNSTFADVLV--I 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 215 LAKLPDApkgpKGISLFLVPKimvnedGSLGERnavsCGSIEHKMGIKASSTCAMNFDGA----KGWLVG-----ELNKG 285
Cdd:PLN02526 192 FARNTTT----NQINGFIVKK------GAPGLK----ATKIENKIGLRMVQNGDIVLKDVfvpdEDRLPGvnsfqDTNKV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 286 LAamftmmnYERLGVGIQGLGASERSYQSAIEYARDRVQSRSPEGAklpekaadpiivhpdvrrMLLTQKALIggaRALS 365
Cdd:PLN02526 258 LA-------VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAA------------------FQINQEKLV---RMLG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 366 TYVAKWL---DLAKFGEGEEKKHAEAlvalltPVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEG 442
Cdd:PLN02526 310 NIQAMFLvgwRLCKLYESGKMTPGHA------SLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEG 383
|
330
....*....|...
gi 1151112981 443 TNGIQALdLIGRK 455
Cdd:PLN02526 384 TYDINAL-VTGRE 395
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
4-33 |
7.43e-07 |
|
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam02770, pfam00441, pfam02771. This family is one of the enzymes involved in AcylCoA interaction in beta-oxidation.
Pssm-ID: 463571 Cd Length: 32 Bit Score: 45.79 E-value: 7.43e-07
10 20 30
....*....|....*....|....*....|
gi 1151112981 4 YKAPLREMNFLLHEVFEADKlWARLPALAD 33
Cdd:pfam12418 2 YKAPLRDMRFVLYEVLGAEA-LAALPGFAD 30
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
100-217 |
5.99e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 49.11 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 100 EFGGMGMPKMLGAQVEEMICSANISFALYPVLTNGAC-LAIDAHASEELKQKYLPNMYAGT----WAgamdlTEPHAGTD 174
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCtYLLSTVGSKELKGKYLTAMSDGTimmgWA-----TEEGCGSD 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1151112981 175 LGIIRTKAEPQEDGSYSITGSK--IFITGGDHdlseniiHLVLAK 217
Cdd:PTZ00457 148 ISMNTTKASLTDDGSYVLTGQKrcEFAASATH-------FLVLAK 185
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
299-444 |
1.53e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 38.87 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151112981 299 GVGIQGLGASERSYQSAIEYARDRVQSrspegaklpeKAADPIIVHPDVRRMLLTQKALIGGARALsTYVAKWLDLAKFG 378
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRA----------YFGVPLAEDPATQLALAEAAARIDAARLL-LERAAARIEAAAA 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151112981 379 EGEEkkHAEALVALLTpVAKAFFTDKGLECTVLGQQVFGGHGYIREWGQEQLVRDVRITQIYEGTN 444
Cdd:pfam08028 70 AGKP--VTPALRAEAR-RAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| |
