|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
4-581 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 564.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 4 YQAPLRDMRFVLNEVFDAPKLWQALPALAevVDAETADAILEEAGKITANSIAPLNRSGDEEGCRW-DGGAVSTPAGYRE 82
Cdd:PTZ00456 26 YQPRIRDVQFLVEEVFNMYDHYEKLGKTD--VTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLlKDGNVTTPKGFKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 83 AYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSG 162
Cdd:PTZ00456 104 AYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 163 SMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDLTDNIIHLVLAKLPDAPAGSRGISLFLVPKVLVNDDG 242
Cdd:PTZ00456 184 TMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPDG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 243 SLGERNSLSCGSIEHKMGIQASATCVMNFDGATGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARER 322
Cdd:PTZ00456 264 SLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 323 IQSRAPTGPVAQDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVALQLDIAKFSDDEAARQRAEAQVALLTPVAKAFL 402
Cdd:PTZ00456 344 RSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGCL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 403 TDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLVGRKIVGS-GGTMYQAFVDEIRAFVA---- 477
Cdd:PTZ00456 424 TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLkGGNEVARFGKRVSKLVRahlf 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 478 SAGAdLREFTEPLKAALDNLDELTAWVIDQAKTNPNEIGAASVEYLHVFGYTAYAYMWARMAAVALAKQGEGD----FYQ 553
Cdd:PTZ00456 504 SRGA-LGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGQdadgFYQ 582
|
570 580
....*....|....*....|....*...
gi 1332876544 554 SKLGTARFYFARLLPRIHSLTASVKAGS 581
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAGP 610
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
43-458 |
7.28e-173 |
|
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: 496.14 E-value: 7.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 43 ILEEAGKITANSIAPLNRSGDEEGCRWDGGAVSTPAGYREAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMnSAS 122
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 123 LAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGG 202
Cdd:cd01153 80 DAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 203 EHDLTDNIIHLVLAKLPDAPAGSRGISLFLVPKVLVNddgslGERNSLSCGSIEHKMGIQASATCVMNFDGATGWMVGEP 282
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 283 NKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERIQSRAPTgpvaQDKAADPIIVHPDVRRMLLTMKALNEGGR 362
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 363 AFSSYVALQLDIAKFS-DDEAARQRAEAQVALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIY 441
Cdd:cd01153 311 ALDLYTATVQDLAERKaTEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*..
gi 1332876544 442 EGTNGIQALDLVGRKIV 458
Cdd:cd01153 391 EGTTGIQALDLIGRKIV 407
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-462 |
1.64e-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: 1.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 38 ETADAILEEAGKITANSIAPLNRSGDEEGcrwdggavSTPagyREAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEM 117
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 118 MNSASLAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGsYKVSGTKI 197
Cdd:COG1960 76 LARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 198 FITGGE-HDltdniIHLVLAKLPDAPaGSRGISLFLVPKvlvNDDGslgernsLSCGSIEHKMGIQASATCVMNFDG--- 273
Cdd:COG1960 155 FITNAPvAD-----VILVLARTDPAA-GHRGISLFLVPK---DTPG-------VTVGRIEDKMGLRGSDTGELFFDDvrv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 274 ATGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERIQsraptgpvaqdkAADPIIVHPDVRRMLLT 353
Cdd:COG1960 219 PAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 354 MKALNEGGRAFSSYVALQLDiakfsddeaarqrAEAQVALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVR 433
Cdd:COG1960 287 MAAELEAARALVYRAAWLLD-------------AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 1332876544 434 DCRITQIYEGTNGIQALDLvGRKIVGSGG 462
Cdd:COG1960 354 DARILTIYEGTNEIQRLII-ARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
139-452 |
2.65e-55 |
|
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: 190.19 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 139 IYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGsYKVSGTKIFITGGEHdlTDniIHLVLAKL 218
Cdd:cd00567 48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGD--AD--LFIVLART 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 219 PDAPAGSRGISLFLVPKvlvnddGSLGernsLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNY 295
Cdd:cd00567 123 DEEGPGHRGISAFLVPA------DTPG----VTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 296 ERLGVGIQGLATGERSYQSAIEYARERIQsraptgpvaqdkAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVALQLDia 375
Cdd:cd00567 193 GRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD-- 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876544 376 kfsddeaarqRAEAQVALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDL 452
Cdd:cd00567 259 ----------QGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-450 |
1.88e-54 |
|
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: 189.02 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 38 ETADAILEEAGKITANSIAPLNRSGDEEGcRWDggavstpagyREAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEM 117
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKG-EFP----------REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 118 MNSASLAFGLYPMLTSGACLS-IYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADgSYKVSGTK 196
Cdd:cd01158 70 LAKVDASVAVIVSVHNSLGANpIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 197 IFIT-GGEHDltdniIHLVLAKLpDAPAGSRGISLFLVPKvlvNDDGslgernsLSCGSIEHKMGIQASATCVMNFDGA- 274
Cdd:cd01158 149 MWITnGGEAD-----FYIVFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFEDVr 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 275 --TGWMVGEPNKGLA-AMFTMmNYERLGVGIQGLATGERSYQSAIEYARERIQsraptgpvaqdkAADPIIVHPDVRRML 351
Cdd:cd01158 213 vpKENILGEEGEGFKiAMQTL-DGGRIGIAAQALGIAQAALDAAVDYAKERKQ------------FGKPIADFQGIQFKL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 352 LTMKALNEGGRAFSsYVALQLDIAK--FSDDEAArqraeaqvalltpvAKAFLTDMGLETTVHGQQVFGGHGFIREWGQE 429
Cdd:cd01158 280 ADMATEIEAARLLT-YKAARLKDNGepFIKEAAM--------------AKLFASEVAMRVTTDAVQIFGGYGYTKDYPVE 344
|
410 420
....*....|....*....|.
gi 1332876544 430 QLVRDCRITQIYEGTNGIQAL 450
Cdd:cd01158 345 RYYRDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
131-453 |
3.74e-52 |
|
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: 184.11 E-value: 3.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 131 LTSGACLSIYAHASEELKQKYLP---NMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDlt 207
Cdd:cd01154 115 MTDAAVYALRKYGPEELKQYLPGllsDRYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 208 dniIHLVLAKLPDAPAGSRGISLFLVPKVLvNDdgslGERNSLSCGSIEHKMGIQASATCVMNFDGATGWMVGEPNKGLA 287
Cdd:cd01154 193 ---AALVLARPEGAPAGARGLSLFLVPRLL-ED----GTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIY 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 288 AMFTMMNYERLGVGIQGLATGERSYQSAIEYARERiqsraptgpVAQDKaadPIIVHPDVRRMLLTMKALNEGGRAFSSY 367
Cdd:cd01154 265 YILEMLNISRLDNAVAALGIMRRALSEAYHYARHR---------RAFGK---PLIDHPLMRRDLAEMEVDVEAATALTFR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 368 VALQLDIAkfsddEAARQRAEAQVALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGI 447
Cdd:cd01154 333 AARAFDRA-----AADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
....*.
gi 1332876544 448 QALDLV 453
Cdd:cd01154 408 QALDVL 413
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
68-458 |
5.50e-42 |
|
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: 155.35 E-value: 5.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 68 RWD-GGAVStpagyREAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQV-EEMMNSASLAFGLypMLTSGACLS-IYAHAS 144
Cdd:cd01160 24 EWEkAGEVP-----REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLwEELARAGGSGPGL--SLHTDIVSPyITRAGS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 145 EELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADgSYKVSGTKIFITGGEHdlTDniIHLVLAKLPDAPAG 224
Cdd:cd01160 97 PEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML--AD--VVIVVARTGGEARG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 225 SRGISLFLVpkvlvnDDGSLGernsLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYERLGVG 301
Cdd:cd01160 172 AGGISLFLV------ERGTPG----FSRGRKLKKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 302 IQGLATGERSYQSAIEYARERiqsRAPTGPVAQdkaadpiivHPDVRRMLLTMKALNEGGRAFsSYVALQLDIAKFSDDe 381
Cdd:cd01160 242 AGALAAAEFMLEETRNYVKQR---KAFGKTLAQ---------LQVVRHKIAELATKVAVTRAF-LDNCAWRHEQGRLDV- 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1332876544 382 aarqrAEAQvalltpVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQaLDLVGRKIV 458
Cdd:cd01160 308 -----AEAS------MAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
469-584 |
2.07e-39 |
|
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: 140.38 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 469 VDEIRAFVASAGAD--LREFTEPLKAALDNLDELTAWVIDQA-KTNPNEIGAASVEYLHVFGYTAYAYMWARMAAVALAK 545
Cdd:pfam12806 1 LAEIRAFIAAAAGDpaLAAEAAALAAALAALQEATAWLLARAaKGDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1332876544 546 QGEG----DFYQSKLGTARFYFARLLPRIHSLTASVKAGSDSL 584
Cdd:pfam12806 81 LAAGakdaAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSL 123
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
81-458 |
9.46e-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: 146.40 E-value: 9.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 81 REAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLS-IYAHASEELKQKYLPNMYAGV 159
Cdd:cd01156 36 RDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINqIYRNGSAAQKEKYLPKLISGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 160 WSGSMCLTEPHAGTDLGIIRTKAEPQaDGSYKVSGTKIFITGGehdlTDNIIHLVLAKlPDAPAGSRGISLFLVPKvlvN 239
Cdd:cd01156 116 HIGALAMSEPNAGSDVVSMKLRAEKK-GDRYVLNGSKMWITNG----PDADTLVVYAK-TDPSAGAHGITAFIVEK---G 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 240 DDGslgernsLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYER--LGVGIQGLAtgERSYQS 314
Cdd:cd01156 187 MPG-------FSRAQKLDKLGMRGSNTCELVFEDCevpEENILGGENKGVYVLMSGLDYERlvLAGGPIGIM--QAALDV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 315 AIEYARERIQSRAPTG--PVAQDKAADpiivhpdvrrMLLTMKAlnegGRAFSSYVALQLDIAKFSDDEAARqraeaqvA 392
Cdd:cd01156 258 AIPYAHQRKQFGQPIGefQLVQGKLAD----------MYTRLNA----SRSYLYTVAKACDRGNMDPKDAAG-------V 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1332876544 393 LLTPVAKAflTDMGLEttvhGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALdLVGRKIV 458
Cdd:cd01156 317 ILYAAEKA--TQVALD----AIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM-VIGRELF 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
81-450 |
1.42e-35 |
|
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: 138.37 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 81 REAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMnSASLAFGLypmlTSGA-----CLSIYAHASEELKQKYLPNM 155
Cdd:cd01161 59 RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIV-GMDLGFSV----TLGAhqsigFKGILLFGTEAQKEKYLPKL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 156 YAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGS-YKVSGTKIFITGGehDLTDniIHLVLAKLPDA-PAGSR--GISLF 231
Cdd:cd01161 134 ASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEVKdATGSVkdKITAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 232 LVPKvlvnddgSLGernSLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATG 308
Cdd:cd01161 210 IVER-------SFG---GVTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 309 ERSYQSAIEYARERIQSRAPTGP--VAQDKAADPIIVHPDVRRMLLTMKALNEGGrAFSSYvALQLDIAKFSDDEAArqr 386
Cdd:cd01161 280 KRCIEKAVDYANNRKQFGKKIHEfgLIQEKLANMAILQYATESMAYMTSGNMDRG-LKAEY-QIEAAISKVFASEAA--- 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1332876544 387 aeaqvalltpvakAFLTDMGLettvhgqQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQAL 450
Cdd:cd01161 355 -------------WLVVDEAI-------QIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
81-459 |
5.64e-35 |
|
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: 135.65 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 81 REAyqlyAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVW 160
Cdd:cd01162 39 RKA----AELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 161 SGSMCLTEPHAGTDLGIIRTKAEPQADgSYKVSGTKIFITGGehdlTDNIIHLVLAKlpDAPAGSRGISLFLVPKvlvnd 240
Cdd:cd01162 115 LASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISGA----GDSDVYVVMAR--TGGEGPKGISCFVVEK----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 241 dGSLGernsLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIE 317
Cdd:cd01162 183 -GTPG----LSFGANEKKMGWNAQPTRAVIFEDCrvpVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 318 YARERiqsRAPTGPVAQDKAadpiivhpdVRRMLLTMKALNEGGRAFSSYVALQLDiakfsddeaaRQRAEAqvALLTPV 397
Cdd:cd01162 258 YLEER---KQFGKPLADFQA---------LQFKLADMATELVASRLMVRRAASALD----------RGDPDA--VKLCAM 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1332876544 398 AKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALdLVGRKIVG 459
Cdd:cd01162 314 AKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIARALLT 374
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
127-468 |
5.01e-26 |
|
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: 110.14 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 127 LYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGsYKVSGTKIFITGGehDL 206
Cdd:cd01151 93 FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKTWITNS--PI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 207 TDNIIhlVLAKLpdapAGSRGISLFLVPKvlvnddGSLGernsLSCGSIEHKMGIQASATCVMNFDGAtgwMVGEPN--- 283
Cdd:cd01151 170 ADVFV--VWARN----DETGKIRGFILER------GMKG----LSAPKIQGKFSLRASITGEIVMDNV---FVPEENllp 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 284 --KGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERIQSRAPTGP--VAQDKAADPIIvhpDVRRMLLtmkalne 359
Cdd:cd01151 231 gaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAfqLVQKKLADMLT---EIALGLL------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 360 ggrafssyvaLQLDIAKFSDDEAArqrAEAQVALLtpvaKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQ 439
Cdd:cd01151 301 ----------ACLRVGRLKDQGKA---TPEQISLL----KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVN 363
|
330 340
....*....|....*....|....*....
gi 1332876544 440 IYEGTNGIQALdLVGRKIVGsggtmYQAF 468
Cdd:cd01151 364 TYEGTHDIHAL-ILGRAITG-----IQAF 386
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
101-459 |
5.84e-25 |
|
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: 106.90 E-value: 5.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 101 FGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRT 180
Cdd:cd01157 55 CGGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 181 KAEPQADgSYKVSGTKIFITGGEHdltdNIIHLVLAKL---PDAPAgSRGISLFLVPkvlvnddgslGERNSLSCGSIEH 257
Cdd:cd01157 135 KAEKKGD-EYIINGQKMWITNGGK----ANWYFLLARSdpdPKCPA-SKAFTGFIVE----------ADTPGIQPGRKEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 258 KMGIQASATCVMNFDG----ATGWMVGEPNKGLAAMFTMmNYERLGVGIQGLATGERSYQSAIEYARERiqsraptgpva 333
Cdd:cd01157 199 NMGQRCSDTRGITFEDvrvpKENVLIGEGAGFKIAMGAF-DKTRPPVAAGAVGLAQRALDEATKYALER----------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 334 qDKAADPIIVHPDVRRMLLTMKALNEGGRAFSSYVALQLDIAKFSDDEAArqraeaqvalltpVAKAFLTDMGLETTVHG 413
Cdd:cd01157 267 -KTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYAS-------------IAKAFAADIANQLATDA 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1332876544 414 QQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALdLVGRKIVG 459
Cdd:cd01157 333 VQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL-IISREHLG 377
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
84-457 |
6.86e-23 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 101.11 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 84 YQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLS-IYAHASEELKQKYLPNMYAGVWSG 162
Cdd:PLN02519 65 WKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINqLVRNGTPAQKEKYLPKLISGEHVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 163 SMCLTEPHAGTDLGIIRTKAEpQADGSYKVSGTKIFITGGEHDLTdniihLVLAKLPDAPAGSRGISLFLVPKvlvnddG 242
Cdd:PLN02519 145 ALAMSEPNSGSDVVSMKCKAE-RVDGGYVLNGNKMWCTNGPVAQT-----LVVYAKTDVAAGSKGITAFIIEK------G 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 243 SLGernsLSCGSIEHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYA 319
Cdd:PLN02519 213 MPG----FSTAQKLDKLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 320 RERIQSRAPTGP--VAQDKAADpiivhpdvrrMLLTMKAlnegGRAFSSYVALQLDIAKFSddeaarqRAEAQVALLTPV 397
Cdd:PLN02519 289 RQREQFGRPIGEfqFIQGKLAD----------MYTSLQS----SRSYVYSVARDCDNGKVD-------RKDCAGVILCAA 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 398 AKAflTDMGLETTvhgqQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALdLVGRKI 457
Cdd:PLN02519 348 ERA--TQVALQAI----QCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
81-444 |
8.68e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 98.09 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 81 REAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSAS----LAFGLYPMLTSGaclSIYAHASEELKQKYLPNMY 156
Cdd:PTZ00461 71 RDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDpgfcLAYLAHSMLFVN---NFYYSASPAQRARWLPKVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 157 AGVWSGSMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGehdlTDNIIHLVLAKLPDApagsrgISLFLVPKv 236
Cdd:PTZ00461 148 TGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNG----TVADVFLIYAKVDGK------ITAFVVER- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 237 lvnddGSLGernsLSCGSIEHKMGIQASATCVMNFD----GATGwMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSY 312
Cdd:PTZ00461 217 -----GTKG----FTQGPKIDKCGMRASHMCQLFFEdvvvPAEN-LLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 313 QSAIEYARERiqsraptgpvaqdKA-ADPIIVHPDVRRMLLTMKALNEGGRAFSSYVALQLdiakfSDDEAARQRAEAQV 391
Cdd:PTZ00461 287 ELMTSYASER-------------KAfGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-----HPGNKNRLGSDAAK 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1332876544 392 ALLTPVAKafltdmglETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGT 444
Cdd:PTZ00461 349 LFATPIAK--------KVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-453 |
4.31e-21 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 97.13 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 164 MCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGEHDltdniIHLVLAKLPDapagsrGISLFLVPKVLVNddgs 243
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQAKG------GLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 244 lGERNSLSCGSIEHKMGIQASATCVMNFDGATGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERi 323
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQR- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 324 qsraptgpvaqDKAADPIIVHPDVRRMLLTMKALNEGgrafssYVALQLDIAKfsddeAARQRAEAQVA----LLTPVAK 399
Cdd:PRK11561 325 -----------QVFGKPLIEQPLMRQVLSRMALQLEG------QTALLFRLAR-----AWDRRADAKEAlwarLFTPAAK 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1332876544 400 AFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLV 453
Cdd:PRK11561 383 FVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-457 |
2.46e-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: 87.69 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 283 NKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERIQsraptgpvaqdkAADPIIVHPDVRRMLLTMKALNEGGR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKA------------FGRPLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 363 AfssyvaLQLDIAKFSDDEaarQRAEAQVAlltpVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYE 442
Cdd:pfam00441 69 L------LVYRAAEALDAG---GPDGAEAS----MAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|....*
gi 1332876544 443 GTNGIQaLDLVGRKI 457
Cdd:pfam00441 136 GTSEIQ-RNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
2.01e-16 |
|
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: 74.62 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 163 SMCLTEPHAGTDLGIIRTKAEPQADGSYKVSGTKIFITGGeHDLTdniIHLVLAKlPDAPAGSRGISLFLVPKVLVNddg 242
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNA-GIAD---LFLVLAR-TGGDDRHGGISLFLVPKDAPG--- 72
|
90 100 110
....*....|....*....|....*....|
gi 1332876544 243 slgernsLSCGSIEHKMGIQASATCVMNFD 272
Cdd:pfam02770 73 -------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
88-459 |
4.84e-16 |
|
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: 80.08 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 88 AEGGWVGVGGDPAFGGMGMPKVISAQVEEMMNSASlafGLYPMLTSGACL---SIYAHASEELKQKYLPNMYAG--VWsg 162
Cdd:cd01152 45 AAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG---APVPFNQIGIDLagpTILAYGTDEQKRRFLPPILSGeeIW-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 163 smCL--TEPHAGTDLGIIRTKAEPQADGsYKVSGTKIFITGGEhdLTDNIIHLVLAKlPDAPAgSRGISLFLVPkvlVND 240
Cdd:cd01152 120 --CQgfSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH--YADWAWLLVRTD-PEAPK-HRGISILLVD---MDS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 241 DGslgernsLSCGSIEHKMGiqASATCVMNFDG---ATGWMVGEPNKGLAAMFTMMNYERLGVGiqglatgeRSYQSAIE 317
Cdd:cd01152 190 PG-------VTVRPIRSING--GEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERVSIG--------GSAATFFE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 318 YARERIQSRAPTGPVAQDKaadpiivhPDVRRMLLTMKALNEGGRAFSSYVALQLDIAKFSDDEAArqraeaqvalltpV 397
Cdd:cd01152 253 LLLARLLLLTRDGRPLIDD--------PLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEAS-------------I 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 398 AKAFLTDMGLETTVHGQQVFGGHGFIREWG--------QEQLVRDCRITQIYEGTNGIQaLDLVGRKIVG 459
Cdd:cd01152 312 AKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQ-RNIIAERLLG 380
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
81-458 |
7.30e-16 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 79.77 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 81 REAYQLYAEGGWVGVGGDPAFGGMgmPKVISAQveeMMNSASLA--FGLYPMLTSGACL-SIYAHASEE-LKQKYLPNMY 156
Cdd:PRK12341 40 REFMRALADNGISMLGVPEEFGGT--PADYVTQ---MLVLEEVSkcGAPAFLITNGQCIhSMRRFGSAEqLRKTAESTLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 157 AGVWSGSMCLTEPHAGTDLGIIRTKAEpQADGSYKVSGTKIFITGGEhdltDNIIHLVLAKLPDAPAGSRGISLFLVPKv 236
Cdd:PRK12341 115 TGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITGAK----EYPYMLVLARDPQPKDPKKAFTLWWVDS- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 237 lvNDDGSlgERNSLscgsieHKMGIQASATCVMNFDGAT---GWMVGEPNKGLaaMFTMMNY--ERLGVGIQGLATGERS 311
Cdd:PRK12341 189 --SKPGI--KINPL------HKIGWHMLSTCEVYLDNVEveeSDLVGEEGMGF--LNVMYNFemERLINAARSLGFAECA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 312 YQSAIEYARERIQSRAPTGP--VAQDKAADPIIVHPDVRRMLLtmkalneggrafssyvalqldiakfsddEAARQRAEA 389
Cdd:PRK12341 257 FEDAARYANQRIQFGKPIGHnqLIQEKLTLMAIKIENMRNMVY----------------------------KVAWQADNG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 390 Q-VALLTPVAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQaLDLVGRKIV 458
Cdd:PRK12341 309 QsLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRQIL 377
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
38-158 |
9.77e-12 |
|
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: 62.10 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 38 ETADAILEEAGKITANSIAPLNRSGDEEGcrwdggavstpAGYREAYQLYAEGGWVGVGGDPAFGGMGMPKVISAQVEEM 117
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEG-----------EFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEE 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1332876544 118 MNSASLAFGLYPMLTSG-ACLSIYAHASEELKQKYLPNMYAG 158
Cdd:pfam02771 71 LARADASVALALSVHSSlGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
101-457 |
4.83e-10 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 61.77 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 101 FGGMGMPKVISAQV-EEMMNSASLAFGLYPMltSGACLSIYAHASEELKQKYLPNMYAG--VWSGSMclTEPHAGTDLGI 177
Cdd:PRK03354 60 HGGLDAGFVTLAAVwMELGRLGAPTYVLYQL--PGGFNTFLREGTQEQIDKIMAFRGTGkqMWNSAI--TEPGAGSDVGS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 178 IRTKAEpQADGSYKVSGTKIFITGGEHdlTDNIIhlVLAKLPDAPAGSRGISLFLvpkvlvndDGSLG--ERNSLscgsi 255
Cdd:PRK03354 136 LKTTYT-RRNGKVYLNGSKCFITSSAY--TPYIV--VMARDGASPDKPVYTEWFV--------DMSKPgiKVTKL----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 256 eHKMGIQASATCVMNFDGA---TGWMVGEPNKGLAAMFTMMNYERLGVGIQGLATGERSYQSAIEYARERIQSRAPTG-- 330
Cdd:PRK03354 198 -EKLGLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGrf 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 331 PVAQDKAADPIIVHPDVRRMLLTmkalneggrafssyVALQLDIAKFSDDEAArqraeaqvalltpVAKAFLTDMGLETT 410
Cdd:PRK03354 277 QLIQEKFAHMAIKLNSMKNMLYE--------------AAWKADNGTITSGDAA-------------MCKYFCANAAFEVV 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1332876544 411 VHGQQVFGGHGFIREWGQEQLVRDCRITQIYEGTNGIQALDLvGRKI 457
Cdd:PRK03354 330 DSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL-GRAV 375
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-34 |
3.51e-09 |
|
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam02770, pfam00441, pfam02771. This family is one of the enzymes involved in AcylCoA interaction in beta-oxidation.
Pssm-ID: 463571 Cd Length: 32 Bit Score: 52.34 E-value: 3.51e-09
10 20 30
....*....|....*....|....*....|..
gi 1332876544 3 DYQAPLRDMRFVLNEVFDAPKlWQALPALAEV 34
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEA-LAALPGFADA 31
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
132-459 |
3.29e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 52.93 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 132 TSGACLSIYAHASEELKQKYLPNMYAGVWSGSMCLTEPHAGTDLGIIRTKAEpQADGSYKVSGTKIFItgGEHDLTDNII 211
Cdd:PLN02526 114 SSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI--GNSTFADVLV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 212 hlVLAKlpdaPAGSRGISLFLVPKvlvnddGSLGernsLSCGSIEHKMGIQASATCVMNFD-----------GATGWMvg 280
Cdd:PLN02526 191 --IFAR----NTTTNQINGFIVKK------GAPG----LKATKIENKIGLRMVQNGDIVLKdvfvpdedrlpGVNSFQ-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 281 EPNKGLAAMFTMMNYERLGVGIqGLatgersYQSAIEYARERIQSRAPTGP--VAQDKaadpiIVH--PDVRRMLLT--- 353
Cdd:PLN02526 253 DTNKVLAVSRVMVAWQPIGISM-GV------YDMCHRYLKERKQFGAPLAAfqINQEK-----LVRmlGNIQAMFLVgwr 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 354 MKALNEGGRAFSSYVALqldiakfsddeaarqraeaqvalltpvAKAFLTDMGLETTVHGQQVFGGHGFIREWGQEQLVR 433
Cdd:PLN02526 321 LCKLYESGKMTPGHASL---------------------------GKAWITKKARETVALGRELLGGNGILADFLVAKAFC 373
|
330 340
....*....|....*....|....*.
gi 1332876544 434 DCRITQIYEGTNGIQALdLVGRKIVG 459
Cdd:PLN02526 374 DLEPIYTYEGTYDINAL-VTGREITG 398
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
101-217 |
1.79e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 41.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1332876544 101 FGGMGMPKVISAQVEEMMNSASLAFGLYPMLTSGACLSIYAH-ASEELKQKYLPNMYAGV----WSgsmclTEPHAGTDL 175
Cdd:PTZ00457 74 YGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTvGSKELKGKYLTAMSDGTimmgWA-----TEEGCGSDI 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1332876544 176 GIIRTKAEPQADGSYKVSGTK--IFITGGEHdltdniiHLVLAK 217
Cdd:PTZ00457 149 SMNTTKASLTDDGSYVLTGQKrcEFAASATH-------FLVLAK 185
|
|
| |
