|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-583 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 556.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 3 EYNAPLRDMRFLLNDVFDAPALWQRLPRLAerIDADTADAILEEAAKVTGGLLAPLNRSGDEEGAQW-QDGAVRTPAGFR 81
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLGKTD--VTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLlKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 82 EAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMYAANASFSLYSTLSAGACLALDAHGSEELKNRYLPNMYAGTWA 161
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 162 GSMCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGGEQDLTENIIHLVLAKLPDAPAGSRGISLFLVPKFLVGDD 241
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 242 GALGARNAVHCGSIEHKMGIKASATCVMNFDGASGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARE 321
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 322 RLQSRAPTGPVARDKAADPIIVHPDVRRMLLTMKALTEGGRAFSTYVGQQLDLAKYAEDQEERSQAEALVALLTPVAKAF 401
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 402 FTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALDLMGRKVVA-NGGLFLSIFSREVRAFAAG-- 478
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSlKGGNEVARFGKRVSKLVRAhl 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 479 -ANAELAEFVTPLLTALDLLDNLTQGIVARAGNDPREIGAASVEYLHLFGYTAYAYLW---ARMAAAAQRQREVDPAFHD 554
Cdd:PTZ00456 503 fSRGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWlrmAEVAQKKVAAGQDADGFYQ 582
|
570 580
....*....|....*....|....*....
gi 489205678 555 GKLATARFYFARILPRVHSLAAAVEAGSE 583
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAGPS 611
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
43-458 |
5.04e-169 |
|
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: 486.51 E-value: 5.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 43 ILEEAAKVTGGLLAPLNRSGDEEGAQWQDGAVRTPAGFREAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMYAAN 122
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 123 ASFSlYSTLSAGACLALDAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGG 202
Cdd:cd01153 81 APLM-YASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 203 EQDLTENIIHLVLAKLPDAPAGSRGISLFLVPKFLVGddgalGARNAVHCGSIEHKMGIKASATCVMNFDGASGWLVGEV 282
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 283 NKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQSRAPTgpvaRDKAADPIIVHPDVRRMLLTMKALTEGGR 362
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 363 AFSTYVGQQLDLAKYAEDQEE-RSQAEALVALLTPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIY 441
Cdd:cd01153 311 ALDLYTATVQDLAERKATEGEdRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*..
gi 489205678 442 EGTNGIQALDLMGRKVV 458
Cdd:cd01153 391 EGTTGIQALDLIGRKIV 407
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-462 |
3.83e-115 |
|
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: 347.60 E-value: 3.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 38 DTADAILEEAAKVTGGLLAPLNRSGDEEGaqwqdgavRTPagfREAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEM 117
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 118 MYAANASFSLYSTLSAGACLALDAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGsYRISGTKI 197
Cdd:COG1960 76 LARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 198 FITGGEQ-DlteniIHLVLAKLPDAPaGSRGISLFLVPKFLVGddgalgarnaVHCGSIEHKMGIKASATCVMNFDG--- 273
Cdd:COG1960 155 FITNAPVaD-----VILVLARTDPAA-GHRGISLFLVPKDTPG----------VTVGRIEDKMGLRGSDTGELFFDDvrv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 274 ASGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQsraptgpvardkAADPIIVHPDVRRMLLT 353
Cdd:COG1960 219 PAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 354 MKALTEGGRAFSTYVGQQLDlakyaedqeersqAEALVALLTPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVR 433
Cdd:COG1960 287 MAAELEAARALVYRAAWLLD-------------AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 489205678 434 DVRIAQIYEGTNGIQALDLmGRKVVANGG 462
Cdd:COG1960 354 DARILTIYEGTNEIQRLII-ARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
138-452 |
6.81e-58 |
|
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: 197.12 E-value: 6.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 138 ALDAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGsYRISGTKIFITGGeqdlTENIIHLVLAK 217
Cdd:cd00567 47 LLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG----GDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 218 LPDAPAGSRGISLFLVPKflvgddgalgARNAVHCGSIEHKMGIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMN 294
Cdd:cd00567 122 TDEEGPGHRGISAFLVPA----------DTPGVTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 295 YERLSIGIQGIGCAEMSYQSAVAYARERLQsraptgpvardkAADPIIVHPDVRRMLLTMKALTEGGRAFSTYVGQQLDl 374
Cdd:cd00567 192 VGRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD- 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205678 375 akyaedqeersQAEALVALLTPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALDL 452
Cdd:cd00567 259 -----------QGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-448 |
3.71e-53 |
|
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: 185.55 E-value: 3.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 38 DTADAILEEAAKVTGGLLAPLNRSGDEEGaqwqdgavRTPagfREAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEM 117
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKG--------EFP---REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 118 MYAANASFSLysTLSAGACLALDA---HGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADgSYRISG 194
Cdd:cd01158 70 LAKVDASVAV--IVSVHNSLGANPiikFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 195 TKIFIT-GGEQDlteniIHLVLAKLpDAPAGSRGISLFLVPKflvGDDGalgarnaVHCGSIEHKMGIKASATCVMNFDG 273
Cdd:cd01158 147 SKMWITnGGEAD-----FYIVFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFED 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 274 A---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQsraptgpvardkAADPIIVHPDVRRM 350
Cdd:cd01158 211 VrvpKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQ------------FGKPIADFQGIQFK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 351 LLTMKALTEGGRAFsTYVGQQLdlakyaEDQEERSQAEAlvalltPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQ 430
Cdd:cd01158 279 LADMATEIEAARLL-TYKAARL------KDNGEPFIKEA------AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVER 345
|
410
....*....|....*...
gi 489205678 431 LVRDVRIAQIYEGTNGIQ 448
Cdd:cd01158 346 YYRDAKITEIYEGTSEIQ 363
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
130-453 |
4.16e-49 |
|
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: 176.02 E-value: 4.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 130 TLSAGACLALDAHGSEELK---NRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGGEQDl 206
Cdd:cd01154 114 TMTDAAVYALRKYGPEELKqylPGLLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 207 teniIHLVLAKLPDAPAGSRGISLFLVPKFLVGddgalGARNAVHCGSIEHKMGIKASATCVMNFDGASGWLVGEVNKGL 286
Cdd:cd01154 193 ----AALVLARPEGAPAGARGLSLFLVPRLLED-----GTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 287 AAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERlqsraptgpVARDKaadPIIVHPDVRRMLLTMKALTEGGRAFSt 366
Cdd:cd01154 264 YYILEMLNISRLDNAVAALGIMRRALSEAYHYARHR---------RAFGK---PLIDHPLMRRDLAEMEVDVEAATALT- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 367 yvgqqLDLAKYAEDQEERSQAEALVA-LLTPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTN 445
Cdd:cd01154 331 -----FRAARAFDRAAADKPVEAHMArLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTG 405
|
....*...
gi 489205678 446 GIQALDLM 453
Cdd:cd01154 406 NIQALDVL 413
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
81-458 |
7.16e-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: 154.97 E-value: 7.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 81 REAYATYAEGGWVGLTGNPAHGGMGMP-KMLAVQFEEMMYA--ANASFSLYSTLsagACLALDAHGSEELKNRYLPNMYA 157
Cdd:cd01160 33 REVWRKAGEQGLLGVGFPEEYGGIGGDlLSAAVLWEELARAggSGPGLSLHTDI---VSPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 158 GTWAGSMCLTEPHAGTDLGIIRTKAEPQADgSYRISGTKIFITGGeqdlTENIIHLVLAKLPDAPAGSRGISLFLVPKfl 237
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNG----MLADVVIVVARTGGEARGAGGISLFLVER-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 238 vGDDGALGARNAvhcgsieHKMGIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQS 314
Cdd:cd01160 183 -GTPGFSRGRKL-------KKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 315 AVAYARERlqsRAPTGPVARdkaadpiivHPDVRRMLLTMKALTEGGRAFstyvgqqLDLAKYAEDQEERSQAEAlvall 394
Cdd:cd01160 255 TRNYVKQR---KAFGKTLAQ---------LQVVRHKIAELATKVAVTRAF-------LDNCAWRHEQGRLDVAEA----- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489205678 395 tPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQaLDLMGRKVV 458
Cdd:cd01160 311 -SMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
42-455 |
8.72e-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: 146.43 E-value: 8.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 42 AILEEAAKVTGGLLAPlnrsgdeEGAQWqDGAVRTPAG-FREAyatyAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMYA 120
Cdd:cd01162 7 AIQEVARAFAAKEMAP-------HAADW-DQKKHFPVDvLRKA----AELGFGGIYIRDDVGGSGLSRLDASIIFEALST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 121 ANASFSLYSTLSAGACLALDAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADgSYRISGTKIFIT 200
Cdd:cd01162 75 GCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFIS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 201 G-GEQDlteniIHLVLAKlpDAPAGSRGISLFLVPKflvgddGALGARnavhCGSIEHKMGIKASATCVMNFDGAS---G 276
Cdd:cd01162 154 GaGDSD-----VYVVMAR--TGGEGPKGISCFVVEK------GTPGLS----FGANEKKMGWNAQPTRAVIFEDCRvpvE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 277 WLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQsraptgpvardkAADPIIVHPDVRRMLLTMKA 356
Cdd:cd01162 217 NRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQ------------FGKPLADFQALQFKLADMAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 357 LTEGGRAFSTYVGQQLDlakyaedqEERSQAEALVALltpvAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVR 436
Cdd:cd01162 285 ELVASRLMVRRAASALD--------RGDPDAVKLCAM----AKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLR 352
|
410 420
....*....|....*....|...
gi 489205678 437 IAQIYEGTNGIQ----ALDLMGR 455
Cdd:cd01162 353 VHQILEGTNEIMrliiARALLTR 375
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
88-450 |
5.48e-38 |
|
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: 144.92 E-value: 5.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 88 AEGGWVGLTGNPAHGGMGMPK-MLAVQFEEMMYAANASFSLYSTLSAGAcLALDAHGSEELKNRYLPNMYAGTWAGSMCL 166
Cdd:cd01161 66 KELGLFGLQVPEEYGGLGLNNtQYARLAEIVGMDLGFSVTLGAHQSIGF-KGILLFGTEAQKEKYLPKLASGEWIAAFAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 167 TEPHAGTDLGIIRTKAEPQADGS-YRISGTKIFIT-GGEQDlteniIHLVLAKLPDA-PAGSR--GISLFLVPKFLVGdd 241
Cdd:cd01161 145 TEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITnGGIAD-----IFTVFAKTEVKdATGSVkdKITAFIVERSFGG-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 242 galgarnaVHCGSIEHKMGIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAY 318
Cdd:cd01161 218 --------VTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDY 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 319 ARERLQsraptgpvardkAADPIIVHPDVRRMLLTMKALTEGGRAFSTYVGQQLDLAKYAEDQEErsqaEALVALLTPVA 398
Cdd:cd01161 290 ANNRKQ------------FGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIE----AAISKVFASEA 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489205678 399 KAFFTDTGLescvlgqQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQAL 450
Cdd:cd01161 354 AWLVVDEAI-------QIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
81-459 |
3.39e-34 |
|
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: 133.69 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 81 REAYATYAEGGWVGLTGNPAHGGMGMPKML-AVQFEEMMYAANA---SFSLYSTLsagaCL-ALDAHGSEELKNRYLPNM 155
Cdd:cd01156 36 RDLWRKMGKLGLLGITAPEEYGGSGMGYLAhVIIMEEISRASGSvalSYGAHSNL----CInQIYRNGSAAQKEKYLPKL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 156 YAGTWAGSMCLTEPHAGTDLGIIRTKAEPQaDGSYRISGTKIFITGG-EQDlteniIHLVLAKlPDAPAGSRGISLFLVP 234
Cdd:cd01156 112 ISGEHIGALAMSEPNAGSDVVSMKLRAEKK-GDRYVLNGSKMWITNGpDAD-----TLVVYAK-TDPSAGAHGITAFIVE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 235 KflvGDDGALGARNAvhcgsieHKMGIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMS 311
Cdd:cd01156 185 K---GMPGFSRAQKL-------DKLGMRGSNTCELVFEDCevpEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 312 YQSAVAYARERLQSRAPTG--PVARDKAADpiivhpdvrrMLLTMKAltegGRAFSTYVGQQLdlakyaeDQEERSQAEA 389
Cdd:cd01156 255 LDVAIPYAHQRKQFGQPIGefQLVQGKLAD----------MYTRLNA----SRSYLYTVAKAC-------DRGNMDPKDA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 390 LVALLTPVAKAffTDTGLESCvlgqQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALdLMGRKVVA 459
Cdd:cd01156 314 AGVILYAAEKA--TQVALDAI----QILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM-VIGRELFK 376
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
471-588 |
1.29e-29 |
|
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: 113.41 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 471 EVRAF--AAGANAELAEFVTPLLTALDLLDNLTQGIVARAG-NDPREIGAASVEYLHLFGYTAYAYLWA---RMAAAAQR 544
Cdd:pfam12806 3 EIRAFiaAAAGDPALAAEAAALAAALAALQEATAWLLARAAkGDPDEAGAGAVPYLMLFGDVVLGWLWLrqaLAAQAKLA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489205678 545 QREVDPAFHDGKLATARFYFARILPRVHSLAAAVEAGSESLYGL 588
Cdd:pfam12806 83 AGAKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
81-444 |
5.17e-26 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 110.80 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 81 REAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMyaanasfslySTLSAGACLALDAH-----------GSEELKN 149
Cdd:PTZ00461 71 RDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHEL----------SKYDPGFCLAYLAHsmlfvnnfyysASPAQRA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 150 RYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGGeqdlTENIIHLVLAKLPDApagsrgIS 229
Cdd:PTZ00461 141 RWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNG----TVADVFLIYAKVDGK------IT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 230 LFLVPKflvgddGALGarnaVHCGSIEHKMGIKASATCVMNFD----GASGwLVGEVNKGLAAMFTMMNYERLSIGIQGI 305
Cdd:PTZ00461 211 AFVVER------GTKG----FTQGPKIDKCGMRASHMCQLFFEdvvvPAEN-LLGEEGKGMVGMMRNLELERVTLAAMAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 306 GCAEMSYQSAVAYARERlqsraptgpvardKA-ADPIIVHPDVRRMLLTMKALTEGGRAFSTYVGQQLdlakyAEDQEER 384
Cdd:PTZ00461 280 GIAERSVELMTSYASER-------------KAfGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-----HPGNKNR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 385 SQAEALVALLTPVAKAFFTDTglescvlgQQVFGGHGYIREWGQEQLVRDVRIAQIYEGT 444
Cdd:PTZ00461 342 LGSDAAKLFATPIAKKVADSA--------IQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-453 |
2.02e-24 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 107.14 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 164 MCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGGEQDlteniIHLVLAKLPDapagsrGISLFLVPKFLVGddga 243
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQAKG------GLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 244 lGARNAVHCGSIEHKMGIKASATCVMNFDGASGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARErl 323
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQ-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 324 qsraptgpvaRDKAADPIIVHPDVRRMLLTMKALTEGGRAFstyvgqQLDLAKyAEDQEERSQAEALVALLTPVAKAFFT 403
Cdd:PRK11561 324 ----------RQVFGKPLIEQPLMRQVLSRMALQLEGQTAL------LFRLAR-AWDRRADAKEALWARLFTPAAKFVIC 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489205678 404 DTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALDLM 453
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
89-457 |
3.54e-24 |
|
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: 104.75 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 89 EGGWVGLTGNpAHGGMGMPKM-LAVQFEEMMYAANASFSLYSTLSAGACLALDAHGSEELKNRYLPNMYAGTWAGSMCLT 167
Cdd:cd01151 55 ELGLLGATIK-GYGCAGLSSVaYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 168 EPHAGTDLGIIRTKAEPQADGsYRISGTKIFITGGE-QDlteniIHLVLAKLpdapAGSRGISLFLVPKflvgddGALGA 246
Cdd:cd01151 134 EPNHGSDPGGMETRARKDGGG-YKLNGSKTWITNSPiAD-----VFVVWARN----DETGKIRGFILER------GMKGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 247 RNAvhcgSIEHKMGIKASATCVMNFDGAsgwLVGEVN-----KGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARE 321
Cdd:cd01151 198 SAP----KIQGKFSLRASITGEIVMDNV---FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 322 RLQSRAPtgpVARDKAadpiivhpdVRRMLLTMKALTEGGRAFSTYVGQQLDLAKYAEDQeersqaealVALLtpvaKAF 401
Cdd:cd01151 271 RKQFGRP---LAAFQL---------VQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ---------ISLL----KRN 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489205678 402 FTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALdLMGRKV 457
Cdd:cd01151 326 NCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL-ILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
94-457 |
2.76e-23 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 102.26 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 94 GLTGNPAHGGMGMPKML-AVQFEEMMYAANA---SFSLYSTLsagaCL-ALDAHGSEELKNRYLPNMYAGTWAGSMCLTE 168
Cdd:PLN02519 75 GITAPEEYGGLGLGYLYhCIAMEEISRASGSvglSYGAHSNL----CInQLVRNGTPAQKEKYLPKLISGEHVGALAMSE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 169 PHAGTDLGIIRTKAEpQADGSYRISGTKIFITGGEQDLTeniihLVLAKLPDAPAGSRGISLFLVPKflvgddGALGARN 248
Cdd:PLN02519 151 PNSGSDVVSMKCKAE-RVDGGYVLNGNKMWCTNGPVAQT-----LVVYAKTDVAAGSKGITAFIIEK------GMPGFST 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 249 AVHCgsieHKMGIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQS 325
Cdd:PLN02519 219 AQKL----DKLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQF 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 326 RAPTGP--VARDKAADPIIVHPDVRRMLLTMKALTEGGRAfstyvgQQLDLAKYAEDQEERSQAEALVALltpvakafft 403
Cdd:PLN02519 295 GRPIGEfqFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV------DRKDCAGVILCAAERATQVALQAI---------- 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489205678 404 dtglescvlgqQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALdLMGRKV 457
Cdd:PLN02519 359 -----------QCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
143-450 |
1.21e-21 |
|
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: 97.27 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 143 GSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADgSYRISGTKIFITGGeqdlTENIIHLVLAKL---P 219
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNG----GKANWYFLLARSdpdP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 220 DAPAgSRGISLFLVPKFLVGddgalgarnaVHCGSIEHKMGIKASATCVMNFDG----ASGWLVGEvNKGLAAMFTMMNY 295
Cdd:cd01157 172 KCPA-SKAFTGFIVEADTPG----------IQPGRKELNMGQRCSDTRGITFEDvrvpKENVLIGE-GAGFKIAMGAFDK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 296 ERLSIGIQGIGCAEMSYQSAVAYARERlqsraptgpvarDKAADPIIVHPDVRRMLLTMKALTEGGRaFSTYvgqqldLA 375
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALER------------KTFGKLIAEHQAVSFMLADMAMKVELAR-LAYQ------RA 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489205678 376 KYAEDQEERSQAEAlvalltPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQAL 450
Cdd:cd01157 301 AWEVDSGRRNTYYA------SIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-452 |
2.49e-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: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 283 NKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQsraptgpvardkAADPIIVHPDVRRMLLTMKALTEGGR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKA------------FGRPLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 363 AFSTYVGQQLDlakyaEDQEERSQAealvalltPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYE 442
Cdd:pfam00441 69 LLVYRAAEALD-----AGGPDGAEA--------SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|
gi 489205678 443 GTNGIQALDL 452
Cdd:pfam00441 136 GTSEIQRNII 145
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
47-463 |
2.63e-19 |
|
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: 90.10 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 47 AAKVTGGLLAPLN---RSGDEEGAQWQdgavrtpagfreayATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMYAANA 123
Cdd:cd01152 15 AAHLPPELREESAlgyREGREDRRRWQ--------------RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 124 sfsLYSTLSAGACLA---LDAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEPQADGsYRISGTKIFIT 200
Cdd:cd01152 81 ---PVPFNQIGIDLAgptILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 201 GGEqdlTENIIHLVLAKLPDAPAgSRGISLFLVPkflVGDDGalgarnaVHCGSIEHKMGikASATCVMNFDG---ASGW 277
Cdd:cd01152 157 GAH---YADWAWLLVRTDPEAPK-HRGISILLVD---MDSPG-------VTVRPIRSING--GEFFNEVFLDDvrvPDAN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 278 LVGEVNKGLAAMFTMMNYERLSIGiqgigcaemsyqSAVAYARERLQSRAPTgpVARDKAadPIIVHPDVRRMLLTMKAL 357
Cdd:cd01152 221 RVGEVNDGWKVAMTTLNFERVSIG------------GSAATFFELLLARLLL--LTRDGR--PLIDDPLVRQRLARLEAE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 358 TEGGRAFSTYVGQQLDLAKyaedqeeRSQAEAlvalltPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDV-- 435
Cdd:cd01152 285 AEALRLLVFRLASALAAGK-------PPGAEA------SIAKLFGSELAQELAELALELLGTAALLRDPAPGAELAGRwe 351
|
410 420 430
....*....|....*....|....*....|....
gi 489205678 436 ------RIAQIYEGTNGIQaldlmgRKVVANGGL 463
Cdd:cd01152 352 adylrsRATTIYGGTSEIQ------RNIIAERLL 379
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
143-447 |
2.15e-17 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 84.39 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 143 GSEE-LKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEpQADGSYRISGTKIFITGGeqdlTENIIHLVLAKLPDA 221
Cdd:PRK12341 100 GSAEqLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITGA----KEYPYMLVLARDPQP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 222 PAGSRGISLFLVPKFLVGDdgalgARNAVHcgsiehKMGIKASATCVMNFDGA---SGWLVGEvnKGLAAMFTMMNY--E 296
Cdd:PRK12341 175 KDPKKAFTLWWVDSSKPGI-----KINPLH------KIGWHMLSTCEVYLDNVeveESDLVGE--EGMGFLNVMYNFemE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 297 RLSIGIQGIGCAEMSYQSAVAYARERLQSRAPTGP--VARDKAADPIIVHPDVRRMLLTmkalteggrafstyvgqqldl 374
Cdd:PRK12341 242 RLINAARSLGFAECAFEDAARYANQRIQFGKPIGHnqLIQEKLTLMAIKIENMRNMVYK--------------------- 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489205678 375 AKYAEDQEERSQAEAlvalltPVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGI 447
Cdd:PRK12341 301 VAWQADNGQSLRTSA------ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
4.62e-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: 76.55 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 163 SMCLTEPHAGTDLGIIRTKAEPQADGSYRISGTKIFITGGeqdlTENIIHLVLAKlPDAPAGSRGISLFLVPKFLVGddg 242
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNA----GIADLFLVLAR-TGGDDRHGGISLFLVPKDAPG--- 72
|
90 100 110
....*....|....*....|....*....|
gi 489205678 243 algarnaVHCGSIEHKMGIKASATCVMNFD 272
Cdd:pfam02770 73 -------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
101-457 |
1.47e-09 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 60.23 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 101 HGGMGMPKM-LAVQFEEMMYAANASFSLYStLSAGACLALdAHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIR 179
Cdd:PRK03354 60 HGGLDAGFVtLAAVWMELGRLGAPTYVLYQ-LPGGFNTFL-REGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 180 TKAEpQADGSYRISGTKIFITGGEQdlTENIIhlVLAKLPDAPAGSRGISLFLvpkflvgDDGALGARNavhcgSIEHKM 259
Cdd:PRK03354 138 TTYT-RRNGKVYLNGSKCFITSSAY--TPYIV--VMARDGASPDKPVYTEWFV-------DMSKPGIKV-----TKLEKL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 260 GIKASATCVMNFDGA---SGWLVGEVNKGLAAMFTMMNYERLSIGIQGIGCAEMSYQSAVAYARERLQSRAPTG--PVAR 334
Cdd:PRK03354 201 GLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGrfQLIQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 335 DKAADPIIVHPDVRRMLLTmkalteggrafstyvgqqldlAKYAEDQEERSQAEAlvalltPVAKAFFTDTGLESCVLGQ 414
Cdd:PRK03354 281 EKFAHMAIKLNSMKNMLYE---------------------AAWKADNGTITSGDA------AMCKYFCANAAFEVVDSAM 333
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489205678 415 QVFGGHGYIREWGQEQLVRDVRIAQIYEGTNGIQALDLmGRKV 457
Cdd:PRK03354 334 QVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL-GRAV 375
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
81-158 |
3.46e-09 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 54.78 E-value: 3.46e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489205678 81 REAYATYAEGGWVGLTGNPAHGGMGMPKMLAVQFEEMMYAANASFSL-YSTLSAGACLALDAHGSEELKNRYLPNMYAG 158
Cdd:pfam02771 34 RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALaLSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
120-457 |
3.46e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 56.01 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 120 AANASFSLYSTLSAGACLALdaHGSEELKNRYLPNMYAGTWAGSMCLTEPHAGTDLGIIRTKAEpQADGSYRISGTKIFI 199
Cdd:PLN02526 104 ASCSTFILVHSSLAMLTIAL--CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 200 tgGEQDLTENIIhlVLAKlpdaPAGSRGISLFLVPKflvgddGALGARnavhCGSIEHKMGIKASATCVMNFDGA----S 275
Cdd:PLN02526 181 --GNSTFADVLV--IFAR----NTTTNQINGFIVKK------GAPGLK----ATKIENKIGLRMVQNGDIVLKDVfvpdE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 276 GWLVG-----EVNKGLAamftmmnYERLSIGIQGIGCAEMSYQSAVAYARERLQSRAPTGPVArdkaadpiIVHPDVRRM 350
Cdd:PLN02526 243 DRLPGvnsfqDTNKVLA-------VSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQ--------INQEKLVRM 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 351 LLTMKALteggrafsTYVGQQLdLAKYAEDQEERSQAEalvalltpVAKAFFTDTGLESCVLGQQVFGGHGYIREWGQEQ 430
Cdd:PLN02526 308 LGNIQAM--------FLVGWRL-CKLYESGKMTPGHAS--------LGKAWITKKARETVALGRELLGGNGILADFLVAK 370
|
330 340
....*....|....*....|....*..
gi 489205678 431 LVRDVRIAQIYEGTNGIQALdLMGRKV 457
Cdd:PLN02526 371 AFCDLEPIYTYEGTYDINAL-VTGREI 396
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
4-33 |
1.61e-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: 47.33 E-value: 1.61e-07
10 20 30
....*....|....*....|....*....|
gi 489205678 4 YNAPLRDMRFLLNDVFDAPAlWQRLPRLAE 33
Cdd:pfam12418 2 YKAPLRDMRFVLYEVLGAEA-LAALPGFAD 30
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
101-196 |
1.17e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 41.79 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205678 101 HGGMGMPKML-AVQFEEMmyAANASFSLYSTL--SAGACLALDAHGSEELKNRYLPNMYAGT----WAgsmclTEPHAGT 173
Cdd:PTZ00457 74 YGGLGLGHTAhALIYEEV--GTNCDSKLLSTIqhSGFCTYLLSTVGSKELKGKYLTAMSDGTimmgWA-----TEEGCGS 146
|
90 100
....*....|....*....|...
gi 489205678 174 DLGIIRTKAEPQADGSYRISGTK 196
Cdd:PTZ00457 147 DISMNTTKASLTDDGSYVLTGQK 169
|
|
| |
