|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
4-599 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 736.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 4 YKAPLRDIRFVRDELLGYEAHYQSLpGAEDATPDMVNAILEEGAKFCEQVIAPLNRVGDLEGCTWSADG-VKTPTGFKEA 82
Cdd:PTZ00456 26 YQPRIRDVQFLVEEVFNMYDHYEKL-GKTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLLKDGnVTTPKGFKEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 83 YQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWTGT 162
Cdd:PTZ00456 105 YQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 163 MCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPNAEGN 242
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPDGS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 243 AGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERL 322
Cdd:PTZ00456 265 LETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERR 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 323 QMRSLTGPKAPEKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEEQKKAADSMLAFLTPIAKAFMT 402
Cdd:PTZ00456 345 SMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGCLT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 403 EVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLLGRKVLMTQG-EALKGFTKIVHKFCQANE-A 480
Cdd:PTZ00456 425 EWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGgNEVARFGKRVSKLVRAHLfS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 481 NEAVKEFVAPLAQLNKEWGDLTMKVGMAAMKDREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAAGTGEEAFYKAK 560
Cdd:PTZ00456 505 RGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGQDADGFYQCK 584
|
570 580 590
....*....|....*....|....*....|....*....
gi 15595703 561 LQTARFYFQRILPRTRAHVAAMLSGAnNLMEMAEEDFAL 599
Cdd:PTZ00456 585 VDTCQYVFQRILPRADAHFQIMQAGP-SIMASKEENWDL 622
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
42-456 |
3.59e-180 |
|
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: 515.02 E-value: 3.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 42 ILEEGAKFCEQVIAPLNRVGDLEGCTWSADGVKTPTGFKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVgQAN 121
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 122 WSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAG 201
Cdd:cd01153 80 DAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 202 EHDMADNIVHIVLARLPDAPQGTKGISLFIVPKFLPNaegnaGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPP 281
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 282 NKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMRSLTgpkaPEKPADPIIVHPDVRRMLLTMKAFAEGNR 361
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 362 AMLYFAAKQVDIVQRSQDE-EQKKAADSMLAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLY 440
Cdd:cd01153 311 ALDLYTATVQDLAERKATEgEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*.
gi 15595703 441 EGTTGVQALDLLGRKV 456
Cdd:cd01153 391 EGTTGIQALDLIGRKI 406
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
41-461 |
1.96e-117 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 353.76 E-value: 1.96e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 41 AILEEGAKFCEQVIAPLNRVGDLEGctwsadgvKTPtgfKEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQA 120
Cdd:COG1960 11 ALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 121 NWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGsYKVTGTKIFISA 200
Cdd:COG1960 80 DASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKTFITN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 201 GEHdmADniVHIVLARLPDAPqGTKGISLFIVPKFLPNaegnagernaVSCGSIEHKMGIHGNATCVMNFD---AATGFL 277
Cdd:COG1960 159 APV--AD--VILVLARTDPAA-GHRGISLFLVPKDTPG----------VTVGRIEDKMGLRGSDTGELFFDdvrVPAENL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 278 IGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQmrsltgpkapekPADPIIVHPDVRRMLLTMKAFA 357
Cdd:COG1960 224 LGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQ------------FGRPIADFQAVQHRLADMAAEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 358 EGNRAMLYFAAKQVDivqrsqdeeqkkaADSMLAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRIS 437
Cdd:COG1960 292 EAARALVYRAAWLLD-------------AGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARIL 358
|
410 420
....*....|....*....|....
gi 15595703 438 MLYEGTTGVQALDlLGRKVLMTQG 461
Cdd:COG1960 359 TIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
133-452 |
1.51e-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: 204.05 E-value: 1.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 133 GAMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGsYKVTGTKIFISAGehDMADniVHI 212
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG--GDAD--LFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 213 VLARLPDAPQGTKGISLFIVPKflpnaegnagERNAVSCGSIEHKMGIHGNATCVMNFD------AAtgfLIGPPNKGLN 286
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPA----------DTPGVTVGRIWDKMGMRGSGTGELVFDdvrvpeDN---LLGEEGGGFE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 287 CMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQmrsltgpkapekPADPIIVHPDVRRMLLTMKAFAEGNRAMLYF 366
Cdd:cd00567 185 LAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ------------FGKPLAEFQAVQFKLADMAAELEAARLLLYR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 367 AAKQVDivqrsqdeeqkkAADSMLAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGV 446
Cdd:cd00567 253 AAWLLD------------QGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEI 320
|
....*.
gi 15595703 447 QALDLL 452
Cdd:cd00567 321 QRLIIA 326
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
42-449 |
3.64e-49 |
|
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: 175.15 E-value: 3.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 42 ILEEGAKFCEQVIAPLNRVGDLEGctwsadgvKTPtgfKEAYQQFVEGGWPSLAHDVEHGGQGLP-ESLGLAISEmVGQA 120
Cdd:cd01158 6 IRKTVRDFAEKEIAPLAAEMDEKG--------EFP---REVIKEMAELGLMGIPIPEEYGGAGLDfLAYAIAIEE-LAKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 121 NWSWGMYPGLSHG-AMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADgSYKVTGTKIFIS 199
Cdd:cd01158 74 DASVAVIVSVHNSlGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 200 AGEHdmADniVHIVLARLpDAPQGTKGISLFIVPKflpNAEGnagernaVSCGSIEHKMGIHGNATCVMNFD-----AAT 274
Cdd:cd01158 153 NGGE--AD--FYIVFAVT-DPSKGYRGITAFIVER---DTPG-------LSVGKKEDKLGIRGSSTTELIFEdvrvpKEN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 275 gfLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMrsltgpkapekpADPIIVHPDVRRMLLTMK 354
Cdd:cd01158 218 --ILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQF------------GKPIADFQGIQFKLADMA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 355 AFAEGNRAMLYFAAkqvdivqRSQDEEQ---KKAAdsmlafltpIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNV 431
Cdd:cd01158 284 TEIEAARLLTYKAA-------RLKDNGEpfiKEAA---------MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYY 347
|
410
....*....|....*...
gi 15595703 432 RDSRISMLYEGTTGVQAL 449
Cdd:cd01158 348 RDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
133-452 |
3.89e-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: 176.41 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 133 GAMNTLHAHGTAEQQATYLTKLVSGE---WTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGehdMADni 209
Cdd:cd01154 118 AAVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAP---LAD-- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 210 VHIVLARLPDAPQGTKGISLFIVPKFLPNaegnaGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMF 289
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLFLVPRLLED-----GTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 290 TFMNTARLGTALQGLAHAEVGFQGGIAYARERlqmrsltgpKAPEKPadpIIVHPDVRRMLLTMKAFAEGNRAMLYFAAK 369
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHR---------RAFGKP---LIDHPLMRRDLAEMEVDVEAATALTFRAAR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 370 QVDivqRSQDEEQKKAAdsMLAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQAL 449
Cdd:cd01154 336 AFD---RAAADKPVEAH--MARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
...
gi 15595703 450 DLL 452
Cdd:cd01154 411 DVL 413
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
471-592 |
1.69e-44 |
|
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: 154.24 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 471 VHKFCQANEANEAVKEFVAPLAQLNKEWGDLTMKVGMAAMK-DREEVGAASVDYLMYSGYACLAYFWADMARLAAEKLAA 549
Cdd:pfam12806 4 IRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAKLAA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15595703 550 GTGEEAFYKAKLQTARFYFQRILPRTRAHVAAMLSGANNLMEM 592
Cdd:pfam12806 84 GAKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
99-457 |
4.46e-36 |
|
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: 139.12 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 99 EHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLR 178
Cdd:cd01162 54 DVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 179 TKAEPQADgSYKVTGTKIFIS-AGEHDmadniVHIVLARlpDAPQGTKGISLFIVPKFLPnaegnagernAVSCGSIEHK 257
Cdd:cd01162 134 TRAVREGD-HYVLNGSKAFISgAGDSD-----VYVVMAR--TGGEGPKGISCFVVEKGTP----------GLSFGANEKK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 258 MGIHGNATCVMNFD---AATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMrsltgpkape 334
Cdd:cd01162 196 MGWNAQPTRAVIFEdcrVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQF---------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 335 kpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDivqrsqdeeqKKAADSMLafLTPIAKAFMTEVGFESANHGVQ 414
Cdd:cd01162 266 --GKPLADFQALQFKLADMATELVASRLMVRRAASALD----------RGDPDAVK--LCAMAKRFATDECFDVANQALQ 331
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15595703 415 IFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALdLLGRKVL 457
Cdd:cd01162 332 LHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIARALL 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
80-457 |
3.15e-33 |
|
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: 130.70 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 80 KEAYQQFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANwswGMYPGLS-HG--AMNTLHAHGTAEQQATYLTKLVS 156
Cdd:cd01160 33 REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG---GSGPGLSlHTdiVSPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 157 GEWTGTMCLTEPHCGTDLGMLRTKAEPQADgSYKVTGTKIFISAGEHdmADniVHIVLARLPDAPQGTKGISLFIVPKFL 236
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML--AD--VVIVVARTGGEARGAGGISLFLVERGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 237 PnaegnagernAVSCGSIEHKMGIHGNATCVMNFD---AATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQG 313
Cdd:cd01160 185 P----------GFSRGRKLKKMGWKAQDTAELFFDdcrVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 314 GIAYARERlqmrsltgpKAPEKPadpIIVHPDVRRMLLTMKAFAEGNRAMLYfaakqvDIVQRSQDEEQKKAADSMlafl 393
Cdd:cd01160 255 TRNYVKQR---------KAFGKT---LAQLQVVRHKIAELATKVAVTRAFLD------NCAWRHEQGRLDVAEASM---- 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595703 394 tpiAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQaLDLLGRKVL 457
Cdd:cd01160 313 ---AKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
99-443 |
1.33e-32 |
|
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: 129.90 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 99 EHGGQGLPESLGLAISEMVGQAnwswgmypgLSHGAmnTLHAH-----------GTAEQQATYLTKLVSGEWTGTMCLTE 167
Cdd:cd01161 78 EYGGLGLNNTQYARLAEIVGMD---------LGFSV--TLGAHqsigfkgillfGTEAQKEKYLPKLASGEWIAAFALTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 168 PHCGTDLGMLRTKAEPQADGS-YKVTGTKIFISAGehDMADniVHIVLARLP--DAPQGTK-GISLFIVpkflpnaegna 243
Cdd:cd01161 147 PSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEvkDATGSVKdKITAFIV----------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 244 gERN--AVSCGSIEHKMGIHGNATCVMNFDAA---TGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYA 318
Cdd:cd01161 212 -ERSfgGVTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 319 RERLQMrsltgpkapekpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDivQRSQDEEQKKAAdsmlafltpIAK 398
Cdd:cd01161 291 NNRKQF------------GKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMD--RGLKAEYQIEAA---------ISK 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15595703 399 AFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGT 443
Cdd:cd01161 348 VFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGT 392
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
97-454 |
4.08e-31 |
|
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: 124.83 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 97 DVEHGGQGLPESLGLAISEMVGQANWSWGmypgLSHGA-----MNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCG 171
Cdd:cd01156 53 PEEYGGSGMGYLAHVIIMEEISRASGSVA----LSYGAhsnlcINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 172 TDLGMLRTKAEPQaDGSYKVTGTKIFISAGEHdmADniVHIVLARlPDAPQGTKGISLFIVPKFLPnaegnagernAVSC 251
Cdd:cd01156 129 SDVVSMKLRAEKK-GDRYVLNGSKMWITNGPD--AD--TLVVYAK-TDPSAGAHGITAFIVEKGMP----------GFSR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 252 GSIEHKMGIHGNATCVMNFD---AATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMRSLT 328
Cdd:cd01156 193 AQKLDKLGMRGSNTCELVFEdceVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 329 G--PKAPEKPADpiivhpdvrrMLLTMKAfaegNRAMLYFAAKQVDIVQRSqdeeQKKAADSMLafltpiakaFMTEVGF 406
Cdd:cd01156 273 GefQLVQGKLAD----------MYTRLNA----SRSYLYTVAKACDRGNMD----PKDAAGVIL---------YAAEKAT 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15595703 407 ESANHGVQIFGGHGFIAEHGMEQNVRDSRismLYE---GTTGVQALdLLGR 454
Cdd:cd01156 326 QVALDAIQILGGNGYINDYPTGRLLRDAK---LYEigaGTSEIRRM-VIGR 372
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
41-456 |
2.13e-23 |
|
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: 102.44 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 41 AILEEGAKFCEQVIAPLNrvgdlegctwsADGVKTPTGFKEAYQQFVEGGWpsLAHDVE-HGGQGLPE-SLGLAISEM-- 116
Cdd:cd01151 19 AIRDTAREFCQEELAPRV-----------LEAYREEKFDRKIIEEMGELGL--LGATIKgYGCAGLSSvAYGLIAREVer 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 117 VGQANWSwgMYPGLSHGAMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGsYKVTGTKI 196
Cdd:cd01151 86 VDSGYRS--FMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 197 FIsaGEHDMADniVHIVLARLpdapQGTKGISLFIVPKFLPNAEGNAgernavscgsIEHKMGIHGNAT-------CVMN 269
Cdd:cd01151 163 WI--TNSPIAD--VFVVWARN----DETGKIRGFILERGMKGLSAPK----------IQGKFSLRASITgeivmdnVFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 270 FDAATgfligPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMrsltgpkapekpADPIIVHPDVRRM 349
Cdd:cd01151 225 EENLL-----PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQF------------GRPLAAFQLVQKK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 350 LLTMkafaEGNRAMLYFAAKQVdivqrSQDEEQKKAADSMLAFLtpiaKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQ 429
Cdd:cd01151 288 LADM----LTEIALGLLACLRV-----GRLKDQGKATPEQISLL----KRNNCGKALEIARTAREMLGGNGISDEYHIIR 354
|
410 420
....*....|....*....|....*..
gi 15595703 430 NVRDSRISMLYEGTTGVQALdLLGRKV 456
Cdd:cd01151 355 HMVNLESVNTYEGTHDIHAL-ILGRAI 380
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
163-452 |
1.19e-22 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 101.75 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 163 MCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEHDmadniVHIVLArlpdapQGTKGISLFIVPKFLPNaegn 242
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLA------QAKGGLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 243 aGERNAVSCGSIEHKMGIHGNATCVMNFDAATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERL 322
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 323 QMrsltgpkapekpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDivqrsQDEEQKKAADSMLafLTPIAKAFMT 402
Cdd:PRK11561 326 VF------------GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-----RRADAKEALWARL--FTPAAKFVIC 386
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15595703 403 EVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDLL 452
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
142-457 |
4.16e-22 |
|
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: 98.43 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 142 GTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADgSYKVTGTKIFISAGEHDMAdnivHIVLARL---P 218
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGKANW----YFLLARSdpdP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 219 DAPQGtKGISLFIVPKFLPnaegnagernAVSCGSIEHKMGIHGNATCVMNFD----AATGFLIGPPNKGLNCMFTFMNT 294
Cdd:cd01157 172 KCPAS-KAFTGFIVEADTP----------GIQPGRKELNMGQRCSDTRGITFEdvrvPKENVLIGEGAGFKIAMGAFDKT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 295 aRLGTALQGLAHAEVGFQGGIAYARERlqmrsltgpKAPEKPadpIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIV 374
Cdd:cd01157 241 -RPPVAAGAVGLAQRALDEATKYALER---------KTFGKL---IAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 375 QRSqdeeqkkaadsmlAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALdLLGR 454
Cdd:cd01157 308 RRN-------------TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL-IISR 373
|
...
gi 15595703 455 KVL 457
Cdd:cd01157 374 EHL 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
282-454 |
3.41e-21 |
|
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: 90.01 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 282 NKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMRSltgpkapekpadPIIVHPDVRRMLLTMKAFAEGNR 361
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------------PLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 362 AMLYFAAKQVDivqrsqDEEQKKAADSMlafltpiAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYE 441
Cdd:pfam00441 69 LLVYRAAEALD------AGGPDGAEASM-------AKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|...
gi 15595703 442 GTTGVQaLDLLGR 454
Cdd:pfam00441 136 GTSEIQ-RNIIAR 147
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
99-456 |
4.47e-19 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 89.55 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 99 EHGGQGLPESLGLAISEMVGQANWSwgmyPGLSHGA-----MNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTD 173
Cdd:PLN02519 81 EYGGLGLGYLYHCIAMEEISRASGS----VGLSYGAhsnlcINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 174 LGMLRTKAEpQADGSYKVTGTKIFISAGEhdMADNIVhiVLARlPDAPQGTKGISLFIVPKFLPnaegnagernAVSCGS 253
Cdd:PLN02519 157 VVSMKCKAE-RVDGGYVLNGNKMWCTNGP--VAQTLV--VYAK-TDVAAGSKGITAFIIEKGMP----------GFSTAQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 254 IEHKMGIHGNATCVMNFD---AATGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERLQMrsltgp 330
Cdd:PLN02519 221 KLDKLGMRGSDTCELVFEncfVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQF------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 331 kapekpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDivqrSQDEEQKKAADSMLafltpiakaFMTEVGFESAN 410
Cdd:PLN02519 295 ------GRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCD----NGKVDRKDCAGVIL---------CAAERATQVAL 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15595703 411 HGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALdLLGRKV 456
Cdd:PLN02519 356 QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
130-443 |
7.12e-18 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 86.14 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 130 LSHGAM--NTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGEhdMAD 207
Cdd:PTZ00461 120 LAHSMLfvNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGT--VAD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 208 niVHIVLARLPDApqgtkgISLFIVPKFLPnaegnagernAVSCGSIEHKMGIHGNATCVMNFD---AATGFLIGPPNKG 284
Cdd:PTZ00461 198 --VFLIYAKVDGK------ITAFVVERGTK----------GFTQGPKIDKCGMRASHMCQLFFEdvvVPAENLLGEEGKG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 285 LNCMFTFMNTARLGTALQGLAHAEVGFQGGIAYARERlqmrsltgpKAPEKpadPIIVHPDVRRMLLTMKAFAEGNRAML 364
Cdd:PTZ00461 260 MVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER---------KAFGK---PISNFGQIQRYIAEGYADTEAAKALV 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595703 365 YFAAKQVdivqrSQDEEQKKAADSMLAFLTPIAKafmtevgfESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGT 443
Cdd:PTZ00461 328 YSVSHNV-----HPGNKNRLGSDAAKLFATPIAK--------KVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
85-457 |
2.41e-17 |
|
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: 84.32 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 85 QFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQAnwswGM-YPGLSHGAM---NTLHAHGTAEQQATYLTKLVSGE-- 158
Cdd:cd01152 43 ALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAA----GApVPFNQIGIDlagPTILAYGTDEQKRRFLPPILSGEei 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 159 WtgtmCL--TEPHCGTDLGMLRTKAEPQADGsYKVTGTKIFISAGEhdMADNivHIVLARL-PDAPQgTKGISLFIVPKf 235
Cdd:cd01152 119 W----CQgfSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH--YADW--AWLLVRTdPEAPK-HRGISILLVDM- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 236 lpNAEGnagernaVSCGSIEHKMGIHGnaTCVMNFD---AATGFLIGPPNKGLN-CMFTFMNtarlgtalqglahaEVGF 311
Cdd:cd01152 188 --DSPG-------VTVRPIRSINGGEF--FNEVFLDdvrVPDANRVGEVNDGWKvAMTTLNF--------------ERVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 312 QGGI-AYARERLQMRSLTGPkapeKPADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAkqvdivqRSQDEEQKKAADSml 390
Cdd:cd01152 243 IGGSaATFFELLLARLLLLT----RDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLA-------SALAAGKPPGAEA-- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595703 391 afltPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNV--------RDSRISMLYEGTTGVQaLDLLGRKVL 457
Cdd:cd01152 310 ----SIAKLFGSELAQELAELALELLGTAALLRDPAPGAELagrweadyLRSRATTIYGGTSEIQ-RNIIAERLL 379
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
162-271 |
1.27e-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: 75.39 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 162 TMCLTEPHCGTDLGMLRTKAEPQADGSYKVTGTKIFISAGehDMADniVHIVLARlPDAPQGTKGISLFIVPKflpNAEG 241
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNA--GIAD--LFLVLAR-TGGDDRHGGISLFLVPK---DAPG 72
|
90 100 110
....*....|....*....|....*....|
gi 15595703 242 nagernaVSCGSIEHKMGIHGNATCVMNFD 271
Cdd:pfam02770 73 -------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
76-443 |
1.51e-15 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 78.62 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 76 PTGFKEAyqqFVEGGWPSLAHDVEHGGQGLPESLGLAISEMVGQANwswGMYPGLSHG-AMNTLHAHGTAEQQA-TYLTK 153
Cdd:PRK12341 39 PREFMRA---LADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCG---APAFLITNGqCIHSMRRFGSAEQLRkTAEST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 154 LVSGEWTGTMCLTEPHCGTDLGMLRTKAEpQADGSYKVTGTKIFIS-AGEHDMAdnivhIVLARLPDAPQGTKGISLFIV 232
Cdd:PRK12341 113 LETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITgAKEYPYM-----LVLARDPQPKDPKKAFTLWWV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 233 PkflPNAEGNagERNAVscgsieHKMGIHGNATCVMNFD---AATGFLIGPPNKG-LNCMFTFmNTARLGTALQGLAHAE 308
Cdd:PRK12341 187 D---SSKPGI--KINPL------HKIGWHMLSTCEVYLDnveVEESDLVGEEGMGfLNVMYNF-EMERLINAARSLGFAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 309 VGFQGGIAYARERLQMrsltgpkapekpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQVDIVQRSQDEeqkkaads 388
Cdd:PRK12341 255 CAFEDAARYANQRIQF------------GKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTS-------- 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15595703 389 mlaflTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGT 443
Cdd:PRK12341 315 -----AALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGT 364
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
84-457 |
2.37e-12 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 68.70 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 84 QQFVEG----GWPSLAHDVEHGGQGLPESLGLAISEMVGQANWSWGMYPGLSHGaMNTLHAHGTAEQQATYLTKLVSGEW 159
Cdd:PRK03354 40 ERFVKAladmGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG-FNTFLREGTQEQIDKIMAFRGTGKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 160 TGTMCLTEPHCGTDLGMLRTKAEpQADGSYKVTGTKIFISAGehdmADNIVHIVLARlpDAPQGTKGI-SLFIVPKFLPN 238
Cdd:PRK03354 119 MWNSAITEPGAGSDVGSLKTTYT-RRNGKVYLNGSKCFITSS----AYTPYIVVMAR--DGASPDKPVyTEWFVDMSKPG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 239 AEGNAgernavscgsiEHKMGIHGNATCVMNFDAA---TGFLIGPPNKGLNCMFTFMNTARLGTALQGLAHAEVGFQGGI 315
Cdd:PRK03354 192 IKVTK-----------LEKLGLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 316 AYARERLQMrsltgpkapekpADPIIVHPDVRRMLLTMKAFAEGNRAMLYFAAKQvdivqrsQDEEQKKAADSMLafltp 395
Cdd:PRK03354 261 RYANQRVQF------------GEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK-------ADNGTITSGDAAM----- 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595703 396 iAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEGTTGVQALDlLGRKVL 457
Cdd:PRK03354 317 -CKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILT-LGRAVL 376
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
41-158 |
5.03e-11 |
|
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: 59.78 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 41 AILEEGAKFCEQVIAPLNRVGDLEGctwsadgvktpTGFKEAYQQFVEGGWPSLAHDVEHGGQGL-PESLGLAISEMvGQ 119
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDEEG-----------EFPRELWKKLGELGLLGITIPEEYGGAGLdYLAYALVAEEL-AR 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15595703 120 ANWSWGMYPGLSHG-AMNTLHAHGTAEQQATYLTKLVSGE 158
Cdd:pfam02771 74 ADASVALALSVHSSlGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-35 |
7.32e-08 |
|
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: 48.49 E-value: 7.32e-08
10 20 30
....*....|....*....|....*....|...
gi 15595703 3 DYKAPLRDIRFVRDELLGYEAhYQSLPGAEDAT 35
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEA-LAALPGFADAD 32
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
110-442 |
6.42e-07 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 52.33 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 110 GLAISEMVGQANWSWGMYPGLSHG-AMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKA--EPQAD 186
Cdd:cd01150 84 MLALTNSLGGYDLSLGAKLGLHLGlFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 187 ----GSYKVTGTKIFISagehDMADNIVH-IVLARL--PDAPQGTKGislFIVP-------KFLPnaegnagernAVSCG 252
Cdd:cd01150 164 efviNTPDFTATKWWPG----NLGKTATHaVVFAQLitPGKNHGLHA---FIVPirdpkthQPLP----------GVTVG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 253 SIEHKMGIHG-------------------NATCVMNFDAATGFLIGPPNKglncmftfmntaRLGTALQGLAHAEVGFQG 313
Cdd:cd01150 227 DIGPKMGLNGvdngflqfrnvriprenllNRFGDVSPDGTYVSPFKDPNK------------RYGAMLGTRSGGRVGLIY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 314 GIAYArerLQM-----------RSLTGPKaPEKPADPIIVHPDVRRMLLTMKAFAegnRAMLYFAAKQVDIVQRSQDEEQ 382
Cdd:cd01150 295 DAAMS---LKKaatiairysavRRQFGPK-PSDPEVQILDYQLQQYRLFPQLAAA---YAFHFAAKSLVEMYHEIIKELL 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595703 383 KKAADSM--LAFLTPIAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEG 442
Cdd:cd01150 368 QGNSELLaeLHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
134-456 |
2.60e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 50.24 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 134 AMNTLHAHGTAEQQATYLTKLVSGEWTGTMCLTEPHCGTDLGMLRTKAEpQADGSYKVTGTKIFIsaGEHDMADniVHIV 213
Cdd:PLN02526 117 AMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI--GNSTFAD--VLVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 214 LARLPDapqgTKGISLFIVPKFLPnaegnagernAVSCGSIEHKMGIHgnatCVMNFDAATGFLIGPPNKGLNCMFTFMN 293
Cdd:PLN02526 192 FARNTT----TNQINGFIVKKGAP----------GLKATKIENKIGLR----MVQNGDIVLKDVFVPDEDRLPGVNSFQD 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 294 T------ARLGTALQGLAHAEVGFQGGIAYARERLQmrsLTGPKAPEKpadpiIVHPDVRRMLltmkafaeGN-RAMLYF 366
Cdd:PLN02526 254 TnkvlavSRVMVAWQPIGISMGVYDMCHRYLKERKQ---FGAPLAAFQ-----INQEKLVRML--------GNiQAMFLV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 367 AAKQVDIVQRSQdeeqkkaadsmlafLTP----IAKAFMTEVGFESANHGVQIFGGHGFIAEHGMEQNVRDSRISMLYEG 442
Cdd:PLN02526 318 GWRLCKLYESGK--------------MTPghasLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEG 383
|
330
....*....|....
gi 15595703 443 TTGVQALdLLGRKV 456
Cdd:PLN02526 384 TYDINAL-VTGREI 396
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
99-195 |
1.24e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 44.87 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595703 99 EHGGQGLPESLGLAISEMVGqANWSWGMYPGLSHGAMNT--LHAHGTAEQQATYLTKLVSGE----WTgtmclTEPHCGT 172
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVG-TNCDSKLLSTIQHSGFCTylLSTVGSKELKGKYLTAMSDGTimmgWA-----TEEGCGS 146
|
90 100
....*....|....*....|...
gi 15595703 173 DLGMLRTKAEPQADGSYKVTGTK 195
Cdd:PTZ00457 147 DISMNTTKASLTDDGSYVLTGQK 169
|
|
| |
