|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
38-439 |
0e+00 |
|
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: 593.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 38 ILNEAARFAETVLEPLNTPADREGCTVVDGRVRVPTGFADAFRRHAGDGWLAMDVPERFGGQALPLVLQAACAPLFERGC 117
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 118 VALMMASGSTRAACHLLAEtAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFR-EGAWRIEGRKIWISFG 196
Cdd:cd01153 81 APLMYASGTQGAAATLLAH-GTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQaDGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 197 DHDMAMRIGHCLLARTGE-ETGTRGLSLFLVPDEI-DGERNGVTVERIEEKMGLHGSPTCALRFDGARGLLLGEEGRGLA 274
Cdd:cd01153 160 EHDMSENIVHLVLARSEGaPPGVKGLSLFLVPKFLdDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 275 QLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDP--AKPAVAIAHHPDIRRQLQEARLRTETLRAATLELATV 352
Cdd:cd01153 240 QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLikAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTATV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 353 MDLARMEPKEEL-RGDLQALSRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAI 431
Cdd:cd01153 320 QDLAERKATEGEdRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQAL 399
|
....*...
gi 2187933646 432 DLLTRRLW 439
Cdd:cd01153 400 DLIGRKIV 407
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
37-442 |
4.32e-98 |
|
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: 301.76 E-value: 4.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 37 AILNEAARFAETVLEPLNTPADREGctvvdgrvRVPTGFADAFRRHagdGWLAMDVPERFGGQALPLVLQAACAPLFERG 116
Cdd:COG1960 11 ALRDEVREFAEEEIAPEAREWDREG--------EFPRELWRKLAEL---GLLGLTIPEEYGGLGLSLVELALVLEELARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 117 CVALMMASGSTRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFG 196
Cdd:COG1960 80 DASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 197 D-HDMamrigHCLLARTGEETGTRGLSLFLVPDEIDgernGVTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGRG 272
Cdd:COG1960 160 PvADV-----ILVLARTDPAAGHRGISLFLVPKDTP----GVTVGRIEDKMGLRGSDTGELFFDDVRvpaENLLGEEGKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 273 LAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATV 352
Cdd:COG1960 231 FKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRP------IADFQAVQHRLADMAAELEAARALVYRAAWL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 353 MDLARmepkeelrgDLQALSrwllPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAID 432
Cdd:COG1960 305 LDAGE---------DAALEA----AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLI 371
|
410
....*....|
gi 2187933646 433 LLTRRLWREG 442
Cdd:COG1960 372 IARRLLGRPG 381
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
27-454 |
8.78e-90 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 287.92 E-value: 8.78e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 27 RGDCDDALVVAILNEAARFAETVLEPLNTPADREGCTVV-DGRVRVPTGFADAFRRHAGDGWLAMDVPERFGGQALPLVL 105
Cdd:PTZ00456 52 KTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLLkDGNVTTPKGFKEAYQALKAGGWTGISEPEEYGGQALPLSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 106 QAACAPLFERGCVALMMASGSTRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAV-FREGAW 184
Cdd:PTZ00456 132 GFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEpSADGSY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 185 RIEGRKIWISFGDHDMAMRIGHCLLART-GEETGTRGLSLFLVPDEIDGERNGVTVER------IEEKMGLHGSPTCALR 257
Cdd:PTZ00456 212 KITGTKIFISAGDHDLTENIVHIVLARLpNSLPTTKGLSLFLVPRHVVKPDGSLETAKnvkcigLEKKMGIKGSSTCQLS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 258 FDGARGLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQ----GG--DPAKPAVAIAHHPDIRRQ 331
Cdd:PTZ00456 292 FENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSmralSGtkEPEKPADRIICHANVRQN 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 332 LQEARLRTETLRAATLELATVMDLARMEPKEELRGDLQALSRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQ 411
Cdd:PTZ00456 372 ILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQ 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2187933646 412 YLRDARVMTIYEGTTGMQAIDLLTRR-LWREGGKGLDVFLKRAR 454
Cdd:PTZ00456 452 ILRDARIGTLYEGTTGIQALDFIGRKvLSLKGGNEVARFGKRVS 495
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
132-434 |
4.42e-74 |
|
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: 237.95 E-value: 4.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 132 HLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFGDHdmamRIGHCLLAR 211
Cdd:cd00567 46 ALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD----ADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 212 TGEET-GTRGLSLFLVPDeidgERNGVTVERIEEKMGLHGSPTCALRFDGARGL---LLGEEGRGLAQLFAMIELMRLQT 287
Cdd:cd00567 122 TDEEGpGHRGISAFLVPA----DTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPednLLGEEGGGFELAMKGLNVGRLLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 288 GCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDLARMEPkeelrgd 367
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKP------LAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEA------- 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2187933646 368 lqalsRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAIDLL 434
Cdd:cd00567 265 -----RLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
38-429 |
2.95e-64 |
|
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: 213.67 E-value: 2.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 38 ILNEAARFAETVLEPLNTPADREGctvvdgrvRVPtgfADAFRRHAGDGWLAMDVPERFGGQALPLVLQAACAPLFERGC 117
Cdd:cd01158 6 IRKTVRDFAEKEIAPLAAEMDEKG--------EFP---REVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 118 --VALMMaSGSTRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISF 195
Cdd:cd01158 75 asVAVIV-SVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 196 GDH-DMAMrighcLLARTGEETGTRGLSLFLVPDEIDGerngVTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGR 271
Cdd:cd01158 154 GGEaDFYI-----VFAVTDPSKGYRGITAFIVERDTPG----LSVGKKEDKLGIRGSSTTELIFEDVRvpkENILGEEGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 272 GLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPAKPAVAIAHH-PDIRRQLQEARLRTetLRAATLE-- 348
Cdd:cd01158 225 GFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKlADMATEIEAARLLT--YKAARLKdn 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 349 -LATVMDLArmepkeelrgdlqalsrwllpLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTG 427
Cdd:cd01158 303 gEPFIKEAA---------------------MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSE 361
|
..
gi 2187933646 428 MQ 429
Cdd:cd01158 362 IQ 363
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
34-440 |
3.75e-47 |
|
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: 169.47 E-value: 3.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 34 LVVAILNEAARFAEtVLEPLNTPADREGCTVvdGRVRVPTGFADAFRRHAGDGwLAMDVPERFGGQAlPLVLQAA----C 109
Cdd:cd01154 29 LAGGELYELARLAD-RNPPVLEMWDRWGRRV--DRVWVHPAWHALMRRLIEEG-VINIEDGPAGEGR-RHVHFAAgyllS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 110 APLFERGCvALMMASGSTRAACHLLAETAEgavadEWVPRLAAGE----WAATICISEPDAGSDLARLRSRAVFREG-AW 184
Cdd:cd01154 104 DAAAGLLC-PLTMTDAAVYALRKYGPEELK-----QYLPGLLSDRyktgLLGGTWMTEKQGGSDLGANETTAERSGGgVY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 185 RIEGRKIWISFGDHDMAMrighcLLART-GEETGTRGLSLFLVPDEI-DGERNGVTVERIEEKMGLHGSPTCALRFDGAR 262
Cdd:cd01154 178 RLNGHKWFASAPLADAAL-----VLARPeGAPAGARGLSLFLVPRLLeDGTRNGYRIRRLKDKLGTRSVATGEVEFDDAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 263 GLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETL 342
Cdd:cd01154 253 AYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKP------LIDHPLMRRDLAEMEVDVEAA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 343 RAATLELATVMDLArmepkEELRGDLQALSRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIY 422
Cdd:cd01154 327 TALTFRAARAFDRA-----AADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIW 401
|
410
....*....|....*...
gi 2187933646 423 EGTTGMQAIDLLtRRLWR 440
Cdd:cd01154 402 EGTGNIQALDVL-RVLVK 418
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
146-441 |
1.18e-42 |
|
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: 156.06 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 146 WVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWIS-FGDHDMamrigHCLLARTGEEtGTRGLSLF 224
Cdd:cd01162 105 FLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISgAGDSDV-----YVVMARTGGE-GPKGISCF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 225 LVPDEIDGERNGvtveRIEEKMGLHGSPTCALRFDGAR---GLLLGEEGRGLaqLFAMIELM--RLQTGCQGLGLASAAI 299
Cdd:cd01162 179 VVEKGTPGLSFG----ANEKKMGWNAQPTRAVIFEDCRvpvENRLGGEGQGF--GIAMAGLNggRLNIASCSLGAAQAAL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 300 DIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDlarmepkeelRGDLQALSrwLLPLV 379
Cdd:cd01162 253 DLARAYLEERKQFGKP------LADFQALQFKLADMATELVASRLMVRRAASALD----------RGDPDAVK--LCAMA 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2187933646 380 KNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAIdLLTRRLWRE 441
Cdd:cd01162 315 KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL-IIARALLTR 375
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
42-426 |
1.44e-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: 147.56 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 42 AARFAETVLEPLNTPADREgctvvdgrvrvpTGFADAFRRHAGD-GWLAMDVPERFGGQALPLVLQAACAPLFERGCVAL 120
Cdd:cd01156 13 VREFAQKEIAPLAAKIDRD------------NEFPRDLWRKMGKlGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 121 MMASGSTRAAC-HLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFG-DH 198
Cdd:cd01156 81 ALSYGAHSNLCiNQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGpDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 199 DMAMrighcLLARTGEETGTRGLSLFLVpdeidgERN--GVTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGRGL 273
Cdd:cd01156 161 DTLV-----VYAKTDPSAGAHGITAFIV------EKGmpGFSRAQKLDKLGMRGSNTCELVFEDCEvpeENILGGENKGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 274 AQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVM 353
Cdd:cd01156 230 YVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQP------IGEFQLVQGKLADMYTRLNASRSYLYTVAKAC 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2187933646 354 DLARMEPKEelrgdlqALSRWLlplvknFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTT 426
Cdd:cd01156 304 DRGNMDPKD-------AAGVIL------YAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTS 363
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
79-438 |
3.22e-39 |
|
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: 146.88 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 79 FRRHAGDGWLAMDVPERFGGQALPLVLQAACAPLFER-GCVALMMASGSTRAACHLlAETAEGAVADEWVPRLAAGEWAA 157
Cdd:cd01160 36 WRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARaGGSGPGLSLHTDIVSPYI-TRAGSPEQKERVLPQMVAGKKIG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 158 TICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFGDH-DMAMrighcLLARTG-EETGTRGLSLFLVpdeiDGERN 235
Cdd:cd01160 115 AIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLaDVVI-----VVARTGgEARGAGGISLFLV----ERGTP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 236 GVTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQG 312
Cdd:cd01160 186 GFSRGRKLKKMGWKAQDTAELFFDDCRvpaENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 313 GDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDLARMEPKEelrgdlqalsrwlLPLVKNFGADAGFTVSN 392
Cdd:cd01160 266 GKT------LAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAE-------------ASMAKYWATELQNRVAY 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2187933646 393 QAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAiDLLTRRL 438
Cdd:cd01160 327 ECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMK-ELISRQM 371
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
86-425 |
6.55e-37 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 141.07 E-value: 6.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 86 GWLAMDVPERFGGQALPLVLQAACAPLFER-GCVALMMASGSTRAACHLLAETAEgAVADEWVPRLAAGEWAATICISEP 164
Cdd:cd01161 69 GLFGLQVPEEYGGLGLNNTQYARLAEIVGMdLGFSVTLGAHQSIGFKGILLFGTE-AQKEKYLPKLASGEWIAAFALTEP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 165 DAGSDLARLRSRAVFREGA--WRIEGRKIWISFGDHDMAMRIghclLART--GEETGTR--GLSLFLVpdeidgERN--G 236
Cdd:cd01161 148 SSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTV----FAKTevKDATGSVkdKITAFIV------ERSfgG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 237 VTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGG 313
Cdd:cd01161 218 VTNGPPEKKMGIKGSNTAEVYFEDVKipvENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 314 DPAKPAVAIahhpdirrqlQEARLRTETLRAATlELATVMDLARMEPKEELRGDLQAlsrwllPLVKNFGADAGFTVSNQ 393
Cdd:cd01161 298 KKIHEFGLI----------QEKLANMAILQYAT-ESMAYMTSGNMDRGLKAEYQIEA------AISKVFASEAAWLVVDE 360
|
330 340 350
....*....|....*....|....*....|..
gi 2187933646 394 AIQILGGAGYTREWPLEQYLRDARVMTIYEGT 425
Cdd:cd01161 361 AIQIHGGMGFMREYGVERVLRDLRIFRIFEGT 392
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
86-442 |
2.86e-31 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 125.37 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 86 GWLAMDVPERFGGQALPLVLQAACAPLFERGCVALMMASGSTRAAC-HLLAETAEGAVADEWVPRLAAGEWAATICISEP 164
Cdd:PLN02519 72 NLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCiNQLVRNGTPAQKEKYLPKLISGEHVGALAMSEP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 165 DAGSDLARLRSRAVFREGAWRIEGRKIWISFGDHDMAMRIghclLARTGEETGTRGLSLFLVPDEIDGERngvTVERIEe 244
Cdd:PLN02519 152 NSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVV----YAKTDVAAGSKGITAFIIEKGMPGFS---TAQKLD- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 245 KMGLHGSPTCALRFDGA---RGLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpava 321
Cdd:PLN02519 224 KLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRP------ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 322 IAHHPDIRRQLQEARLRTETLRAATLELATVMDLARMEPKEelrgdlqalsrwlLPLVKNFGADAGFTVSNQAIQILGGA 401
Cdd:PLN02519 298 IGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKD-------------CAGVILCAAERATQVALQAIQCLGGN 364
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2187933646 402 GYTREWPLEQYLRDARVMTIYEGTTGMQAIdLLTRRLWREG 442
Cdd:PLN02519 365 GYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGRELFKEE 404
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
70-425 |
5.35e-30 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 120.99 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 70 RVPTGFADAFrrhAGDGWLAMDVPERFGGQ-----ALPLVLQAAC-----APLFERG-CVALMMASGSTRAachlLAETA 138
Cdd:PRK12341 37 TYPREFMRAL---ADNGISMLGVPEEFGGTpadyvTQMLVLEEVSkcgapAFLITNGqCIHSMRRFGSAEQ----LRKTA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 139 EGAvadewvprLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISfgdhdMAMRIGHCL-LARTGEETG 217
Cdd:PRK12341 110 EST--------LETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFIT-----GAKEYPYMLvLARDPQPKD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 218 TR-GLSLFLVPDEidgeRNGVTVERIEeKMGLHGSPTCALRFDGA---RGLLLGEEGRGLAQLFAMIELMRLQTGCQGLG 293
Cdd:PRK12341 177 PKkAFTLWWVDSS----KPGIKINPLH-KIGWHMLSTCEVYLDNVeveESDLVGEEGMGFLNVMYNFEMERLINAARSLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 294 LASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDlarmepkeelrgdlQALS- 372
Cdd:PRK12341 252 FAECAFEDAARYANQRIQFGKP------IGHNQLIQEKLTLMAIKIENMRNMVYKVAWQAD--------------NGQSl 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2187933646 373 RWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGT 425
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGT 364
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
39-431 |
5.46e-30 |
|
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: 121.15 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 39 LNEAAR-FAETVLEPLNTPADREGctvvdgRVRVPTgfadaFRRHAGDGWLAMDVPERFGGQALPLVLQAACAPLFERGC 117
Cdd:cd01157 8 FQETARkFAREEIIPVAAEYDKSG------EYPWPL-----IKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 118 VALMMASGSTRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFGD 197
Cdd:cd01157 77 TGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 198 HDMamriGHCLLARTGEETGT---RGLSLFLVpdeiDGERNGVTVERIEEKMGLHGSPTCALRFDGAR---GLLLGEEGR 271
Cdd:cd01157 157 KAN----WYFLLARSDPDPKCpasKAFTGFIV----EADTPGIQPGRKELNMGQRCSDTRGITFEDVRvpkENVLIGEGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 272 GLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELAT 351
Cdd:cd01157 229 GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKL------IAEHQAVSFMLADMAMKVELARLAYQRAAW 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 352 VMDLARMepkeelrgdlqalSRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAI 431
Cdd:cd01157 303 EVDSGRR-------------NTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
37-425 |
2.92e-25 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 108.10 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 37 AILNEAARFAETVLEPLNTPADregctvVDGRVRVptgfaDAFRRHAGDGWLAMDVPERFGGQALPLVLQ-------AAC 109
Cdd:PTZ00461 43 ALRETVAKFSREVVDKHAREDD------INMHFNR-----DLFKQLGDLGVMGVTVPEADGGAGMDAVAAviihhelSKY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 110 APLFergCVALMMASgstRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAV-FREGAWRIEG 188
Cdd:PTZ00461 112 DPGF---CLAYLAHS---MLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKkDSNGNYVLNG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 189 RKIWISfgdhdmamrighcllartgeeTGTRGlSLFLVPDEIDGERNGVTVERIE---------EKMGLHGSPTCALRFD 259
Cdd:PTZ00461 186 SKIWIT---------------------NGTVA-DVFLIYAKVDGKITAFVVERGTkgftqgpkiDKCGMRASHMCQLFFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 260 GA---RGLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEAR 336
Cdd:PTZ00461 244 DVvvpAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKP------ISNFGQIQRYIAEGY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 337 LRTETLRAATLELATvmdlaRMEPKEELRGDLQALSRWLLPLVKNfgadagftVSNQAIQILGGAGYTREWPLEQYLRDA 416
Cdd:PTZ00461 318 ADTEAAKALVYSVSH-----NVHPGNKNRLGSDAAKLFATPIAKK--------VADSAIQVMGGMGYSRDMPVERLWRDA 384
|
....*....
gi 2187933646 417 RVMTIYEGT 425
Cdd:PTZ00461 385 KLLEIGGGT 393
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
270-438 |
5.85e-24 |
|
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: 97.71 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 270 GRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLEL 349
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRP------LIDFQLVRHKLAEMAAEIEAARLLVYRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 350 ATVMDLARMEPKEelrgdlqalsrwlLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQ 429
Cdd:pfam00441 75 AEALDAGGPDGAE-------------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQ 141
|
....*....
gi 2187933646 430 aIDLLTRRL 438
Cdd:pfam00441 142 -RNIIARRL 149
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
161-434 |
5.66e-23 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 102.52 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 161 ISEPDAGSDLARLRSRAV-FREGAWRIEGRKIWISFGDHDmamriGHCLLARTgeetgTRGLSLFLVPDEI-DGERNGVT 238
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAErLADGSYRLVGHKWFFSVPQSD-----AHLVLAQA-----KGGLSCFFVPRFLpDGQRNAIR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 239 VERIEEKMGLHGSPTCALRFDGARGLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakp 318
Cdd:PRK11561 254 LERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFGKP--- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 319 avaIAHHPDIRRQLQEARLRTETLRAATLELATVMDlARMEPKEelrgdlQALSRWLLPLVKNFGADAGFTVSNQAIQIL 398
Cdd:PRK11561 331 ---LIEQPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKE------ALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
|
250 260 270
....*....|....*....|....*....|....*.
gi 2187933646 399 GGAGYTREWPLEQYLRDARVMTIYEGTTGMQAIDLL 434
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL 436
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
36-431 |
4.32e-22 |
|
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: 98.20 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 36 VAILNEAARFAETVLEPLNTPADREGCTvvdgrvrvptgFADAFRRHAGDGWLAMdVPERFGGQALPLVLQAACAPLFER 115
Cdd:cd01151 18 RAIRDTAREFCQEELAPRVLEAYREEKF-----------DRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 116 ---GCVALMMASGSTraACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIW 192
Cdd:cd01151 86 vdsGYRSFMSVQSSL--VMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 193 ISFGD-HDMAMrighcLLARTGEETGTRGlslFLVPDEIDgernGVTVERIEEKMGLHGSPTCALRFDGARgllLGEEGR 271
Cdd:cd01151 164 ITNSPiADVFV-----VWARNDETGKIRG---FILERGMK----GLSAPKIQGKFSLRASITGEIVMDNVF---VPEENL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 272 -----GLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAAT 346
Cdd:cd01151 229 lpgaeGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRP------LAAFQLVQKKLADMLTEIALGLLAC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 347 LELATVMDLARMEPKEelrgdlqalsrwlLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGT- 425
Cdd:cd01151 303 LRVGRLKDQGKATPEQ-------------ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTh 369
|
410
....*....|....*..
gi 2187933646 426 -----------TGMQAI 431
Cdd:cd01151 370 dihalilgraiTGIQAF 386
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
41-429 |
1.84e-21 |
|
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: 96.26 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 41 EAARFAETVLEPL--NTPADREGctvvDGRVRVPTGFADAFRRH---AGDGWLAMDVPERFGGQALPLVLQAACAPLFER 115
Cdd:cd01152 2 SEEAFRAEVRAWLaaHLPPELRE----ESALGYREGREDRRRWQralAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 116 GCVALMMASGSTRAACHLLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWIS- 194
Cdd:cd01152 78 AGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 195 --FGDHdmamrigHCLLARTG-EETGTRGLSLFLVPdeIDGErnGVTVERIEEKMGlhGSPTCALRFDGAR---GLLLGE 268
Cdd:cd01152 158 ahYADW-------AWLLVRTDpEAPKHRGISILLVD--MDSP--GVTVRPIRSING--GEFFNEVFLDDVRvpdANRVGE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 269 EGRGLAQLFAMIELMRLQTGcqglglASAAIDiaetYAQERQQGGDPAKPAVAIAHHPDIRRQLQEARLRTETLRAATLE 348
Cdd:cd01152 225 VNDGWKVAMTTLNFERVSIG------GSAATF----FELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 349 LATVMdlarMEPKeelRGDLQAlsrwllPLVKNFGADAGFTVSNQAIQILGGAGYTREWPL--------EQYLRDARVMT 420
Cdd:cd01152 295 LASAL----AAGK---PPGAEA------SIAKLFGSELAQELAELALELLGTAALLRDPAPgaelagrwEADYLRSRATT 361
|
....*....
gi 2187933646 421 IYEGTTGMQ 429
Cdd:cd01152 362 IYGGTSEIQ 370
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
158-259 |
3.29e-21 |
|
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: 88.11 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 158 TICISEPDAGSDLARLRSRAVFREGA-WRIEGRKIWISFGDH-DMAMrighcLLARTGEETGTRGLSLFLVPDEidgeRN 235
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIaDLFL-----VLARTGGDDRHGGISLFLVPKD----AP 71
|
90 100
....*....|....*....|....
gi 2187933646 236 GVTVERIEEKMGLHGSPTCALRFD 259
Cdd:pfam02770 72 GVSVRRIETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
92-433 |
1.31e-15 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 78.72 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 92 VPERFGGqalplvlqaacaplFERGCVALM---MASGSTRAACHLLAETAEG--AVADEWVPR--------LAAGEWAAT 158
Cdd:PRK03354 56 IPEEHGG--------------LDAGFVTLAavwMELGRLGAPTYVLYQLPGGfnTFLREGTQEqidkimafRGTGKQMWN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 159 ICISEPDAGSDLARLRSRAVFREGAWRIEGRKIWISFGDHDMAMRIghclLARTGEETGTRGLSLFLVpdeiDGERNGVT 238
Cdd:PRK03354 122 SAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVV----MARDGASPDKPVYTEWFV----DMSKPGIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 239 VERIEeKMGLHGSPTCALRFDGAR---GLLLGEEGRGLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDP 315
Cdd:PRK03354 194 VTKLE-KLGLRMDSCCEITFDDVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 316 akpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDLARMEpkeelRGDLQalsrwllpLVKNFGADAGFTVSNQAI 395
Cdd:PRK03354 273 ------IGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-----SGDAA--------MCKYFCANAAFEVVDSAM 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 2187933646 396 QILGGAGYTREWPLEQYLRDARVMTIYEGTTGMQAIDL 433
Cdd:PRK03354 334 QVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL 371
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
145-424 |
6.95e-12 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). 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 ACAD 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. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 67.03 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 145 EWVPRLAAGEWAATICISEPD-AGSDLARLRSRAVFREGAWRIEGRKIWIS-FGDHDMAMRIghcLLARTGEETGTRGL- 221
Cdd:cd01155 115 QWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSgAGDPRCKIAI---VMGRTDPDGAPRHRq 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 222 -SLFLVPdeIDGErnGVTVERIEEKMGLHGSPT--CALRFDGAR---GLLLGEEGRGLAqlfamIELMRLQTG----C-Q 290
Cdd:cd01155 192 qSMILVP--MDTP--GVTIIRPLSVFGYDDAPHghAEITFDNVRvpaSNLILGEGRGFE-----IAQGRLGPGrihhCmR 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 291 GLGLASAAIDIAETYAQERQQGGDPakpavaIAHHPDIRRQLQEARLRTETLRAATLELATVMDlaRMEPKEelrgdlqa 370
Cdd:cd01155 263 LIGAAERALELMCQRAVSREAFGKK------LAQHGVVAHWIAKSRIEIEQARLLVLKAAHMID--TVGNKA-------- 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2187933646 371 lSRWLLPLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEG 424
Cdd:cd01155 327 -ARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
118-315 |
2.10e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 59.48 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 118 VALMMASGSTRAACH------LLAETAEGAVADEWVPRLAAGEWAATICISEPDAGSDLARLRSRAVFREGAWRIEGRKI 191
Cdd:PLN02526 99 VARVDASCSTFILVHsslamlTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 192 WI---SFGDhdmamrighcLLARTGEETGTRGLSLFLVpdeiDGERNGVTVERIEEKMGLHGSPTCALRFDGArglLLGE 268
Cdd:PLN02526 179 WIgnsTFAD----------VLVIFARNTTTNQINGFIV----KKGAPGLKATKIENKIGLRMVQNGDIVLKDV---FVPD 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2187933646 269 EGR-----GLAQLFAMIELMRLQTGCQGLGLASAAIDIAETYAQERQQGGDP 315
Cdd:PLN02526 242 EDRlpgvnSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAP 293
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
37-154 |
3.96e-08 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 51.31 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 37 AILNEAARFAETVLEPLNTPADREGctvvdgrvRVPtgfADAFRRHAGDGWLAMDVPERFGGQALPLVLQAACAPLFERG 116
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDEEG--------EFP---RELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2187933646 117 CVAL-MMASGSTRAACHLLAE--TAEgaVADEWVPRLAAGE 154
Cdd:pfam02771 75 DASVaLALSVHSSLGAPPILRfgTEE--QKERYLPKLASGE 113
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
236-482 |
2.70e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 43.69 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 236 GVTVERIEEKMGLHGSPTCALRFDGAR----GLL-----LGEEGRGLAQL------FAMIeLMRLQTGCQGLGLAS---- 296
Cdd:PLN02636 267 GVEIRDCGHKVGLNGVDNGALRFRSVRiprdNLLnrfgdVSRDGKYTSSLptinkrFAAT-LGELVGGRVGLAYGSvgvl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 297 -AAIDIAETYAQERQQGGDPAKPAVAIAHHPDIRRQLQEARLRTETLRAATLELATVMDLARMEPKEELRGDLQALSRWL 375
Cdd:PLN02636 346 kASNTIAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEMKKTHDDQLVADVHALSAGL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 376 LPLVKNFGADAgFTVSNQAIqilGGAGYTREWPLEQYLRDARVMTIYEG--TTGMQ--AIDLLTRRLWREGGKGLDVFLK 451
Cdd:PLN02636 426 KAYITSYTAKA-LSTCREAC---GGHGYAAVNRFGSLRNDHDIFQTFEGdnTVLLQqvAADLLKQYKEKFQGGTLSVTWN 501
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2187933646 452 RARSELADYRSDKTKAAAS------------VLDAFEAESRRM 482
Cdd:PLN02636 502 YLRESMNTYLSQPNPVTTRwegeehlrdpkfQLDAFRYRTSRL 544
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
290-426 |
1.61e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 38.87 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2187933646 290 QGLGLASAAIDIAETYAQERQQGGDpakpAVAIAHHPDIRRQLQEARLRTETLRAATLELATVMDLARmEPKEELRGDLQ 369
Cdd:pfam08028 5 AALGAARAALAEFTERARGRVRAYF----GVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAA-AAGKPVTPALR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2187933646 370 ALSRwllpLVKNFGADAGFTVSNQAIQILGGAGYTREWPLEQYLRDARVMTIYEGTT 426
Cdd:pfam08028 80 AEAR----RAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| |
