|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
1-511 |
0e+00 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 614.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 1 MTWPTHDVTNQAPPLQDYNLFTADPALREALARAGGGWAEEQLTRQGAELGTAASYKQGRLANQNTPVLRAFDARGFRRD 80
Cdd:PRK11561 1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 81 QIEFHPAWHALMSDIARRGLHTGPWAR-PQPGAHVARAAGFILQTQIEAGSMCPTTMTYGAIPAMSRdALLA--RDWLPT 157
Cdd:PRK11561 81 DVRFHPAWHLLMQGLCANRVHNLAWEEdARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQ-MLPApfQDWLTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 158 LMRPEYDPRDLPPAQKRGGLIGMGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFSAPQCDAHLVLAQTAGGLSCFF 237
Cdd:PRK11561 160 LLSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 238 VPRWAPDGSKNPVLIQRLKDKLGNRSNASSEVEFQGAWGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVH 317
Cdd:PRK11561 240 VPRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 318 YARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDEAQSLLRRLLTPAGKFRICKRGAELAAEAMEV 397
Cdd:PRK11561 320 HAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 398 LGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRALGKNPRTADALMAELAQAQGRNAHFDAHLQRFSAALRDTDA 477
Cdd:PRK11561 400 LGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAE 479
|
490 500 510
....*....|....*....|....*....|....
gi 1026941777 478 QQsrARALTHDLVLALQAALLLRHAPEPIAQAFC 511
Cdd:PRK11561 480 EQ--GREITQQLFLLGCGAQMLRHASPPLAQAWC 511
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
21-439 |
4.83e-164 |
|
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: 472.24 E-value: 4.83e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 21 FTADPALREALARAGGGWAEEQLTRQGaELGTAASYKQGRLANQNTPVLRAFDARGFRRDQIEFHPAWHALMSDIARRGL 100
Cdd:cd01154 1 YLDDPVLQQTLRYFGDPEEEPDLSRLG-ELAGGELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 101 HTGPWAR-PQPGAHVARAAGFILqTQIEAGSMCPTTMTYGAIPAMSRDA-LLARDWLPTLMRPEYdprdlppaqKRGGLI 178
Cdd:cd01154 80 INIEDGPaGEGRRHVHFAAGYLL-SDAAAGLLCPLTMTDAAVYALRKYGpEELKQYLPGLLSDRY---------KTGLLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 179 GMGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFSAPQCDAHLVLAQTAG------GLSCFFVPRWAPDGSKNPVLI 252
Cdd:cd01154 150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGapagarGLSLFLVPRLLEDGTRNGYRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 253 QRLKDKLGNRSNASSEVEFQGAWGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAALIDQ 332
Cdd:cd01154 230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 333 PLMRNVLADMALEVEAAIALALRLAQAFD-SQHD-EAQSLLRRLLTPAGKFRICKRGAELAAEAMEVLGGNGYVEEDMQA 410
Cdd:cd01154 310 PLMRRDLAEMEVDVEAATALTFRAARAFDrAAADkPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
|
410 420
....*....|....*....|....*....
gi 1026941777 411 RIYREMPVNSIWEGSGNVMCLDVLRALGK 439
Cdd:cd01154 390 RLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| AidB_N |
pfam18158 |
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive ... |
10-165 |
1.62e-70 |
|
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive response protein AidB present in E. coli. AidB is upregulated in response to small doses of DNA-methylating agents initiates a response that mitigates the mutagenic and cytotoxic effects of DNA methylation. Tetramer formation is thought to be carried out by the N-terminal domain.
Pssm-ID: 436317 [Multi-domain] Cd Length: 156 Bit Score: 222.89 E-value: 1.62e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 10 NQAPPLQDYNLFTADPALREALARAGGGWAEEQLTRQGAELGTAASYKQGRLANQNTPVLRAFDARGFRRDQIEFHPAWH 89
Cdd:pfam18158 1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026941777 90 ALMSDIARRGLHTGPWARPQPGAHVARAAGFILQTQIEAGSMCPTTMTYGAIPAMSRDALLARDWLPTLMRPEYDP 165
Cdd:pfam18158 81 ALMALAIEAGLHASPWTDARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVPALRAEPALAEEWLPKLLSRDYDP 156
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
67-442 |
8.17e-58 |
|
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: 197.37 E-value: 8.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 67 PVLRAFDARGfrrdqiEFHPAWHALMsdiARRGLHTGPWARPQPGAHVARAAGFILQTQIEAGSM---CPTTMTYGAIPA 143
Cdd:COG1960 26 PEAREWDREG------EFPRELWRKL---AELGLLGLTIPEEYGGLGLSLVELALVLEELARADAslaLPVGVHNGAAEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 144 MSR---DALLARdWLPTLMRPEYdprdlppaqkrggLIGMGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHKWFFS-APQ 219
Cdd:COG1960 97 LLRfgtEEQKER-YLPRLASGEW-------------IGAFALTEPGAGSDAAALRTTAVRDG-DGYVLNGQKTFITnAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 220 CDAHLVLAQTAG-----GLSCFFVPRWAPDgsknpVLIQRLKDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILE 291
Cdd:COG1960 162 ADVILVLARTDPaaghrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDVRvpaENLLGEEGKGFKIAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 292 MGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDeaqsll 371
Cdd:COG1960 237 TLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED------ 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1026941777 372 RRLLTPAGKFRICKRGAELAAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRALGKNPR 442
Cdd:COG1960 311 AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
168-435 |
5.36e-47 |
|
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: 166.69 E-value: 5.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 168 LPPAQKRGGLIGMGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHKWFFS-APQCDAHLVLAQTAG------GLSCFFVPR 240
Cdd:cd00567 61 LPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG-DGYVLNGRKIFISnGGDADLFIVLARTDEegpghrGISAFLVPA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 241 WAPDGSknpvlIQRLKDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVH 317
Cdd:cd00567 140 DTPGVT-----VGRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 318 YARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDEAqsllrRLLTPAGKFRICKRGAELAAEAMEV 397
Cdd:cd00567 215 YAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEA-----RLEAAMAKLFATEAAREVADLAMQI 289
|
250 260 270
....*....|....*....|....*....|....*...
gi 1026941777 398 LGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLR 435
Cdd:cd00567 290 HGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
168-435 |
3.39e-39 |
|
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: 147.54 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 168 LPPAQKRGGLIGMGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFSAPQCDA-----HLVLAQTAG------GLSCF 236
Cdd:cd01153 109 IPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMsenivHLVLARSEGappgvkGLSLF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 237 FVPRWAPDGSKNPVLIQRLKDKLGNRSNASSEVEFQGAWGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAV 316
Cdd:cd01153 189 LVPKFLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 317 HYARHRQAFGAALIDQP--------LMRNVLADMALEVEAAIALALRLAQAFDSQHDEAQS--------LLRRLLTPAGK 380
Cdd:cd01153 269 AYAKERKQGGDLIKAAPavtiihhpDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATEgedrkalsALADLLTPVVK 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1026941777 381 FRICKRGAELAAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLR 435
Cdd:cd01153 349 GFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIG 403
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
168-437 |
2.00e-25 |
|
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: 107.74 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 168 LPPAQKrGGLIG-MGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WFFSAPQCDAHLVLAQT-----AGGLSCFFVPR 240
Cdd:cd01158 105 LPPLAT-GEKIGaFALSEPGAGSDAAALKTTAKKDG-DDYVLNGSKmWITNGGEADFYIVFAVTdpskgYRGITAFIVER 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 241 WAPDGSknpvlIQRLKDKLGNRSNASSEVEFQGAWGH---LLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVH 317
Cdd:cd01158 183 DTPGLS-----VGKKEDKLGIRGSSTTELIFEDVRVPkenILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVD 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 318 YARHRQAFGAALIDQPLMRNVLADMALEVEAAialalrlaqafdsqhdeaqsllrRLLT-----------PAGK-FRICK 385
Cdd:cd01158 258 YAKERKQFGKPIADFQGIQFKLADMATEIEAA-----------------------RLLTykaarlkdngePFIKeAAMAK 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1026941777 386 RGAELAA-----EAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRAL 437
Cdd:cd01158 315 LFASEVAmrvttDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHL 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
179-439 |
2.32e-25 |
|
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: 107.88 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 179 GMGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WFFSAPQCDAHLVLAQT-----AGGLSCFFVPRWAPDGSKNPVLi 252
Cdd:cd01156 119 ALAMSEPNAGSDVVSMKLRAEKKG-DRYVLNGSKmWITNGPDADTLVVYAKTdpsagAHGITAFIVEKGMPGFSRAQKL- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 253 qrlkDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAAL 329
Cdd:cd01156 197 ----DKLGMRGSNTCELVFEDCEvpeENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 330 IDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDEAQSLLRRLLTPAgkfricKRGAELAAEAMEVLGGNGYVEEDMQ 409
Cdd:cd01156 273 GEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAA------EKATQVALDAIQILGGNGYINDYPT 346
|
250 260 270
....*....|....*....|....*....|
gi 1026941777 410 ARIYREMPVNSIWEGSGNVMCLDVLRALGK 439
Cdd:cd01156 347 GRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-437 |
2.08e-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: 99.25 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 283 GRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDS 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1026941777 363 QHDEaqsllrRLLTPAGKFRICKRGAELAAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRAL 437
Cdd:pfam00441 81 GGPD------GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
179-271 |
9.17e-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: 86.95 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 179 GMGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFS-APQCDAHLVLAQTA-----GGLSCFFVPRWAPDgsknpVLI 252
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIADLFLVLARTGgddrhGGISLFLVPKDAPG-----VSV 75
|
90
....*....|....*....
gi 1026941777 253 QRLKDKLGNRSNASSEVEF 271
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVF 94
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
126-437 |
1.87e-20 |
|
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: 93.28 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 126 IEAGSM-CPTTMTYGAIPAMSR-------DALLARDWLPtlmrpeydprdlppaqkrgGLIGMG------MTEKQGGSDL 191
Cdd:cd01162 69 FEALSTgCVSTAAYISIHNMCAwmidsfgNDEQRERFLP-------------------DLCTMEklasycLTEPGSGSDA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 192 RSNTTRAEPDGaGGYRLTGHKWFFS-APQCDAHLVLAQTAG----GLSCFFVPRWAPDGSknpvlIQRLKDKLGNRSNAS 266
Cdd:cd01162 130 AALRTRAVREG-DHYVLNGSKAFISgAGDSDVYVVMARTGGegpkGISCFVVEKGTPGLS-----FGANEKKMGWNAQPT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 267 SEVEFQGA---WGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAALIDQPLMRNVLADMA 343
Cdd:cd01162 204 RAVIFEDCrvpVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 344 LEVEAAIALALRLAQAFDSQHDEAQSLL---RRLLTPAGkFRICKrgaelaaEAMEVLGGNGYVEEDMQARIYREMPVNS 420
Cdd:cd01162 284 TELVASRLMVRRAASALDRGDPDAVKLCamaKRFATDEC-FDVAN-------QALQLHGGYGYLKDYPVEQYVRDLRVHQ 355
|
330
....*....|....*..
gi 1026941777 421 IWEGSGNVMCLDVLRAL 437
Cdd:cd01162 356 ILEGTNEIMRLIIARAL 372
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
166-439 |
2.01e-20 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 93.40 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 166 RDLPPAQKR--------GGLIG-MGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WFFSAPQCDAHLVLAQT---AG- 231
Cdd:PLN02519 123 RNGTPAQKEkylpklisGEHVGaLAMSEPNSGSDVVSMKCKAERVD-GGYVLNGNKmWCTNGPVAQTLVVYAKTdvaAGs 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 232 -GLSCFFVPRWAPDGSKnpvlIQRLkDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGL 307
Cdd:PLN02519 202 kGITAFIIEKGMPGFST----AQKL-DKLGMRGSDTCELVFENCFvpeENVLGQEGKGVYVMMSGLDLERLVLAAGPLGL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 308 MRQALSQAVHYARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDEAQSLLRRLLTPAgkfricKRG 387
Cdd:PLN02519 277 MQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAA------ERA 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1026941777 388 AELAAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRALGK 439
Cdd:PLN02519 351 TQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFK 402
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
180-434 |
7.80e-20 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 93.01 E-value: 7.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 180 MGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFSAPQCD-----AHLVLAQ------TAGGLSCFFVPRWA--PDGS 246
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDlteniVHIVLARlpnslpTTKGLSLFLVPRHVvkPDGS 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 247 ----KNPVLIQrLKDKLGNRSNASSEVEFQGAWGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHR 322
Cdd:PTZ00456 265 letaKNVKCIG-LEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 323 QAF------------GAALIDQPLMR-NVLADMALeVEAAIALALRLAQAFDSQHDEAQSLLRR-------LLTPAGKFR 382
Cdd:PTZ00456 344 RSMralsgtkepekpADRIICHANVRqNILFAKAV-AEGGRALLLDVGRLLDIHAAAKDAATREaldheigFYTPIAKGC 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1026941777 383 ICKRGAELAAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVL 434
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFI 474
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
170-438 |
1.45e-18 |
|
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: 87.56 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 170 PAQKR--------GGLIG-MGMTEKQGGSDLRSNTTRAEPDGAGgYRLTGHKWFFS-APQCDAHLVLAQT------AGGL 233
Cdd:cd01160 97 PEQKErvlpqmvaGKKIGaIAMTEPGAGSDLQGIRTTARKDGDH-YVLNGSKTFITnGMLADVVIVVARTggeargAGGI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 234 SCFFVPRWAPDGSKNpvliqRLKDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQ 310
Cdd:cd01160 176 SLFLVERGTPGFSRG-----RKLKKMGWKAQDTAELFFDDCRvpaENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 311 ALSQAVHYARHRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAqafdsQHDEAQSLLRRLLTPAgKFRICKRGAEL 390
Cdd:cd01160 251 MLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCA-----WRHEQGRLDVAEASMA-KYWATELQNRV 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1026941777 391 AAEAMEVLGGNGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRALG 438
Cdd:cd01160 325 AYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
170-436 |
5.50e-17 |
|
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: 82.79 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 170 PAQKRGGLIG-MGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WFFSAPQCDAHLVLA--QTAGGLSCFFVPRWAPdG 245
Cdd:cd01151 119 PKLASGELIGcFGLTEPNHGSDPGGMETRARKDG-GGYKLNGSKtWITNSPIADVFVVWArnDETGKIRGFILERGMK-G 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 246 SKNPvliqRLKDKLGNRSNASSEVEFQGAW----GHLLGEEGRGVP-TILEMgtyTRLDCVLGTTGLMRQALSQAVHYAR 320
Cdd:cd01151 197 LSAP----KIQGKFSLRASITGEIVMDNVFvpeeNLLPGAEGLRGPfKCLNN---ARYGIAWGALGAAEDCYHTARQYVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 321 HRQAFGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDsqhdeaQSLLRRLLTPAGKFRICKRGAELAAEAMEVLGG 400
Cdd:cd01151 270 DRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKD------QGKATPEQISLLKRNNCGKALEIARTAREMLGG 343
|
250 260 270
....*....|....*....|....*....|....*.
gi 1026941777 401 NGYVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRA 436
Cdd:cd01151 344 NGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRA 379
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
182-435 |
9.09e-16 |
|
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: 79.43 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 182 MTEKQGGSDLRSNTTRAEPDGAGG-YRLTGHK-WFFSAPQCDAHLVLAQT---------AGGLSCFFVPRwapdgSKNPV 250
Cdd:cd01161 144 LTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKiWITNGGIADIFTVFAKTevkdatgsvKDKITAFIVER-----SFGGV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 251 LIQRLKDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVP---TILEMGtytRLDCVLGTTGLMRQALSQAVHYARHRQA 324
Cdd:cd01161 219 TNGPPEKKMGIKGSNTAEVYFEDVKipvENVLGEVGDGFKvamNILNNG---RFGMGAALIGTMKRCIEKAVDYANNRKQ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 325 FGAALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQHDEAQSL---LRRLLTPAGKFRICKrgaelaaEAMEVLGGN 401
Cdd:cd01161 296 FGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIeaaISKVFASEAAWLVVD-------EAIQIHGGM 368
|
250 260 270
....*....|....*....|....*....|....
gi 1026941777 402 GYVEEDMQARIYREMPVNSIWEGSGnvmclDVLR 435
Cdd:cd01161 369 GFMREYGVERVLRDLRIFRIFEGTN-----EILR 397
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
154-422 |
4.99e-15 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 77.29 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 154 WLPTLMRPEYdprdlppaqkrgglIG-MGMTEKQGGSDLRSNTTRAEPDGAGGYRLTGHK-WFFSAPQCDAHLVLAQTAG 231
Cdd:PTZ00461 142 WLPKVLTGEH--------------VGaMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKiWITNGTVADVFLIYAKVDG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 232 GLSCFFVPRWAPDGSKNPVLiqrlkDKLGNRSNASSEVEFQGA---WGHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLM 308
Cdd:PTZ00461 208 KITAFVVERGTKGFTQGPKI-----DKCGMRASHMCQLFFEDVvvpAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 309 RQALSQAVHYARHRQAFGAALIDQPLMRNVLADMALEVEaaialaLRLAQAFDSQHDEAQSLLRRLLTPAGKFRICKRGA 388
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTE------AAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAK 356
|
250 260 270
....*....|....*....|....*....|....
gi 1026941777 389 ELAAEAMEVLGGNGYVeedmqariyREMPVNSIW 422
Cdd:PTZ00461 357 KVADSAIQVMGGMGYS---------RDMPVERLW 381
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
180-429 |
1.13e-13 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 72.84 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 180 MGMTEKQGGSDLRSNTTRAEPDGAGGYrLTGHKWFFS-APQCDAHLVLAQ------TAGGLSCFFVPRWAPDGSKNPVli 252
Cdd:PRK12341 122 LALTEPGAGSDNNSATTTYTRKNGKVY-LNGQKTFITgAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKPGIKINPL-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 253 qrlkDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAAL 329
Cdd:PRK12341 199 ----HKIGWHMLSTCEVYLDNVEveeSDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 330 IDQPLMRNVLADMALEVEAAIALALRLAQafdsQHDEAQSLlrRLLTPAGKFRICKRGAELAAEAMEVLGGNGYVEEDMQ 409
Cdd:PRK12341 275 GHNQLIQEKLTLMAIKIENMRNMVYKVAW----QADNGQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARV 348
|
250 260
....*....|....*....|
gi 1026941777 410 ARIYREMPVNSIWEGSGNVM 429
Cdd:PRK12341 349 SRFWRDVRCERIGGGTDEIM 368
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
182-437 |
7.58e-12 |
|
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: 67.23 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 182 MTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WFFSAPQCDAHLVLAQTAGGLSC--------FFVPRWAPDgsknpVLI 252
Cdd:cd01157 120 VTEPGAGSDVAGIKTKAEKKG-DEYIINGQKmWITNGGKANWYFLLARSDPDPKCpaskaftgFIVEADTPG-----IQP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 253 QRLKDKLGNRSNASSEVEFQGAW---GHLLGEEGRGVPtiLEMGTY--TRLDCVLGTTGLMRQALSQAVHYARHRQAFGA 327
Cdd:cd01157 194 GRKELNMGQRCSDTRGITFEDVRvpkENVLIGEGAGFK--IAMGAFdkTRPPVAAGAVGLAQRALDEATKYALERKTFGK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 328 ALIDQPLMRNVLADMALEVEAAIALALRLAQAFDSQhdeaqsllRRLLTPAGkfrICKRGA-----ELAAEAMEVLGGNG 402
Cdd:cd01157 272 LIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--------RRNTYYAS---IAKAFAadianQLATDAVQIFGGNG 340
|
250 260 270
....*....|....*....|....*....|....*
gi 1026941777 403 YVEEDMQARIYREMPVNSIWEGSGNVMCLDVLRAL 437
Cdd:cd01157 341 FNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREH 375
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
182-442 |
2.25e-10 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 62.54 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 182 MTEKQGGSDLRS-NTTRAEPDGAggYRLTGHKWFFSAPQCDAHLV-LAQTAGGLSCFFVPRWAPDGSKNPVLIQRLkDKL 259
Cdd:PRK03354 124 ITEPGAGSDVGSlKTTYTRRNGK--VYLNGSKCFITSSAYTPYIVvMARDGASPDKPVYTEWFVDMSKPGIKVTKL-EKL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 260 GNRSNASSEVEFQGAW---GHLLGEEGRGVPTILEMGTYTRLDCVLGTTGLMRQALSQAVHYARHRQAFGAALIDQPLMR 336
Cdd:PRK03354 201 GLRMDSCCEITFDDVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 337 NVLADMALEVEAAIALALRLAQAFDsqhdeaQSLLRRLLTPAGKFRICKRGAELAAEAMEVLGGNGYVEEDMQARIYREM 416
Cdd:PRK03354 281 EKFAHMAIKLNSMKNMLYEAAWKAD------NGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDL 354
|
250 260
....*....|....*....|....*.
gi 1026941777 417 PVNSIWEGSGNVMCLDVLRALGKNPR 442
Cdd:PRK03354 355 RVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
61-347 |
4.29e-08 |
|
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: 55.43 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 61 LANQNTPVLRAfDARGFRRDQIEFHPAWHALMsdiARRGLHTGPWARPQPGAHVARAAGFILQTQIEAGSMcPTtmtyga 140
Cdd:cd01152 14 LAAHLPPELRE-ESALGYREGREDRRRWQRAL---AAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGA-PV------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 141 ipamsRDALLARDWL-PTLMR---PEYDPRDLPPAqKRGGLI-GMGMTEKQGGSDLRSNTTRAEPDGaGGYRLTGHK-WF 214
Cdd:cd01152 83 -----PFNQIGIDLAgPTILAygtDEQKRRFLPPI-LSGEEIwCQGFSEPGAGSDLAGLRTRAVRDG-DDWVVNGQKiWT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026941777 215 FSAPQCDAHLVLAQTAG------GLSCFFVPRWAPDgsknpVLIQRLKDKLGNRSnaSSEVEFQGAW---GHLLGEEGRG 285
Cdd:cd01152 156 SGAHYADWAWLLVRTDPeapkhrGISILLVDMDSPG-----VTVRPIRSINGGEF--FNEVFLDDVRvpdANRVGEVNDG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026941777 286 VPTILEMGTYTRLdCVLGTTGLMRQALSQAVHYARHRqafGAALIDQPLMRNVLADMALEVE 347
Cdd:cd01152 229 WKVAMTTLNFERV-SIGGSAATFFELLLARLLLLTRD---GRPLIDDPLVRQRLARLEAEAE 286
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
176-229 |
7.56e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 39.09 E-value: 7.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1026941777 176 GLIGMG-MTEKQGGSDLRSNTTRAEPDGAGGYRLTGHKWFFSAPQCDAHLVLAQT 229
Cdd:PTZ00457 132 GTIMMGwATEEGCGSDISMNTTKASLTDDGSYVLTGQKRCEFAASATHFLVLAKT 186
|
|
| |
