|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
1-538 |
0e+00 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 1137.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 1 MHWQTHTVFNQPIPLNNSNLYLSDGALCEAVTREGAGWDSDFLASIGQQLGTAESLELGRLANVNPPELLRYDAQGRRLD 80
Cdd:PRK11561 1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 81 DVRFHPAWHLLMQALCTNRVHNLAWEEDARSGAFVARAARFMLHAQVEAGSLCPITMTFAATPLLLQMLPTPFQDWTTPL 160
Cdd:PRK11561 81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 161 LSDRYDSHLLPGGQKRGLLIGMGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDAHLVLAQTTGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 241 PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFQDAIGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 321 AHQRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGMPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQAGVYDLLSEAFVEVKGQDRYFDRAVRRLQQQLRKPAEE 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721348 481 LGREITHQLFLLGCGAQMLKYASPPMAQAWCQVMLDTRGGVRLSEQIQNDLLLRATGG 538
Cdd:PRK11561 481 QGREITQQLFLLGCGAQMLRHASPPLAQAWCQMMLDTRGGVRLSEQVQNDLLLRATGG 538
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
21-441 |
0e+00 |
|
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: 619.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 21 YLSDGALCEAVTREGAGWDSDFLASIGQQLGtAESLELGRLANVNPPELLRYDAQGRRLDDVRFHPAWHLLMQALCTNRV 100
Cdd:cd01154 1 YLDDPVLQQTLRYFGDPEEEPDLSRLGELAG-GELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 101 HNLAWEEDARSGAFVARAARFMLHAQvEAGSLCPITMTFAATPLLLQMLPTPFQDWTTPLLSDRYdshllpggqKRGLLI 180
Cdd:cd01154 80 INIEDGPAGEGRRHVHFAAGYLLSDA-AAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRY---------KTGLLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 181 GMGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDAHLVLAQT------TGGLSCFFVPRFLPDGQRNAIRL 254
Cdd:cd01154 150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPegapagARGLSLFLVPRLLEDGTRNGYRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 255 ERLKDKLGNRSNASCEVEFQDAIGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQ 334
Cdd:cd01154 230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 335 PLMCHVLSRMALQLEGQTALLFRLARAWDRRADAK--EALWARLFTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESELP 412
Cdd:cd01154 310 PLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpvEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
|
410 420
....*....|....*....|....*....
gi 1476721348 413 RLYREMPVNSIWEGSGNIMCLDVLRVLNK 441
Cdd:cd01154 390 RLHREAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| AidB_N |
pfam18158 |
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive ... |
10-167 |
3.44e-68 |
|
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: 216.72 E-value: 3.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 10 NQPIPLNNSNLYLSDGALCEAVTREGAGWDSDFLASIGQQLGTAESLELGRLANVNPPELLRYDAQGRRLDDVRFHPAWH 89
Cdd:pfam18158 1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721348 90 LLMQALCTNRVHNLAWeEDARSGAFVARAARFMLHAQVEAGSLCPITMTFAATPlLLQMLPTPFQDWTTPLLSDRYDS 167
Cdd:pfam18158 81 ALMALAIEAGLHASPW-TDARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVP-ALRAEPALAEEWLPKLLSRDYDP 156
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
61-444 |
3.63e-61 |
|
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: 206.23 E-value: 3.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 61 LANVNPPELLRYDAQGRrlddvrFHPAWhllMQALCTNRVHNLAW-EEDARSGA-FVARAARFMLHAQVEAGSLCPITMT 138
Cdd:COG1960 20 AEEEIAPEAREWDREGE------FPREL---WRKLAELGLLGLTIpEEYGGLGLsLVELALVLEELARADASLALPVGVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 139 FAATPLLLQmLPTPFQ--DWTTPLLSdrydshllpgGQKRGlliGMGMAEKQGGSDVMSNTTRAERlEDGSYRLVGHKWF 216
Cdd:COG1960 91 NGAAEALLR-FGTEEQkeRYLPRLAS----------GEWIG---AFALTEPGAGSDAAALRTTAVR-DGDGYVLNGQKTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 217 FS-VPQSDAHLVLAQTTG-----GLSCFFVPRFLPDgqrnaIRLERLKDKLGNRSNASCEVEFQD---AIGWLLGQEGEG 287
Cdd:COG1960 156 ITnAPVADVILVLARTDPaaghrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDvrvPAENLLGEEGKG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 288 IRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDRRAD 367
Cdd:COG1960 231 FKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476721348 368 akealwARLFTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQAG 444
Cdd:COG1960 311 ------AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
93-437 |
4.29e-51 |
|
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: 177.86 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 93 QALCTNRVHNLAWEEDARSGAFVARAARFMLHAQVEAGSLcpitmtFAATPLLLQMLPTPFQDWTTPLLSDrydshllpg 172
Cdd:cd00567 3 QRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLL------LGAALLLAYGTEEQKERYLPPLASG--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 173 gqkrGLLIGMGMAEKQGGSDVMSNTTRAERlEDGSYRLVGHKWFFS-VPQSDAHLVLAQT------TGGLSCFFVPRFLP 245
Cdd:cd00567 68 ----EAIAAFALTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIFISnGGDADLFIVLARTdeegpgHRGISAFLVPADTP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 246 dgqrnAIRLERLKDKLGNRSNASCEVEFQDA---IGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAH 322
Cdd:cd00567 143 -----GVTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 323 QRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWD--RRADAKEALWARLFTP-AAKFVickrgmpfVAEAMEV 399
Cdd:cd00567 218 QRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDqgPDEARLEAAMAKLFATeAAREV--------ADLAMQI 289
|
330 340 350
....*....|....*....|....*....|....*...
gi 1476721348 400 LGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd00567 290 HGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
182-437 |
6.65e-41 |
|
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: 152.54 E-value: 6.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 182 MGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDA-----HLVLAQTTG------GLSCFFVPRFLPDGQRN 250
Cdd:cd01153 121 MCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMsenivHLVLARSEGappgvkGLSLFLVPKFLDDGERN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 251 AIRLERLKDKLGNRSNASCEVEFQDAIGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNP 330
Cdd:cd01153 201 GVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 331 LIQQP---LMCHVLSRMALQ-----LEGQTALLFRLARAWD---RRADAKEA-----LWARLFTPAAKFVICKRGMPFVA 394
Cdd:cd01153 281 IKAAPavtIIHHPDVRRSLMtqkayAEGSRALDLYTATVQDlaeRKATEGEDrkalsALADLLTPVVKGFGSEAALEAVS 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1476721348 395 EAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd01153 361 DAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIG 403
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
285-439 |
7.80e-29 |
|
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: 111.58 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 285 GEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDR 364
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476721348 365 RADAKEAlwarlfTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:pfam00441 81 GGPDGAE------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
176-430 |
6.75e-28 |
|
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: 115.06 E-value: 6.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 176 RGLLIG-MGMAEKQGGSDVMSNTTRAERlEDGSYRLVGHK-WFFSVPQSDAHLVLAQTTG-----GLSCFFVPRFLPdgq 248
Cdd:cd01158 110 TGEKIGaFALSEPGAGSDAAALKTTAKK-DGDDYVLNGSKmWITNGGEADFYIVFAVTDPskgyrGITAFIVERDTP--- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 249 rnAIRLERLKDKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFD---CALGshaMMRRAFSLAIYHAH 322
Cdd:cd01158 186 --GLSVGKKEDKLGIRGSSTTELIFEDVRvpkENILGEEGEGFKIAMQTLDGGRIGiaaQALG---IAQAALDAAVDYAK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 323 QRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDRRAD-AKEALWARLF-TPAAkfvickrgMPFVAEAMEVL 400
Cdd:cd01158 261 ERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfIKEAAMAKLFaSEVA--------MRVTTDAVQIF 332
|
250 260 270
....*....|....*....|....*....|
gi 1476721348 401 GGIGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01158 333 GGYGYTKDYPVERYYRDAKITEIYEGTSEI 362
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
181-441 |
2.60e-27 |
|
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: 113.27 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 181 GMGMAEKQGGSDVMSNTTRAERlEDGSYRLVGHK-WFFSVPQSDAHLVLAQTTG-----GLSCFFVPRFLPdGQRNAIRL 254
Cdd:cd01156 119 ALAMSEPNAGSDVVSMKLRAEK-KGDRYVLNGSKmWITNGPDADTLVVYAKTDPsagahGITAFIVEKGMP-GFSRAQKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 255 erlkDKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLIlkMGGMT--RFDCALGSHAMMRRAFSLAIYHAHQRHVFGN 329
Cdd:cd01156 197 ----DKLGMRGSNTCELVFEDCEvpeENILGGENKGVYVL--MSGLDyeRLVLAGGPIGIMQAALDVAIPYAHQRKQFGQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 330 PLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKFVICKrgmpfvaEAMEVLGGIGYCEE 408
Cdd:cd01156 271 PIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRgNMDPKDAAGVILYAAEKATQVAL-------DAIQILGGNGYIND 343
|
250 260 270
....*....|....*....|....*....|...
gi 1476721348 409 SELPRLYREMPVNSIWEGSGNIMCLDVLRVLNK 441
Cdd:cd01156 344 YPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
182-444 |
3.99e-23 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 103.41 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 182 MGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSD-----AHLVLAQ------TTGGLSCFFVPRFL--PDG- 247
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDlteniVHIVLARlpnslpTTKGLSLFLVPRHVvkPDGs 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 248 ---QRNaIRLERLKDKLGNRSNASCEVEFQDAIGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAH-- 322
Cdd:PTZ00456 265 letAKN-VKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARer 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 323 --QRHVFGNPLIQQP---LMCHVLSRMALQL-----EGQTALLFRLARAWDRRADAKEALWAR-------LFTPAAKFVI 385
Cdd:PTZ00456 344 rsMRALSGTKEPEKPadrIICHANVRQNILFakavaEGGRALLLDVGRLLDIHAAAKDAATREaldheigFYTPIAKGCL 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1476721348 386 CKRGMPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLNKQAG 444
Cdd:PTZ00456 424 TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIgrKVLSLKGG 484
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
184-444 |
4.37e-23 |
|
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: 101.39 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 184 MAEKQGGSDVMSNTTRAERLEDGS-YRLVGHK-WFFSVPQSDAHLVLAQT-----TG----GLSCFFVPRFLpDGQRNAI 252
Cdd:cd01161 144 LTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKiWITNGGIADIFTVFAKTevkdaTGsvkdKITAFIVERSF-GGVTNGP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 253 RlerlKDKLGNRSNASCEVEFQDA---IGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGN 329
Cdd:cd01161 223 P----EKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 330 PLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKFVICKrgmpfvaEAMEVLGGIGYC 406
Cdd:cd01161 299 KIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEyqiEAAISKVFASEAAWLVVD-------EAIQIHGGMGFM 371
|
250 260 270
....*....|....*....|....*....|....*...
gi 1476721348 407 EESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQAG 444
Cdd:cd01161 372 REYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
182-431 |
2.27e-22 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 99.03 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 182 MGMAEKQGGSDVMSNTTRAERlEDGSYRLVGHKWFFS-VPQSDAHLVLAQ------TTGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:PRK12341 122 LALTEPGAGSDNNSATTTYTR-KNGKVYLNGQKTFITgAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKP-----GIKI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 255 ERLKdKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPL 331
Cdd:PRK12341 196 NPLH-KIGWHMLSTCEVYLDNVEveeSDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 332 IQQPLMCHVLSRMALQLEGQTALLFRLAraWdrRADAKEALwaRLFTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESEL 411
Cdd:PRK12341 275 GHNQLIQEKLTLMAIKIENMRNMVYKVA--W--QADNGQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARV 348
|
250 260
....*....|....*....|
gi 1476721348 412 PRLYREMPVNSIWEGSGNIM 431
Cdd:PRK12341 349 SRFWRDVRCERIGGGTDEIM 368
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
103-431 |
2.66e-21 |
|
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: 95.64 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 103 LAWEEDARSGAFvarAARFMLHAQVEAGSLcpitmTFAATPLLLQmlptpfqdwttpllsdrydsHLLPG---GQKRGLL 179
Cdd:cd01160 65 VLWEELARAGGS---GPGLSLHTDIVSPYI-----TRAGSPEQKE--------------------RVLPQmvaGKKIGAI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 180 igmGMAEKQGGSDVMSNTTRAERleDGS-YRLVGHKWFFSVP-QSDAHLVLAQTT------GGLSCFFVPRFLPDGQRNa 251
Cdd:cd01160 117 ---AMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGmLADVVIVVARTGgeargaGGISLFLVERGTPGFSRG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 252 irleRLKDKLGNRSNASCEVEFQDA---IGWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFG 328
Cdd:cd01160 191 ----RKLKKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 329 NPLIQQPLMCHVLSRMALQLEGQTALLFRLA-RAWDRRADAKEALWARLFtpaakfviCKRGMPFVA-EAMEVLGGIGYC 406
Cdd:cd01160 267 KTLAQLQVVRHKIAELATKVAVTRAFLDNCAwRHEQGRLDVAEASMAKYW--------ATELQNRVAyECVQLHGGWGYM 338
|
330 340
....*....|....*....|....*
gi 1476721348 407 EESELPRLYREMPVNSIWEGSGNIM 431
Cdd:cd01160 339 REYPIARAYRDARVQPIYGGTTEIM 363
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
181-273 |
1.32e-20 |
|
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: 86.57 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 181 GMGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFS-VPQSDAHLVLAQT-----TGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIADLFLVLARTggddrHGGISLFLVPKDAP-----GVSV 75
|
90
....*....|....*....
gi 1476721348 255 ERLKDKLGNRSNASCEVEF 273
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVF 94
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
182-442 |
7.22e-20 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 91.86 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 182 MGMAEKQGGSDVMSNTTRAERLeDGSYRLVGHK-WFFSVPQSDAHLVLAQT-----TGGLSCFFVPRFLPdGQRNAIRLe 255
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAERV-DGGYVLNGNKmWCTNGPVAQTLVVYAKTdvaagSKGITAFIIEKGMP-GFSTAQKL- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 256 rlkDKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLI 332
Cdd:PLN02519 223 ---DKLGMRGSDTCELVFENCFvpeENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 333 QQPLMCHVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTpaakfviCKRGMPFVAEAMEVLGGIGYCEESEL 411
Cdd:PLN02519 300 EFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgKVDRKDCAGVILCA-------AERATQVALQAIQCLGGNGYINEYPT 372
|
250 260 270
....*....|....*....|....*....|.
gi 1476721348 412 PRLYREMPVNSIWEGSGNIMCLDVLRVLNKQ 442
Cdd:PLN02519 373 GRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
182-430 |
1.41e-16 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 81.91 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 182 MGMAEKQGGSDVMSNTTRAERLEDGSYRLVGHK-WFFSVPQSDAHLVLAQTTGGLSCFFVPRFLPdGQRNAIRLerlkDK 260
Cdd:PTZ00461 155 MGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKiWITNGTVADVFLIYAKVDGKITAFVVERGTK-GFTQGPKI----DK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 261 LGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQPLM 337
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVvpaENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 338 CHVLSRMALQLEGQTALLFRLARawDRRADAKEALW---ARLF-TPAAKFVickrgmpfVAEAMEVLGGIGYCEESELPR 413
Cdd:PTZ00461 310 QRYIAEGYADTEAAKALVYSVSH--NVHPGNKNRLGsdaAKLFaTPIAKKV--------ADSAIQVMGGMGYSRDMPVER 379
|
250
....*....|....*..
gi 1476721348 414 LYREMPVNSIweGSGNI 430
Cdd:PTZ00461 380 LWRDAKLLEI--GGGTI 394
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
184-442 |
4.80e-16 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 79.88 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 184 MAEKQGGSDVMSNTTRAERlEDGSYRLVGHKWFFSVPQSDAHLVL------AQTTGGLSCFFVPRFLPdgqrnAIRLERL 257
Cdd:PRK03354 124 ITEPGAGSDVGSLKTTYTR-RNGKVYLNGSKCFITSSAYTPYIVVmardgaSPDKPVYTEWFVDMSKP-----GIKVTKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 258 kDKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQ 334
Cdd:PRK03354 198 -EKLGLRMDSCCEITFDDVEldeKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 335 PLMCHVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKFVIckrgmpfVAEAMEVLGGIGYCEESELPR 413
Cdd:PRK03354 277 QLIQEKFAHMAIKLNSMKNMLYEAAWKADNgTITSGDAAMCKYFCANAAFEV-------VDSAMQVLGGVGIAGNHRISR 349
|
250 260
....*....|....*....|....*....
gi 1476721348 414 LYREMPVNSIWEGSGNIMCLDVLRVLNKQ 442
Cdd:PRK03354 350 FWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
186-439 |
1.68e-11 |
|
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: 66.07 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 186 EKQGGSDVMSNTTRAERLEDgSYRLVGHK-WFFSVPQSDAHLVLAQTTGGLSCffvPR------FLPDGQRNAIRLERLK 258
Cdd:cd01157 122 EPGAGSDVAGIKTKAEKKGD-EYIINGQKmWITNGGKANWYFLLARSDPDPKC---PAskaftgFIVEADTPGIQPGRKE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 259 DKLGNRSNASCEVEFQDAI---GWLLGQEGEGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQP 335
Cdd:cd01157 198 LNMGQRCSDTRGITFEDVRvpkENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 336 LMCHVLSRMALQLEgqTALLFRLARAWDRRADAKEALWARLftpaAKFVICKRGMPFVAEAMEVLGGIGYCEESELPRLY 415
Cdd:cd01157 278 AVSFMLADMAMKVE--LARLAYQRAAWEVDSGRRNTYYASI----AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLM 351
|
250 260
....*....|....*....|....
gi 1476721348 416 REMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:cd01157 352 RDAKIYQIYEGTSQIQRLIISREH 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
170-433 |
3.01e-09 |
|
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: 58.91 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 170 LPGgQKRGLLIG-MGMAEKQGGSDVMSNTTRAERLEDGsYRLVGHK-WFFSVPQSDAHLVLA--QTTGGLSCFFVPRFLP 245
Cdd:cd01151 118 LPK-LASGELIGcFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKtWITNSPIADVFVVWArnDETGKIRGFILERGMK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 246 dgqrnAIRLERLKDKLGNRSNASCEVEFQDAigwLLGQEG-----EGIRLILKMGGMTRFDCALGSHAMMRRAFSLAIYH 320
Cdd:cd01151 196 -----GLSAPKIQGKFSLRASITGEIVMDNV---FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQY 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 321 AHQRHVFGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWDRRADAKEAlwarlfTPAAKFVICKRGMPFVAEAMEVL 400
Cdd:cd01151 268 VLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ------ISLLKRNNCGKALEIARTAREML 341
|
250 260 270
....*....|....*....|....*....|...
gi 1476721348 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCL 433
Cdd:cd01151 342 GGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
174-401 |
8.81e-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: 54.28 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 174 QKRGLLIGM---------GMAEKQGGSDVMSNTTRAERlEDGSYRLVGHKWFFSVPQ-SDAHLVLAQTTG------GLSC 237
Cdd:cd01152 104 QKRRFLPPIlsgeeiwcqGFSEPGAGSDLAGLRTRAVR-DGDDWVVNGQKIWTSGAHyADWAWLLVRTDPeapkhrGISI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 238 FFVPRFLPDGQRNAIRlerlkdkLGNRSNASCEVEFQD---AIGWLLGQEGEGIRLILKMGGMTRFdcALGSHAMMRRAF 314
Cdd:cd01152 183 LLVDMDSPGVTVRPIR-------SINGGEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERV--SIGGSAATFFEL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721348 315 SLAIYHAHQRHvfGNPLIQQPLMCHVLSRMALQLEGQTALLFRLARAWD--RRADAKEAL----WARLFTPAAKFvickr 388
Cdd:cd01152 254 LLARLLLLTRD--GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAagKPPGAEASIaklfGSELAQELAEL----- 326
|
250
....*....|...
gi 1476721348 389 gmpfvaeAMEVLG 401
Cdd:cd01152 327 -------ALELLG 332
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
180-231 |
5.37e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 39.48 E-value: 5.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1476721348 180 IGMGMAEKQG-GSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDAHLVLAQT 231
Cdd:PTZ00457 134 IMMGWATEEGcGSDISMNTTKASLTDDGSYVLTGQKRCEFAASATHFLVLAKT 186
|
|
| |
