|
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: 1154.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 1 MHWQTHTVFNQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLD 80
Cdd:PRK11561 1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 81 DVRFHPAWHLLMQGLCANRVHNLAWEDEARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPL 160
Cdd:PRK11561 81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 241 PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPGIYDMLSEAFAEVKGQDRHYDRMVRQLQQHLRKPIEE 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284 481 LGREITQQLFLLGCGAQMLRYASPPVAQAWCQMMLDTRGGRRLSEQVQNDLLLRATGG 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: 583.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 21 YLSDGALCEAVIREGAGWDSDVLASIGQQLGtAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWHLLMQGLCANRV 100
Cdd:cd01154 1 YLDDPVLQQTLRYFGDPEEEPDLSRLGELAG-GELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 101 HNLAWEDEARQGTFVARAARFMLHAQvEAGTLCPVTMTFAATPLLLQMLPSQFHDWFTPLLSDRYdshllpggqKRGLLI 180
Cdd:cd01154 80 INIEDGPAGEGRRHVHFAAGYLLSDA-AAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRY---------KTGLLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 181 GMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKG------GLSCFFVPRFLPDGQRNAIRL 254
Cdd:cd01154 150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGapagarGLSLFLVPRLLEDGTRNGYRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 255 ERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQ 334
Cdd:cd01154 230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 335 PMMRQVLSRMALQLEGQTALLFRLARAWDRRADAK--EALWARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELP 412
Cdd:cd01154 310 PLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpvEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
|
410 420
....*....|....*....|....*....
gi 740851284 413 RLYREMPVNSIWEGSGNIMCLDVLRVLAK 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 |
9.34e-66 |
|
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: 210.18 E-value: 9.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 10 NQPVPLNNSNLYLSDGALCEAVIREGAGWDSDVLASIGQQLGTAESLELGRLANAFPPELLRYDPQGQRLDDVRFHPAWH 89
Cdd:pfam18158 1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740851284 90 LLMQGLCANRVHNLAWEDeARQGTFVARAARFMLHAQVEAGTLCPVTMTFAATPlLLQMLPSQFHDWFTPLLSDRYDS 167
Cdd:pfam18158 81 ALMALAIEAGLHASPWTD-ARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVP-ALRAEPALAEEWLPKLLSRDYDP 156
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
61-444 |
3.82e-64 |
|
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: 213.93 E-value: 3.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 61 LANAFPPELLRYDPQGqrlddvRFHPAWhllMQGLCANRVHNLAWEDEA--RQGTFVARAARFMLHAQVEAGTLCPVTMT 138
Cdd:COG1960 20 AEEEIAPEAREWDREG------EFPREL---WRKLAELGLLGLTIPEEYggLGLSLVELALVLEELARADASLALPVGVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 139 FAATPLLLQML-PSQFHDWFTPLLSdrydshllpgGQKRGlliGMGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFF 217
Cdd:COG1960 91 NGAAEALLRFGtEEQKERYLPRLAS----------GEWIG---AFALTEPGAGSDAAALRTTAVR-DGDGYVLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 218 S-VPQSDAHLVLAQ---AKG--GLSCFFVPRFLPDgqrnaIRLERLKDKLGNRSNASCEVEFHD---AIGWLLGEEGEGI 288
Cdd:COG1960 157 TnAPVADVILVLARtdpAAGhrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDvrvPAENLLGEEGKGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 289 RHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADa 368
Cdd:COG1960 232 KIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGED- 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740851284 369 kealwARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:COG1960 311 -----AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
97-437 |
2.97e-55 |
|
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: 188.65 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 97 ANRVHNLAWEDEARQGTFVARAARfmlhaqvEAGTLcpvtmtFAATPLLLQMLPSQFHDWFTPLLSDrydshllpggqkr 176
Cdd:cd00567 14 AAEELEPYARERRETPEEPWELLA-------ELGLL------LGAALLLAYGTEEQKERYLPPLASG------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 177 GLLIGMGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFLPdgqr 249
Cdd:cd00567 68 EAIAAFALTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIFISnGGDADLFIVLARtdeegpGHRGISAFLVPADTP---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 250 nAIRLERLKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQV 326
Cdd:cd00567 143 -GVTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 327 FGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAkealwARLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYC 406
Cdd:cd00567 222 FGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDE-----ARLEAAMAKLFATEAAREVADLAMQIHGGRGYS 296
|
330 340 350
....*....|....*....|....*....|.
gi 740851284 407 EESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd00567 297 REYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
182-437 |
1.06e-43 |
|
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: 159.86 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSDA-----HLVLAQAKG------GLSCFFVPRFLPDGQRN 250
Cdd:cd01153 121 MCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMsenivHLVLARSEGappgvkGLSLFLVPKFLDDGERN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 251 AIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKP 330
Cdd:cd01153 201 GVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 331 LIEQP---------MMRQVLSRMALqLEGQTALLFRLARAWD---RRADAKEA-----LWARLFTPAAKYSVCKSGMPFV 393
Cdd:cd01153 281 IKAAPavtiihhpdVRRSLMTQKAY-AEGSRALDLYTATVQDlaeRKATEGEDrkalsALADLLTPVVKGFGSEAALEAV 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 740851284 394 AEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd01153 360 SDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIG 403
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
129-430 |
1.74e-30 |
|
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: 122.38 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 129 AGTLCPVTMTFAATPLLLQMLPSQFHDWFTPLLSdrydshllpgGQKRGlliGMGMTEKQGGSDVLSNTTQAERLADgSY 208
Cdd:cd01158 77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLAT----------GEKIG---AFALSEPGAGSDAAALKTTAKKDGD-DY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 209 RLVGHK-WFFSVPQSDAHLVLAQAKG-----GLSCFFVPRFLPdgqrnAIRLERLKDKLGNRSNASCEVEFHDAI---GW 279
Cdd:cd01158 143 VLNGSKmWITNGGEADFYIVFAVTDPskgyrGITAFIVERDTP-----GLSVGKKEDKLGIRGSSTTELIFEDVRvpkEN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 280 LLGEEGEGIRHILKMGGMTRFD---CALGshsMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLF 356
Cdd:cd01158 218 ILGEEGEGFKIAMQTLDGGRIGiaaQALG---IAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740851284 357 RLARAWDRRAD-AKEALWARLFTPAAKYSVCKsgmpfvaEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01158 295 KAARLKDNGEPfIKEAAMAKLFASEVAMRVTT-------DAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEI 362
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
285-439 |
1.29e-28 |
|
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: 110.81 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 285 GEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDR 364
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740851284 365 RADAKEAlwarlfTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:pfam00441 81 GGPDGAE------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
152-430 |
4.41e-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: 112.89 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 152 QFHDWFTPLLSDRYDSHLLPGGQkrgllIG-MGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKwFFSVPQSDAHLVLAQ 230
Cdd:cd01156 94 QIYRNGSAAQKEKYLPKLISGEH-----IGaLAMSEPNAGSDVVSMKLRAEK-KGDRYVLNGSK-MWITNGPDADTLVVY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 231 AKG-------GLSCFFVPRFLPdGQRNAIRLerlkDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHIlkMGGMT-- 298
Cdd:cd01156 167 AKTdpsagahGITAFIVEKGMP-GFSRAQKL----DKLGMRGSNTCELVFEDCEvpeENILGGENKGVYVL--MSGLDye 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 299 RFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLF 377
Cdd:cd01156 240 RLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRgNMDPKDAAGVILY 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 740851284 378 TPAAKYSVCKsgmpfvaEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01156 320 AAEKATQVAL-------DAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEI 365
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
182-444 |
5.95e-26 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 111.88 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQ------AKGGLSCFFVPRFL--PDG- 247
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDlteniVHIVLARlpnslpTTKGLSLFLVPRHVvkPDGs 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 248 ---QRNaIRLERLKDKLGNRSNASCEVEFHDAIGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQR 324
Cdd:PTZ00456 265 letAKN-VKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 325 ------------QVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWAR-------LFTPAAKYSV 385
Cdd:PTZ00456 344 rsmralsgtkepEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREaldheigFYTPIAKGCL 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740851284 386 CKSGMPFVAEAMEVLGGVGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLAKQPG 444
Cdd:PTZ00456 424 TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIgrKVLSLKGG 484
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
182-431 |
2.47e-25 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 107.89 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:PRK12341 122 LALTEPGAGSDNNSATTTYTR-KNGKVYLNGQKTFITgAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKP-----GIKI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 255 ERLKdKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPL 331
Cdd:PRK12341 196 NPLH-KIGWHMLSTCEVYLDNVEveeSDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 332 IEQPMMRQVLSRMALQLEGQTALLFRLarAWdrRADAKEALwaRLFTPAAKYSVCKSGMPFVAEAMEVLGGVGYCEESEL 411
Cdd:PRK12341 275 GHNQLIQEKLTLMAIKIENMRNMVYKV--AW--QADNGQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARV 348
|
250 260
....*....|....*....|
gi 740851284 412 PRLYREMPVNSIWEGSGNIM 431
Cdd:PRK12341 349 SRFWRDVRCERIGGGTDEIM 368
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
184-444 |
8.99e-25 |
|
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: 106.40 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQ---------AKGGLSCFFVPRFLpDGQRNAI 252
Cdd:cd01161 144 LTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKiWITNGGIADIFTVFAKtevkdatgsVKDKITAFIVERSF-GGVTNGP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 253 RlerlKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIR---HILKMGgmtRFDCALGSHSMMRRAFSVAIYHAHQRQV 326
Cdd:cd01161 223 P----EKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKvamNILNNG---RFGMGAALIGTMKRCIEKAVDYANNRKQ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 327 FGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKYSVCKsgmpfvaEAMEVLGGV 403
Cdd:cd01161 296 FGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEyqiEAAISKVFASEAAWLVVD-------EAIQIHGGM 368
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 740851284 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:cd01161 369 GFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
103-431 |
1.92e-20 |
|
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: 92.95 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 103 LAWEDEARQGTFvarAARFMLHAQVEAGTLcpvtmTFAATPLLLQmlpsqfhdwftpllsdrydsHLLPG---GQKRGLL 179
Cdd:cd01160 65 VLWEELARAGGS---GPGLSLHTDIVSPYI-----TRAGSPEQKE--------------------RVLPQmvaGKKIGAI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 180 igmGMTEKQGGSDVLSNTTQAERlaDGS-YRLVGHKWFFSVP-QSDAHLVLAQ------AKGGLSCFFVPRFLPDGQRNa 251
Cdd:cd01160 117 ---AMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGmLADVVIVVARtggearGAGGISLFLVERGTPGFSRG- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 252 irleRLKDKLGNRSNASCEVEFHDA---IGWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFG 328
Cdd:cd01160 191 ----RKLKKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 329 KPLIEQPMMRQVLSRMALQLEGQTALLFRLA-RAWDRRADAKEAlwarlftPAAKYsVCKSGMPFVA-EAMEVLGGVGYC 406
Cdd:cd01160 267 KTLAQLQVVRHKIAELATKVAVTRAFLDNCAwRHEQGRLDVAEA-------SMAKY-WATELQNRVAyECVQLHGGWGYM 338
|
330 340
....*....|....*....|....*
gi 740851284 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 ... |
181-274 |
4.65e-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: 85.02 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 181 GMGMTEKQGGSDVLSNTTQAERLADGSYRLVGHKWFFS-VPQSDAHLVLAQ-----AKGGLSCFFVPRFLPdgqrnAIRL 254
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIADLFLVLARtggddRHGGISLFLVPKDAP-----GVSV 75
|
90 100
....*....|....*....|
gi 740851284 255 ERLKDKLGNRSNASCEVEFH 274
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVFD 95
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
182-442 |
1.97e-19 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 90.32 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLaDGSYRLVGHK-WFFSVPQSDAHLVLAQ---AKG--GLSCFFVPRFLPdGQRNAIRLe 255
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAERV-DGGYVLNGNKmWCTNGPVAQTLVVYAKtdvAAGskGITAFIIEKGMP-GFSTAQKL- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 256 rlkDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLI 332
Cdd:PLN02519 223 ---DKLGMRGSDTCELVFENCFvpeENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 333 EQPMMRQVLSRMALQLEGQTALLFRLARAWDR-RADAKEALWARLFTPAAKYSVcksgmpfVAEAMEVLGGVGYCEESEL 411
Cdd:PLN02519 300 EFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgKVDRKDCAGVILCAAERATQV-------ALQAIQCLGGNGYINEYPT 372
|
250 260 270
....*....|....*....|....*....|.
gi 740851284 412 PRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PLN02519 373 GRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
184-442 |
9.69e-19 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 87.96 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERlADGSYRLVGHKWFFSVPQSDAHLVL------AQAKGGLSCFFVPRFLPdgqrnAIRLERL 257
Cdd:PRK03354 124 ITEPGAGSDVGSLKTTYTR-RNGKVYLNGSKCFITSSAYTPYIVVmardgaSPDKPVYTEWFVDMSKP-----GIKVTKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 258 kDKLGNRSNASCEVEFhDAIGW----LLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIE 333
Cdd:PRK03354 198 -EKLGLRMDSCCEITF-DDVELdekdMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 334 QPMMRQVLSRMALQLEGQTALLFRLARAWDR----RADAKealwarlftpAAKYSVCKSGMPFVAEAMEVLGGVGYCEES 409
Cdd:PRK03354 276 FQLIQEKFAHMAIKLNSMKNMLYEAAWKADNgtitSGDAA----------MCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
250 260 270
....*....|....*....|....*....|...
gi 740851284 410 ELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PRK03354 346 RISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
182-430 |
1.21e-18 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 88.07 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 182 MGMTEKQGGSDVLSNTTQAERLADGSYRLVGHK-WFFSVPQSDAHLVLAQAKGGLSCFFVPRFLPdGQRNAIRLerlkDK 260
Cdd:PTZ00461 155 MGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKiWITNGTVADVFLIYAKVDGKITAFVVERGTK-GFTQGPKI----DK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 261 LGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKPLIEQPMM 337
Cdd:PTZ00461 230 CGMRASHMCQLFFEDVVvpaENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 338 RQVLSRMALQLEGQTALLFRLARawDRRADAKEALW---ARLF-TPAAKYsvcksgmpfVAE-AMEVLGGVGYCEESELP 412
Cdd:PTZ00461 310 QRYIAEGYADTEAAKALVYSVSH--NVHPGNKNRLGsdaAKLFaTPIAKK---------VADsAIQVMGGMGYSRDMPVE 378
|
250
....*....|....*...
gi 740851284 413 RLYREMPVNSIweGSGNI 430
Cdd:PTZ00461 379 RLWRDAKLLEI--GGGTI 394
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
184-439 |
3.92e-13 |
|
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: 71.08 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 184 MTEKQGGSDVLSNTTQAERLADgSYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPDGQRNair 253
Cdd:cd01157 120 VTEPGAGSDVAGIKTKAEKKGD-EYIINGQKmwitnggkanWYFLLARSDPD-PKCPASKAFTGFIVEADTPGIQPG--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 254 leRLKDKLGNRSNASCEVEFHDAI---GWLLGEEGEGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYHAHQRQVFGKP 330
Cdd:cd01157 195 --RKELNMGQRCSDTRGITFEDVRvpkENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 331 LIEQPMMRQVLSRMALQLEgqTALLFRLARAWDRRADAKEALWARLftpaAKYSVCKSGMPFVAEAMEVLGGVGYCEESE 410
Cdd:cd01157 273 IAEHQAVSFMLADMAMKVE--LARLAYQRAAWEVDSGRRNTYYASI----AKAFAADIANQLATDAVQIFGGNGFNSEYP 346
|
250 260
....*....|....*....|....*....
gi 740851284 411 LPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:cd01157 347 VEKLMRDAKIYQIYEGTSQIQRLIISREH 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
170-433 |
3.81e-08 |
|
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: 55.44 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 170 LPGgQKRGLLIG-MGMTEKQGGSDVLSNTTQAERLADGsYRLVGHK-WFFSVPQSDAHLVLA--QAKGGLSCFFVPRFLP 245
Cdd:cd01151 118 LPK-LASGELIGcFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKtWITNSPIADVFVVWArnDETGKIRGFILERGMK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 246 dgqrnAIRLERLKDKLGNRSNASCEVEFHDAigwLLGEEG-----EGIRHILKMGGMTRFDCALGSHSMMRRAFSVAIYH 320
Cdd:cd01151 196 -----GLSAPKIQGKFSLRASITGEIVMDNV---FVPEENllpgaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQY 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 321 AHQRQVFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEAlwarlfTPAAKYSVCKSGMPFVAEAMEVL 400
Cdd:cd01151 268 VLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ------ISLLKRNNCGKALEIARTAREML 341
|
250 260 270
....*....|....*....|....*....|...
gi 740851284 401 GGVGYCEESELPRLYREMPVNSIWEGSGNIMCL 433
Cdd:cd01151 342 GGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
303-417 |
1.12e-05 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 45.03 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 303 ALGshsMMRRAFSVAIYHAHQRQ--VFGKPLIEQPMMRQVLSRMALQLEGQTALLFRLA-RAWDRRADAKE---ALWARL 376
Cdd:pfam08028 6 ALG---AARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAaRIEAAAAAGKPvtpALRAEA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 740851284 377 fTPAAKYSV--CKSGmpfVAEAMEVLGGVGYCEESELPRLYRE 417
Cdd:pfam08028 83 -RRAAAFATelAVAA---VDALFRAAGGSALFQDSPLQRIWRD 121
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
174-401 |
1.44e-04 |
|
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: 44.26 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 174 QKRGLLIGM---------GMTEKQGGSDVLSNTTQAERLADGsYRLVGHKWFFSVPQ-SDAHLVLAQAKG------GLSC 237
Cdd:cd01152 104 QKRRFLPPIlsgeeiwcqGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAHyADWAWLLVRTDPeapkhrGISI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 238 FFVPRFLPDGQRNAIRlerlkdkLGNRSNASCEVEFHD---AIGWLLGEEGEGIRHILKMGGMTRFdcALGSHSMMRRAF 314
Cdd:cd01152 183 LLVDMDSPGVTVRPIR-------SINGGEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERV--SIGGSAATFFEL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740851284 315 SVAIYHAHQRQvfGKPLIEQPMMRQVLSRMALQLEGQTALLFRLARAWD--RRADAKEAL----WARLFTPAAKYsvcks 388
Cdd:cd01152 254 LLARLLLLTRD--GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAagKPPGAEASIaklfGSELAQELAEL----- 326
|
250
....*....|...
gi 740851284 389 gmpfvaeAMEVLG 401
Cdd:cd01152 327 -------ALELLG 332
|
|
|