|
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: 1141.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 1 MHWQTHTVFNQPAPLSNSNLFLSDCALRDAVAREGAEWDVDLLASIGQQLGTAESLELGRLANVNPPELLRYDATGARLD 80
Cdd:PRK11561 1 MHWQTHTVFNQPIPLNNSNLFLSDGALCEAVTREGAGWDSDLLASIGQQLGTAESLELGRLANANPPELLRYDAQGQRLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 81 DVRFHPAWHLLMQGLCANRVHNLAWEEEARKGSFVARAARFVLHAQVEAGTLCPVTMTFAATPLLQRSLPKPFHEWLTPL 160
Cdd:PRK11561 81 DVRFHPAWHLLMQGLCANRVHNLAWEEDARSGAFVARAARFMLHAQVEAGTLCPITMTFAATPLLLQMLPAPFQDWLTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 161 MSDRYDPHLAPGAQKRGLLIGMGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
Cdd:PRK11561 161 LSDRYDSHLLPGGQKRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDAHLVLAQAKGGLSCFFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 241 PRFLPDGQRNAVRLERLKDKLGNRSNASSEAEFLDASGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYH 320
Cdd:PRK11561 241 PRFLPDGQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 321 AHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRNDPQEAAWARLFTPAAKYSVCKAGIPFVAEAMEVL 400
Cdd:PRK11561 321 AHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAAKFVICKRGIPFVAEAMEVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 401 GGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPGILDLLADDFAQVKGQDRHFDRSWRQLQQKLRKPQEA 480
Cdd:PRK11561 401 GGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQPGVYDLLSEAFVEVKGQDRHFDRAVRQLQQRLRKPAEE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 550713936 481 QGREIAQQLFLLGAGSQMLRHASPPVAQAWCRMMLDTRGGTLMSEQVQNDLLLRATGR 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: 564.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 21 FLSDCALRDAVAREGAEWDVDLLASIGQQLGtAESLELGRLANVNPPELLRYDATGARLDDVRFHPAWHLLMQGLCANRV 100
Cdd:cd01154 1 YLDDPVLQQTLRYFGDPEEEPDLSRLGELAG-GELYELARLADRNPPVLEMWDRWGRRVDRVWVHPAWHALMRRLIEEGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 101 HNLAWEEEARKGSFVARAARFVLHAQvEAGTLCPVTMTFAATPLLQRSLPKPFHEWLTPLMSDRYdphlapgaqKRGLLI 180
Cdd:cd01154 80 INIEDGPAGEGRRHVHFAAGYLLSDA-AAGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRY---------KTGLLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 181 GMGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHKWFFSVPQSDAHLVLAQAKG------GLSCFFVPRFLPDGQRNAVRL 254
Cdd:cd01154 150 GTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLADAALVLARPEGapagarGLSLFLVPRLLEDGTRNGYRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 255 ERLKDKLGNRSNASSEAEFLDASGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKNLIDQ 334
Cdd:cd01154 230 RRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 335 PLMRDVLSRMALVLEGHTALLFRLARAWDNR--NDPQEAAWARLFTPAAKYSVCKAGIPFVAEAMEVLGGAGYCEESELP 412
Cdd:cd01154 310 PLMRRDLAEMEVDVEAATALTFRAARAFDRAaaDKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
|
410 420
....*....|....*....|....*....
gi 550713936 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 |
6.63e-69 |
|
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: 218.65 E-value: 6.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 10 NQPAPLSNSNLFLSDCALRDAVAREGAEWDVDLLASIGQQLGTAESLELGRLANVNPPELLRYDATGARLDDVRFHPAWH 89
Cdd:pfam18158 1 NQPPPLEDYNLFASDPALQEAVAREGAAWATEALAALGALAGSAEALELARLANRNPPQLHTHDRFGRRIDEVEFHPAYH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550713936 90 LLMQGLCANRVHNLAWeEEARKGSFVARAARFVLHAQVEAGTLCPVTMTFAATPLLQRSlPKPFHEWLTPLMSDRYDP 167
Cdd:pfam18158 81 ALMALAIEAGLHASPW-TDARPGAHVARAALFYLHAQVEAGHLCPLTMTYAAVPALRAE-PALAEEWLPKLLSRDYDP 156
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
61-444 |
5.31e-60 |
|
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: 203.15 E-value: 5.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 61 LANVNPPELLRYDATGarlddvRFHPAWhllMQGLCANRVHNLAWEEEA--RKGSFVARAARFVLHAQVEAGTLCPVTMT 138
Cdd:COG1960 20 AEEEIAPEAREWDREG------EFPREL---WRKLAELGLLGLTIPEEYggLGLSLVELALVLEELARADASLALPVGVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 139 FAATPLLQRslpkpfheWLTPLMSDRYDPHLAPGAqkrgLLIGMGMTEKQGGSDVLSNTTKAEKcSDGSYRLVGHKWFFS 218
Cdd:COG1960 91 NGAAEALLR--------FGTEEQKERYLPRLASGE----WIGAFALTEPGAGSDAAALRTTAVR-DGDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 219 -VPQSDAHLVLAQ---AKG--GLSCFFVPRFLPDgqrnaVRLERLKDKLGNRSNASSEAEFLD---ASGWLLGEEGEGVR 289
Cdd:COG1960 158 nAPVADVILVLARtdpAAGhrGISLFLVPKDTPG-----VTVGRIEDKMGLRGSDTGELFFDDvrvPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 290 QILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRNDPQ 369
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550713936 370 EAAwarlftPAAKYSVCKAGIPFVAEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:COG1960 313 LEA------AMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
93-437 |
1.03e-52 |
|
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: 182.10 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 93 QGLCANRVHNLAWEEEARKGSFVARAARFVLHAQVEAG-TLCPVTMTFAATPLLQRslpkpfhEWLTPLMSDrydphlap 171
Cdd:cd00567 3 QRELRDSAREFAAEELEPYARERRETPEEPWELLAELGlLLGAALLLAYGTEEQKE-------RYLPPLASG-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 172 gaqkrGLLIGMGMTEKQGGSDVLSNTTKAEKcSDGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFL 244
Cdd:cd00567 68 -----EAIAAFALTEPGAGSDLAGIRTTARK-DGDGYVLNGRKIFISnGGDADLFIVLARtdeegpGHRGISAFLVPADT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 245 PdgqrnAVRLERLKDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHA 321
Cdd:cd00567 142 P-----GVTVGRIWDKMGMRGSGTGELVFDDVrvpEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 322 HQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDnrndpQEAAWARLFTPAAKYSVCKAGIPFVAEAMEVLG 401
Cdd:cd00567 217 KQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLD-----QGPDEARLEAAMAKLFATEAAREVADLAMQIHG 291
|
330 340 350
....*....|....*....|....*....|....*.
gi 550713936 402 GAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd00567 292 GRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
158-437 |
2.66e-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: 159.09 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 158 TPLMSDRYDPHLAPGaqkrGLLIGMGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHKWFFSVPQSDA-----HLVLAQAK 232
Cdd:cd01153 101 TEAQREKWIPRLAEG----EWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMsenivHLVLARSE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 233 G------GLSCFFVPRFLPDGQRNAVRLERLKDKLGNRSNASSEAEFLDASGWLLGEEGEGVRQILKMGGLTRFDCALGS 306
Cdd:cd01153 177 GappgvkGLSLFLVPKFLDDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 307 HGLMRRALSVALYHAHQRQTFGKNLIDQP-----LMRDV----LSRMALVlEGHTALLFRLARAWD-------NRNDPQE 370
Cdd:cd01153 257 TGLAEAAYLNALAYAKERKQGGDLIKAAPavtiiHHPDVrrslMTQKAYA-EGSRALDLYTATVQDlaerkatEGEDRKA 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550713936 371 A-AWARLFTPAAKYSVCKAGIPFVAEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
Cdd:cd01153 336 LsALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALDLIG 403
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
285-439 |
1.17e-30 |
|
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: 116.58 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 285 GEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDN 364
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550713936 365 RNDPQEAAwarlftPAAKYSVCKAGIPFVAEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:pfam00441 81 GGPDGAEA------SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
154-430 |
2.51e-29 |
|
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: 119.05 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 154 HEWLTPLMSDRYDPHLAPGAQkrgllIG-MGMTEKQGGSDVLSNTTKAEKcSDGSYRLVGHKwFFSVPQSDAHLVLAQAK 232
Cdd:cd01156 96 YRNGSAAQKEKYLPKLISGEH-----IGaLAMSEPNAGSDVVSMKLRAEK-KGDRYVLNGSK-MWITNGPDADTLVVYAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 233 G-------GLSCFFVPRFLPdGQRNAVRLerlkDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQIlkMGGLT--RF 300
Cdd:cd01156 169 TdpsagahGITAFIVEKGMP-GFSRAQKL----DKLGMRGSNTCELVFEDCevpEENILGGENKGVYVL--MSGLDyeRL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 301 DCALGSHGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRN-DPQEAAWARLFTP 379
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNmDPKDAAGVILYAA 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 550713936 380 AAKYSVCKagipfvaEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01156 322 EKATQVAL-------DAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEI 365
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
129-430 |
8.68e-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: 114.67 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 129 AGTLCPVTMTFAATPLLQRSLPKPFHEWLTPLMSdrydphlapgaqkrGLLIG-MGMTEKQGGSDVLSNTTKAEKCSDgS 207
Cdd:cd01158 77 VAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLAT--------------GEKIGaFALSEPGAGSDAAALKTTAKKDGD-D 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 208 YRLVGHK-WFFSVPQSDAHLVLAQAKG-----GLSCFFVPRFLPdgqrnAVRLERLKDKLGNRSNASSEAEFLDA---SG 278
Cdd:cd01158 142 YVLNGSKmWITNGGEADFYIVFAVTDPskgyrGITAFIVERDTP-----GLSVGKKEDKLGIRGSSTTELIFEDVrvpKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 279 WLLGEEGEGVR---QILKMGGLTRFDCALGshgLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALL 355
Cdd:cd01158 217 NILGEEGEGFKiamQTLDGGRIGIAAQALG---IAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLT 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550713936 356 FRLARAWDN-RNDPQEAAWARLFTPAAKYSVCKagipfvaEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNI 430
Cdd:cd01158 294 YKAARLKDNgEPFIKEAAMAKLFASEVAMRVTT-------DAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEI 362
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
158-444 |
6.23e-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: 107.17 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 158 TPLMSDRYDPHLAPGAQkrglLIGMGMTEKQGGSDVLSNTTKAEKCSDGS-YRLVGHK-WFFSVPQSDAHLVLAQ----- 230
Cdd:cd01161 122 TEAQKEKYLPKLASGEW----IAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKiWITNGGIADIFTVFAKtevkd 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 231 ----AKGGLSCFFVPRFLpdgqrNAVRLERLKDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQILKMGGLTRFDCA 303
Cdd:cd01161 198 atgsVKDKITAFIVERSF-----GGVTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 304 LGSHGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRNDPQ---EAAWARLFTPA 380
Cdd:cd01161 273 AALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEyqiEAAISKVFASE 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550713936 381 AKYSVCKagipfvaEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQPG 444
Cdd:cd01161 353 AAWLVVD-------EAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHAG 409
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
182-444 |
4.06e-24 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 106.49 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 182 MGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHKWFFSVPQSD-----AHLVLAQ------AKGGLSCFFVPRFL--PDG- 247
Cdd:PTZ00456 185 MCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDlteniVHIVLARlpnslpTTKGLSLFLVPRHVvkPDGs 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 248 ---QRNaVRLERLKDKLGNRSNASSEAEFLDASGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQR 324
Cdd:PTZ00456 265 letAKN-VKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 325 QTF------------GKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWD---NRNDPQEAAWAR----LFTPAAKYSV 385
Cdd:PTZ00456 344 RSMralsgtkepekpADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDihaAAKDAATREALDheigFYTPIAKGCL 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550713936 386 CKAGIPFVAEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLAKQPG 444
Cdd:PTZ00456 424 TEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIgrKVLSLKGG 484
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
158-442 |
2.17e-21 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 96.48 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 158 TPLMSDRYDPHLAPGAQkrgllIG-MGMTEKQGGSDVLSNTTKAEKcSDGSYRLVGHK-WFFSVPQSDAHLVLAQ---AK 232
Cdd:PLN02519 126 TPAQKEKYLPKLISGEH-----VGaLAMSEPNSGSDVVSMKCKAER-VDGGYVLNGNKmWCTNGPVAQTLVVYAKtdvAA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 233 G--GLSCFFVPRFLPdGQRNAVRLerlkDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQILKMGGLTRFDCALGSH 307
Cdd:PLN02519 200 GskGITAFIIEKGMP-GFSTAQKL----DKLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 308 GLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDN-RNDPQEAAWARLFTPAAKYSVc 386
Cdd:PLN02519 275 GLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNgKVDRKDCAGVILCAAERATQV- 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 550713936 387 kagipfVAEAMEVLGGAGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PLN02519 354 ------ALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
103-431 |
1.80e-19 |
|
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: 90.25 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 103 LAWEEEARKGSFvarAARFVLHAQVeagtlcpvtmtfaATPLLQRSLpkpfhewlTPLMSDRYDPHLAPGAQkrglLIGM 182
Cdd:cd01160 65 VLWEELARAGGS---GPGLSLHTDI-------------VSPYITRAG--------SPEQKERVLPQMVAGKK----IGAI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 183 GMTEKQGGSDVLSNTTKAEKcsDGS-YRLVGHKWFFSVP-QSDAHLVLAQ------AKGGLSCFFVPRFLPDGQRNavrl 254
Cdd:cd01160 117 AMTEPGAGSDLQGIRTTARK--DGDhYVLNGSKTFITNGmLADVVIVVARtggearGAGGISLFLVERGTPGFSRG---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 255 eRLKDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKNL 331
Cdd:cd01160 191 -RKLKKMGWKAQDTAELFFDDCrvpAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 332 IDQPLMRDVLSRMALVLEGHTALLFRLA-RAWDNRNDPQEAAWARLFTPAAKYSVckagipfVAEAMEVLGGAGYCEESE 410
Cdd:cd01160 270 AQLQVVRHKIAELATKVAVTRAFLDNCAwRHEQGRLDVAEASMAKYWATELQNRV-------AYECVQLHGGWGYMREYP 342
|
330 340
....*....|....*....|.
gi 550713936 411 LPRLYREMPVNSIWEGSGNIM 431
Cdd:cd01160 343 IARAYRDARVQPIYGGTTEIM 363
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
182-431 |
1.94e-18 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 87.09 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 182 MGMTEKQGGSDVLSNTTKAEKcSDGSYRLVGHKWFFS-VPQSDAHLVLAQ------AKGGLSCFFVPRFLPDGQRNAVRl 254
Cdd:PRK12341 122 LALTEPGAGSDNNSATTTYTR-KNGKVYLNGQKTFITgAKEYPYMLVLARdpqpkdPKKAFTLWWVDSSKPGIKINPLH- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 255 erlkdKLGnrSNASSEAE-FLD----ASGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGK 329
Cdd:PRK12341 200 -----KIG--WHMLSTCEvYLDnvevEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 330 NLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRNDPQEAAwarlftPAAKYSVCKAGIPFVAEAMEVLGGAGYCEES 409
Cdd:PRK12341 273 PIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSA------ALAKLYCARTAMEVIDDAIQIMGGLGYTDEA 346
|
250 260
....*....|....*....|..
gi 550713936 410 ELPRLYREMPVNSIWEGSGNIM 431
Cdd:PRK12341 347 RVSRFWRDVRCERIGGGTDEIM 368
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
153-430 |
2.03e-18 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 87.69 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 153 FHEWLTPLMSDRYDPHLAPGAQkrgllIG-MGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHK-WFFSVPQSDAHLVLAQ 230
Cdd:PTZ00461 130 FYYSASPAQRARWLPKVLTGEH-----VGaMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKiWITNGTVADVFLIYAK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 231 AKGGLSCFFVPRFLPdGQRNAVRLerlkDKLGNRSNASSEAEF----LDASGwLLGEEGEGVRQILKMGGLTRFDCALGS 306
Cdd:PTZ00461 205 VDGKITAFVVERGTK-GFTQGPKI----DKCGMRASHMCQLFFedvvVPAEN-LLGEEGKGMVGMMRNLELERVTLAAMA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 307 HGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVLSRMALVLEGHTALLFRLAR--AWDNRNDPQEAAwARLF-TPAAKY 383
Cdd:PTZ00461 279 VGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHnvHPGNKNRLGSDA-AKLFaTPIAKK 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 550713936 384 svckagipfVAE-AMEVLGGAGYCEESELPRLYREMPVNSIweGSGNI 430
Cdd:PTZ00461 358 ---------VADsAIQVMGGMGYSRDMPVERLWRDAKLLEI--GGGTI 394
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
181-273 |
4.51e-18 |
|
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: 79.25 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 181 GMGMTEKQGGSDVLSNTTKAEKCSDGSYRLVGHKWFFS-VPQSDAHLVLAQ-----AKGGLSCFFVPRFLPdgqrnAVRL 254
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIADLFLVLARtggddRHGGISLFLVPKDAP-----GVSV 75
|
90
....*....|....*....
gi 550713936 255 ERLKDKLGNRSNASSEAEF 273
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVF 94
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
184-442 |
1.60e-17 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 84.50 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 184 MTEKQGGSDVLS-NTTKAEKcsDGSYRLVGHKWFFSVPQSDAHLVL------AQAKGGLSCFFVPRFLPdgqrnAVRLER 256
Cdd:PRK03354 124 ITEPGAGSDVGSlKTTYTRR--NGKVYLNGSKCFITSSAYTPYIVVmardgaSPDKPVYTEWFVDMSKP-----GIKVTK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 257 LkDKLGNRSNASSEAEF----LDASGwLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKNLI 332
Cdd:PRK03354 197 L-EKLGLRMDSCCEITFddveLDEKD-MFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 333 DQPLMRDVLSRMALVLEGHTALLFRLARAWDNRN-DPQEAAwarlftpAAKYSVCKAGIPFVAEAMEVLGGAGYCEESEL 411
Cdd:PRK03354 275 RFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTiTSGDAA-------MCKYFCANAAFEVVDSAMQVLGGVGIAGNHRI 347
|
250 260 270
....*....|....*....|....*....|.
gi 550713936 412 PRLYREMPVNSIWEGSGNIMCLDVLRVLAKQ 442
Cdd:PRK03354 348 SRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
184-439 |
5.96e-14 |
|
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: 73.39 E-value: 5.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 184 MTEKQGGSDVLSNTTKAEKCSDgSYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPDGQRNavr 253
Cdd:cd01157 120 VTEPGAGSDVAGIKTKAEKKGD-EYIINGQKmwitnggkanWYFLLARSDPD-PKCPASKAFTGFIVEADTPGIQPG--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 254 leRLKDKLGNRSNASSEAEFLDA---SGWLLGEEGEGVRQILKMGGLTRFDCALGSHGLMRRALSVALYHAHQRQTFGKN 330
Cdd:cd01157 195 --RKELNMGQRCSDTRGITFEDVrvpKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 331 LIDQPLMRDVLSRMALVLEghTALLFRLARAWDNRNDPQEAAWARLftpaAKYSVCKAGIPFVAEAMEVLGGAGYCEESE 410
Cdd:cd01157 273 IAEHQAVSFMLADMAMKVE--LARLAYQRAAWEVDSGRRNTYYASI----AKAFAADIANQLATDAVQIFGGNGFNSEYP 346
|
250 260
....*....|....*....|....*....
gi 550713936 411 LPRLYREMPVNSIWEGSGNIMCLDVLRVL 439
Cdd:cd01157 347 VEKLMRDAKIYQIYEGTSQIQRLIISREH 375
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
155-415 |
1.84e-05 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 47.00 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 155 EWLTPLMSdrydphlapGAQKRGLLigmgMTEKQ-GGSDVLSNTTKAEKCSDgSYRLVGHKWFFS---VPQSDAHLVLAQ 230
Cdd:cd01155 115 QWLEPLLD---------GKIRSAFA----MTEPDvASSDATNIECSIERDGD-DYVINGRKWWSSgagDPRCKIAIVMGR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 231 AKGGL-------SCFFVPRFLPdgqrnAVRLERLKDKLGNRSNASSEAEF------LDASGwLLGEEGEGVRQILKMGGL 297
Cdd:cd01155 181 TDPDGaprhrqqSMILVPMDTP-----GVTIIRPLSVFGYDDAPHGHAEItfdnvrVPASN-LILGEGRGFEIAQGRLGP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 298 TRFDCALGSHGLMRRALSVALYHAHQRQTFGKNLIDQPLMRDVL--SRMALvlegHTALLFRLARAWdnRNDPQEAAWAR 375
Cdd:cd01155 255 GRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIakSRIEI----EQARLLVLKAAH--MIDTVGNKAAR 328
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 550713936 376 LFTPAAKYSVCKAGIPFVAEAMEVLGGAGYCEESELPRLY 415
Cdd:cd01155 329 KEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMY 368
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
174-404 |
1.72e-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: 43.88 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 174 QKRGLLIGM---------GMTEKQGGSDVLSNTTKAEKCSDGsYRLVGHKWFFSVPQ-SDAHLVLAQAKG------GLSC 237
Cdd:cd01152 104 QKRRFLPPIlsgeeiwcqGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAHyADWAWLLVRTDPeapkhrGISI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 238 FFVPRFLPdgqrnAVRLERLKDKLGnrsNASSEAEFLD----ASGWLLGEEGEGVRQIlkMGGLTRFDCALGSHGLMRRA 313
Cdd:cd01152 183 LLVDMDSP-----GVTVRPIRSING---GEFFNEVFLDdvrvPDANRVGEVNDGWKVA--MTTLNFERVSIGGSAATFFE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 314 LSVALYHAHQRQTFGknLIDQPLMRDVLSRMALVLEGHTALLFRLARAWDNRNDPQEAA------WARLFTPAAKYsvck 387
Cdd:cd01152 253 LLLARLLLLTRDGRP--LIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEAsiaklfGSELAQELAEL---- 326
|
250
....*....|....*..
gi 550713936 388 agipfvaeAMEVLGGAG 404
Cdd:cd01152 327 --------ALELLGTAA 335
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
308-417 |
1.90e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 38.48 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550713936 308 GLMRRALSVALYHAHQRQT--FGKNLIDQPLMRDVLSRMALVLEGHTALLFRLA-RAWDNR-----NDPQEAAWARLftp 379
Cdd:pfam08028 8 GAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAaRIEAAAaagkpVTPALRAEARR--- 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 550713936 380 AAKYSV--CKAGipfVAEAMEVLGGAGYCEESELPRLYRE 417
Cdd:pfam08028 85 AAAFATelAVAA---VDALFRAAGGSALFQDSPLQRIWRD 121
|
|
| |
