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Conserved domains on  [gi|71985184|ref|NP_001022062|]
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Very long-chain specific acyl-CoA dehydrogenase, mitochondrial [Caenorhabditis elegans]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 10100190)

acyl-CoA dehydrogenase (ACAD) family protein similar to mitochondrial very long-chain specific acyl-CoA dehydrogenase (VLCAD), which is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

CATH:  1.10.540.10
EC:  1.3.8.-
Gene Ontology:  GO:0016627|GO:0006631|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 41-449 0e+00

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: 741.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  41 SFVMNLFRGKAVTDQVFPYPLNMTDEQKETLGMVMSPLEKMLVEVNDVVKNDETSDIPRAVLDQFAELGTFGVLVPPELE 120
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 121 GSGFNNSQMARVAEIVGaYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTR 200
Cdd:cd01161  81 GLGLNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 201 AELSADGKHYVLNGGKIWISNGGFADVFTVFAQTPVKQADGSTKDKMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHF 280
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 281 DNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYA 360
Cdd:cd01161 240 EDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYA 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 361 TESIVYMLSSNMDRGIK-EYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLF 439
Cdd:cd01161 320 TESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399

                       410
                ....*....|
gi 71985184 440 IALTGAQHAG 449
Cdd:cd01161 400 IALTGLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 41-449 0e+00

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: 741.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  41 SFVMNLFRGKAVTDQVFPYPLNMTDEQKETLGMVMSPLEKMLVEVNDVVKNDETSDIPRAVLDQFAELGTFGVLVPPELE 120
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 121 GSGFNNSQMARVAEIVGaYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTR 200
Cdd:cd01161  81 GLGLNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 201 AELSADGKHYVLNGGKIWISNGGFADVFTVFAQTPVKQADGSTKDKMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHF 280
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 281 DNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYA 360
Cdd:cd01161 240 EDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYA 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 361 TESIVYMLSSNMDRGIK-EYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLF 439
Cdd:cd01161 320 TESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399

                       410
                ....*....|
gi 71985184 440 IALTGAQHAG 449
Cdd:cd01161 400 IALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 61-441 3.03e-138

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: 407.69  E-value: 3.03e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  61 LNMTDEQKETLGMVMSPLEKMLVEVNDvvKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYD 140
Cdd:COG1960   3 FELTEEQRALRDEVREFAEEEIAPEAR--EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 141 LGFGVVMGAHQSIGYkGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWIS 220
Cdd:COG1960  81 ASLALPVGVHNGAAE-ALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVR--DGDGYVLNGQKTFIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 221 NGGFADVFTVFAQTpvkqaDGSTKDK-MSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFK 299
Cdd:COG1960 158 NAPVADVILVLART-----DPAAGHRgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 300 VAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEY 379
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985184 380 QLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 92-440 1.68e-60

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 206.65  E-value: 1.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   92 DETSDIPRAVlDQFAELGTF---GVLVPPELEGSGFNNSQ----MARVAEIVGAYDLGFGvvmgAHQSIGYKGILLEGTD 164
Cdd:PLN02519  53 DATNSFPKDV-NLWKLMGDFnlhGITAPEEYGGLGLGYLYhciaMEEISRASGSVGLSYG----AHSNLCINQLVRNGTP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  165 AQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGkhYVLNGGKIWISNGGFADVFTVFAQTPVkqADGSTK 244
Cdd:PLN02519 128 AQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKTDV--AAGSKG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  245 dkMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCI 324
Cdd:PLN02519 204 --ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  325 QKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEYQLEAAIgKVLASENAWLVCDDAIQV 404
Cdd:PLN02519 282 DVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV-ILCAAERATQVALQAIQC 360

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 71985184  405 HGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFI 440
Cdd:PLN02519 361 LGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 295-441 5.50e-39

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: 140.08  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   295 GEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDR 374
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985184   375 GIKEyQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 41-449 0e+00

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: 741.98  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  41 SFVMNLFRGKAVTDQVFPYPLNMTDEQKETLGMVMSPLEKMLVEVNDVVKNDETSDIPRAVLDQFAELGTFGVLVPPELE 120
Cdd:cd01161   1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 121 GSGFNNSQMARVAEIVGaYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTR 200
Cdd:cd01161  81 GLGLNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 201 AELSADGKHYVLNGGKIWISNGGFADVFTVFAQTPVKQADGSTKDKMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHF 280
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYF 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 281 DNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYA 360
Cdd:cd01161 240 EDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYA 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 361 TESIVYMLSSNMDRGIK-EYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLF 439
Cdd:cd01161 320 TESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLF 399

                       410
                ....*....|
gi 71985184 440 IALTGAQHAG 449
Cdd:cd01161 400 IALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 61-441 3.03e-138

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: 407.69  E-value: 3.03e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  61 LNMTDEQKETLGMVMSPLEKMLVEVNDvvKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYD 140
Cdd:COG1960   3 FELTEEQRALRDEVREFAEEEIAPEAR--EWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 141 LGFGVVMGAHQSIGYkGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWIS 220
Cdd:COG1960  81 ASLALPVGVHNGAAE-ALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVR--DGDGYVLNGQKTFIT 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 221 NGGFADVFTVFAQTpvkqaDGSTKDK-MSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFK 299
Cdd:COG1960 158 NAPVADVILVLART-----DPAAGHRgISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 300 VAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEY 379
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985184 380 QLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 65-441 6.34e-115

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: 347.72  E-value: 6.34e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  65 DEQKETLGMVMSPLEKMLVEVndVVKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFG 144
Cdd:cd01158   1 EEHQMIRKTVRDFAEKEIAPL--AAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 145 VVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAElsADGKHYVLNGGKIWISNGGF 224
Cdd:cd01158  79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAK--KDGDDYVLNGSKMWITNGGE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 225 ADVFTVFAQT-PVKQADGstkdkMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMN 303
Cdd:cd01158 157 ADFYIVFAVTdPSKGYRG-----ITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQ 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 304 ILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEYQLEA 383
Cdd:cd01158 232 TLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG-EPFIKEA 310

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71985184 384 AIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01158 311 AMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 158-441 3.05e-108

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: 328.86  E-value: 3.05e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 158 ILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWISNGGFADVFTVFAQTpvk 237
Cdd:cd00567  48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARK--DGDGYVLNGRKIFISNGGDADLFIVLART--- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 238 QADGSTKDKMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACT 317
Cdd:cd00567 123 DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVAL 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 318 GAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEYQLEAAIGKVLASENAWLV 397
Cdd:cd00567 203 GAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAAREV 282

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71985184 398 CDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd00567 283 ADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 92-441 1.40e-86

Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.


Pssm-ID: 173851 [Multi-domain]  Cd Length: 375  Bit Score: 274.32  E-value: 1.40e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  92 DETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHQSIGYKgILLEGTDAQKQKYL 171
Cdd:cd01162  28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM-IDSFGNDEQRERFL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 172 PDLATGRKFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWISNGGFADVFTVFAQTPVKQADGstkdkMSAFI 251
Cdd:cd01162 107 PDLCTMEKLASYCLTEPGSGSDAAALRTRAVR--EGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPKG-----ISCFV 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 252 VERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHI 331
Cdd:cd01162 180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 332 TTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFM 411
Cdd:cd01162 260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYL 339

                       330       340       350
                ....*....|....*....|....*....|
gi 71985184 412 RETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01162 340 KDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 92-441 3.23e-82

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: 263.12  E-value: 3.23e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  92 DETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYL 171
Cdd:cd01156  29 DRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRNGSAAQKEKYL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 172 PDLATGRKFAAFALTEPTTGSDASSVRTRAElsADGKHYVLNGGKIWISNGGFADVFTVFAQT-PVKQADGstkdkMSAF 250
Cdd:cd01156 109 PKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNGSKMWITNGPDADTLVVYAKTdPSAGAHG-----ITAF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 251 IVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDH 330
Cdd:cd01156 182 IVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPY 261

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 331 ITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGF 410
Cdd:cd01156 262 AHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRG-NMDPKDAAGVILYAAEKATQVALDAIQILGGNGY 340

                       330       340       350
                ....*....|....*....|....*....|.
gi 71985184 411 MRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01156 341 INDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 92-441 3.77e-77

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: 249.72  E-value: 3.77e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  92 DETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVgAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYL 171
Cdd:cd01160  26 EKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGPGLSLHTDIVSPYITRAGSPEQKERVL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 172 PDLATGRKFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWISNGGFADVFTVFAQTpvkQADGSTKDKMSAFI 251
Cdd:cd01160 105 PQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART---GGEARGAGGISLFL 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 252 VERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHI 331
Cdd:cd01160 180 VERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYV 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 332 TTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFM 411
Cdd:cd01160 260 KQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQG-RLDVAEASMAKYWATELQNRVAYECVQLHGGWGYM 338

                       330       340       350
                ....*....|....*....|....*....|
gi 71985184 412 RETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01160 339 REYPIARAYRDARVQPIYGGTTEIMKELIS 368
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 92-440 1.68e-60

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 206.65  E-value: 1.68e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   92 DETSDIPRAVlDQFAELGTF---GVLVPPELEGSGFNNSQ----MARVAEIVGAYDLGFGvvmgAHQSIGYKGILLEGTD 164
Cdd:PLN02519  53 DATNSFPKDV-NLWKLMGDFnlhGITAPEEYGGLGLGYLYhciaMEEISRASGSVGLSYG----AHSNLCINQLVRNGTP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  165 AQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGkhYVLNGGKIWISNGGFADVFTVFAQTPVkqADGSTK 244
Cdd:PLN02519 128 AQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKTDV--AAGSKG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  245 dkMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCI 324
Cdd:PLN02519 204 --ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACL 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  325 QKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEYQLEAAIgKVLASENAWLVCDDAIQV 404
Cdd:PLN02519 282 DVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGV-ILCAAERATQVALQAIQC 360

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 71985184  405 HGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFI 440
Cdd:PLN02519 361 LGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 47-428 1.12e-57

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 199.39  E-value: 1.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   47 FRGKAVTDQVFPYPLNMTDEQKetlgMVMSPLEKMLVEVND--VVKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGF 124
Cdd:PTZ00461  21 AATMTSASRAFMDLYNPTPEHA----ALRETVAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  125 NNSQMARVAEIVGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELS 204
Cdd:PTZ00461  97 DAVAAVIIHHELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  205 ADGKhYVLNGGKIWISNGGFADVFTVFAQTpvkqaDGstkdKMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLK 284
Cdd:PTZ00461 177 SNGN-YVLNGSKIWITNGTVADVFLIYAKV-----DG----KITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVV 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  285 IPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESI 364
Cdd:PTZ00461 247 VPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKAL 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71985184  365 VYMLSSNMDRGIKEyQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRI 428
Cdd:PTZ00461 327 VYSVSHNVHPGNKN-RLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEI 389
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 93-446 1.40e-57

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: 198.35  E-value: 1.40e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  93 ETSDIPRAVLDQFAELGTFGVLvPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLP 172
Cdd:cd01151  41 REEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLP 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 173 DLATGRKFAAFALTEPTTGSDASSVRTRAElsADGKHYVLNGGKIWISNGGFADVFTVFAQTpvkqadgSTKDKMSAFIV 252
Cdd:cd01151 120 KLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIADVFVVWARN-------DETGKIRGFIL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 253 ERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLgKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHIT 332
Cdd:cd01151 191 ERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVL 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 333 TRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMR 412
Cdd:cd01151 270 DRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG-KATPEQISLLKRNNCGKALEIARTAREMLGGNGISD 348

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 71985184 413 ETGLERVLRDLRIFRIFEGANDVLRLFI--ALTGAQ 446
Cdd:cd01151 349 EYHIIRHMVNLESVNTYEGTHDIHALILgrAITGIQ 384
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 63-441 6.28e-57

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: 196.65  E-value: 6.28e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  63 MTDEQKETLGMVMSPLEKMLVEVndVVKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEivgayDLG 142
Cdd:cd01157   1 LTEQQKEFQETARKFAREEIIPV--AAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITE-----ELA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 143 FGV--VMGAHQ--SIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADgkHYVLNGGKIW 218
Cdd:cd01157  74 YGCtgVQTAIEanSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD--EYIINGQKMW 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 219 ISNGGFADVFTVFAQT-PVKQADGSTKdkMSAFIVERAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVENLLGKEGEG 297
Cdd:cd01157 152 ITNGGKANWYFLLARSdPDPKCPASKA--FTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAG 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 298 FKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIK 377
Cdd:cd01157 230 FKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRR 309

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71985184 378 EyQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01157 310 N-TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 74-433 9.87e-52

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: 183.36  E-value: 9.87e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  74 VMSPLEKmLVEVNDVVKNDETSDIPRAV---LDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAH 150
Cdd:cd01153  12 VLAPLNA-DGDREGPVFDDGRVVVPPPFkeaLDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 151 QSIgyKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGKhYVLNGGKIWISNG--GFAD-- 226
Cdd:cd01153  91 GAA--ATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGS-WRINGVKRFISAGehDMSEni 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 227 VFTVFAQTPvkQADGSTKDkMSAFIV-------ERafGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPvenLLGKEGEGFK 299
Cdd:cd01153 168 VHLVLARSE--GAPPGVKG-LSLFLVpkflddgER--NGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLA 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 300 VAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMD------ 373
Cdd:cd01153 240 QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDlytatv 319

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71985184 374 -----RGIKEYQLEAA----------IGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGAN 433
Cdd:cd01153 320 qdlaeRKATEGEDRKAlsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTT 394
PRK12341 PRK12341
acyl-CoA dehydrogenase;
63-436 7.35e-45

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 163.75  E-value: 7.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   63 MTDEQKETLGMVMSPLEKMLVEvNDVVKNDETSDIPRAVLDQFAELGtFGVL-VPPELEGSGFNN-SQMARVAEIvgAYD 140
Cdd:PRK12341   5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNG-ISMLgVPEEFGGTPADYvTQMLVLEEV--SKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  141 LGFGVVMGAHQSIgyKGILLEGTDAQKQKYLPD-LATGRKFAAFALTEPTTGSDASSVRTRAElSADGKHYvLNGGKIWI 219
Cdd:PRK12341  81 GAPAFLITNGQCI--HSMRRFGSAEQLRKTAEStLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVY-LNGQKTFI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  220 SNGGFADVFTVFAQTPvkqADGSTKDKMSAFIVERAFGGVTSGPQEKkMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFK 299
Cdd:PRK12341 157 TGAKEYPYMLVLARDP---QPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGFL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  300 VAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIkEY 379
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQ-SL 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985184  380 QLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVL 436
Cdd:PRK12341 312 RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 92-438 3.92e-40

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 150.75  E-value: 3.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   92 DETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAydLGFGVVMGAHQSIGYKGILLEGTDAQKQKYL 171
Cdd:PRK03354  33 DRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR--LGAPTYVLYQLPGGFNTFLREGTQEQIDKIM 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  172 PDLATGRKFAAFALTEPTTGSDASSVRTRAElSADGKHYvLNGGKIWISNGGFADVFTVFAqtpvKQADGSTKDKMSAFI 251
Cdd:PRK03354 111 AFRGTGKQMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCFITSSAYTPYIVVMA----RDGASPDKPVYTEWF 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  252 VERAFGGVTSGPQEKkMGIKGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHI 331
Cdd:PRK03354 185 VDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYA 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  332 TTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEyQLEAAIGKVLASENAWLVCDDAIQVHGGMGFM 411
Cdd:PRK03354 264 NQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIA 342

                        330       340
                 ....*....|....*....|....*..
gi 71985184  412 RETGLERVLRDLRIFRIFEGANDVLRL 438
Cdd:PRK03354 343 GNHRISRFWRDLRVDRVSGGSDEMQIL 369
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 295-441 5.50e-39

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: 140.08  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   295 GEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDR 374
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71985184   375 GIKEyQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:pfam00441  81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 104-441 1.33e-38

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: 146.34  E-value: 1.33e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 104 QFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAY-----DLGFGVVMGAHQsigykgILLEGTDAQKQKYLPDLATGR 178
Cdd:cd01152  43 ALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAgapvpFNQIGIDLAGPT------ILAYGTDEQKRRFLPPILSGE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 179 KFAAFALTEPTTGSDASSVRTRAELsaDGKHYVLNGGKIWISNGGFADVFTVFAQTP--VKQADGstkdkMSAFIVERAF 256
Cdd:cd01152 117 EIWCQGFSEPGAGSDLAGLRTRAVR--DGDDWVVNGQKIWTSGAHYADWAWLLVRTDpeAPKHRG-----ISILLVDMDS 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 257 GGVTSGPQEKKMGikGSNTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGR---FGIPA-ACTGAMKHCIQKTVDhit 332
Cdd:cd01152 190 PGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERvsiGGSAAtFFELLLARLLLLTRD--- 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 333 trvqfGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGiKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMR 412
Cdd:cd01152 265 -----GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAG-KPPGAEASIAKLFGSELAQELAELALELLGTAALLR 338

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71985184 413 ETGL--------ERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:cd01152 339 DPAPgaelagrwEADYLRSRATTIYGGTSEIQRNIIA 375
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 77-443 4.05e-37

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: 142.53  E-value: 4.05e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  77 PLEKMLVEVndVVKNDETSDIPRAVLDQFAE----LGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHQS 152
Cdd:cd01155  20 PAEQEFLEY--YAEGGDRWWTPPPIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSFFAPEVFNCQAPD 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 153 IGYKGILLE-GTDAQKQKYLPDLATGRKFAAFALTEP-TTGSDASSVRTRAElsADGKHYVLNGGKIWISNGGFAD--VF 228
Cdd:cd01155  98 TGNMEVLHRyGSEEQKKQWLEPLLDGKIRSAFAMTEPdVASSDATNIECSIE--RDGDDYVINGRKWWSSGAGDPRckIA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 229 TVFAQTpvkQADGSTKDKM-SAFIVERAFGGVTsgpQEKKMGIKGSNTT-----EVHFDNLKIPVENLLGKEGEGFKVAM 302
Cdd:cd01155 176 IVMGRT---DPDGAPRHRQqSMILVPMDTPGVT---IIRPLSVFGYDDAphghaEITFDNVRVPASNLILGEGRGFEIAQ 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 303 NILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDR-GIKEYQL 381
Cdd:cd01155 250 GRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTvGNKAARK 329

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985184 382 EAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIALT 443
Cdd:cd01155 330 EIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARM 391
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 164-439 1.92e-31

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: 126.72  E-value: 1.92e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 164 DAQKQKYLPDLATGRK----FAAFALTEPTTGSDASSVRTRAELSADGKhYVLNGGKiWISNGGFADVFTVFAQTPvkQA 239
Cdd:cd01154 128 PEELKQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-WFASAPLADAALVLARPE--GA 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 240 DGSTKDkMSAFIVERAFGGVTSGPQE-----KKMGIKGSNTTEVHFDNlkiPVENLLGKEGEGFKVAMNILNNGRFGIPA 314
Cdd:cd01154 204 PAGARG-LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDD---AEAYLIGDEGKGIYYILEMLNISRLDNAV 279

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 315 ACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEYQLEA-------AIGK 387
Cdd:cd01154 280 AALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAK 359

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71985184 388 VLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEG-----ANDVLRLF 439
Cdd:cd01154 360 LIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGtgniqALDVLRVL 416
PLN02526 PLN02526
acyl-coenzyme A oxidase
 50-435 6.05e-28

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 116.49  E-value: 6.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   50 KAVTDQVFP------YPLN--MTDEQKETLGMVMSPLEKMLVEVndVVKNDETSDIPRAVLDQFAELGTFGVLVP----P 117
Cdd:PLN02526   8 QATPASIFPpsvsdyYQFDdlLTPEEQALRKRVRECMEKEVAPI--MTEYWEKAEFPFHIIPKLGSLGIAGGTIKgygcP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  118 ELE--GSGFNNSQMARVAEIVGAYDLgfgvvmgAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDAS 195
Cdd:PLN02526  86 GLSitASAIATAEVARVDASCSTFIL-------VHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDAS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  196 SVRTRAELSADGkhYVLNGGKIWISNGGFADVFTVFAQTpvkqadgSTKDKMSAFIVERAFGGVTSGPQEKKMGIKGSNT 275
Cdd:PLN02526 159 SLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARN-------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQN 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  276 TEVHFDNLKIPVENLLgKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMI 355
Cdd:PLN02526 230 GDIVLKDVFVPDEDRL-PGVNSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRML 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  356 SKLYATESIVYML-----SSNMDRGikeyqlEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFE 430
Cdd:PLN02526 309 GNIQAMFLVGWRLcklyeSGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382


                 ....*
gi 71985184  431 GANDV 435
Cdd:PLN02526 383 GTYDI 387
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 182-281 3.11e-27

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: 105.44  E-value: 3.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   182 AFALTEPTTGSDASSVRTRAeLSADGKHYVLNGGKIWISNGGFADVFTVFAQTpvkqADGSTKDKMSAFIVERAFGGVTS 261
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLART----GGDDRHGGISLFLVPKDAPGVSV 75

                          90       100
                  ....*....|....*....|
gi 71985184   262 GPQEKKMGIKGSNTTEVHFD 281
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 99-431 7.15e-27

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 115.35  E-value: 7.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   99 RAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGvvMGAHQSIG-YKGILLEGTDAQKQKYLPDLATG 177
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFS--MYPGLSIGaANTLMAWGSEEQKEQYLTKLVSG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  178 RKFAAFALTEPTTGSDASSVRTRAELSADGKhYVLNGGKIWISNG--GFAD--VFTVFAQTPVKQAdgSTKDkMSAFIVE 253
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGdhDLTEniVHIVLARLPNSLP--TTKG-LSLFLVP 255

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  254 R----------AFGGVTSGPQEKKMGIKGSNTTEVHFDNlkiPVENLLGKEGEGFKVAMNILNNGRFGIPA--------A 315
Cdd:PTZ00456 256 RhvvkpdgsleTAKNVKCIGLEKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTALegvchaelA 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  316 CTGAMKH--------------CIQKTVD----HITTR--VQFGKKLQEFGNIQEKLVEMISKLYATESIVyMLSSNMDRG 375
Cdd:PTZ00456 333 FQNALRYarerrsmralsgtkEPEKPADriicHANVRqnILFAKAVAEGGRALLLDVGRLLDIHAAAKDA-ATREALDHE 411

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71985184  376 IKEYqleAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEG 431
Cdd:PTZ00456 412 IGFY---TPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEG 464
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 64-177 1.63e-23

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 95.61  E-value: 1.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184    64 TDEQKETLGMVMSPLEKMLVEVndVVKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGF 143
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEIAPH--AAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 71985184   144 GVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATG 177
Cdd:pfam02771  79 ALALSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
 41-572 3.37e-21

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 97.26  E-value: 3.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   41 SFVMNLFRGKAVTDQVFPYPLNMTD-EQKETLgmvmspleKMLVEvnDVVKNDETsdipravldqfaeLGT-FGVLVPPE 118
Cdd:PTZ00457  17 SYAAGLFNFKIVPEEMFPYPCRKLDgDEAENL--------QSLLE--QIRSNDKI-------------LGNlYGARIATE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  119 LEGSGFNNSQMARVAEIVGAYdlGFGVVMGAHQSIGYKGILLE--GTDAQKQKYLPDLATGRKFAAFAlTEPTTGSDASS 196
Cdd:PTZ00457  74 YGGLGLGHTAHALIYEEVGTN--CDSKLLSTIQHSGFCTYLLStvGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISM 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  197 VRTRAELSADGKhYVLNGGKiWISNGGFADVFTVFAQT---PVKQADGSTKDKMSAFIVERAFGGVTSgpqekkmgikgs 273
Cdd:PTZ00457 151 NTTKASLTDDGS-YVLTGQK-RCEFAASATHFLVLAKTltqTAAEEGATEVSRNSFFICAKDAKGVSV------------ 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  274 NTTEVHFDNlkIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQktvdhittrvQFGKKLQEFGnIQEKLVE 353
Cdd:PTZ00457 217 NGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQ----------ELRGSNAEEG-ATDTVAS 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  354 MISKLYATESIVYMLSSNMDRGIKEYQLEAAIGKVL--ASENAWLvcdDAIQVHGGMgfmrETGLERVLRDLRIFRIFEG 431
Cdd:PTZ00457 284 FACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFvqSTTNQLL---SILETATPP----STTLEKCFANARLFLSMME 356

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  432 ANDVLRLFIALTGAQHAGkhLAEQASGVGGLIGLAVSRVTGGNTGSNFGQVVDASLQDSAKVldqqiaLFGQTVQGLLMK 511
Cdd:PTZ00457 357 SRDFLYSSAVCCGVEDYG--LFFQRASTLQMMQARTLRSLGVRDRVPIKNLPDCSLIDEAVV------AFGNAVEATFVR 428

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71985184  512 HKKGIIDRQYEMHRVADAAINIYSSAAVLSRATYAIKNKSSSADFERKVATYYVDKAMKSS 572
Cdd:PTZ00457 429 SGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRA 489
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 46-409 3.68e-21

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 98.11  E-value: 3.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   46 LFRGKAVTDQVFPYPL-NMTDEQKETL-GMVMSPLEkMLVEVnDVVKNDEtsDIPRAVLDQFAELGTFGVLVPPELEGSG 123
Cdd:PRK13026  60 LFSGKPDWQKLHSYPKpTLTAEEQAFIdNEVETLLT-MLDDW-DIVQNRK--DLPPEVWDYLKKEGFFALIIPKEYGGKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  124 FN---NSQ-MARVAeivgAYDLGFGV-VMgAHQSIGYKGILLE-GTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASS- 196
Cdd:PRK13026 136 FSayaNSTiVSKIA----TRSVSAAVtVM-VPNSLGPGELLTHyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAi 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  197 ----VRTRAELsaDGKHYV---LNGGKIWISNGGFADVFTVFAQtpVKQADGSTKDKMSAFI----VERAFGGVTSGPQE 265
Cdd:PRK13026 211 pdtgIVCRGEF--EGEEVLglrLTWDKRYITLAPVATVLGLAFK--LRDPDGLLGDKKELGItcalIPTDHPGVEIGRRH 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  266 KKMGI---KGSNTTEVHFdnlkIPVENLLG---KEGEGFKVAMNILNNGRfGI--PAACTGAMKHCIQKTVDHITTRVQF 337
Cdd:PRK13026 287 NPLGMafmNGTTRGKDVF----IPLDWIIGgpdYAGRGWRMLVECLSAGR-GIslPALGTASGHMATRTTGAYAYVRRQF 361

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71985184  338 GKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIKEyQLEAAIGKVLASENAWLVCDDAIQVHGGMG 409
Cdd:PRK13026 362 GMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PLN02876 PLN02876
acyl-CoA dehydrogenase
 119-435 4.84e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 94.48  E-value: 4.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  119 LEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHQSIGYKGILLE-GTDAQKQKYLPDLATGRKFAAFALTEPTTgsdASSV 197
Cdd:PLN02876 489 LLGAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQV---ASSD 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  198 RTRAELSA--DGKHYVLNGGKIWISngGFAD----VFTVFAQTPVKQAdgstKDKMSAFIVERAfggVTSGPQEKK---- 267
Cdd:PLN02876 566 ATNIECSIrrQGDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAP----KHKQQSMILVDI---QTPGVQIKRpllv 636

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  268 MGIKGS--NTTEVHFDNLKIPVENLLGKEGEGFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKKLQEFG 345
Cdd:PLN02876 637 FGFDDAphGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG 716

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  346 NIQEKLVEMISKLYATESIVYMLSSNMDR-GIKEYQLEAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLR 424
Cdd:PLN02876 717 SFLSDLAKCRVELEQTRLLVLEAADQLDRlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATAR 796

                        330
                 ....*....|.
gi 71985184  425 IFRIFEGANDV 435
Cdd:PLN02876 797 TLRIADGPDEV 807
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 136-450 3.10e-17

Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.


Pssm-ID: 173839 [Multi-domain]  Cd Length: 610  Bit Score: 85.46  E-value: 3.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 136 VGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGKHYVLN-- 213
Cdd:cd01150  91 LGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINtp 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 214 ---GGKIWISNGGF-ADVFTVFAQ--TPVKqadgstKDKMSAFIVE-------RAFGGVTSGPQEKKMGIKGSNTTEVHF 280
Cdd:cd01150 171 dftATKWWPGNLGKtATHAVVFAQliTPGK------NHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDNGFLQF 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 281 DNLKIPVENLLGKEGE----------------GFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGKK---- 340
Cdd:cd01150 245 RNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKpsdp 324

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 341 ---LQEFGNIQEKLVEMISKLYA----TESIVYMLSSNMDRGIKEyQLEA-----AIGKVLASENAWLvCDDAIQVH--- 405
Cdd:cd01150 325 evqILDYQLQQYRLFPQLAAAYAfhfaAKSLVEMYHEIIKELLQG-NSELlaelhALSAGLKAVATWT-AAQGIQECrea 402

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 71985184 406 -GGMGFMRETGLERVLRDLRIFRIFEGANDVLRLFIA---LTGAQHAGK 450
Cdd:cd01150 403 cGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTAnylLKKYAQAFS 451
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 77-412 7.47e-17

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 84.48  E-value: 7.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   77 PLEKMLVEVNDVVKNDETSDIPRAVLDQFAELGTFGVLVPPE---LEGSGFNNSQ-MARVAEIVGAydlgFGVVMGAHQS 152
Cdd:PRK09463  90 PVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEyggLEFSAYAHSRvLQKLASRSGT----LAVTVMVPNS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  153 IGyKGILLE--GTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASS-----VRTRAELSADGKHYV-LNGGKIWISnggF 224
Cdd:PRK09463 166 LG-PGELLLhyGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSipdtgVVCKGEWQGEEVLGMrLTWNKRYIT---L 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  225 ADVFTVF-----AQTPvkqaDGSTKDKMSAFI----VERAFGGVTSGPQEKKMGikgsntteVHFDN-------LKIPVE 288
Cdd:PRK09463 242 APIATVLglafkLYDP----DGLLGDKEDLGItcalIPTDTPGVEIGRRHFPLN--------VPFQNgptrgkdVFIPLD 309

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  289 NLLGKE---GEGFKVAMNILNNGRfGI--PAACTGAMKHCIQKTVDHITTRVQFGKKLQEFGNIQEKLVEMISKLYATES 363
Cdd:PRK09463 310 YIIGGPkmaGQGWRMLMECLSVGR-GIslPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDA 388

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 71985184  364 IVYMLSSNMDRGIKEYQLeAAIGKVLASENAWLVCDDAIQVHGGMGFMR 412
Cdd:PRK09463 389 ARTLTTAAVDLGEKPSVL-SAIAKYHLTERGRQVINDAMDIHGGKGICL 436
PLN02636 PLN02636
acyl-coenzyme A oxidase
 132-436 2.71e-16

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 82.60  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  132 VAEIVGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGKHYV 211
Cdd:PLN02636 126 ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  212 LN-----GGKIWISN----GGFADVFTVFaQTPVKQADGSTKDKMSAFIV-------ERAFGGVTSGPQEKKMGIKGSNT 275
Cdd:PLN02636 206 INtpndgAIKWWIGNaavhGKFATVFARL-KLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDN 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  276 TEVHFDNLKIPVENLLGKEGE----------------GFKVAMNILNNGRFGIPAACTGAMKHCIQKTVDHITTRVQFGK 339
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGP 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  340 KLQEFGNI------QEKLVEMISKLY----ATESIVYMLS----SNMDRGIKE-YQLEAAIGKVLASENA--WLVCDDAI 402
Cdd:PLN02636 365 PKQPEISIldyqsqQHKLMPMLASTYafhfATEYLVERYSemkkTHDDQLVADvHALSAGLKAYITSYTAkaLSTCREAC 444

                        330       340       350
                 ....*....|....*....|....*....|....
gi 71985184  403 QVHGGMGFMRETGLErvlRDLRIFRIFEGANDVL 436
Cdd:PLN02636 445 GGHGYAAVNRFGSLR---NDHDIFQTFEGDNTVL 475
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
 185-446 1.62e-12

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 70.17  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  185 LTEPTTGSDASSVRTRAELSADGKhYVLNGGKiWISNGGFADVFTVFAQTpvkqadgstKDKMSAFIVERAF-----GGV 259
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpdgqrNAI 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  260 TSGPQEKKMGIKGSNTTEVHFDNlkiPVENLLGKEGEGFKvamNILNNG---RFGIPAACTGAMKHCIQKTVDHITTRVQ 336
Cdd:PRK11561 253 RLERLKDKLGNRSNASSEVEFQD---AIGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQV 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  337 FGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRgiKEYQLEAAIGKVLASENAWLVCD-------DAIQVHGGMG 409
Cdd:PRK11561 327 FGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR--RADAKEALWARLFTPAAKFVICKrgipfvaEAMEVLGGIG 404

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 71985184  410 FMRETGLERVLRDLRIFRIFEGAN-----DVLRLFIALTGAQ 446
Cdd:PRK11561 405 YCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVY 446
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
311-433 3.93e-11

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 60.82  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   311 GIPAACTGAMKHCIQKTVDHITTRVQ--FGKKLQEFGNIQEKLVEMISKLYATESIVYMLSSNMDRGIK-------EYQL 381
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAagkpvtpALRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71985184   382 EAAIGKVLASENAWLVCDDAIQVHGGMGFMRETGLERVLRDLRIFRIFEGAN 433
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 87-293 2.15e-10

Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.


Pssm-ID: 173852 [Multi-domain]  Cd Length: 377  Bit Score: 62.73  E-value: 2.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  87 DVVKNDETSDIPRAVLDQFAELGTFGVLVPPELEGSGFNNSQMARVAEIVGAYDLGFGVVMGAHqsIGYKGILLEGTDAQ 166
Cdd:cd01163  13 GAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFVEALLLAGPEQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184 167 KQKYLPDLATGRKFAAFALTEPTTGSDASSVRTraeLSADGKHYVLNGGKIWISNGGFADVFTVFAQTPVkqadgstkDK 246
Cdd:cd01163  91 FRKRWFGRVLNGWIFGNAVSERGSVRPGTFLTA---TVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEE--------GK 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 71985184 247 MSAFIVERAFGGVTSGPQEKKMGIK--GSNTteVHFDNLKIPVENLLGK 293
Cdd:cd01163 160 LVFAAVPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLPR 206
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 143-441 4.75e-08

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 56.01  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  143 FGVVMGAHQSIGykgillegTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAELSADGKHYVLN-----GGKI 217
Cdd:PTZ00460  99 FAMVIPAFQVLG--------TDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKF 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  218 WISNGGFADVFT-VFAQTPVkqaDGSTKDkMSAFIVE-------RAFGGVTSGPQEKKMGIKGSNTTEVHFDNLKIPVEN 289
Cdd:PTZ00460 171 WPGELGFLCNFAlVYAKLIV---NGKNKG-VHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDS 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  290 LLGKegegfkvAMNILNNGRF---GIPAACTGAMKHCIQKTVDHIT---------------TRVQF-GKKLQE-----FG 345
Cdd:PTZ00460 247 LLAR-------YIKVSEDGQVerqGNPKVSYASMMYMRNLIIDQYPrfaaqaltvairysiYRQQFtNDNKQEnsvleYQ 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  346 NIQEKLVEMISKLYA----TESIVYMLSSNMDRGIKE----YQLEAAIGKVLASENAWLVCDDAIQVH---GGMGFMRET 414
Cdd:PTZ00460 320 TQQQKLLPLLAEFYAcifgGLKIKELVDDNFNRVQKNdfslLQLTHAILSAAKANYTYFVSNCAEWCRlscGGHGYAHYS 399

                        330       340
                 ....*....|....*....|....*..
gi 71985184  415 GLERVLRDLRIFRIFEGANDVLRLFIA 441
Cdd:PTZ00460 400 GLPAIYFDMSPNITLEGENQIMYLQLA 426
PLN02312 PLN02312
acyl-CoA oxidase
 45-291 1.15e-06

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 51.70  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184   45 NLFRGKAVTDQVFPYP-LNMTDEQKETlgMVMSPLEKMLVevNDVVKNDETSDIPRAVLDQFAELgtfgvlvppelegsg 123
Cdd:PLN02312  79 DLFNSKRRGGRVFVSPdYNQTMEQQRE--ITMKRILYLLE--RGVFRGWLTETGPEAELRKLALL--------------- 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  124 fnnsqmarvaEIVGAYDLGFGVVMGAHQSIGYKGILLEGTDAQKQKYLPDLATGRKFAAFALTEPTTGSDASSVRTRAEL 203
Cdd:PLN02312 140 ----------EVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTY 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  204 SADGKHYVLN-----GGKIWIsnGGFADVFT---VFAQTPVkqaDGsTKDKMSAFIVE--RAFGGVTSGPQ----EKKMG 269
Cdd:PLN02312 210 DPKTEEFVINtpcesAQKYWI--GGAANHAThtiVFSQLHI---NG-KNEGVHAFIAQirDQDGNICPNIRiadcGHKIG 283

                        250       260
                 ....*....|....*....|..
gi 71985184  270 IKGSNTTEVHFDNLKIPVENLL 291
Cdd:PLN02312 284 LNGVDNGRIWFDNLRIPRENLL 305
PLN02443 PLN02443
acyl-coenzyme A oxidase
 161-340 4.11e-03

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 40.21  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  161 EGTDAQKQKYLPdLATgrKFA---AFALTEPTTGSDASSVRTRAELSADGKHYVLN-----GGKIWisNGGFADVFT--- 229
Cdd:PLN02443 113 QGTEEQQKKWLP-LAY--KMQiigCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThav 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71985184  230 VFAQTPVKQADGStkdkMSAFIVE-------RAFGGVTSGPQEKKMGIKGSNTTE---VHFDNLKIPVENLLGKEG---- 295
Cdd:PLN02443 188 VYARLITNGKDHG----IHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtr 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71985184  296 EGFKVAMNI---LNNG-----RFGIPAACTGAMKHCIQKTVDHITTRVQFGKK 340
Cdd:PLN02443 264 EGKYVQSDVprqLVYGtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGSQ 316
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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