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Q06319

- ACDS_MEGEL

UniProt

Q06319 - ACDS_MEGEL

Protein

Acyl-CoA dehydrogenase, short-chain specific

Gene
N/A
Organism
Megasphaera elsdenii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Has an optimum specificity for 4-carbon length fatty acyl-CoAs.

    Catalytic activityi

    Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei367 – 3671Proton acceptor

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: InterPro
    2. butyryl-CoA dehydrogenase activity Source: UniProtKB-EC
    3. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. fatty acid metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11937.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-CoA dehydrogenase, short-chain specific (EC:1.3.8.1)
    Alternative name(s):
    Butyryl-CoA dehydrogenase
    Short name:
    BCAD
    SCAD
    OrganismiMegasphaera elsdenii
    Taxonomic identifieri907 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesNegativicutesSelenomonadalesVeillonellaceaeMegasphaera

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi367 – 3671E → Q: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 383383Acyl-CoA dehydrogenase, short-chain specificPRO_0000201190Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    383
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2216
    Turni23 – 275
    Helixi28 – 347
    Helixi39 – 468
    Helixi50 – 523
    Helixi57 – 593
    Helixi62 – 654
    Helixi69 – 8214
    Helixi84 – 9613
    Helixi98 – 1047
    Helixi107 – 1126
    Helixi114 – 1196
    Beta strandi124 – 1274
    Beta strandi133 – 1353
    Helixi137 – 1393
    Beta strandi143 – 1464
    Beta strandi152 – 16211
    Turni163 – 1664
    Beta strandi168 – 1769
    Beta strandi178 – 1814
    Beta strandi184 – 1918
    Beta strandi197 – 2026
    Beta strandi213 – 22311
    Helixi225 – 2273
    Beta strandi228 – 2303
    Helixi235 – 27137
    Helixi279 – 2813
    Helixi283 – 31230
    Helixi317 – 34226
    Helixi343 – 3475
    Helixi353 – 3608
    Helixi361 – 3644
    Turni365 – 3673
    Helixi370 – 38112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BUCX-ray2.50A/B1-383[»]
    ProteinModelPortaliQ06319.
    SMRiQ06319. Positions 1-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06319.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q06319-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFNLTDIQQ DFLKLAHDFG EKKLAPTVTE RDHKGIYDKE LIDELLSLGI    50
    TGAYFEEKYG GSGDDGGDVL SYILAVEELA KYDAGVAITL SATVSLCANP 100
    IWQFGTEAQK EKFLVPLVEG TKLGAFGLTE PNAGTDASGQ QTIATKNDDG 150
    TYTLNGSKIF ITNGGAADIY IVFAMTDKSK GNHGITAFIL EDGTPGFTYG 200
    KKEDKMGIHT SQTMELVFQD VKVPAENMLG EEGKGFKIAM MTLDGGRIGV 250
    AAQALGIAEA ALADAVEYSK QRVQFGKPLC KFQSISFKLA DMKMQIEAAR 300
    NLVYKAACKK QEGKPFTVDA AIAKRVASDV AMRVTTEAVQ IFGGYGYSEE 350
    YPVARHMRDA KITQIYEGTN EVQLMVTGGA LLR 383
    Length:383
    Mass (Da):41,408
    Last modified:October 1, 1996 - v1
    Checksum:i3D68AAE34D9BBAB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04528 Unassigned DNA. Translation: AAA03594.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04528 Unassigned DNA. Translation: AAA03594.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BUC X-ray 2.50 A/B 1-383 [» ]
    ProteinModelPortali Q06319.
    SMRi Q06319. Positions 1-383.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-11937.

    Miscellaneous databases

    EvolutionaryTracei Q06319.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii."
      Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., Macgillivray R.T.A., Stankovich M.T.
      Biochemistry 32:10736-10742(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50.
    2. "Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii."
      Djordjevic S., Pace C.P., Stankovich M.T., Kim J.-J.P.
      Biochemistry 34:2163-2171(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiACDS_MEGEL
    AccessioniPrimary (citable) accession number: Q06319
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3