ACDS_MEGEL
ID ACDS_MEGEL Reviewed; 383 AA.
AC Q06319;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acyl-CoA dehydrogenase, short-chain specific;
DE EC=1.3.8.1;
DE AltName: Full=Butyryl-CoA dehydrogenase;
DE Short=BCAD;
DE AltName: Full=SCAD;
OS Megasphaera elsdenii.
OC Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-50.
RX PubMed=8399220; DOI=10.1021/bi00091a026;
RA Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., Macgillivray R.T.A.,
RA Stankovich M.T.;
RT "Characterization of wild-type and an active-site mutant in Escherichia
RT coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii.";
RL Biochemistry 32:10736-10742(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=7857927; DOI=10.1021/bi00007a009;
RA Djordjevic S., Pace C.P., Stankovich M.T., Kim J.-J.P.;
RT "Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera
RT elsdenii.";
RL Biochemistry 34:2163-2171(1995).
CC -!- FUNCTION: Has an optimum specificity for 4-carbon length fatty acyl-
CC CoAs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC ChEBI:CHEBI:87488; EC=1.3.8.1;
CC Evidence={ECO:0000250|UniProtKB:P52042};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L04528; AAA03594.1; -; Unassigned_DNA.
DR RefSeq; WP_014017064.1; NZ_NQMW01000006.1.
DR PDB; 1BUC; X-ray; 2.50 A; A/B=1-383.
DR PDBsum; 1BUC; -.
DR AlphaFoldDB; Q06319; -.
DR SMR; Q06319; -.
DR DrugBank; DB03059; Acetoacetyl-CoA.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR GeneID; 36311878; -.
DR BioCyc; MetaCyc:MON-11937; -.
DR EvolutionaryTrace; Q06319; -.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Oxidoreductase.
FT CHAIN 1..383
FT /note="Acyl-CoA dehydrogenase, short-chain specific"
FT /id="PRO_0000201190"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT MUTAGEN 367
FT /note="E->Q: Loss of activity."
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:1BUC"
FT TURN 23..27
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:1BUC"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 213..223
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1BUC"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 235..271
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 283..312
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 317..342
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:1BUC"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1BUC"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:1BUC"
SQ SEQUENCE 383 AA; 41408 MW; 3D68AAE34D9BBAB8 CRC64;
MDFNLTDIQQ DFLKLAHDFG EKKLAPTVTE RDHKGIYDKE LIDELLSLGI TGAYFEEKYG
GSGDDGGDVL SYILAVEELA KYDAGVAITL SATVSLCANP IWQFGTEAQK EKFLVPLVEG
TKLGAFGLTE PNAGTDASGQ QTIATKNDDG TYTLNGSKIF ITNGGAADIY IVFAMTDKSK
GNHGITAFIL EDGTPGFTYG KKEDKMGIHT SQTMELVFQD VKVPAENMLG EEGKGFKIAM
MTLDGGRIGV AAQALGIAEA ALADAVEYSK QRVQFGKPLC KFQSISFKLA DMKMQIEAAR
NLVYKAACKK QEGKPFTVDA AIAKRVASDV AMRVTTEAVQ IFGGYGYSEE YPVARHMRDA
KITQIYEGTN EVQLMVTGGA LLR
