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Database: UniProt
Entry: A0A075JMA7_9BACI
LinkDB: A0A075JMA7_9BACI
Original site: A0A075JMA7_9BACI 
ID   A0A075JMA7_9BACI        Unreviewed;       401 AA.
AC   A0A075JMA7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AIF42507.1};
GN   ORFNames=X953_03845 {ECO:0000313|EMBL:AIF42507.1};
OS   Virgibacillus sp. SK37.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF42507.1, ECO:0000313|Proteomes:UP000027985};
RN   [1] {ECO:0000313|EMBL:AIF42507.1, ECO:0000313|Proteomes:UP000027985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK37 {ECO:0000313|EMBL:AIF42507.1,
RC   ECO:0000313|Proteomes:UP000027985};
RA   Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT   "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT   halophilic bacterium isolated from Thai fish sauce fermentation.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP007161; AIF42507.1; -; Genomic_DNA.
DR   RefSeq; WP_040954401.1; NZ_CP007161.1.
DR   AlphaFoldDB; A0A075JMA7; -.
DR   STRING; 403957.X953_03845; -.
DR   KEGG; vir:X953_03845; -.
DR   HOGENOM; CLU_018204_0_2_9; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000027985; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
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   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027985}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          230..374
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   401 AA;  44615 MW;  0603526703E797B9 CRC64;
     MDFNFSEEQT MLRKTVRDFT DKEIMPYIGQ WDREGKFDPA ILTKLASLGL MGVCIPEEYG
     GSGMDYNSLA IVCEELERGD TAFRTAVSVH TGLNSMTLLQ WGTEEQKQKY LVPQAKGEKI
     GAFGLTEPAA GSDVSALQST AQKQGDYYIL NGQKTWISLC DTADHFLVFA YTGDRAEKHK
     AISAFIVERT WDGFSSKATK GKLGIRAGNT GELFFENVKV PKENLLGEEG EGFKIAMAAL
     DNGRFTVAAG AVGQIMACLE ASVKYCQERE TFGKSIGKHQ LVQQMIANME AGLQMSRLLV
     YRAGELKNDG KRNTRETSLA KWQACDFANK AADDAVQIHG AYGFSDEYPV ERYLRNSKAP
     VIYEGTREIH TVMQAEYVLG YRKDKELNRM LPAWGQSQLI K
//
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