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Database: UniProt
Entry: A0A133Y011_9BACT
LinkDB: A0A133Y011_9BACT
Original site: A0A133Y011_9BACT 
ID   A0A133Y011_9BACT        Unreviewed;       379 AA.
AC   A0A133Y011;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KXB36500.1};
GN   ORFNames=HMPREF1869_00711 {ECO:0000313|EMBL:KXB36500.1};
OS   Bacteroidales bacterium KA00251.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1497953 {ECO:0000313|EMBL:KXB36500.1, ECO:0000313|Proteomes:UP000070662};
RN   [1] {ECO:0000313|EMBL:KXB36500.1, ECO:0000313|Proteomes:UP000070662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00251 {ECO:0000313|EMBL:KXB36500.1,
RC   ECO:0000313|Proteomes:UP000070662};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXB36500.1}.
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DR   EMBL; LSCS01000044; KXB36500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133Y011; -.
DR   STRING; 1497953.HMPREF1869_00711; -.
DR   PATRIC; fig|1497953.3.peg.701; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000070662; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 1.
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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000070662}.
FT   DOMAIN          6..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..377
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  41943 MW;  014A62903B26C593 CRC64;
     MDFSHTPQEL LFLQMIREFA EKEVKPLAAE IDEQERFPLE TVEKMGKIGL MGIPIPKEYG
     GAGATNQIYT MCVEELSRVC ATTGVVVSAH TSLCCSPILE FGTEEQKKKY LPKLASGEWI
     GAFGLTEPNA GTDASAQQTF AEERDDHYVL NGNKIFITNA QYGHVYVIFA MTDKSQGNKG
     ISAFIVEKGF PGFSIGKPEL KLGIRGSATC ELIMENCIVP KENLLGRVGQ GFKIAMKTLD
     GGRVGIASQA LGIAQGAMDE TVKYTKERKQ FGRSIAKFQN TQFQMADMQV RVDAARLLVR
     KAAYLKDQGQ PYSFEAAEAK LFAAETAMFV TTKAVQYHGG YGYTREYPVE RMMRDAKITE
     IYEGTSEVQR MVIASKLFK
//
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