GenomeNet

Database: UniProt
Entry: U7UPW0_9FIRM
LinkDB: U7UPW0_9FIRM
Original site: U7UPW0_9FIRM 
ID   U7UPW0_9FIRM            Unreviewed;       379 AA.
AC   U7UPW0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ERT60939.1};
DE            EC=1.3.8.1 {ECO:0000313|EMBL:ERT60939.1};
DE   Flags: Fragment;
GN   ORFNames=HMPREF1250_0012 {ECO:0000313|EMBL:ERT60939.1};
OS   Megasphaera vaginalis.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT60939.1, ECO:0000313|Proteomes:UP000017090};
RN   [1] {ECO:0000313|EMBL:ERT60939.1, ECO:0000313|Proteomes:UP000017090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT60939.1,
RC   ECO:0000313|Proteomes:UP000017090};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERT60939.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWXA01000013; ERT60939.1; -; Genomic_DNA.
DR   RefSeq; WP_023053225.1; NZ_AWXA01000013.1.
DR   AlphaFoldDB; U7UPW0; -.
DR   STRING; 1111454.HMPREF1250_0012; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000017090; Unassembled WGS sequence.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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:UP000017090}.
FT   DOMAIN          6..117
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..373
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   NON_TER         379
FT                   /evidence="ECO:0000313|EMBL:ERT60939.1"
SQ   SEQUENCE   379 AA;  41321 MW;  FDF056BE00D3406C CRC64;
     MDFNCTEDQE MFVKLAKDFG VKKLLPTVTE RDHKHEYDEA LVEEMLGMGL AGTYFPEEFG
     GAGADVLSYI MTVEELAKYD AGVSITLSAT VSLCANPIWQ FGNEEQKKKY LTPLCEGTKL
     GAFGLTEPNA GTDASGQQTV AVKEGDYYVL NGSKIFITNG GAADIYIVFA MTDKTQGNKG
     ISAFILEKGM EGFTFGKKED KMGINTSQTM ELVFQDVKVP AENLLGEEGK GFKIAMMTLD
     GGRIGVAAQA LGIAEAALED AIKYSKERVQ FGKPLCKFQA ISFKLADMAT KIEAARLLVY
     KAAMKKQEGK PFSVDAAMAK MYASDIAMEV TVDAVQIFGG YGYSEEYPVA RHMRDAKITQ
     IYEGTNEVQR MVTSGALLR
//
DBGET integrated database retrieval system