ID A0A150L9J9_9BACI Unreviewed; 400 AA.
AC A0A150L9J9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KYD09023.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:KYD09023.1};
GN ORFNames=B4135_3934 {ECO:0000313|EMBL:KYD09023.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD09023.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD09023.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD09023.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
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:KYD09023.1}.
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DR EMBL; LQYT01000133; KYD09023.1; -; Genomic_DNA.
DR RefSeq; WP_061570063.1; NZ_LZRR01000052.1.
DR AlphaFoldDB; A0A150L9J9; -.
DR STRING; 301148.B4135_3934; -.
DR PATRIC; fig|301148.3.peg.2001; -.
DR OrthoDB; 2985879at2; -.
DR Proteomes; UP000075683; 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 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}.
FT DOMAIN 7..120
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 131..226
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 248..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 400 AA; 43971 MW; 8F509AAB85E06A6F CRC64;
MISFELSERQ KQMQELAHWF AEHEIRPIAM EAERLKQVPG DWLEKVNKMG IHLNPSSFAG
GRGKSGGTKK ENEANRMGVI AMEELAWGDA AVTLSLPGPG LGGPPIQTSG TDEQKERFLS
IFTADEPRWG AYALTEPEAG SDASAIRTTA RKTEGGYILN GQKIFITNGA RASWVVVFAT
VDPGLGRLGQ RAFVVEKGTK GFSAPKIVEK MGLRANETAE LLFEDCFVPE ENLLGGEALY
ERKAAKTAGF QVAMKTFDST RPIVAAMAVG IARAAFEYTL DLVKREFPKQ GKFYRLAAEL
LAEAEQDIAA ARLLTWEAAW KADLGMENAK EAAMCKAFAG KIALAVCAKC LELLGPAGLQ
DHPVEKWYRD VKVFDIFEGT NEIQHLVIAR RQYAPYRIRV
//
