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Database: UniProt
Entry: A0A127W3B4_SPOPS
LinkDB: A0A127W3B4_SPOPS
Original site: A0A127W3B4_SPOPS 
ID   A0A127W3B4_SPOPS        Unreviewed;       396 AA.
AC   A0A127W3B4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:AMQ08045.1};
GN   ORFNames=AZE41_20075 {ECO:0000313|EMBL:AMQ08045.1};
OS   Sporosarcina psychrophila (Bacillus psychrophilus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ08045.1, ECO:0000313|Proteomes:UP000071057};
RN   [1] {ECO:0000313|EMBL:AMQ08045.1, ECO:0000313|Proteomes:UP000071057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ08045.1,
RC   ECO:0000313|Proteomes:UP000071057};
RA   Yan W.;
RT   "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT   psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL   Submitted (MAR-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}.
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DR   EMBL; CP014616; AMQ08045.1; -; Genomic_DNA.
DR   RefSeq; WP_067213383.1; NZ_CP014616.1.
DR   AlphaFoldDB; A0A127W3B4; -.
DR   STRING; 1476.AZE41_20075; -.
DR   KEGG; spsy:AZE41_20075; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000071057; 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; 3.
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          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..373
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   396 AA;  44024 MW;  C92B4BADBC3109C2 CRC64;
     MDFGFTEEQK MLRKTARQFV DAEIMPHIQK WDAQGGFDQA IWKKLADLGF MGVCIPEKYG
     GSGMDYNSLA ILCEELERGD TAFRTAVSVH IGLNSMSLLQ WGDEEQKQKY LVPQAKGEKI
     GAFGLTEPGA GSDVAAMATT AVRDGDDYVL NGQKTWISLC DVADHFLVFA YTDKAKKHHG
     ISAFIVERTT PGFSSKAIKG KYGIRAGNTG ELFFEDMRIP AANLVGEEGD GFKIAMASLD
     NGRFTVAAGA VGLIMGCLEE SVKYCHARET FGKEIGRHQL VQQMIANMEA GYQMSRLLVY
     RAGDMKNNGL RNTRETSLAK WQACDFANKA ADDAFQIHGA YGYSDEYPVA RFLRNSKAPV
     IYEGTREIHT VMQAEYVLGY REDKKLSNRL PEWPFE
//
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