ID A0A133SHT9_9FIRM Unreviewed; 387 AA.
AC A0A133SHT9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative butyryl-CoA dehydrogenase {ECO:0000313|EMBL:KXA69247.1};
GN ORFNames=HMPREF3201_01238 {ECO:0000313|EMBL:KXA69247.1};
OS Megasphaera sp. MJR8396C.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1603888 {ECO:0000313|EMBL:KXA69247.1, ECO:0000313|Proteomes:UP000070314};
RN [1] {ECO:0000313|EMBL:KXA69247.1, ECO:0000313|Proteomes:UP000070314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR9396C {ECO:0000313|EMBL:KXA69247.1,
RC ECO:0000313|Proteomes:UP000070314};
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:KXA69247.1}.
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DR EMBL; LRVC01000049; KXA69247.1; -; Genomic_DNA.
DR RefSeq; WP_062412144.1; NZ_KQ958179.1.
DR AlphaFoldDB; A0A133SHT9; -.
DR STRING; 1603888.HMPREF3201_01238; -.
DR PATRIC; fig|1603888.3.peg.1194; -.
DR Proteomes; UP000070314; 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 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; 1.
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}.
FT DOMAIN 7..113
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 126..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 233..380
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 387 AA; 41954 MW; 4AE1DAC9E1B6E5C9 CRC64;
MGYILNKDQQ DLVALARDFA EKKVAPFVHE LDEAKEPGQK LLDIYQEAVD IGFCGLEIPE
EYGGMGQDYY TVAAVYEELS KVDAGVATAI AASGLGLKPV LQHGNDAQKK LYAEYLTGEK
GSGFCAFCLT EANAGSDAAA GTTVAVKQGD EYVINGTKCF ITNGGVASVY TVFAITDKSK
GVKGISAFIV ERDRPGVSVG KEEDKMGIRL SNTTEVIFQD VHIPADHLIG EEGKGFVYAM
QTLDLARPMV ASLAVGIAQR AINEAVKYAK ERVTFGKPII KHEVISFKLA DMDMKTEVAR
SAIINFLNTY YAEPKRSYTR EAAIAKCFAG DISVEVALEA VQILGGFGYS REYPVEKLVR
DAKIMQIYEG TNEVQRMVIA GFVAAQK
//
