ID A0A0F2PSG3_9FIRM Unreviewed; 379 AA.
AC A0A0F2PSG3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KJS15522.1};
GN ORFNames=VR69_13290 {ECO:0000313|EMBL:KJS15522.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS15522.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS15522.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS15522.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS15522.1}.
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DR EMBL; LADO01000051; KJS15522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PSG3; -.
DR STRING; 1629717.VR69_13290; -.
DR PATRIC; fig|1629717.3.peg.1727; -.
DR Proteomes; UP000033446; 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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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 5..116
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 120..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 227..376
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 379 AA; 41294 MW; A9E3484E25CAF6BD CRC64;
MIRLTEEQIM LRQMTRELAL EKFAPRAAEI DQTGEFPWDN VKLLADYELL GINVPEEYGG
AGSDTLSHAI AIEEVARVCG STSVILTTQA LAIAPVFLAG TDEQKKKYLT PMASGKVLGA
FGLTEPGAGS DASRISTTAA RDGDYYVLNG VKHFITNGGE AEIYTIVAMT DKSKGVKGIS
TFFVEKGTPG FTFGKKESKM GIRGSTTREL IFENCRIPKE NLLGREGEGF KIVMKSIDHT
RTGVAAQALG IAQGALDAAL EYSKQREQFG QPICEFQGIQ FMLADMATQI EAARALVYQS
AVAIDDHAED LSKISAMAKL FASDTAMKVT TDAVQIFGGY GYSTEYPVER YMRDAKITQI
YEGTNQIQRI VIARSLIKQ
//