ID   A0A0F2SL77_9FIRM        Unreviewed;       460 AA.
AC   A0A0F2SL77;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KJS50232.1};
GN   ORFNames=VR66_04000 {ECO:0000313|EMBL:KJS50232.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS50232.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS50232.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS50232.1};
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   -!- 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:KJS50232.1}.
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DR   EMBL; LADV01000039; KJS50232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2SL77; -.
DR   PATRIC; fig|1629714.3.peg.5709; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          27..206
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   460 AA;  50473 MW;  92BDB87E938B1DA7 CRC64;
     MVQVLGKDRV KKELEDLICY SYDSTNMIEM PGVVVFPKTT IEVSSLLKIA THWRIPVTTR
     GGGTNLVGGT VPQEGTIVLS TQLFNQIVEV DEENLVAVVE PGLITRDLHR AVEARGLFYP
     PDPASLNMST IGGNVAENAG GPRGFKYGVT RDYLLGLTVV LMDGRIIKAG GRTIKNVSGY
     DLTRFFAGSE GTLGVITEIT VRLIPLPEYK RTMLVLFDEL GQAAETVSAI IKGKVVPTTL
     ELMDHEIIDL IEQRDPVGFP RDVGAAMLFE VDGGQNEVQA QIEKIERICL NQGARSVKLA
     ANQEEADNLW RGRRNAFGVM AQSFTNVYPE DATVPRNKVP EMIKRMKEIG KKFNVGMLIL
     GHMGDGNLHP NICINDDQPG ALERAEQAID ALFAAALECG GTLSGEHGIG RAKKKYLSWQ
     FDADTIAVMK ELKRTLDPYG LLNPGKIFEV DREEGHNNVR
//