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Database: UniProt
Entry: L7VR99_9BACT
LinkDB: L7VR99_9BACT
Original site: L7VR99_9BACT 
ID   L7VR99_9BACT            Unreviewed;       542 AA.
AC   L7VR99;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Glucose-methanol-choline (GMC) oxidoreductase:NAD binding site {ECO:0000313|EMBL:AGC71487.1};
OS   uncultured bacterium A1Q1_fos_1880.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=1256556 {ECO:0000313|EMBL:AGC71487.1};
RN   [1] {ECO:0000313|EMBL:AGC71487.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Abrams M., Caldwell A., Vandaei E., Lee W., Perrott J., Khan S.Y., Ta J.,
RA   Romero D., Nguyen V., Pourmand N., Ouverney C.C.;
RT   "Metagenomic Characterization of a Microbial Community in Wastewater
RT   Detects High Levels of Antibiotic Resistance.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; JX649874; AGC71487.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7VR99; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..48
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          175..316
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          420..529
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   542 AA;  58846 MW;  B23A06037ECB627A CRC64;
     MAEPIRTQVV IVGAGVAGML VAYRLAQAGV QVVVLEAGPP VNRAEALATY RTALIKVPEA
     PYPDTPYAPR PTVADLEGYY VQEGPTLFKS TYVRRVGGTT WHWLGTSLRH LPADFQLQSR
     YGVAVDWPLT YAQLEPWYGA AERELGVAGD GKQDLGSPRT GEFPMQPLPL TYLDKQIALA
     AAKLGYTVHL TPQARNSVTY DGRPPCCGSS SCVPICPIGA KYDATVHVRK AQALGVQVID
     QAVVHFIEVD SAGQVTGIRF KRPDGSEERA EASIYVLAAH AIETPKLLLM SRTDALPNGV
     ANSSDQVGRN LMDHPVQLSW ALAKEPVYPY RSPLENAGIE DFRDGDFRRE RAAFRMAIGE
     DGWSFPGTTP TALAPELVKQ GLRGEALVAE LNRQVARQFR FANLIEQLPD PENRIVPAFD
     HLDALGLPRP RITYQLGEFV ERGMAEARRV SEQIFQAMGA TAIQHSEEHE GAGHVMGTYR
     MGNDPKTSVV TADQRCHDHP NLFLVGSGVF PTVGTANPTL TIAALALRAA ETIKAELTGG
     VT
//
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