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Database: UniProt
Entry: A0A1Y1RPD8_9MICC
LinkDB: A0A1Y1RPD8_9MICC
Original site: A0A1Y1RPD8_9MICC 
ID   A0A1Y1RPD8_9MICC        Unreviewed;       509 AA.
AC   A0A1Y1RPD8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ORC17442.1};
GN   ORFNames=A7979_03330 {ECO:0000313|EMBL:ORC17442.1};
OS   Rothia nasimurium.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=85336 {ECO:0000313|EMBL:ORC17442.1, ECO:0000313|Proteomes:UP000192359};
RN   [1] {ECO:0000313|EMBL:ORC17442.1, ECO:0000313|Proteomes:UP000192359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PT-32 {ECO:0000313|EMBL:ORC17442.1,
RC   ECO:0000313|Proteomes:UP000192359};
RA   Gaiser R.A., Van Baarlen P., Wells J.M.;
RT   "Draft genome sequence of a porcine commensal Rothia nasimurium.";
RL   Submitted (MAY-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|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:ORC17442.1}.
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DR   EMBL; LXWF01000033; ORC17442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1RPD8; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000192359; Unassembled WGS sequence.
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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192359}.
FT   DOMAIN          248..262
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         214
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   509 AA;  54891 MW;  D6ECCC5EF75F03FD CRC64;
     MTDFLIVGGG SAGAVLTRRL IDAGKTVTLV EAGLQEPNPD IDHLNDLGKL WHSDQDWDYF
     TSPQPGAHNR RLHLPRGKVL GGSHALNACI WVRGAAADYD SWAYLGNPGW GWNEVLPYFI
     KAENYDGGPS ESRGTDGLLD VRQDFSRSPL QESMVEAAQQ AGHKLNPDYN SGDPEGVSRM
     QLNVRDDKRF NVWHAYLKPV ADHENLTLIT GARVEKVLFE GTSAVGILMH TQEGRQEVYA
     SKVVLSAGAL GSPEILLRSG IGPARELRDL GIELVAEAPG VGKNLHDHLL VPVIYTADKP
     IPTPQVAPAE VHLFARSSPA QHLPDTQPIF FSFPMYSQAY GPGEMTGPAE AFTLMAGIVR
     PQSRGALTLT GSRLDDPVTV DLGVFEADAD LQAMVQSIKQ CRAIGRQPAL AEEWGATEIW
     PGPEVSDDEL EQYARDAVVT YHHQVGTCAM GTGTQAVVSP HNLAVYGVEN LHVIDASIMP
     IVPTGNTNAP SIMIAEKAAD ALMSADLGQ
//
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