ID   A0A1J0WNT2_9RHOB        Unreviewed;       535 AA.
AC   A0A1J0WNT2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:APE45891.1};
GN   ORFNames=BOO69_20190 {ECO:0000313|EMBL:APE45891.1};
OS   Sulfitobacter alexandrii.
OG   Plasmid unnamed4 {ECO:0000313|EMBL:APE45891.1,
OG   ECO:0000313|Proteomes:UP000181897}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE45891.1, ECO:0000313|Proteomes:UP000181897};
RN   [1] {ECO:0000313|EMBL:APE45891.1, ECO:0000313|Proteomes:UP000181897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM1-D1 {ECO:0000313|EMBL:APE45891.1,
RC   ECO:0000313|Proteomes:UP000181897};
RC   PLASMID=unnamed4 {ECO:0000313|EMBL:APE45891.1,
RC   ECO:0000313|Proteomes:UP000181897};
RA   Yang Q., Zhang X., Tian X.;
RT   "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT   associated with marine dinoflagellate Alexandrium minutum in East China
RT   Sea.";
RL   Submitted (NOV-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, ECO:0000256|RuleBase:RU003968}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP018080; APE45891.1; -; Genomic_DNA.
DR   RefSeq; WP_071974203.1; NZ_CP018080.1.
DR   AlphaFoldDB; A0A1J0WNT2; -.
DR   KEGG; suam:BOO69_20190; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000181897; Plasmid unnamed4.
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; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 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   ECO:0000256|RuleBase:RU003968}; Plasmid {ECO:0000313|EMBL:APE45891.1}.
FT   DOMAIN          82..105
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          254..268
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         92..95
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   535 AA;  59130 MW;  61687A05C7FD26BF CRC64;
     MADYVVIGGG SSGGVVAARL SEDPNTTVTL LEAGGPGNSK FVSIPGMFAG LIQDYKINKL
     NWRFRTAPQK KLNNRSLYHP RGKMLGGSSG MNGMVYIRGE SGDYDRWSEL GNEGWSYDEV
     LPYFRKAENN ERGADDYHGD SGPLHVSNGD ESFDFYSAFL ASGEKLDYPK TADFNGANRE
     GLGIYQFTTK NGERASVKFC YLDPIMDRKN LDIQVKATVR RIVMEDGRAV AVEYDQDGQT
     KRVEVGKEVI VSGGAFGSPQ ILMLSGIGPR DELEKHGITV QHELPGVGEN LHDHPDVMFV
     FKSKKRTGIS LGPLGTLKNL AAFYQYFTKR KGWLANPPTA AGGFLRSEPG KNNPDFQLHM
     VPLPYRNHAH DYMSMIKWGF TMIVNIGHPR SRGRLTLKDA NPGSEPNIDL NLLDHVDDLK
     DMRNAFKVTQ EILHGPPLKD KIAKPLYPKR YLDTDAEIDD FLRAEVNHAY HPVGTCKMGR
     DDMAVVDARL KVRGLANVRV ADASIMPEII NGNTNATCIM IGEKAADMIK QDAAA
//