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Database: UniProt
Entry: H2FXW6_OCESG
LinkDB: H2FXW6_OCESG
Original site: H2FXW6_OCESG 
ID   H2FXW6_OCESG            Unreviewed;       549 AA.
AC   H2FXW6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:AEY01120.1};
GN   OrderedLocusNames=GU3_06820 {ECO:0000313|EMBL:AEY01120.1};
OS   Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Oceanimonas.
OX   NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY01120.1, ECO:0000313|Proteomes:UP000007742};
RN   [1] {ECO:0000313|EMBL:AEY01120.1, ECO:0000313|Proteomes:UP000007742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GK1 {ECO:0000313|EMBL:AEY01120.1,
RC   ECO:0000313|Proteomes:UP000007742};
RX   PubMed=22461556; DOI=10.1128/JB.00023-12;
RA   Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA   Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT   "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT   from Gavkhouni Wetland in Iran.";
RL   J. Bacteriol. 194:2123-2124(2012).
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}.
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DR   EMBL; CP003171; AEY01120.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2FXW6; -.
DR   STRING; 511062.GU3_06820; -.
DR   KEGG; oce:GU3_06820; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   Proteomes; UP000007742; Chromosome.
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; 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:UP000007742}.
FT   DOMAIN          256..270
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         220
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   549 AA;  60262 MW;  CC6974D0B4298A2F CRC64;
     MSMEFDFIIV GAGSAGCILA SRLSESGRHS VLLLEAGEKD SSPWFKLPVG FAKTYYNPRY
     NYMYYSEEEA GMAGRKVYAP RGKVQGGSGS INAMIYVRGQ ASDFDDWAAA GNEGWSYREV
     LPYFKKLEQH PAGDNEFHAS SGPIGITPMK GRAHPICDYY LRAAEQLGWP LNDDFNGAGV
     EGAGIYETNI RNGQRDSSNT AYLKPALSRP NLSLQRVSMV QRVLVDEQQQ ATGVEVLYQG
     RLQQYRARRE VILSAGAVDS PKLLQLSGIG DRATLTCHGI EVRCHLPAVG ENLQDHLCVS
     YYYRANMKTL NDTFRSFWGK AWSGLEYLIN RSGPLSMSVN QAGGFFRGSD TEQAPNIQLY
     FNPMSYQIPK DSNARLEPEP YSGFLVAFNA CRPTSKGRIE LASSNPQHAA LIKPNYLSTD
     KDINEVIQGS RLIRALMQAP ALREITAEEV LPGKAVESEE EMLTYFRENA GSIYHLCGSC
     AMGPDPRTAV VDSRLRVHGL NGLRVIDASI FPSITSGNTN AATMMVAEKG ADMVLADHAD
     SAGRGHVDS
//
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