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Database: UniProt
Entry: A0A095BA02_9SPHN
LinkDB: A0A095BA02_9SPHN
Original site: A0A095BA02_9SPHN 
ID   A0A095BA02_9SPHN        Unreviewed;       528 AA.
AC   A0A095BA02;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KGB59177.1};
GN   ORFNames=FG95_00083 {ECO:0000313|EMBL:KGB59177.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB59177.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB59177.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB59177.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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   -!- 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:KGB59177.1}.
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DR   EMBL; JNFC01000001; KGB59177.1; -; Genomic_DNA.
DR   RefSeq; WP_037553192.1; NZ_JNFC01000001.1.
DR   AlphaFoldDB; A0A095BA02; -.
DR   STRING; 1120705.FG95_00083; -.
DR   PATRIC; fig|1120705.3.peg.84; -.
DR   eggNOG; COG2303; Bacteria.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000029625; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT   DOMAIN          79..102
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          251..265
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         89..92
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         216
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   528 AA;  56756 MW;  B434AA8B60B442B4 CRC64;
     MDQFDIIVIG GGSAGSAAAG RLAEDGKRAV CLVEAGGRND NMLIKTPGFM PFIRNSSNYK
     YETVPQKGLN GRTGYQPRGR GLGGSSAINA MVYIRGHAFD YDQWESLGAT GWSYADVLPW
     FKRAEHNERG ADDFHGSGGP LNVMDQRWPN VTSRRFVESA AALQLPRTAD FNGASQEGFG
     LYQVTQKAGE RWSAARAYVE PLREHGNFAV RTGALVERIL IENGRATGVE IRRGSKRETL
     RARGGVVLSA GAFNSPQILM LSGIGPGAHL KDKGIAVALD RAGVGANLQD HIDYVSSWET
     RSADPFGDSA SGTWRMLKAI FEHRRQRTGI MTTCFAEAGG FWKSRPDLPA PDIQYHFVPA
     MLEDHGRTKV KGHGFSCHAC VLRPESRGSV TLASGDAAAA PVIDPGFLTD ARDMATLRAG
     VRMMHRIAAA PPLSDYAGVD RHPVDLDDDA ALDALIRARA DTVYHPVGTC RMGNDVDAVV
     DPALKLKGVE GLWVADASVM PRLVSGNTNA PSIMIGERAA DFVKAALA
//
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