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Database: UniProt
Entry: F0G0J9_9BURK
LinkDB: F0G0J9_9BURK
Original site: F0G0J9_9BURK 
ID   F0G0J9_9BURK            Unreviewed;       513 AA.
AC   F0G0J9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Putative GMC oxidoreductase {ECO:0000313|EMBL:EGD04981.1};
DE   Flags: Fragment;
GN   ORFNames=B1M_08722 {ECO:0000313|EMBL:EGD04981.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD04981.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGD04981.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGD04981.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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}.
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:EGD04981.1}.
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DR   EMBL; AEXE01000455; EGD04981.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0G0J9; -.
DR   PATRIC; fig|987057.7.peg.1421; -.
DR   Proteomes; UP000003049; 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; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          216..230
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGD04981.1"
SQ   SEQUENCE   513 AA;  56467 MW;  12F3D8290F37BB2B CRC64;
     PDRYMWIHVP IGYGKTMFHP VYNWGFHTDP DPNMHNRRLY WPRGRTLGGC SSINGLIYVR
     GQRQDYDHWA ALGNRGWSWR ECLPYFRRLE HNTLGDGPTR GTGGPLWAST IRQRHELVDA
     FVAASNRLGV RTVDDFNTGD QEGVGYYQLT TRNGLRCSTA VAYLKPARGR PNLHVETDAQ
     ALKVLFDGTQ ASGVRYVRHG ELDEVRARRE VVLAAGALQS PQLLQVSGVG PAALLNRHGI
     AVVADRAGVG ENLQDHLQIR LIYEVTKPIT TNDALHSWVG RAKMGLQWAL LRGGPLAVGI
     NQGGMFCRAL PEESATPDIQ FHFSTLSADS AGGSVHAFPG CTYSICQLRP ESRGSVRIRS
     DDARDAPSIQ PNYLDTERDR RTTVAGVRFA RRVAATEPMA SLMKREVRPG ADAQTDDELL
     EFCREYGQTI FHPSGTAKMG VASDPLAVVD ERLRVYGTRG LRVVDCSIMP TLVSGNTNVP
     IVMVAEKASD MILEDAREVD RGCSVVPAAV AVA
//
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