ID   Q0B8J1_BURCM            Unreviewed;       539 AA.
AC   Q0B8J1;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ABI89532.1};
GN   OrderedLocusNames=Bamb_3978 {ECO:0000313|EMBL:ABI89532.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI89532.1, ECO:0000313|Proteomes:UP000000662};
RN   [1] {ECO:0000313|Proteomes:UP000000662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000441; ABI89532.1; -; Genomic_DNA.
DR   RefSeq; WP_011658979.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0B8J1; -.
DR   GeneID; 69546897; -.
DR   KEGG; bam:Bamb_3978; -.
DR   PATRIC; fig|339670.21.peg.4255; -.
DR   eggNOG; COG2303; Bacteria.
DR   Proteomes; UP000000662; Chromosome 2.
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; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          10..42
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          235..321
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          411..531
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   539 AA;  59572 MW;  CD2992F0F285780B CRC64;
     MADTDTQKAD VVVVGSGVAG AIVAHQLAMA GKSVILLEAG PRMPRGEIVE RFRNQPDKTD
     FMAPYPSSPW APHPEYGPPN DYLVLKGEHK FNSQYIRAVG GTTWHWAASA WRFIPNDFKM
     KTVYGVGRDW PIQYDDLEHY YQRAEEELGV WGPGPEEDLY SPRKQAYPMP PLPLSFNEQT
     IKSALNGYDP KFHVVTEPVA RNSRPYDGRP TCCGNNNCMP ICPIGAMYNG IVHVEKAEQA
     GAKLIDSAVV YKLETGPDKR IVAAIYKDKT GADHRVEGKY FVVAANGIET PKILLMSANR
     DFPNGVANSS DMVGRNLMDH PGTGVSFYAS DKLWPGRGPQ EMTSLIGFRD GPFRATEAAK
     KIHLSNMSRI NQETQKIFKA GKLMKSDELD AQIRDRSARY VQFDCFHEIL PQPENRIVPS
     KTATDAIGIP RPEITYAIDD YVKRGAVHTR EVYATAAKVL GGTDVVFNDE FAPNNHITGS
     TIMGADARDS VVDKDCRTFD HPNLFISSSS TMPTVGTVNV TLTIAALALR MSDTLKKEV
//