ID   Q2YIV2_BRUA2            Unreviewed;       532 AA.
AC   Q2YIV2;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase:Pyridine nucleotide-disulphide oxidoreductase, class I:GMC oxidoreductase {ECO:0000313|EMBL:CAJ12443.1};
DE            EC=1.1.99.- {ECO:0000313|EMBL:CAJ12443.1};
GN   OrderedLocusNames=BAB2_0277 {ECO:0000313|EMBL:CAJ12443.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12443.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ12443.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ12443.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040265; CAJ12443.1; -; Genomic_DNA.
DR   RefSeq; WP_002965689.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YIV2; -.
DR   STRING; 359391.BAB2_0277; -.
DR   GeneID; 3827764; -.
DR   KEGG; bmf:BAB2_0277; -.
DR   PATRIC; fig|359391.11.peg.2228; -.
DR   HOGENOM; CLU_002865_7_1_5; -.
DR   PhylomeDB; Q2YIV2; -.
DR   PHI-base; PHI:9126; -.
DR   Proteomes; UP000002719; Chromosome II.
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   Oxidoreductase {ECO:0000313|EMBL:CAJ12443.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002719}.
FT   DOMAIN          254..268
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         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   532 AA;  58227 MW;  F1580158DA9EBB98 CRC64;
     MTDTYDYIVV GAGTAGCALA NRLSADQNRS VLLLEAGGKD NYAWIHIPVG YLYCIGNPRT
     DWCFTTEAEP GLNGRSLNYP RGKVLGGCSS INGMIYMRGQ ACDYDLWRQA GCDGWGWDDV
     LPLFKKSEDY FAGASALHGM GGEWRVENAR LHWDILDAFR DAALAAGIPA TDDFNRGDNE
     GVSYFKVNQK HGIRWNTAKA FLRPALDRKN LTVETGAHVR CIEIEGLRAT GVTFDQDGNI
     RTVKARREVI LAAGAVGSPQ ILELSGIGRG DVLQQAGIPL KLERRQLGEN LQDHLQLRCA
     YKVTGIATLN EKASTLVGKA MIGLEYLLRR SGPMAMAPSQ LGVFTRSDPS YETANLQYHV
     QPLSLEKFGD AVHPFPTFTA SVCNLRPESR GSIHIKSPDH RAQPAIRPNY LATETDRRIA
     ADAIRLTRHI VSQAPLQKYR PEEFKPGPNY ATQEDLEKAA GDIGTTIFHP VGTCRMGQDA
     EAIVDPRLRF NGIAGLRVAD ASIMPAITSG NTNSPTLMIA EKAAQMIIAD NR
//