ID A9M9C9_BRUC2 Unreviewed; 494 AA.
AC A9M9C9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ABX63076.1};
GN OrderedLocusNames=BCAN_A2091 {ECO:0000313|EMBL:ABX63076.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX63076.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX63076.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) 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; CP000872; ABX63076.1; -; Genomic_DNA.
DR RefSeq; WP_004692082.1; NC_010103.1.
DR AlphaFoldDB; A9M9C9; -.
DR GeneID; 55591616; -.
DR KEGG; bcs:BCAN_A2091; -.
DR HOGENOM; CLU_008878_4_2_5; -.
DR PhylomeDB; A9M9C9; -.
DR Proteomes; UP000001385; Chromosome I.
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; 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; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 79..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 426..483
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 494 AA; 54315 MW; 73EDFD4F809E19C1 CRC64;
MGGQPDIVII GSGIGGATMA AGLAASGADI LILEAGARLA DRPENRDPRA IFQRGFFRPK
ELWYETSGAP FNPGNYYNVG GNSKFYGAVL IRYRREDFEE LAHLEGVSPT WPFSYDELEP
WYCKAEELFQ VRGELGDDPT EPHHSKPYPY AAIRDERPIA DMRARLKKAG LHPASLPLGV
DIERWLAKAR TPWDAHPNCD DGKMDAETCP LAQALQYANV RLETSAQVRR LEAGPDGKAI
TAVHYVKNGE ALVLRPKLVI LSAGAVQSAA LLLRSGLANR SDQVGRNFMN HNASAVIAFD
PRYRNDSVYQ KTFGFNDYYL SDGAGGPPLG NVQLLGRVSG AILKSNMRHV PEWLLNRIAG
HTIDFYAMSE DLPSPESRVS VDGDRIILHW VRSNWKAHLM LVEKLKSALR AVGFPVVLSR
AFDRCTPSHQ CGTARIGNDP ATAPLDPYCR AYDHPNLYVV DASFLPTSAA VNPALTIAAQ
ALRVADRIKR EGFA
//
