ID Q63YG3_BURPS Unreviewed; 547 AA.
AC Q63YG3;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:CAH34212.1};
GN OrderedLocusNames=BPSL0224 {ECO:0000313|EMBL:CAH34212.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34212.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH34212.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH34212.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571965; CAH34212.1; -; Genomic_DNA.
DR RefSeq; WP_004550980.1; NZ_CP009538.1.
DR RefSeq; YP_106852.1; NC_006350.1.
DR AlphaFoldDB; Q63YG3; -.
DR STRING; 272560.BPSL0224; -.
DR KEGG; bps:BPSL0224; -.
DR PATRIC; fig|272560.51.peg.1488; -.
DR eggNOG; COG2303; Bacteria.
DR Proteomes; UP000000605; Chromosome 1.
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:UP000000605}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 254..268
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 547 AA; 58703 MW; 6C797CB909806BA0 CRC64;
MQYDYIIVGG GSGGASLAGR LADACPDATI ALIEAGGHTE RNLLVNMPVG IAALVPFKLG
TNYGYETVPQ PGLGGRRGYQ PRGRGLGGSS AINAMIYTRG HPLDYDEWEQ LGCTGWGWRD
VLPYFRRAEG NARGANEWHG ADGPLTVSDL RFRNPFSERF IAAAHEAGYP LNDDFNGEHQ
EGVGFYQVTH RDGSRCSVAR AYVYGRTRPN LHVIVDATVL RVVFDGKRAT GVEFARAGRT
EQLAARAEVI LSAGAFNTPQ LLMCSGVGPA AQLRRHGVAL VHDAPDVGEN LIDHIDFIIN
KRVNSSELVG ICMRGIAKMT PALFSYLSGR RGMMTSNVAE AGGFIKSEPG LDRPDLQLHF
CTALVDDHNR NMHWGFGYSL HVCALRPKSR GNVALASGDA RVAPLIDPRF FSDERDLDLL
VTGAKAMRRI LCAAPLASQG GRELYTDPGD TDAQLRAAIV AHADTIYHPV GTCRMGTDAR
AVVDPQLRVK GVDGLRVVDA SVMPTLIGGN TNAPTVMIAE RAADFIVAAR NGQAAPARER
IAATHGG
//
