ID Q2T5D8_BURTA Unreviewed; 537 AA.
AC Q2T5D8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=GMC family oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=BTH_II1415 {ECO:0000313|EMBL:ABC34827.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC34827.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC34827.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000085; ABC34827.1; -; Genomic_DNA.
DR RefSeq; WP_009897186.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T5D8; -.
DR KEGG; bte:BTH_II1415; -.
DR HOGENOM; CLU_008878_4_1_4; -.
DR OMA; MAPYPST; -.
DR Proteomes; UP000001930; 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; 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 8..40
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 233..319
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 409..529
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 537 AA; 59400 MW; 68C3BDB2254B1432 CRC64;
MAETQQADVV VVGSGVAGAI VAHQLAMAGK SVILLEAGPR MPRWEIVERF RNQPDKMDFM
APYPSSAWAP HPEYAPPNDY LVLKGEHKFN SQYIRAVGGT TWHWAASAWR FIPNDFKMKT
VYGVGRDWPI QYDDLEHFYQ RAEEELGVWG PGAEEDLLSP RKAPYPMPPL PLSYNERTIK
AALNDHDPKY HVVTEPVARN SRPYDGRPTC CGNNNCMPIC PIGAMYNGIV HVEKAEQAGA
KLIENAVVHK LEVGPQKKIV AALYKDPKGA EHRVEGKYFV LAANGIETPK LMLMSTSHDF
PNGVGNSSDM VGRNLMDHPG TGVSFYASEK LWPGRGPQEM TSLIGFRDGP FRATEAAKKI
HLSNLSRIDQ ETQKIFKAGK LLKPAELDAQ IRDRSARYVQ FDCFHEILPQ PENRIVPSKT
ATDAIGIPRP EITYAIDDYV KRGAAHTREV YASAAQVLGG TDVVFNDEFA PNNHITGATI
MGADPRDSVV DKDCRTFDHP NLFISSSATM PTVGTVNVTL TIAALALRIS DQLKKEI
//