GenomeNet

Database: UniProt
Entry: Q2T5D8_BURTA
LinkDB: Q2T5D8_BURTA
Original site: Q2T5D8_BURTA 
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}.
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; 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
//
DBGET integrated database retrieval system