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Database: UniProt
Entry: R4WNK9_9BURK
LinkDB: R4WNK9_9BURK
Original site: R4WNK9_9BURK 
ID   R4WNK9_9BURK            Unreviewed;       545 AA.
AC   R4WNK9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Putative 2-keto-gluconate dehydrogenase {ECO:0000313|EMBL:BAN26129.1};
GN   ORFNames=BRPE64_CCDS00460 {ECO:0000313|EMBL:BAN26129.1};
OS   Caballeronia insecticola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN26129.1, ECO:0000313|Proteomes:UP000013966};
RN   [1] {ECO:0000313|Proteomes:UP000013966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA   Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA   Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT   "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT   Symbiont of the Bean Bug Riptortus pedestris.";
RL   Genome Announc. 1:340-344(2013).
RN   [2] {ECO:0000313|EMBL:BAN26129.1, ECO:0000313|Proteomes:UP000013966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RPE64 {ECO:0000313|EMBL:BAN26129.1};
RX   PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA   Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA   Peeters C., Kikuchi Y., Vandamme P.;
RT   "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT   bug Riptortus pedestris.";
RL   Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; AP013060; BAN26129.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4WNK9; -.
DR   STRING; 758793.BRPE64_CCDS00460; -.
DR   KEGG; buo:BRPE64_CCDS00460; -.
DR   PATRIC; fig|758793.3.peg.4374; -.
DR   HOGENOM; CLU_008878_4_0_4; -.
DR   Proteomes; UP000013966; Chromosome 3.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
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          108..327
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          413..531
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   545 AA;  59572 MW;  12FD284364626170 CRC64;
     MNDAPVSGYE QRNYAETDMD QGNKVQYKHG DGNVVVIIGS GAGGGTLANE LAQKGIDVVV
     LEAGKLHTQG DFSTSEWDAF KMLSWLDTRT TSGTWRVAKD FPNLPAWICK TVGGTTTHWA
     GASLRIQPHE FKAKTNYGDI QGANLLDWPI TRADLDPYYD RAEKKMGVTR TNGLPGLPGN
     NNFKVMSAGA TKVGYKECNT GHMAINSTVR DDRTHCFQRG FCFQGCRMGA KWSTLYTELP
     RAQATGHMEL RSGAHVVKIE HDAHGKATGV VYYDADGRLQ RQKARVVAVA GNAIETPRLL
     FNSESSKFPD GLANGSGQLG RNYMRHTTGS VYGVFNEKVE MFKGTTMAGI IEDEAVFDPK
     RGFAGGYHME TISLGLPFYA AFLDPGAWGP NFTAALDAYP YTAGMWIVGE DMPRESNRIT
     LNTSVKDQYG LPVPNVHFDD HPNDEAMREH AFKQGSAVYE AAGAKATYIV PPYPSTHNLG
     TARMSARPED GVCNAHGQTH EVANLFISDG SQFTTGAAEN PTLTIVTLAI RQADYISQQM
     KQRRV
//
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