ID   GNO_GLUOX               Reviewed;         256 AA.
AC   P50199; Q5FNX3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Gluconate 5-dehydrogenase;
DE            EC=1.1.1.69;
DE   AltName: Full=5-keto-D-gluconate 5-reductase;
GN   Name=gno; OrderedLocusNames=GOX2187;
OS   Gluconobacter oxydans (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-19, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 19357 / DSM 3503 / IFO 14819 / LMG 1408 / NCIB 9013;
RX   MEDLINE=95270578; PubMed=7751271;
RA   Klasen R., Bringer-Meyer S., Sahm H.;
RT   "Biochemical characterization and sequence analysis of the
RT   gluconate:NADP 5-oxidoreductase gene from Gluconobacter oxydans.";
RL   J. Bacteriol. 177:2637-2643(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: Involved in the non-phosphorylative, ketogenic oxidation
CC       of glucose and oxidizes gluconate to 5-ketogluconate. Dependent on
CC       NADP, almost inactive with NAD.
CC   -!- CATALYTIC ACTIVITY: D-gluconate + NAD(P)(+) = 5-dehydro-D-
CC       gluconate + NAD(P)H.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; X80019; CAA56322.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW61923.1; -; Genomic_DNA.
DR   PIR; A57149; A57149.
DR   RefSeq; YP_192579.1; -.
DR   HSSP; P08074; 1CYD.
DR   GeneID; 3250506; -.
DR   GenomeReviews; CP000009_GR; GOX2187.
DR   KEGG; gox:GOX2187; -.
DR   NMPDR; fig|290633.1.peg.2124; -.
DR   HOGENOM; P50199; -.
DR   OMA; P50199; NAGMQRR.
DR   BioCyc; GOXY290633:GOX2187-MON; -.
DR   BRENDA; 1.1.1.69; 3050.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008874; F:gluconate 5-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    256       Gluconate 5-dehydrogenase.
FT                                /FTId=PRO_0000054701.
FT   NP_BIND      15     39       NADP (By similarity).
FT   ACT_SITE    160    160       Proton acceptor (By similarity).
FT   BINDING     147    147       Substrate (By similarity).
SQ   SEQUENCE   256 AA;  27256 MW;  38B03C0399C0A07A CRC64;
     MSHPDLFSLS GARALVTGAS RGIGLTLAKG LARYGAEVVL NGRNAESLDS AQSGFEAEGL
     KASTAVFDVT DQDAVIDGVA AIERDMGPID ILINNAGIQR RAPLEEFSRK DWDDLMSTNV
     NAVFFVGQAV ARHMIPRGRG KIVNICSVQS ELARPGIAPY TATKGAVKNL TKGMATDWGR
     HGLQINGLAP GYFATEMTER LVADEEFTDW LCKRTPAGRW GQVEELVGAA VFLSSRASSF
     VNGQVLMVDG GITVSL
//