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   03-AUG-2022, entry version 121.
DE   RecName: Full=Gluconate 5-dehydrogenase {ECO:0000305|PubMed:7751271};
DE            EC=1.1.1.- {ECO:0000269|PubMed:7751271};
DE   AltName: Full=D-gluconate 5-dehydrogenase (NADP) {ECO:0000305|PubMed:7751271};
DE   AltName: Full=Gluconate:NADP 5-oxidoreductase {ECO:0000303|PubMed:7751271};
DE            Short=GNO {ECO:0000303|PubMed:7751271};
GN   Name=gno {ECO:0000303|PubMed:7751271}; OrderedLocusNames=GOX2187;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-19, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 19357 / DSM 3503 / JCM 7642 / NBRC 14819 / LMG 1408 / NCIMB
RC   9013;
RX   PubMed=7751271; DOI=10.1128/jb.177.10.2637-2643.1995;
RA   Klasen R., Bringer-Meyer S., Sahm H.;
RT   "Biochemical characterization and sequence analysis of the gluconate:NADP
RT   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: Catalyzes the reversible NADP-dependent oxidation of
CC       gluconate to 5-ketogluconate. Is involved in the non-phosphorylative,
CC       ketogenic oxidation of glucose. Is almost inactive with NAD as
CC       cosubstrate. Displays high substrate specificity since D-Glucose, D-
CC       sorbitol, and D-mannitol are not oxidized by the enzyme, and 2-
CC       ketogluconate and L-sorbose are not reduced. Can accept D-fructose as a
CC       substrate, with a rate that is only 10% of the rate of 5-ketogluconate
CC       reduction. {ECO:0000269|PubMed:7751271}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:23936, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58143, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000269|PubMed:7751271};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20.6 mM for gluconate {ECO:0000269|PubMed:7751271};
CC         KM=73 uM for NADP {ECO:0000269|PubMed:7751271};
CC       pH dependence:
CC         Optimum pH is 10.0 for gluconate oxidation. Optimum pH is 5.0 for 5-
CC         ketogluconate reduction. {ECO:0000269|PubMed:7751271};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7751271}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7751271}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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; X80019; CAA56322.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW61923.1; -; Genomic_DNA.
DR   PIR; A57149; A57149.
DR   RefSeq; WP_011253698.1; NZ_LT900338.1.
DR   AlphaFoldDB; P50199; -.
DR   SMR; P50199; -.
DR   STRING; 290633.GOX2187; -.
DR   EnsemblBacteria; AAW61923; AAW61923; GOX2187.
DR   KEGG; gox:GOX2187; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_1_5; -.
DR   OMA; FPQWGAY; -.
DR   BioCyc; MetaCyc:MON-17960; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008874; F:gluconate 5-dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Gluconate 5-dehydrogenase"
FT                   /id="PRO_0000054701"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         15..39
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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