ID   GMDH_GLUOX              Reviewed;         266 AA.
AC   Q5FPE5;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glucose 1-dehydrogenase {ECO:0000305};
DE            EC=1.1.1.119 {ECO:0000269|PubMed:20676631};
GN   OrderedLocusNames=GOX2015 {ECO:0000312|EMBL:AAW61751.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=621H;
RX   PubMed=20676631; DOI=10.1007/s00253-010-2779-9;
RA   Rauch B., Pahlke J., Schweiger P., Deppenmeier U.;
RT   "Characterization of enzymes involved in the central metabolism of
RT   Gluconobacter oxydans.";
RL   Appl. Microbiol. Biotechnol. 88:711-718(2010).
CC   -!- FUNCTION: Oxidizes both D-glucose and D-mannose, but is 15 times more
CC       catalytically efficient with mannose. Strictly dependent on NADP.
CC       {ECO:0000269|PubMed:20676631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.119; Evidence={ECO:0000269|PubMed:20676631};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.47 mM for mannose {ECO:0000269|PubMed:20676631};
CC         KM=29.6 mM for glucose {ECO:0000269|PubMed:20676631};
CC         KM=27.7 uM for NADP {ECO:0000269|PubMed:20676631};
CC         Vmax=178 umol/min/mg enzyme {ECO:0000269|PubMed:20676631};
CC         Note=kcat is 84.8 sec(-1) with glucose as substrate. kcat is 106
CC         sec(-1) with mannose as substrate. {ECO:0000269|PubMed:20676631};
CC   -!- SUBUNIT: Homotetramer or homooctamer. {ECO:0000269|PubMed:20676631}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CP000009; AAW61751.1; -; Genomic_DNA.
DR   RefSeq; WP_011253528.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FPE5; -.
DR   SMR; Q5FPE5; -.
DR   STRING; 290633.GOX2015; -.
DR   EnsemblBacteria; AAW61751; AAW61751; GOX2015.
DR   KEGG; gox:GOX2015; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_3_5; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..266
FT                   /note="Glucose 1-dehydrogenase"
FT                   /id="PRO_0000434581"
FT   ACT_SITE        162
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|UniProtKB:P40288"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  28678 MW;  125CBA2E69B7AD35 CRC64;
     MPAPYKDRFA GKKVLVTGAS QGIGEATALR FAEEGAQVAL NGRKEDKLIA VREKLPKVSG
     GEHPIATGDI SKEDDVKRLV AESIKAMGGL DVLVCNAGYQ IPSPSEDIKL EDFEGVMAVN
     VTGVMLPCRE VIRYWLENGI KGTIIVNSSV HQIIPKPHYL GYSASKGAVG NIVRTLALEY
     ATRGIRVNAV APGAIVTPIN MSWIDDPEQY KAVSSHIPMK RPGESREIAD AITFLAAEDS
     TYITGQTLYV DGGLTLYGDF ENNWSS