ID   GCNK_GLUOX              Reviewed;         178 AA.
AC   Q5FQ97;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Gluconokinase {ECO:0000303|PubMed:20676631};
DE            EC=2.7.1.12 {ECO:0000269|PubMed:20676631};
DE   AltName: Full=Gluconate kinase {ECO:0000305};
GN   OrderedLocusNames=GOX1709 {ECO:0000312|EMBL:AAW61449.1};
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, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, 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: Phosphorylates gluconate to 6-phosphogluconate.
CC       {ECO:0000269|PubMed:20676631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC         Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC         EC=2.7.1.12; Evidence={ECO:0000269|PubMed:20676631};
CC   -!- ACTIVITY REGULATION: Activated by magnesium.
CC       {ECO:0000269|PubMed:20676631}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.56 mM for gluconate {ECO:0000269|PubMed:20676631};
CC         KM=67 uM for ATP {ECO:0000269|PubMed:20676631};
CC         Vmax=30 umol/min/mg enzyme {ECO:0000269|PubMed:20676631};
CC         Note=kcat is 9.8 sec(-1). {ECO:0000269|PubMed:20676631};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC       {ECO:0000269|PubMed:20676631}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20676631}.
CC   -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC       {ECO:0000305}.
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DR   EMBL; CP000009; AAW61449.1; -; Genomic_DNA.
DR   RefSeq; WP_011253231.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FQ97; -.
DR   SMR; Q5FQ97; -.
DR   STRING; 290633.GOX1709; -.
DR   EnsemblBacteria; AAW61449; AAW61449; GOX1709.
DR   KEGG; gox:GOX1709; -.
DR   eggNOG; COG3265; Bacteria.
DR   HOGENOM; CLU_077168_4_1_5; -.
DR   OMA; MLESQFA; -.
DR   UniPathway; UPA00792; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd02021; GntK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006001; Therm_gnt_kin.
DR   PANTHER; PTHR43442; PTHR43442; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01313; therm_gnt_kin; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Gluconate utilization; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..178
FT                   /note="Gluconokinase"
FT                   /id="PRO_0000434477"
FT   BINDING         19..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   178 AA;  19720 MW;  1D071BE600D7607B CRC64;
     MTEHETQMGL KPRFLVVMGV SGTGKTTVAT GLATRLGWHF QEGDALHPPA NVEKMSTGQP
     LTDADRAPWL ALCHDWLREQ VKAGHGAVLT CSALKRSYRE QLRGDDLPIE FVHIDTSTGE
     LADRLQRREG HFMPASLLPS QLATLEVPGD DEPVIRVSGE KHPDVVLEEL IRHFQAED