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Database: UniProt
Entry: A0A085F396_9BURK
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ID   A0A085F396_9BURK        Unreviewed;       169 AA.
AC   A0A085F396;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Gluconokinase {ECO:0000256|ARBA:ARBA00012054, ECO:0000256|RuleBase:RU363066};
DE            EC=2.7.1.12 {ECO:0000256|ARBA:ARBA00012054, ECO:0000256|RuleBase:RU363066};
GN   Name=idnK {ECO:0000313|EMBL:KFC65941.1};
GN   ORFNames=FG94_03499 {ECO:0000313|EMBL:KFC65941.1};
OS   Massilia sp. LC238.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC65941.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC65941.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC65941.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001329,
CC         ECO:0000256|RuleBase:RU363066};
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC       {ECO:0000256|ARBA:ARBA00004875}.
CC   -!- SIMILARITY: Belongs to the gluconokinase GntK/GntV family.
CC       {ECO:0000256|ARBA:ARBA00008420, ECO:0000256|RuleBase:RU363066}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFC65941.1}.
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DR   EMBL; JNNN01000065; KFC65941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085F396; -.
DR   STRING; 1502852.FG94_03499; -.
DR   PATRIC; fig|1502852.3.peg.3445; -.
DR   eggNOG; COG3265; Bacteria.
DR   Proteomes; UP000028601; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd02021; GntK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR031322; Shikimate/glucono_kinase.
DR   InterPro; IPR006001; Therm_gnt_kin.
DR   NCBIfam; TIGR01313; therm_gnt_kin; 1.
DR   PANTHER; PTHR43442; GLUCONOKINASE-RELATED; 1.
DR   PANTHER; PTHR43442:SF3; GLUCONOKINASE-RELATED; 1.
DR   Pfam; PF01202; SKI; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363066};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU363066};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363066};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363066}.
SQ   SEQUENCE   169 AA;  18682 MW;  C2418AADD9E5C078 CRC64;
     MDKRTAWVVM GVSACGKSDI GTRLAQALGA PFIEGDRFHP PENVAKMSAG IPLDDEDRGG
     WLQALRAEIE RAWQTDPVVV LSCSALKRAY RDVLRGDDGD VRFVHLHGDR DLIAQRMAAR
     SGHFMPVSLL DSQLRTLEPL QPDERGVTLD VREPPQRLVE QVMATRGAS
//
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