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}.
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; 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
//