ID A7ZSW9_ECO24 Unreviewed; 175 AA.
AC A7ZSW9;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=gntK {ECO:0000313|EMBL:ABV21043.1};
GN OrderedLocusNames=EcE24377A_3915 {ECO:0000313|EMBL:ABV21043.1};
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV21043.1, ECO:0000313|Proteomes:UP000001122};
RN [1] {ECO:0000313|Proteomes:UP000001122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX PubMed=18676672; DOI=10.1128/JB.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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}.
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DR EMBL; CP000800; ABV21043.1; -; Genomic_DNA.
DR RefSeq; WP_000108330.1; NC_009801.1.
DR AlphaFoldDB; A7ZSW9; -.
DR SMR; A7ZSW9; -.
DR GeneID; 75202281; -.
DR KEGG; ecw:EcE24377A_3915; -.
DR HOGENOM; CLU_077168_1_0_6; -.
DR Proteomes; UP000001122; Chromosome.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363066}.
SQ SEQUENCE 175 AA; 19543 MW; 5859A38413E8A586 CRC64;
MSTTNHDHHI YVLMGVSGSG KSAVASEVAH QLHAAFLDGD FLHPRRNIEK MASGEPLNDD
DRKPWLQALN DAAFAMQRTN KVSLIVCSAL KKHYRDLLRE GNPNLSFIYL KGDFDVIESR
LKARKGHFFK TQMLVTQFET LQEPGADETD VLVVDIDQPL EGVVASTIEV IKKGK
//