ID   KDGK_ECOLI              Reviewed;         309 AA.
AC   P37647; P78117; Q2M7I8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   04-NOV-2026, entry version 169.
DE   RecName: Full=2-dehydro-3-deoxygluconokinase;
DE            EC=2.7.1.45;
DE   AltName: Full=2-keto-3-deoxygluconokinase;
DE   AltName: Full=3-deoxy-2-oxo-D-gluconate kinase;
DE   AltName: Full=KDG kinase;
GN   Name=kdgK; Synonyms=yhjI; OrderedLocusNames=b3526, JW5668;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=4944816; DOI=10.1016/s0300-9084(71)80118-9;
RA   Pouyssegur J., Stoeber F.;
RT   "Study of the common degradative pathway of hexuronates in Escherichia coli
RT   K 12. Purification, properties and individuality of 2-keto-3-deoxy-D-
RT   gluconnokinase.";
RL   Biochimie 53:771-781(1971).
CC   -!- FUNCTION: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate
CC       (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG).
CC       {ECO:0000269|PubMed:4944816}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-
CC         phospho-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:14797,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57569,
CC         ChEBI:CHEBI:57990, ChEBI:CHEBI:456216; EC=2.7.1.45;
CC         Evidence={ECO:0000269|PubMed:4944816};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 uM for ATP {ECO:0000269|PubMed:4944816};
CC         KM=1 uM for KDG {ECO:0000269|PubMed:4944816};
CC       pH dependence:
CC         Optimum pH is around 6. {ECO:0000269|PubMed:4944816};
CC   -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC       degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC       3-deoxy-D-gluconate: step 1/2.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18503.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00039; AAB18503.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76551.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77768.1; -; Genomic_DNA.
DR   PIR; S47747; S47747.
DR   RefSeq; NP_417983.2; NC_000913.3.
DR   RefSeq; WP_000037562.1; NZ_CP009789.1.
DR   AlphaFoldDB; P37647; -.
DR   SMR; P37647; -.
DR   BioGRID; 4262528; 10.
DR   BioGRID; 852349; 2.
DR   DIP; DIP-10056N; -.
DR   FunCoup; P37647; 488.
DR   IntAct; P37647; 5.
DR   STRING; 511145.b3526; -.
DR   jPOST; P37647; -.
DR   PaxDb; 511145-b3526; -.
DR   EnsemblBacteria; AAC76551; AAC76551; b3526.
DR   GeneID; 948041; -.
DR   KEGG; ecj:JW5668; -.
DR   KEGG; eco:b3526; -.
DR   KEGG; ecoc:C3026_19105; -.
DR   PATRIC; fig|511145.12.peg.3636; -.
DR   EchoBASE; EB2163; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_8_1_6; -.
DR   InParanoid; P37647; -.
DR   OMA; AAGYCCG; -.
DR   OrthoDB; 9776822at2; -.
DR   PhylomeDB; P37647; -.
DR   BioCyc; EcoCyc:DEOXYGLUCONOKIN-MONOMER; -.
DR   BioCyc; MetaCyc:DEOXYGLUCONOKIN-MONOMER; -.
DR   UniPathway; UPA00856; UER00828.
DR   PRO; PR:P37647; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IDA:EcoCyc.
DR   GO; GO:0019698; P:D-galacturonate catabolic process; IMP:EcoCyc.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IMP:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   CDD; cd01166; KdgK; 1.
DR   FunFam; 3.40.1190.20:FF:000011; 2-dehydro-3-deoxygluconokinase, putative; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR050306; PfkB_Carbo_kinase.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; NF052444; DhDoxglucKinKdgK; 1.
DR   PANTHER; PTHR43085:SF15; 2-DEHYDRO-3-DEOXYGLUCONOKINASE; 1.
DR   PANTHER; PTHR43085; HEXOKINASE FAMILY MEMBER; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..309
FT                   /note="2-dehydro-3-deoxygluconokinase"
FT                   /id="PRO_0000080085"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         28..32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         102..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         168..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         228..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         261..264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ   SEQUENCE   309 AA;  33962 MW;  53FCD14696BCFA33 CRC64;
     MSKKIAVIGE CMIELSEKGA DVKRGFGGDT LNTSVYIARQ VDPAALTVHY VTALGTDSFS
     QQMLDAWHGE NVDTSLTQRM ENRLPGLYYI ETDSTGERTF YYWRNEAAAK FWLESEQSAA
     ICEELANFDY LYLSGISLAI LSPTSREKLL SLLRECRANG GKVIFDNNYR PRLWASKEET
     QQVYQQMLEC TDIAFLTLDD EDALWGQQPV EDVIARTHNA GVKEVVVKRG ADSCLVSIAG
     EGLVDVPAVK LPKEKVIDTT AAGDSFSAGY LAVRLTGGSA EDAAKRGHLT ASTVIQYRGA
     IIPREAMPA
//