KDGK_ECOLI
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 03-AUG-2022, entry version 154.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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;
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_SSZK01000039.1.
DR AlphaFoldDB; P37647; -.
DR SMR; P37647; -.
DR BioGRID; 4262528; 7.
DR BioGRID; 852349; 2.
DR DIP; DIP-10056N; -.
DR IntAct; P37647; 5.
DR STRING; 511145.b3526; -.
DR jPOST; P37647; -.
DR PaxDb; P37647; -.
DR PRIDE; P37647; -.
DR EnsemblBacteria; AAC76551; AAC76551; b3526.
DR EnsemblBacteria; BAE77768; BAE77768; BAE77768.
DR GeneID; 948041; -.
DR KEGG; ecj:JW5668; -.
DR KEGG; eco:b3526; -.
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; MAMFYAN; -.
DR PhylomeDB; P37647; -.
DR BioCyc; EcoCyc:DEOXYGLUCONOKIN-MON; -.
DR BioCyc; MetaCyc:DEOXYGLUCONOKIN-MON; -.
DR UniPathway; UPA00856; UER00828.
DR PRO; PR:P37647; -.
DR Proteomes; UP000000318; Chromosome.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IMP:EcoCyc.
DR GO; GO:0042840; P:D-glucuronate catabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 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
