KDGK_ECOLW
ID KDGK_ECOLW Reviewed; 309 AA.
AC E0J5J4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
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; OrderedLocusNames=ECW_m3789, WFL_18505;
GN ORFNames=EschWDRAFT_3851;
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Tremaine M.,
RA Landick R., Keating D., Woyke T.J.;
RT "The draft genome of Escherichia coli W.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=22075923; DOI=10.1007/s10295-011-1052-2;
RA Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L.,
RA Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.;
RT "Optical mapping and sequencing of the Escherichia coli KO11 genome reveal
RT extensive chromosomal rearrangements, and multiple tandem copies of the
RT Zymomonas mobilis pdc and adhB genes.";
RL J. Ind. Microbiol. Biotechnol. 39:629-639(2012).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=13813474;
RA Cynkin M.A., Ashwell G.;
RT "Uronic acid metabolism in bacteria. IV. Purification and properties of 2-
RT keto-3-deoxy-D-gluconokinase in Escherichia coli.";
RL J. Biol. Chem. 235:1576-1579(1960).
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:13813474}.
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:13813474};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 5.6 and 6. {ECO:0000269|PubMed:13813474};
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}.
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DR EMBL; CP002185; ADT77132.1; -; Genomic_DNA.
DR EMBL; CP002967; AFH13342.1; -; Genomic_DNA.
DR EMBL; AEDF01000027; EFN36581.1; -; Genomic_DNA.
DR RefSeq; WP_001296796.1; NZ_WBMH01000032.1.
DR AlphaFoldDB; E0J5J4; -.
DR SMR; E0J5J4; -.
DR EnsemblBacteria; ADT77132; ADT77132; ECW_m3789.
DR GeneID; 66672589; -.
DR KEGG; ell:WFL_18505; -.
DR KEGG; elw:ECW_m3789; -.
DR PATRIC; fig|566546.30.peg.3849; -.
DR HOGENOM; CLU_027634_8_1_6; -.
DR OMA; MAMFYAN; -.
DR UniPathway; UPA00856; UER00828.
DR Proteomes; UP000008525; Chromosome.
DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
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 Transferase.
FT CHAIN 1..309
FT /note="2-dehydro-3-deoxygluconokinase"
FT /id="PRO_0000422661"
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; 33961 MW; 53FCD14C3616FA33 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 ENAAKRGHLT ASTVIQYRGA
IIPREAMPA
