KDGK_DICD3
ID KDGK_DICD3 Reviewed; 310 AA.
AC P45416; E0SFG7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=2-dehydro-3-deoxygluconokinase;
DE EC=2.7.1.45 {ECO:0000269|PubMed:8157608};
DE AltName: Full=2-keto-3-deoxygluconokinase;
DE AltName: Full=3-deoxy-2-oxo-D-gluconate kinase;
DE AltName: Full=KDG kinase {ECO:0000303|PubMed:8157608};
GN Name=kdgK {ECO:0000303|PubMed:8157608}; OrderedLocusNames=Dda3937_02001;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=3937;
RX PubMed=8157608; DOI=10.1128/jb.176.8.2386-2392.1994;
RA Hugouvieux-Cotte-Pattat N., Nasser W., Robert-Baudouy J.;
RT "Molecular characterization of the Erwinia chrysanthemi kdgK gene involved
RT in pectin degradation.";
RL J. Bacteriol. 176:2386-2392(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [3]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA Rudd K.E.;
RL Unpublished observations (AUG-1996).
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:8157608}.
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:8157608};
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 -!- INDUCTION: Expression is probably repressed by KdgR, which binds to its
CC 5'-UTR. {ECO:0000269|PubMed:8157608}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52961.1; Type=Frameshift; Evidence={ECO:0000305|Ref.3};
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DR EMBL; X75047; CAA52961.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002038; ADM96338.1; -; Genomic_DNA.
DR PIR; C55215; C55215.
DR RefSeq; WP_013315827.1; NC_014500.1.
DR AlphaFoldDB; P45416; -.
DR SMR; P45416; -.
DR STRING; 198628.Dda3937_02001; -.
DR EnsemblBacteria; ADM96338; ADM96338; Dda3937_02001.
DR GeneID; 9731507; -.
DR KEGG; ddd:Dda3937_02001; -.
DR PATRIC; fig|198628.6.peg.127; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_8_1_6; -.
DR OMA; MAMFYAN; -.
DR OrthoDB; 1604782at2; -.
DR BioCyc; DDAD198628:DDA3937_RS00580-MON; -.
DR BioCyc; MetaCyc:MON-15644; -.
DR UniPathway; UPA00856; UER00828.
DR Proteomes; UP000006859; 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 Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="2-dehydro-3-deoxygluconokinase"
FT /id="PRO_0000080086"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 29..33
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 103..105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 169..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 229..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 262..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT CONFLICT 18..24
FT /note="QKGADLN -> RKARISI (in Ref. 1; CAA52961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34119 MW; A177AD426D73E0B7 CRC64;
MTTKNIAIIG ECMIELSQKG ADLNRGFGGD TLNTAVYISR QVKPDALDVH YVTALGTDSF
SSEMMASWQK EGVKTDLIQR LDNKLPGLYF IETDATGERT FYYWRNDAAA RYWLESPDAD
TISQQLAQFD YIYLSGISLA ILNQASRARL LTVLRACRAN GGKVIFDNNY RPRLWQSKEE
TRQAYSDMLA CTDIAFLTLD DEDMLWGELP VDEVLKRTHG AGVMEVVIKR GADACLVSIQ
GEALLEVPAI KLPKEKVVDT TAAGDSFSAG YLSVRLNGGS AQDAAKRGHL TASTVIQYRG
AIIPLEAMPA
