ID   KDGK_THEAC              Reviewed;         336 AA.
AC   Q9HLV3;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=2-dehydro-3-deoxygluconokinase {ECO:0000305};
DE            EC=2.7.1.45 {ECO:0000269|Ref.2};
DE   AltName: Full=2-keto-3-deoxy-D-gluconate kinase {ECO:0000303|Ref.2};
DE            Short=KDG kinase {ECO:0000303|Ref.2};
GN   Name=kdgK {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Ta0122 {ECO:0000312|EMBL:CAC11269.1};
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   DOI=10.1007/BF02932290;
RA   Jung J.H., Lee S.B.;
RT   "Identification and characterization of Thermoplasma acidophilum 2-keto-3-
RT   deoxy-D-gluconate kinase: A new class of sugar kinases.";
RL   Biotechnol. Bioprocess Eng. 10:535-539(2005).
CC   -!- FUNCTION: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate
CC       (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Is specific
CC       for KDG. {ECO:0000269|Ref.2}.
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|Ref.2};
CC   -!- ACTIVITY REGULATION: Probably activated by phosphorylation and
CC       inhibited by dephosphorylation. {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.0-5.0. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC       family. {ECO:0000305}.
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DR   EMBL; AL445063; CAC11269.1; -; Genomic_DNA.
DR   RefSeq; WP_010900549.1; NC_002578.1.
DR   AlphaFoldDB; Q9HLV3; -.
DR   SMR; Q9HLV3; -.
DR   STRING; 273075.Ta0122; -.
DR   EnsemblBacteria; CAC11269; CAC11269; CAC11269.
DR   GeneID; 1455773; -.
DR   KEGG; tac:Ta0122; -.
DR   eggNOG; arCOG03659; Archaea.
DR   HOGENOM; CLU_016274_1_0_2; -.
DR   OMA; PANIMRD; -.
DR   OrthoDB; 42111at2157; -.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..336
FT                   /note="2-dehydro-3-deoxygluconokinase"
FT                   /id="PRO_0000449252"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ   SEQUENCE   336 AA;  36414 MW;  F30F99CA2371FD90 CRC64;
     MEEEMMILGV DGGSTKTLAI VFDERSERIM GVGISGPSNF TNAPRETAES NISDAVRKAC
     SEAGTDLDGI GIRVFGLAGI GDSREATELG KDIVRSIVGH ADVYSDGLGA YKFANLNDDG
     VVFAPGTGSV GFIKNGSDPE RFGGWGWFIG DEASASWMAK QAILFAEREH DGIAETGFLD
     VVRRYFGMDL YETVYAISKE KIAKRVVAAL APQVSAMARS GNRYAISIFE ESSSYIADLL
     NAKSRIFGRS GKYSVLGGTM LAGDFYRDMI RKKSSVDVSI YYGYQVAIGD VLIGIEKKGS
     ISVDLRNKMI DQLNSILENK KEDIKKFLFL DSVPTS