KDGK_THETE
ID KDGK_THETE Reviewed; 325 AA.
AC Q704D0;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 45.
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;
OS Thermoproteus tenax.
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=2271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT tenax using genomic and biochemical data.";
RL J. Bacteriol. 186:2179-2194(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15869466; DOI=10.1042/bj20041711;
RA Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J.,
RA Siebers B.;
RT "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic
RT archaea: a re-evaluation.";
RL Biochem. J. 390:529-540(2005).
CC -!- FUNCTION: Involved in the degradation of glucose via the semi-
CC phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation
CC of 2-keto-3-deoxygluconate (KDG) yielding 2-keto-3-deoxy-6-
CC phosphogluconate (KDPG). {ECO:0000269|PubMed:15869466}.
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:15869466};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.178 mM for KDG (at 70 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:15869466};
CC Vmax=43.26 umol/min/mg enzyme (at 70 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:15869466};
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 -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AJ621283; CAF18464.1; -; Genomic_DNA.
DR AlphaFoldDB; Q704D0; -.
DR SMR; Q704D0; -.
DR UniPathway; UPA00856; UER00828.
DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..325
FT /note="2-dehydro-3-deoxygluconokinase"
FT /id="PRO_0000422664"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 49..53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 121..123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 179..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 240..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 269..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ SEQUENCE 325 AA; 34854 MW; 63AA9058A4A6E56C CRC64;
MAEGRCSQGK EPAEAMISLV ALGEPLIQLN AVTPGPLRYV AYFEKHVAGS EANFCIAATM
AGARCSLIAR VGDDEFGRNI VEYLRGRGVD VSHVKVDPGA PTGIYFVQRH FPVPGRSRLI
YYRKGSAGSR VGPDDVDSSL ISSADAVHST GITLALSDSA NRAVHKAFGE AKRRTFDTNI
RPALWPDLAA ARRAILDVLN YGVDVLVTDP DDTQILLGVR DPEEAYRKYR ELGVQTLVYK
LGAEGAYVFW NGGSYFRDAL KVAVEDPTGA GDAVAGYFVA LYLSGVDPRR ALDLAVAASA
LVVGVRGDNE ALPSPREAEE LLKAL
