KDGK_SACS2
ID KDGK_SACS2 Reviewed; 313 AA.
AC Q97U29;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
DE Short=2-dehydro-3-deoxyglucono/galactono-kinase;
DE EC=2.7.1.178 {ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
DE AltName: Full=2-keto-3-deoxy-galactonokinase;
DE AltName: Full=2-keto-3-deoxygluconokinase;
DE AltName: Full=3-deoxy-2-oxo-D-gluconate kinase;
DE AltName: Full=KDG kinase;
DE AltName: Full=KDGal kinase;
GN Name=kdgK; OrderedLocusNames=SSO3195;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=16330030; DOI=10.1016/j.febslet.2005.11.028;
RA Lamble H.J., Theodossis A., Milburn C.C., Taylor G.L., Bull S.D.,
RA Hough D.W., Danson M.J.;
RT "Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the
RT archaeon Sulfolobus solfataricus.";
RL FEBS Lett. 579:6865-6869(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=16794308; DOI=10.1271/bbb.50566;
RA Kim S., Lee S.B.;
RT "Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate
RT kinase in the modified Entner-Doudoroff pathway.";
RL Biosci. Biotechnol. Biochem. 70:1308-1316(2006).
RN [5] {ECO:0007744|PDB:2V78, ECO:0007744|PDB:2VAR}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND
RP 2-KETO-3-DEOXYGLUCONATE, ACTIVE SITE, AND SUBUNIT.
RX PubMed=19018105; DOI=10.1107/s0907444908036111;
RA Potter J.A., Kerou M., Lamble H.J., Bull S.D., Hough D.W., Danson M.J.,
RA Taylor G.L.;
RT "The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase.";
RL Acta Crystallogr. D 64:1283-1287(2008).
CC -!- FUNCTION: Involved in the degradation of glucose and galactose via the
CC semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the
CC phosphorylation of 2-keto-3-deoxygluconate (KDG) and 2-keto-3-
CC deoxygalactonate (KDGal) to produce 2-keto-3-deoxy-6-phosphogluconate
CC (KDPG) and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal), respectively.
CC {ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:16330030,
CC ECO:0000269|PubMed:16794308}.
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=2.7.1.178;
CC Evidence={ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:16330030,
CC ECO:0000269|PubMed:16794308};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-galactonate + ATP = 2-dehydro-3-deoxy-6-
CC phospho-D-galactonate + ADP + H(+); Xref=Rhea:RHEA:16525,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57989,
CC ChEBI:CHEBI:58298, ChEBI:CHEBI:456216; EC=2.7.1.178;
CC Evidence={ECO:0000269|PubMed:15869466, ECO:0000269|PubMed:16330030,
CC ECO:0000269|PubMed:16794308};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for KDG (at 70 degrees Celsius and pH 7.2)
CC {ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
CC KM=2.8 mM for ATP (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
CC KM=3.6 mM for KDG (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
CC KM=8.1 mM for KDGal (at 60 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
CC Vmax=9.7 umol/min/mg enzyme {ECO:0000269|PubMed:16330030,
CC ECO:0000269|PubMed:16794308};
CC Note=kcat is 3.8 sec(-1) for ATP, 5 sec(-1) for KDG and 5.4 sec(-1)
CC for KDGal (at 60 degrees Celsius and pH 7.5).;
CC pH dependence:
CC Optimum pH is between 7 and 8. {ECO:0000269|PubMed:16330030,
CC ECO:0000269|PubMed:16794308};
CC Temperature dependence:
CC Optimum temperature is between 70 and 80 degrees Celsius.
CC {ECO:0000269|PubMed:16330030, ECO:0000269|PubMed:16794308};
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:0000305|PubMed:16794308,
CC ECO:0000305|PubMed:19018105}.
CC -!- MASS SPECTROMETRY: Mass=34870; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16330030};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK43293.1; -; Genomic_DNA.
DR PIR; F90504; F90504.
DR RefSeq; WP_009991690.1; NC_002754.1.
DR PDB; 2V78; X-ray; 2.00 A; A/B/C=1-313.
DR PDB; 2VAR; X-ray; 2.10 A; A/B/C=1-313.
DR PDBsum; 2V78; -.
DR PDBsum; 2VAR; -.
DR AlphaFoldDB; Q97U29; -.
DR SMR; Q97U29; -.
DR STRING; 273057.SSO3195; -.
DR EnsemblBacteria; AAK43293; AAK43293; SSO3195.
DR GeneID; 44128912; -.
DR KEGG; sso:SSO3195; -.
DR PATRIC; fig|273057.12.peg.3299; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_6_0_2; -.
DR InParanoid; Q97U29; -.
DR OMA; MAMFYAN; -.
DR PhylomeDB; Q97U29; -.
DR BioCyc; MetaCyc:MON-17931; -.
DR BRENDA; 2.7.1.178; 6163.
DR UniPathway; UPA00856; UER00828.
DR EvolutionaryTrace; Q97U29; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0008671; F:2-dehydro-3-deoxygalactonokinase activity; IDA:UniProtKB.
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 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="2-dehydro-3-deoxygluconokinase/2-dehydro-3-
FT deoxygalactonokinase"
FT /id="PRO_0000422663"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19018105"
FT BINDING 34..38
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 164..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 226..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 255..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19018105"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:2V78"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:2V78"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:2V78"
SQ SEQUENCE 313 AA; 34875 MW; 43D5787DB4D3A86F CRC64;
MVDVIALGEP LIQFNSFNPG PLRFVNYFEK HVAGSELNFC IAVVRNHLSC SLIARVGNDE
FGKNIIEYSR AQGIDTSHIK VDNESFTGIY FIQRGYPIPM KSELVYYRKG SAGSRLSPED
INENYVRNSR LVHSTGITLA ISDNAKEAVI KAFELAKSRS LDTNIRPKLW SSLEKAKETI
LSILKKYDIE VLITDPDDTK ILLDVTDPDE AYRKYKELGV KVLLYKLGSK GAIAYKDNVK
AFKDAYKVPV EDPTGAGDAM AGTFVSLYLQ GKDIEYSLAH GIAASTLVIT VRGDNELTPT
LEDAERFLNE FKT
