Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase

Gene

kdgK

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of glucose and galactose via the semi-phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) and 2-keto-3-deoxygalactonate (KDGal) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal), respectively.3 Publications

Catalytic activityi

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate.3 Publications
ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-6-phospho-D-galactonate.3 Publications

Kineticsi

Kcat is 3.8 (sec-1) for ATP, 5 (sec-1) for KDG and 5.4 (sec-1) for KDGal (at 60 degrees Celsius and pH 7.5).

  1. KM=0.14 mM for KDG (at 70 degrees Celsius and pH 7.2)2 Publications
  2. KM=2.8 mM for ATP (at 60 degrees Celsius and pH 7.5)2 Publications
  3. KM=3.6 mM for KDG (at 60 degrees Celsius and pH 7.5)2 Publications
  4. KM=8.1 mM for KDGal (at 60 degrees Celsius and pH 7.5)2 Publications
  1. Vmax=9.7 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is between 7 and 8.2 Publications

Temperature dependencei

Optimum temperature is between 70 and 80 degrees Celsius.2 Publications

Pathwayi: 2-dehydro-3-deoxy-D-gluconate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase (kdgK)
  2. 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (eda)
This subpathway is part of the pathway 2-dehydro-3-deoxy-D-gluconate degradation, which is itself part of Carbohydrate acid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate, the pathway 2-dehydro-3-deoxy-D-gluconate degradation and in Carbohydrate acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901Substrate
Binding sitei166 – 1661Substrate
Binding sitei232 – 2321ATP; via carbonyl oxygenBy similarity
Active sitei258 – 2581Proton acceptor1 Publication
Binding sitei258 – 2581Substrate
Binding sitei294 – 2941Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1663ATP
Nucleotide bindingi226 – 2316ATP
Nucleotide bindingi255 – 2584ATP

GO - Molecular functioni

  • 2-dehydro-3-deoxygalactonokinase activity Source: UniProtKB
  • 2-dehydro-3-deoxygluconokinase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • nucleotide binding Source: UniProtKB

GO - Biological processi

  • phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17931.
SSOL273057:GCH2-2982-MONOMER.
BRENDAi2.7.1.178. 6163.
UniPathwayiUPA00856; UER00828.

Names & Taxonomyi

Protein namesi
Recommended name:
2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase (EC:2.7.1.1783 Publications)
Short name:
2-dehydro-3-deoxyglucono/galactono-kinase
Alternative name(s):
2-keto-3-deoxy-galactonokinase
2-keto-3-deoxygluconokinase
3-deoxy-2-oxo-D-gluconate kinase
KDG kinase
KDGal kinase
Gene namesi
Name:kdgK
Ordered Locus Names:SSO3195
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3133132-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinasePRO_0000422663Add
BLAST

Interactioni

Subunit structurei

Homohexamer; trimer of dimers.2 Publications

Protein-protein interaction databases

STRINGi273057.SSO3195.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi11 – 2010Combined sources
Helixi22 – 243Combined sources
Beta strandi27 – 337Combined sources
Helixi35 – 4511Combined sources
Beta strandi50 – 5910Combined sources
Helixi60 – 7112Combined sources
Beta strandi79 – 824Combined sources
Beta strandi89 – 9810Combined sources
Beta strandi102 – 1076Combined sources
Helixi113 – 1153Combined sources
Helixi118 – 1203Combined sources
Helixi123 – 1275Combined sources
Beta strandi129 – 1357Combined sources
Helixi136 – 1416Combined sources
Helixi143 – 15513Combined sources
Beta strandi157 – 1626Combined sources
Helixi167 – 1693Combined sources
Helixi173 – 18614Combined sources
Beta strandi189 – 1946Combined sources
Helixi196 – 2038Combined sources
Helixi208 – 21710Combined sources
Beta strandi220 – 2267Combined sources
Helixi228 – 2303Combined sources
Beta strandi232 – 2365Combined sources
Beta strandi239 – 2435Combined sources
Helixi256 – 26914Combined sources
Helixi274 – 28916Combined sources
Beta strandi291 – 2955Combined sources
Helixi301 – 31010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V78X-ray2.00A/B/C1-313[»]
2VARX-ray2.10A/B/C1-313[»]
ProteinModelPortaliQ97U29.
SMRiQ97U29. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97U29.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 385Substrate bindingCurated
Regioni106 – 1083Substrate binding

Sequence similaritiesi

Belongs to the carbohydrate kinase PfkB family.Curated

Phylogenomic databases

eggNOGiarCOG00014. Archaea.
COG0524. LUCA.
HOGENOMiHOG000235951.
InParanoidiQ97U29.
KOiK18126.
OMAiGAWFKTA.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.

Sequencei

Sequence statusi: Complete.

Q97U29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDVIALGEP LIQFNSFNPG PLRFVNYFEK HVAGSELNFC IAVVRNHLSC
60 70 80 90 100
SLIARVGNDE FGKNIIEYSR AQGIDTSHIK VDNESFTGIY FIQRGYPIPM
110 120 130 140 150
KSELVYYRKG SAGSRLSPED INENYVRNSR LVHSTGITLA ISDNAKEAVI
160 170 180 190 200
KAFELAKSRS LDTNIRPKLW SSLEKAKETI LSILKKYDIE VLITDPDDTK
210 220 230 240 250
ILLDVTDPDE AYRKYKELGV KVLLYKLGSK GAIAYKDNVK AFKDAYKVPV
260 270 280 290 300
EDPTGAGDAM AGTFVSLYLQ GKDIEYSLAH GIAASTLVIT VRGDNELTPT
310
LEDAERFLNE FKT
Length:313
Mass (Da):34,875
Last modified:October 1, 2001 - v1
Checksum:i43D5787DB4D3A86F
GO

Mass spectrometryi

Molecular mass is 34870 Da from positions 1 - 313. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43293.1.
PIRiF90504.
RefSeqiWP_009991690.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK43293; AAK43293; SSO3195.
GeneIDi27429443.
KEGGisso:SSO3195.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43293.1.
PIRiF90504.
RefSeqiWP_009991690.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V78X-ray2.00A/B/C1-313[»]
2VARX-ray2.10A/B/C1-313[»]
ProteinModelPortaliQ97U29.
SMRiQ97U29. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO3195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK43293; AAK43293; SSO3195.
GeneIDi27429443.
KEGGisso:SSO3195.

Phylogenomic databases

eggNOGiarCOG00014. Archaea.
COG0524. LUCA.
HOGENOMiHOG000235951.
InParanoidiQ97U29.
KOiK18126.
OMAiGAWFKTA.

Enzyme and pathway databases

UniPathwayiUPA00856; UER00828.
BioCyciMetaCyc:MONOMER-17931.
SSOL273057:GCH2-2982-MONOMER.
BRENDAi2.7.1.178. 6163.

Miscellaneous databases

EvolutionaryTraceiQ97U29.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR011611. PfkB_dom.
IPR029056. Ribokinase-like.
[Graphical view]
PfamiPF00294. PfkB. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation."
    Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J., Siebers B.
    Biochem. J. 390:529-540(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus."
    Lamble H.J., Theodossis A., Milburn C.C., Taylor G.L., Bull S.D., Hough D.W., Danson M.J.
    FEBS Lett. 579:6865-6869(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  4. "Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway."
    Kim S., Lee S.B.
    Biosci. Biotechnol. Biochem. 70:1308-1316(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  5. "The structure of Sulfolobus solfataricus 2-keto-3-deoxygluconate kinase."
    Potter J.A., Kerou M., Lamble H.J., Bull S.D., Hough D.W., Danson M.J., Taylor G.L.
    Acta Crystallogr. D 64:1283-1287(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND 2-KETO-3-DEOXYGLUCONATE, ACTIVE SITE, SUBUNIT.

Entry informationi

Entry nameiKDGK_SULSO
AccessioniPrimary (citable) accession number: Q97U29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: October 1, 2001
Last modified: July 6, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.