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

Glycerate 2-kinase

Gene

gck

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP or pyrophosphate as phosphate donor.1 Publication

Catalytic activityi

ATP + D-glycerate = ADP + 2-phospho-D-glycerate.

Cofactori

Mg2+1 Publication, Ni2+1 Publication, Mn2+1 Publication, Co2+1 PublicationNote: Magnesium. It could be replaced to some extent by nickel, manganese or cobalt.1 Publication

Kineticsi

  1. KM=44 µM for glycerate (at 45 degrees Celsius and at pH 7.0)1 Publication
  2. KM=102 µM for ATP (at 45 degrees Celsius and at pH 7.0)1 Publication
  1. Vmax=624 µmol/min/mg enzyme with glycerate as substrate (at 45 degrees Celsius and at pH 7.0)1 Publication
  2. Vmax=639 µmol/min/mg enzyme with ATP as substrate (at 45 degrees Celsius and at pH 7.0)1 Publication

pH dependencei

Optimum pH is 7.0 and half of the maximum activity remains at pH 6-10.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius. It has strong activity at moderate temperature 30-50 degrees Celsius and about half of the maximal activity is retained at 100 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581SubstrateBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glycerate 2-kinase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-491-MONOMER.
BRENDAi2.7.1.165. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerate 2-kinase (EC:2.7.1.165)
Short name:
GCK
Alternative name(s):
2-phosphoglycerate forming glycerate kinase
Gene namesi
Name:gck
Ordered Locus Names:PH0495
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glycerate 2-kinasePRO_0000415150Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi70601.PH0495.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2015Combined sources
Helixi23 – 308Combined sources
Beta strandi31 – 333Combined sources
Beta strandi35 – 406Combined sources
Beta strandi43 – 464Combined sources
Beta strandi51 – 577Combined sources
Helixi60 – 7011Combined sources
Beta strandi74 – 818Combined sources
Beta strandi89 – 968Combined sources
Beta strandi98 – 1003Combined sources
Helixi103 – 11816Combined sources
Beta strandi123 – 1297Combined sources
Helixi133 – 1364Combined sources
Helixi146 – 15813Combined sources
Helixi163 – 1719Combined sources
Beta strandi174 – 1763Combined sources
Turni177 – 1793Combined sources
Helixi180 – 1834Combined sources
Beta strandi186 – 1949Combined sources
Turni202 – 2043Combined sources
Helixi205 – 2073Combined sources
Helixi217 – 22610Combined sources
Turni230 – 2323Combined sources
Helixi235 – 24511Combined sources
Beta strandi260 – 2667Combined sources
Helixi268 – 28114Combined sources
Beta strandi285 – 2939Combined sources
Helixi297 – 31418Combined sources
Beta strandi320 – 3289Combined sources
Beta strandi335 – 3373Combined sources
Helixi343 – 3519Combined sources
Turni352 – 3576Combined sources
Beta strandi358 – 3669Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi378 – 3825Combined sources
Helixi385 – 3917Combined sources
Helixi396 – 4016Combined sources
Helixi405 – 4117Combined sources
Beta strandi427 – 4359Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X3LX-ray2.10A1-440[»]
ProteinModelPortaliO58231.
SMRiO58231. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58231.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycerate kinase type-1 family.Curated

Phylogenomic databases

eggNOGiarCOG04170. Archaea.
COG2379. LUCA.
HOGENOMiHOG000018914.
KOiK11529.
OMAiIYEAGHP.

Family and domain databases

Gene3Di3.40.1480.10. 1 hit.
InterProiIPR007835. MOFRL.
IPR025286. MOFRL_assoc_dom.
[Graphical view]
PfamiPF13660. DUF4147. 1 hit.
PF05161. MOFRL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAMDIREIG LRLVGEAIKA ADPYRAVLNA VKVSDDKIIV QGKEFEIKGK
60 70 80 90 100
VYVIALGKAA CEMARAIEDI LDVEDGVAVT KYGYGKELKR IKVIEAGHPI
110 120 130 140 150
PDEKSILGAK EALSILNRAR ENDIVFILIS GGGSALFELP EEGISLEDLK
160 170 180 190 200
LTTDLLLKSG AKIHEINTVR KHISKVKGGK LAKMIKGTGI VLIISDVVGD
210 220 230 240 250
NLEAIASGPT VKDPTTFEDA KRILELYDIW EKVPESVRLH IERGLRGEVE
260 270 280 290 300
ETLKEDLPNV HNFLIASNSI SCEAIAREAQ RLGFKAYIMT TTLEGEAKDA
310 320 330 340 350
GLFIGSIVQE IAERGRPFEP PVVLVFGGET TVTIEGKGGK GGPNQEIALS
360 370 380 390 400
ATRKISDLEA LIVAFDTDGT DGPTDAAGGI VDGTTYKKLR EKGIDVEKVL
410 420 430 440
KEHNSYEALK KVGGLLFTGP TGTNVNSIVI AIVTSKRGRT
Length:440
Mass (Da):47,375
Last modified:August 1, 1998 - v1
Checksum:iC9C3E4FE4207F4B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29583.1.
PIRiB71162.

Genome annotation databases

EnsemblBacteriaiBAA29583; BAA29583; BAA29583.
KEGGipho:PH0495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA29583.1.
PIRiB71162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X3LX-ray2.10A1-440[»]
ProteinModelPortaliO58231.
SMRiO58231. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0495.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA29583; BAA29583; BAA29583.
KEGGipho:PH0495.

Phylogenomic databases

eggNOGiarCOG04170. Archaea.
COG2379. LUCA.
HOGENOMiHOG000018914.
KOiK11529.
OMAiIYEAGHP.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-491-MONOMER.
BRENDAi2.7.1.165. 5244.

Miscellaneous databases

EvolutionaryTraceiO58231.

Family and domain databases

Gene3Di3.40.1480.10. 1 hit.
InterProiIPR007835. MOFRL.
IPR025286. MOFRL_assoc_dom.
[Graphical view]
PfamiPF13660. DUF4147. 1 hit.
PF05161. MOFRL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization."
    Liu B., Hong Y., Wu L., Li Z., Ni J., Sheng D., Shen Y.
    Extremophiles 11:733-739(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A GLYCERATE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT, NOMENCLATURE.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  3. "Crystal structure of the PH0495 protein from Pyrococccus horikoshii OT3."
    Mizutani H., Kunishima N.
    Submitted (MAY-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiGCK_PYRHO
AccessioniPrimary (citable) accession number: O58231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 82 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.