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C6A0Y7 (PGK_THESM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase

EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:TSIB_0215
OrganismThermococcus sibiricus (strain MM 739 / DSM 12597) [Complete proteome] [HAMAP]
Taxonomic identifier604354 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP-Rule MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP-Rule MF_00145

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 413413Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000203351

Regions

Nucleotide binding358 – 3614ATP By similarity
Region19 – 213Substrate binding By similarity
Region57 – 604Substrate binding By similarity

Sites

Binding site341Substrate By similarity
Binding site1141Substrate By similarity
Binding site1541Substrate By similarity
Binding site3321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C6A0Y7 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 2F4F5348F5F10741

FASTA41346,459
        10         20         30         40         50         60 
MFRLSDFNYH DKVIFLRADL NSPVKDGKII SDARFRAVLH TIRYLLEHKA KVVIGTHQSK 

        70         80         90        100        110        120 
PYEEDYLTTE QHAEILSSLL GVKVKYVDDI FGKCARDAIK ALKPSEVLML ENLRFAAEET 

       130        140        150        160        170        180 
KQNPLEYCER THFVRKLSPL IDYVVNEAFA AAHRSQPSLV GFARIRPMIP GFLMEKEIKA 

       190        200        210        220        230        240 
LTRAYESLER PKIYVLGGAK VEDSLNVAEN VLRNEKADLI LTGGLVGHVF TLAKGFDLGD 

       250        260        270        280        290        300 
ANISFLDEKG LIKLVDRAEI ILNEFYPYIR TPVDFAVEYK GERVEIDLLS DKQWIFDERP 

       310        320        330        340        350        360 
ILDIGSRTIE KYSEILKEAS IIVANGPMGV FEIEEFAKGT VEVFKAIGES KAFSIVGGGH 

       370        380        390        400        410 
SIASIYQYNI KGISHISTGG GAMLTFFAGQ SLPVLQALKI SYEKFKNKKE LNQ 

« Hide

References

[1]"Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MM 739 / DSM 12597.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001463 Genomic DNA. Translation: ACS89282.1.
RefSeqYP_002993631.1. NC_012883.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING604354.TSIB_0215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS89282; ACS89282; TSIB_0215.
GeneID8095187.
KEGGtsi:TSIB_0215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAAGHPVGK.

Enzyme and pathway databases

BioCycTSIB604354:GHMS-220-MONOMER.
UniPathwayUPA00109; UER00185.

Family and domain databases

Gene3D3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPMF_00145. Phosphoglyc_kinase.
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. SSF53748. 1 hit.
ProtoNetSearch...

Entry information

Entry namePGK_THESM
AccessionPrimary (citable) accession number: C6A0Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: June 11, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways