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O58965 (PGK_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglycerate kinase
EC=2.7.2.3
Gene names
Name:pgk
Ordered Locus Names:PH1218
ORF Names:PHBK036
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Homodimer By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm 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 term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000146067

Regions

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

Sites

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

Secondary structure

1 ............................................................................. 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O58965 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6912EDE7BD26486E

FASTA41046,403
        10         20         30         40         50         60 
MFRLEDFNFH NKTVFLRVDL NSPMKDGKII SDARFKAVLP TIRYLIESGA KVVIGTHQGK 

        70         80         90        100        110        120 
PYSEDYTTTE EHARVLSELL DQHVEYIEDI FGRYAREKIK ELKSGEVAIL ENLRFSAEEV 

       130        140        150        160        170        180 
KNKPIEECEK TFLVKKLSKV IDYVVNDAFA TAHRSQPSLV GFARIKPMIM GFLMEKEIEA 

       190        200        210        220        230        240 
LMRAYYSKDS PKIYVLGGAK VEDSLKVVEN VLRRERADLV LTGGLVANVF TLAKGFDLGR 

       250        260        270        280        290        300 
KNVEFMKKKG LLDYVKHAEE ILDEFYPYIR TPVDFAVDYK GERVEIDLLS ENRGLLHQYQ 

       310        320        330        340        350        360 
IMDIGKRTAE KYREILMKAR IIVANGPMGV FEREEFAIGT VEVFKAIADS PAFSVLGGGH 

       370        380        390        400        410 
SIASIQKYGI TGITHISTGG GAMLSFFAGE ELPVLRALQI SYEKFKEVVK

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Crystal structure of phosphoglycerate kinase from Pyrococcus horikoshii OT3."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000001 Genomic DNA. Translation: BAA30318.1.
PIRD71065.
RefSeqNP_143113.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUNX-ray2.10A/B1-410[»]
ProteinModelPortalO58965.
SMRO58965. Positions 1-405.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1502980.
STRING70601.PH1218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30318; BAA30318; BAA30318.
GeneID1443540.
KEGGpho:PH1218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAEGKGQDP.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1213-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.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERPTHR11406. PTHR11406. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PIRSFPIRSF000724. Pgk. 1 hit.
PRINTSPR00477. PHGLYCKINASE.
SUPFAMSSF53748. PGK. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO58965.

Entry information

Entry namePGK_PYRHO
AccessionPrimary (citable) accession number: O58965
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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