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P27362 (PGK_PLAF7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:PFI1105w
OrganismPlasmodium falciparum (isolate 3D7) [Reference proteome]
Taxonomic identifier36329 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length416 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

Monomer.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145859

Regions

Nucleotide binding372 – 3754ATP By similarity
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity

Sites

Binding site391Substrate By similarity
Binding site1221Substrate By similarity
Binding site1701Substrate By similarity
Binding site2151ATP
Binding site3121ATP; via carbonyl oxygen By similarity
Binding site3431ATP
Binding site3741ATP

Secondary structure

.................................................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27362 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 91105E552AE944CF

FASTA41645,427
        10         20         30         40         50         60 
MLGNKLSISD LKDIKNKKVL VRVDFNVPIE NGIIKDTNRI TATLPTINHL KKEGASKIIL 

        70         80         90        100        110        120 
ISHCGRPDGL RNEKYTLKPV AETLKGLLGE EVLFLNDCVG KEVEDKINAA KENSVILLEN 

       130        140        150        160        170        180 
LRFHIEEEGK GVDANGNKVK ANKEDVEKFQ NDLTKLADVF INDAFGTAHR AHSSMVGVKL 

       190        200        210        220        230        240 
NVKASGFLMK KELEYFSKAL ENPQRPLLAI LGGAKVSDKI QLIKNLLDKV DRMIIGGGMA 

       250        260        270        280        290        300 
YTFKKVLNNM KIGTSLFDEA GSKIVGEIME KAKAKNVQIF LPVDFKIADN FDNNANTKFV 

       310        320        330        340        350        360 
TDEEGIPDNW MGLDAGPKSI ENYKDVILTS KTVIWNGPQG VFEMPNFAKG SIECLNLVVE 

       370        380        390        400        410 
VTKKGAITIV GGGDTASLVE QQNKKNEISH VSTGGGASLE LLEGKELPGV LALSNK 

« Hide

References

« Hide 'large scale' references
[1]"Glycolytic pathway of the human malaria parasite Plasmodium falciparum: primary sequence analysis of the gene encoding 3-phosphoglycerate kinase and chromosomal mapping studies."
Hicks K.E., Read M., Holloway S.P., Sims P.F.G., Hyde J.E.
Gene 100:123-129(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the human malaria parasite Plasmodium falciparum."
Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S. expand/collapse author list , Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.
Nature 419:498-511(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[3]"Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."
Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D., Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K., Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T., Christodoulou Z. expand/collapse author list , Clark L., Clark R., Corton C., Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R., Sulston J.E., Craig A., Newbold C., Barrell B.G.
Nature 419:527-531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[4]"Biochemical characterization and crystallization of recombinant 3-phosphoglycerate kinase of Plasmodium falciparum."
Pal B., Pybus B., Muccio D.D., Chattopadhyay D.
Biochim. Biophys. Acta 1699:277-280(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-416 IN COMPLEX WITH AMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59249 Genomic DNA. Translation: AAA29727.1.
AL844508 Genomic DNA. Translation: CAD51907.1.
PIRJU0475.
RefSeqXP_001352096.1. XM_001352060.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGImodel-A4-416[»]
1LTKX-ray3.00A/B/C2-416[»]
3OZ7X-ray2.70A/B2-415[»]
3OZAX-ray3.00A/B/C2-416[»]
ProteinModelPortalP27362.
SMRP27362. Positions 2-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1208777. 3 interactions.
IntActP27362. 3 interactions.
MINTMINT-1572586.
STRING5833.PFI1105w-1.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPFI1105w:mRNA; PFI1105w:pep; PFI1105w.
GeneID813501.
KEGGpfa:PFI1105w.

Organism-specific databases

EuPathDBPlasmoDB:PF3D7_0922500.

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAFPVDYVT.
PhylomeDBP27362.

Enzyme and pathway databases

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. SSF53748. 1 hit.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27362.

Entry information

Entry namePGK_PLAF7
AccessionPrimary (citable) accession number: P27362
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways