Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00559 (PGK1_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 100. 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 1

EC=2.7.2.3
Gene names
Name:PGK1
Synonyms:PGK
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

phosphoglycerate kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 417416Phosphoglycerate kinase 1 HAMAP-Rule MF_00145
PRO_0000145829

Regions

Region2 – 186185Globular domain-1 HAMAP-Rule MF_00145
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity
Region187 – 1904Linker HAMAP-Rule MF_00145
Region191 – 417227Globular domain-2 HAMAP-Rule MF_00145
Region406 – 41712Associated with globular domain 1 HAMAP-Rule MF_00145

Sites

Binding site391Substrate By similarity
Binding site1231Substrate By similarity
Binding site1711Substrate By similarity
Binding site2201ATP By similarity
Binding site3131ATP; via carbonyl oxygen By similarity
Binding site3441ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine HAMAP-Rule MF_00145
Modified residue61N6-succinyllysine By similarity
Modified residue111N6-acetyllysine By similarity
Modified residue481N6-acetyllysine; alternate By similarity
Modified residue481N6-succinyllysine; alternate By similarity
Modified residue751N6-acetyllysine By similarity
Modified residue761Phosphotyrosine By similarity
Modified residue861N6-acetyllysine By similarity
Modified residue911N6-acetyllysine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine; alternate By similarity
Modified residue1311N6-malonyllysine; alternate By similarity
Modified residue1461N6-acetyllysine By similarity
Modified residue1911N6-succinyllysine By similarity
Modified residue1961Phosphotyrosine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue2911N6-acetyllysine By similarity
Modified residue3611N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P00559 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5110E246AF96931A

FASTA41744,603
        10         20         30         40         50         60 
MSLSNKLTLD KLNVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL 

        70         80         90        100        110        120 
MSHLGRPDVG PMPDKYSLQP VAVELKSLLG KDVLFLKDCV GPEVEKACAD PAAGSVILLE 

       130        140        150        160        170        180 
NLRFHVEEEG KGKDASGNKV KAEPAKIETF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN 

       190        200        210        220        230        240 
LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM 

       250        260        270        280        290        300 
AFTFLKVLNN MEIGTSLFDE EGAKIVKNLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ 

       310        320        330        340        350        360 
ATVASGIPAG WMGLDCGTES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR GTKALMDEVV 

       370        380        390        400        410 
KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV 

« Hide

References

[1]"Primary structure of 3-phosphoglycerate kinase from horse muscle. II. Amino acid sequence of cyanogen bromide peptides CB1-CB4 and CB6-CB14, sequence of methionine-containing regions, and complete sequence of the enzyme."
Merrett M.
J. Biol. Chem. 256:10293-10305(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-417.
Tissue: Muscle.
[2]"Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme."
Banks R.D., Blake C.C.F., Evans P.R., Haser R., Rice D.W., Hardy G.W., Merrett M., Phillips A.W.
Nature 279:773-777(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Tissue: Muscle.

Cross-references

Sequence databases

PIRKIHOG. A92292.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PGKX-ray3.00A-[»]
ProteinModelPortalP00559.
SMRP00559. Positions 2-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000012929.

Proteomic databases

PRIDEP00559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
HOVERGENHBG008177.
InParanoidP00559.

Enzyme and pathway databases

SABIO-RKP00559.
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

EvolutionaryTraceP00559.

Entry information

Entry namePGK1_HORSE
AccessionPrimary (citable) accession number: P00559
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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