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Protein

Phosphoglycerate kinase 1

Gene

PGK1

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathway: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (LOC100054877), Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Enolase, Enolase
  5. Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKM), Pyruvate kinase (PKLR)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391SubstrateBy similarity
Binding sitei123 – 1231SubstrateBy similarity
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei220 – 2201ATPBy similarity
Binding sitei313 – 3131ATP; via carbonyl oxygenBy similarity
Binding sitei344 – 3441ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • phosphoglycerate kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP00559.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase 1 (EC:2.7.2.3)
Gene namesi
Name:PGK1
Synonyms:PGK
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
ProteomesiUP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 417416Phosphoglycerate kinase 1PRO_0000145829Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei6 – 61N6-succinyllysineBy similarity
Modified residuei11 – 111N6-acetyllysineBy similarity
Modified residuei48 – 481N6-acetyllysine; alternateBy similarity
Modified residuei48 – 481N6-succinyllysine; alternateBy similarity
Modified residuei75 – 751N6-acetyllysineBy similarity
Modified residuei76 – 761PhosphotyrosineBy similarity
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysine; alternateBy similarity
Modified residuei131 – 1311N6-malonyllysine; alternateBy similarity
Modified residuei146 – 1461N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-succinyllysineBy similarity
Modified residuei196 – 1961PhosphotyrosineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei267 – 2671N6-acetyllysineBy similarity
Modified residuei291 – 2911N6-acetyllysineBy similarity
Modified residuei361 – 3611N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00559.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9796.ENSECAP00000012929.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PGKX-ray3.00A-[»]
ProteinModelPortaliP00559.
SMRiP00559. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00559.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 186185Globular domain-1Add
BLAST
Regioni24 – 263Substrate bindingBy similarity
Regioni63 – 664Substrate bindingBy similarity
Regioni187 – 1904Linker
Regioni191 – 417227Globular domain-2Add
BLAST
Regioni406 – 41712Associated with globular domain 1Add
BLAST

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0126.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP00559.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00559-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSNKLTLD KLNVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC
60 70 80 90 100
LDNGAKSVVL MSHLGRPDVG PMPDKYSLQP VAVELKSLLG KDVLFLKDCV
110 120 130 140 150
GPEVEKACAD PAAGSVILLE NLRFHVEEEG KGKDASGNKV KAEPAKIETF
160 170 180 190 200
RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPQKAGGFLM KKELNYFAKA
210 220 230 240 250
LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN
260 270 280 290 300
MEIGTSLFDE EGAKIVKNLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
310 320 330 340 350
ATVASGIPAG WMGLDCGTES SKKYAEAVAR AKQIVWNGPV GVFEWEAFAR
360 370 380 390 400
GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL
410
ELLEGKVLPG VDALSNV
Length:417
Mass (Da):44,603
Last modified:January 23, 2007 - v2
Checksum:i5110E246AF96931A
GO

Sequence databases

PIRiA92292. KIHOG.

Cross-referencesi

Sequence databases

PIRiA92292. KIHOG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PGKX-ray3.00A-[»]
ProteinModelPortaliP00559.
SMRiP00559. Positions 2-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000012929.

Proteomic databases

PRIDEiP00559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0126.
HOGENOMiHOG000227107.
HOVERGENiHBG008177.
InParanoidiP00559.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
SABIO-RKP00559.

Miscellaneous databases

EvolutionaryTraceiP00559.

Family and domain databases

Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase.
InterProiIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
PANTHERiPTHR11406. PTHR11406. 1 hit.
PfamiPF00162. PGK. 1 hit.
[Graphical view]
PIRSFiPIRSF000724. Pgk. 1 hit.
PRINTSiPR00477. PHGLYCKINASE.
SUPFAMiSSF53748. SSF53748. 1 hit.
PROSITEiPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPGK1_HORSE
AccessioniPrimary (citable) accession number: P00559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.