Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate kinase

Gene

pgk

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: 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. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase I (pykF), Pyruvate kinase II (pykA)
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)DescriptionActionsGraphical viewLength
Binding sitei36SubstrateBy similarity1
Binding sitei113SubstrateBy similarity1
Binding sitei146SubstrateBy similarity1
Binding sitei197ATPBy similarity1
Binding sitei314ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi340 – 343ATPBy similarity4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • phosphoglycerate kinase activity Source: EcoCyc

GO - Biological processi

  • glycolytic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PGK.
ECOL316407:JW2893-MONOMER.
MetaCyc:PGK.
BRENDAi2.7.2.3. 2026.
SABIO-RKP0A799.
UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
Gene namesi
Name:pgk
Ordered Locus Names:b2926, JW2893
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10703. pgk.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00001459412 – 387Phosphoglycerate kinaseAdd BLAST386

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A799.
PaxDbiP0A799.
PRIDEiP0A799.

2D gel databases

SWISS-2DPAGEP0A799.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262834. 6 interactors.
DIPiDIP-36163N.
IntActiP0A799. 15 interactors.
MINTiMINT-1229247.
STRINGi511145.b2926.

Structurei

Secondary structure

1387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Beta strandi15 – 19Combined sources5
Beta strandi30 – 32Combined sources3
Helixi35 – 49Combined sources15
Beta strandi53 – 57Combined sources5
Helixi70 – 72Combined sources3
Helixi75 – 84Combined sources10
Beta strandi89 – 93Combined sources5
Beta strandi106 – 109Combined sources4
Helixi112 – 114Combined sources3
Turni116 – 121Combined sources6
Helixi123 – 131Combined sources9
Beta strandi134 – 138Combined sources5
Helixi141 – 143Combined sources3
Turni149 – 153Combined sources5
Helixi154 – 157Combined sources4
Beta strandi158 – 163Combined sources6
Helixi165 – 178Combined sources14
Beta strandi182 – 192Combined sources11
Turni194 – 197Combined sources4
Helixi198 – 205Combined sources8
Beta strandi209 – 215Combined sources7
Helixi216 – 224Combined sources9
Helixi236 – 238Combined sources3
Helixi239 – 246Combined sources8
Beta strandi255 – 266Combined sources12
Beta strandi270 – 273Combined sources4
Helixi274 – 276Combined sources3
Beta strandi282 – 286Combined sources5
Helixi288 – 300Combined sources13
Beta strandi302 – 308Combined sources7
Helixi316 – 318Combined sources3
Helixi320 – 331Combined sources12
Beta strandi332 – 338Combined sources7
Helixi341 – 350Combined sources10
Helixi353 – 355Combined sources3
Beta strandi356 – 359Combined sources4
Helixi364 – 370Combined sources7
Helixi376 – 384Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZMRX-ray2.40A1-387[»]
ProteinModelPortaliP0A799.
SMRiP0A799.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A799.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 23Substrate bindingBy similarity3
Regioni59 – 62Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105BZA. Bacteria.
COG0126. LUCA.
HOGENOMiHOG000227107.
InParanoidiP0A799.
KOiK00927.
OMAiAGHPVGK.
PhylomeDBiP0A799.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
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.

P0A799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ
60 70 80 90 100
GAKVMVTSHL GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD
110 120 130 140 150
VAEGELVVLE NVRFNKGEKK DDETLSKKYA ALCDVFVMDA FGTAHRAQAS
160 170 180 190 200
THGIGKFADV ACAGPLLAAE LDALGKALKE PARPMVAIVG GSKVSTKLTV
210 220 230 240 250
LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD EAKRLLTTCN
260 270 280 290 300
IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN
310 320 330 340 350
AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF
360 370 380
GIADKISYIS TGGGAFLEFV EGKVLPAVAM LEERAKK
Length:387
Mass (Da):41,118
Last modified:January 23, 2007 - v2
Checksum:iFAD7D66D100514B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14436 Genomic DNA. Translation: CAA32604.1.
U28377 Genomic DNA. Translation: AAA69093.1.
U00096 Genomic DNA. Translation: AAC75963.1.
AP009048 Genomic DNA. Translation: BAE76990.1.
PIRiS04733. TVECG.
RefSeqiNP_417401.1. NC_000913.3.
WP_000111269.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75963; AAC75963; b2926.
BAE76990; BAE76990; BAE76990.
GeneIDi947414.
KEGGiecj:JW2893.
eco:b2926.
PATRICi32121266. VBIEscCol129921_3021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14436 Genomic DNA. Translation: CAA32604.1.
U28377 Genomic DNA. Translation: AAA69093.1.
U00096 Genomic DNA. Translation: AAC75963.1.
AP009048 Genomic DNA. Translation: BAE76990.1.
PIRiS04733. TVECG.
RefSeqiNP_417401.1. NC_000913.3.
WP_000111269.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZMRX-ray2.40A1-387[»]
ProteinModelPortaliP0A799.
SMRiP0A799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262834. 6 interactors.
DIPiDIP-36163N.
IntActiP0A799. 15 interactors.
MINTiMINT-1229247.
STRINGi511145.b2926.

2D gel databases

SWISS-2DPAGEP0A799.

Proteomic databases

EPDiP0A799.
PaxDbiP0A799.
PRIDEiP0A799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75963; AAC75963; b2926.
BAE76990; BAE76990; BAE76990.
GeneIDi947414.
KEGGiecj:JW2893.
eco:b2926.
PATRICi32121266. VBIEscCol129921_3021.

Organism-specific databases

EchoBASEiEB0697.
EcoGeneiEG10703. pgk.

Phylogenomic databases

eggNOGiENOG4105BZA. Bacteria.
COG0126. LUCA.
HOGENOMiHOG000227107.
InParanoidiP0A799.
KOiK00927.
OMAiAGHPVGK.
PhylomeDBiP0A799.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.
BioCyciEcoCyc:PGK.
ECOL316407:JW2893-MONOMER.
MetaCyc:PGK.
BRENDAi2.7.2.3. 2026.
SABIO-RKP0A799.

Miscellaneous databases

EvolutionaryTraceiP0A799.
PROiP0A799.

Family and domain databases

CDDicd00318. Phosphoglycerate_kinase. 1 hit.
Gene3Di3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.
HAMAPiMF_00145. Phosphoglyc_kinase. 1 hit.
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...

Entry informationi

Entry nameiPGK_ECOLI
AccessioniPrimary (citable) accession number: P0A799
Secondary accession number(s): P11665, Q2M9R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.