Phosphoglycerate kinase - Escherichia coli (strain K12)

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P0A799 (PGK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoglycerate kinase
EC=2.7.2.3

Gene names

Name:	pgk
Ordered Locus Names:	b2926, JW2893

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Glycolysis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglycerate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5 Ref.6

Chain

2 – 387

386

Phosphoglycerate kinase HAMAP-Rule MF_00145

PRO_0000145941

Regions

Nucleotide binding

340 – 343

ATP By similarity

Region

21 – 23

Substrate binding By similarity

Region

59 – 62

Substrate binding By similarity

Sites

Binding site

Substrate By similarity

Binding site

113

Substrate By similarity

Binding site

146

Substrate By similarity

Binding site

197

ATP By similarity

Binding site

314

ATP By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.7

Secondary structure

387

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A799 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FAD7D66D100514B2
Show »

FASTA

387

41,118

        10         20         30         40         50         60 
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAS LPTIELALKQ GAKVMVTSHL 

        70         80         90        100        110        120 
GRPTEGEYNE EFSLLPVVNY LKDKLSNPVR LVKDYLDGVD VAEGELVVLE NVRFNKGEKK 

       130        140        150        160        170        180 
DDETLSKKYA ALCDVFVMDA FGTAHRAQAS THGIGKFADV ACAGPLLAAE LDALGKALKE 

       190        200        210        220        230        240 
PARPMVAIVG GSKVSTKLTV LDSLSKIADQ LIVGGGIANT FIAAQGHDVG KSLYEADLVD 

       250        260        270        280        290        300 
EAKRLLTTCN IPVPSDVRVA TEFSETAPAT LKSVNDVKAD EQILDIGDAS AQELAEILKN 

       310        320        330        340        350        360 
AKTILWNGPV GVFEFPNFRK GTEIVANAIA DSEAFSIAGG GDTLAAIDLF GIADKISYIS 

       370        380 
TGGGAFLEFV EGKVLPAVAM LEERAKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli." Alefounder P.R., Perham R.N. Mol. Microbiol. 3:723-732(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS520.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24. Strain: K12 / EMG2.
[5]	Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F. Submitted (FEB-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14436 Genomic DNA. Translation: CAA32604.1.
U28377 Genomic DNA. Translation: AAA69093.1.
U00096 Genomic DNA. Translation: AAC75963.1.
AP009048 Genomic DNA. Translation: BAE76990.1.

PIR

TVECG. S04733.

RefSeq

NP_417401.1. NC_000913.2.
YP_491126.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZMR	X-ray	2.40	A	1-387	[»]

ProteinModelPortal

P0A799.

SMR

P0A799. Positions 2-387.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36163N.

IntAct

P0A799. 14 interactions.

MINT

MINT-1229247.

STRING

511145.b2926.

PTM databases

PhosSite

P0810419.

2D gel databases

SWISS-2DPAGE

P0A799.

Proteomic databases

PaxDb

P0A799.

PRIDE

P0A799.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75963; AAC75963; b2926.
BAE76990; BAE76990; BAE76990.

GeneID

12933840.
947414.

KEGG

ecj:Y75_p2857.
eco:b2926.

PATRIC

32121266. VBIEscCol129921_3021.

Organism-specific databases

EchoBASE

EB0697.

EcoGene

EG10703. pgk.

Phylogenomic databases

eggNOG

COG0126.

HOGENOM

HOG000227107.

K00927.

OMA

EKKNDEA.

ProtClustDB

PRK00073.

Enzyme and pathway databases

BioCyc

EcoCyc:PGK.
ECOL316407:JW2893-MONOMER.
MetaCyc:PGK.

SABIO-RK

P0A799.

UniPathway

UPA00109; UER00185.

Gene expression databases

Genevestigator

P0A799.

Family and domain databases

Gene3D

3.40.50.1260. 1 hit.
3.40.50.1270. 1 hit.

HAMAP

MF_00145. Phosphoglyc_kinase.

InterPro

IPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]

PANTHER

PTHR11406. PTHR11406. 1 hit.

Pfam

PF00162. PGK. 1 hit.
[Graphical view]

PIRSF

PIRSF000724. Pgk. 1 hit.

PRINTS

PR00477. PHGLYCKINASE.

SUPFAM

SSF53748. PGK. 1 hit.

PROSITE

PS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A799.

Entry information

Entry name

PGK_ECOLI

Accession

Primary (citable) accession number: P0A799
Secondary accession number(s): P11665, Q2M9R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents