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Q5X8U1 (PGK_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:lpp0152
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00145

Subcellular location

Cytoplasm Potential 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycerate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058005

Regions

Nucleotide binding345 – 3484ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1131Substrate By similarity
Binding site1461Substrate By similarity
Binding site1971ATP By similarity
Binding site3191ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X8U1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9138B0E059386C26

FASTA39642,676
        10         20         30         40         50         60 
MNLIKMSDID LSGKRVLIRE DLNVPIKDGM ITSDQRLQAA LPTIKSALDN GAAVIVLSHL 

        70         80         90        100        110        120 
GRPEEGKYEK KFSLEPVADY LRKNLEYPVR FVKDYLSGVD VKPGELVVCE NVRFNPGEKA 

       130        140        150        160        170        180 
NDEALAKKLA NLCDVFVMDA FGTAHRAQAS TYGVAQYAPV AVAGPLLIRE LEALNQVLKA 

       190        200        210        220        230        240 
PKKPIVAIVG GAKVSSKLSL LKQLVGMVDV LIPGGGIANT FLKAQGFEIG ISLYEPDLLD 

       250        260        270        280        290        300 
EARHILILAK EKGCQIPLPT DVVVGKTFSE TCPAFNKSLS NVAEDDMILD IGPETIRDYV 

       310        320        330        340        350        360 
DLIHEANTII WNGPVGVFEF PQFAYGTRAI AIAIAESDAF SIAGGGDTLA AVDLYDLNQQ 

       370        380        390 
ISYISTGGGA FLECLEGKTL PAVAILQERA KHVKTN 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH11300.1.
RefSeqYP_122502.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X8U1.
SMRQ5X8U1. Positions 2-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp0152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH11300; CAH11300; lpp0152.
GeneID3117439.
KEGGlpp:lpp0152.
PATRIC22320456. VBILegPne27771_0309.

Organism-specific databases

LegioListlpp0152.
CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycLPNE297246:GCO9-170-MONOMER.
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...

Entry information

Entry namePGK_LEGPA
AccessionPrimary (citable) accession number: Q5X8U1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 23, 2004
Last modified: June 11, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways