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C1KY97 (PGK_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 33. 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:Lm4b_02427
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

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_1000203337

Regions

Nucleotide binding352 – 3554ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1561Substrate By similarity
Binding site2061ATP By similarity
Binding site2941ATP; via carbonyl oxygen By similarity
Binding site3251ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C1KY97 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 0FFF1A3D7E69732D

FASTA39642,075
        10         20         30         40         50         60 
MAKKVVTDLD LKDKKVLVRV DFNVPMKDGK ITNDNRIVAA LPTIEYILEQ NGKAILFSHL 

        70         80         90        100        110        120 
GKVKTEEDKE GKSLRPVAAR LSELLGKEVK FVPTTRGPEL EKAIDELKDG EVLLFENTRF 

       130        140        150        160        170        180 
EDIDGKKESK NDPELGKYWA SLGDVFVNDA FGTAHRAHAS NVGIASNLES AAGFLMEKEI 

       190        200        210        220        230        240 
KFIGGVVDNP ARPLVAILGG AKVSDKIGVI ENLLTKADKV LVGGGMTFTF MAAQGQEIGK 

       250        260        270        280        290        300 
SLLEADKVEL AKGLLEKAGN KLVLPVDAVV SKEFSNDAPF HTVSADSIPA DEMGLDIGQA 

       310        320        330        340        350        360 
TIDLFTKELQ GAKTVVWNGP MGVFELSNFA KGTIGVCEAI ANLTDATTII GGGDSAAAAM 

       370        380        390 
DLGFADKFTH ISTGGGASLE YLEGKELPGV ASISDK 

« Hide

References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS06182.1.
RefSeqYP_002759113.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1KY97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_02427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS06182; CAS06182; Lm4b_02427.
GeneID7701606.
KEGGlmc:Lm4b_02427.
PATRIC20308159. VBILisMon88360_2452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227108.
KOK00927.
OMAWEALDIG.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycLMON568819:GJF9-3609-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_LISMC
AccessionPrimary (citable) accession number: C1KY97
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 33 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