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B2G616 (PGK_LACRJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:LAR_0382
OrganismLactobacillus reuteri (strain JCM 1112) [Complete proteome] [HAMAP]
Taxonomic identifier557433 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length401 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_processglycolysis

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 – 401401Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096352

Regions

Nucleotide binding357 – 3604ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1601Substrate By similarity
Binding site2121ATP By similarity
Binding site3301ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2G616 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: D33394B04739DF8A

FASTA40142,960
        10         20         30         40         50         60 
MAKLTVEDLP LEGKKVLMRV DFNVPIKDGV VGDDNRIVAA LPTIKYVIDH GGRAILFSHL 

        70         80         90        100        110        120 
GRIKKEEDKP GLSLRPVAER LSNLLNKPVT FVPVTEGKQL EDAIDNMKNG DVLLVQNTRY 

       130        140        150        160        170        180 
EDVKDGEYVK RESGNDPELG KYWASLGDVF VNDAFGTAHR KHASNVGIAT NMPGKAAAGY 

       190        200        210        220        230        240 
LMEKEIKFLG DAVDNPERPF VAILGGAKVS DKIGVIDNLL DKADKIIIGG GMAYTFYAAK 

       250        260        270        280        290        300 
GIKVGNSLVE KDKIDVAKQI LDKAGDKLVL PIDNVVADKF NNDADTKVVE GDIDNGWMAL 

       310        320        330        340        350        360 
DIGPKSVEEF KNVLKDAKTV VWNGPMGVFE MPNFAKGTLE IGKFLGTLTD ATTIVGGGDS 

       370        380        390        400 
TAAVKELGVA DKLTHISTGG GASLTYLEGN ELPGIAAISD K 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 1112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007281 Genomic DNA. Translation: BAG24898.1.
RefSeqYP_001841378.1. NC_010609.1.

3D structure databases

ProteinModelPortalB2G616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557433.LAR_0382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG24898; BAG24898; LAR_0382.
GeneID6231184.
KEGGlrf:LAR_0382.
PATRIC22258005. VBILacReu111271_0402.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBCLSK2337251.

Enzyme and pathway databases

BioCycLREU557433:GHNR-402-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_LACRJ
AccessionPrimary (citable) accession number: B2G616
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 39 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