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B0SSU3 (PGK_LEPBP) 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:LEPBI_I2081
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris) [Complete proteome] [HAMAP]
Taxonomic identifier456481 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

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_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 – 396396Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096354

Regions

Nucleotide binding349 – 3524ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1181Substrate By similarity
Binding site1511Substrate By similarity
Binding site2011ATP By similarity
Binding site2921ATP; via carbonyl oxygen By similarity
Binding site3231ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SSU3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5AE0ECF02239D1C4

FASTA39642,739
        10         20         30         40         50         60 
MKLPLLEEQN LKGKRVFVRV DFNVPVENGK ATDRTRIEKT LPTLELLISK GAKIILGSHL 

        70         80         90        100        110        120 
GRPKGGPEPK YSMKPVFDVL SELVKTKVSF SESVIGSDVV KMTNALGEGE ILLLENLRFH 

       130        140        150        160        170        180 
KEEEENVASF CKELAKLADV YVNDAFGTAH RAHASTEGVA HLLPAFAGLL MRKEIEVLSG 

       190        200        210        220        230        240 
LLAKPERPFV AIVGGSKVSS KFAILKNLLE KVDHLLIGGG MAYTFLKSRA VPVGKSLVEP 

       250        260        270        280        290        300 
EFESQAFQLI DRAGIQGVDL QIPVDHIIAD AFDPNAKTKS VDKMGIIDGW MGMDIGPKTI 

       310        320        330        340        350        360 
DNYVKAIKDA KTILWNGPMG VFEMDKFSKG TIEIAKAISK SKAKTVVGGG DSIAAVNKAG 

       370        380        390 
VADKITHIST GGGASLEFLE GRTLPGVQCL LPKEEK 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / ATCC 23582 / Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000786 Genomic DNA. Translation: ABZ98183.1.
RefSeqYP_001839459.1. NC_010602.1.

3D structure databases

ProteinModelPortalB0SSU3.
SMRB0SSU3. Positions 1-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING456481.LEPBI_I2081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ98183; ABZ98183; LEPBI_I2081.
GeneID6223070.
KEGGlbi:LEPBI_I2081.
PATRIC22351000. VBILepBif123590_2126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycLBIF456481:GCM0-2068-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_LEPBP
AccessionPrimary (citable) accession number: B0SSU3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 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