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Q04TE9 (PGK_LEPBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:LBJ_1219
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]
Taxonomic identifier355277 [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_1000058009

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
Q04TE9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: F9CA4F7F7978E1D0

FASTA39642,825
        10         20         30         40         50         60 
MELPRLENVD LSGKRVFLRV DFNVPIENGK VTDKTRIEKT LPTIELLIKK GARIIIASHL 

        70         80         90        100        110        120 
GRPKGQTNPE FSLAPVVEVF KGLVKSNVYF SKTVIGDEPI KLSKELRDGE ILVIENVRFH 

       130        140        150        160        170        180 
KEEEENEPGF SKKLAALADV YVNDAFGAAH RAHASTEGIA HLLPAYAGLL MHKEIVELSA 

       190        200        210        220        230        240 
LLAKPARPFV AIIGGSKVSS KIKVLNNLFD KVNHLLIGGG MAYTFLKSRA VPVGNSLVEK 

       250        260        270        280        290        300 
DFEVQAFQLI EKAGVAGVDL QLPVDHIIGD QFNEKAKTKS VDKMGILDGW MGMDIGSKTV 

       310        320        330        340        350        360 
SNYEKIIKNA GTIFWNGPMG VFEMDKFAGG TMAIAKAISK SKAKTVVGGG DSIAAINKAK 

       370        380        390 
VADKITHIST GGGASLEFME GRKLPGVEAL KKKVSE 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JB197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000350 Genomic DNA. Translation: ABJ75821.1.
RefSeqYP_800579.1. NC_008510.1.

3D structure databases

ProteinModelPortalQ04TE9.
SMRQ04TE9. Positions 1-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355277.LBJ_1219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ75821; ABJ75821; LBJ_1219.
GeneID4411065.
KEGGlbj:LBJ_1219.
PATRIC22357694. VBILepBor13265_1561.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLBOR355277:GHYM-1206-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_LEPBJ
AccessionPrimary (citable) accession number: Q04TE9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 48 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