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B3DRV9 (PGK_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:BLD_0432
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

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_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 – 401401Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000096322

Regions

Nucleotide binding358 – 3614ATP By similarity
Region20 – 223Substrate binding By similarity
Region58 – 614Substrate binding By similarity

Sites

Binding site351Substrate By similarity
Binding site1171Substrate By similarity
Binding site1541Substrate By similarity
Binding site2041ATP By similarity
Binding site2981ATP; via carbonyl oxygen By similarity
Binding site3291ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3DRV9 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: EBBCC64FAD95C57F

FASTA40141,866
        10         20         30         40         50         60 
MKTLKDLGDL KGKRVLVRAD FNVPLDGTTI TDDGRIKAAL PTIKTLREEG AKVILMAHLG 

        70         80         90        100        110        120 
RPKGKVVPEL SLAPVAARLG ELLGANVPLA KDTYGEDAQA KVAAMNDGDV VLLENVRFNP 

       130        140        150        160        170        180 
EETSKDADER AAYAKKIAAL GEAFVSDGFG VVHRAQGSNY DVAADLPAAA GLLVEKEVKA 

       190        200        210        220        230        240 
LSKATENPER PFTVVLGGSK VSDKLGVIEN LLDKANRLVI GGGMVFTFLK AKGYEVGTSL 

       250        260        270        280        290        300 
LEEDQLEKVK GYIETAEKNG VELVLPTDVV VNAGFPAGDT PVAPEVVAAD AIPADKMGLD 

       310        320        330        340        350        360 
IGPESQKLFH DKIVDSKTVV WNGPMGVFEV PEFAAGTKAV AQGLVDATAA GAFTIVGGGD 

       370        380        390        400 
SASAVRNLGF PEDGFSHIST GGGASLEFLE GKELPGLKVL E 

« Hide

References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000605 Genomic DNA. Translation: ACD97878.1.
RefSeqYP_001954376.1. NC_010816.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205913.BLD_0432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD97878; ACD97878; BLD_0432.
GeneID6363679.
KEGGblj:BLD_0432.
PATRIC21113790. VBIBifLon134794_0449.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycBLON205913:GJB4-445-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_BIFLD
AccessionPrimary (citable) accession number: B3DRV9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: June 11, 2014
This is version 37 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