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Q1GB26 (PGK_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:Ldb0636
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length403 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 – 403403Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000009620

Regions

Nucleotide binding359 – 3624ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1191Substrate By similarity
Binding site1591Substrate By similarity
Binding site2141ATP By similarity
Binding site3011ATP; via carbonyl oxygen By similarity
Binding site3321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GB26 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: D90FC78FBB9FE397

FASTA40342,712
        10         20         30         40         50         60 
MAKLIVSDVD VKDKKVLVRV DFNVPIKDGV IGDDNRIVAA LPTIKYIIEN GGKAILLSHL 

        70         80         90        100        110        120 
GRIKSDEDKK SLSLAPVAKR LGELLEKPVT FVPSNEGKEV EDAINNMKDG DVVVLENTRF 

       130        140        150        160        170        180 
QDIDNDFGKR ESKNDPKLGE YWASLGDVFV NDAFGTAHRS HASNVGIATA MKAAGKPAAA 

       190        200        210        220        230        240 
GFLLEKEIKF LGNAVANPVH PFVTILGGAK VSDKIGVITN LIPKADHIII GGGMAYTFLK 

       250        260        270        280        290        300 
AQGHNIGKSL VEDDKVEFAK ELLEKAGDKL VLPIDNVAAT EFNNDAASEV VGQDIPDNEM 

       310        320        330        340        350        360 
GLDIGPKTIE LFKKTLEGAK TVVWNGPMGV FEMPNFAKGT LEVGRALADL PDATTIVGGG 

       370        380        390        400 
DSTAAAKQLG IAPKLTHIST GGGASLEYLE GKELPGIACV SDK 

« Hide

References

[1]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954253 Genomic DNA. Translation: CAI97465.1.
RefSeqYP_618714.1. NC_008054.1.

3D structure databases

ProteinModelPortalQ1GB26.
SMRQ1GB26. Positions 3-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390333.Ldb0636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI97465; CAI97465; Ldb0636.
GeneID4085052.
KEGGldb:Ldb0636.
PATRIC22216875. VBILacDel123523_0583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAAGHPVGK.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycLDEL390333:GIXG-632-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_LACDA
AccessionPrimary (citable) accession number: Q1GB26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: June 11, 2014
This is version 55 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