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Q2JXF0 (PGK_SYNJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:CYA_0315
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length412 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 – 412412Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058075

Regions

Nucleotide binding368 – 3714ATP By similarity
Region26 – 283Substrate binding By similarity
Region65 – 684Substrate binding By similarity

Sites

Binding site421Substrate By similarity
Binding site1331Substrate By similarity
Binding site1661Substrate By similarity
Binding site2171ATP By similarity
Binding site3081ATP; via carbonyl oxygen By similarity
Binding site3391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JXF0 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: F4AB57F05B62607F

FASTA41243,225
        10         20         30         40         50         60 
MAKQTLGSLL SSGFDLKGKR VLVRADFNVP LDPQGNITDD TRIRASLPTI QALAQAGAKV 

        70         80         90        100        110        120 
ILTSHLGRPI QKDKATGAIQ IAREGNSLAP VAVRLAQLLG QPVAFAPDCI GPEAEAVVSS 

       130        140        150        160        170        180 
LENGQVALLE NVRFHPEEEA NDPEFARKLA SLADLFVNDA FGSAHRAHAS TAGVTAYLQP 

       190        200        210        220        230        240 
AVAGYLVEKE LQFLSGAIEN PQRPLAAIIG GSKVSTKIGV IERLLEKVDK LLLGGGMIFT 

       250        260        270        280        290        300 
FYQAQGIPTG KSLVETDKLD LARSLMEKAK ARGVELLLPV DVVVADRFDK DANAQTVSIH 

       310        320        330        340        350        360 
AIPEDWMGLD IGPESVKAFQ AALQGCKTVV WNGPMGVFEF DRFAAGTEAI ARTLADLTQA 

       370        380        390        400        410 
GAITIIGGGD SVAAVEKVGL ADKMTHISTG GGASLELLEG KELPGIAALS EA 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000239 Genomic DNA. Translation: ABC98536.1.
RefSeqYP_473799.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JXF0.
SMRQ2JXF0. Positions 1-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321327.CYA_0315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC98536; ABC98536; CYA_0315.
GeneID3898060.
KEGGcya:CYA_0315.
PATRIC23808909. VBISynSp90045_0321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMADMIFDIG.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycSSP321327:GHFX-312-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_SYNJA
AccessionPrimary (citable) accession number: Q2JXF0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 56 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