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A8G2K1 (PGK_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:P9215_02131
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length402 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 – 402402Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000058027

Regions

Nucleotide binding358 – 3614ATP By similarity
Region24 – 263Substrate binding By similarity
Region63 – 664Substrate binding By similarity

Sites

Binding site401Substrate By similarity
Binding site1221Substrate By similarity
Binding site1551Substrate By similarity
Binding site2061ATP By similarity
Binding site2971ATP; via carbonyl oxygen By similarity
Binding site3281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G2K1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 1AB1437A660F106F

FASTA40242,761
        10         20         30         40         50         60 
MSKLSLSSLD KTHLEGKKVL VRVDFNVPLN EDGQITDDTR IRAAIPTIEY LINHSAKVIL 

        70         80         90        100        110        120 
AAHFGRPKGQ VNEKMRLTPV AARLSELLGQ NVALTNSCIG DEAIAQSNSL SNGDVLLLEN 

       130        140        150        160        170        180 
VRFFGEEEKN DLEFAKKLAS HADMYINDAF GAAHRAHAST QGVTNYLSPS VAGFLLEKEL 

       190        200        210        220        230        240 
KYLQGAIDSP KRPLAAIVGG SKVSSKIGVL DSLLDKCDKI MIGGGMIFTF YKARGLDVGK 

       250        260        270        280        290        300 
SLVEEDKLKL AKDLEAKAKA KGVELLLPTD VVLADEFSPD ANSKISRIDS ISGNWMGLDI 

       310        320        330        340        350        360 
GPDSIKVFQN ALAECKTIIW NGPMGVFEFD KFAEGTNAIA TTLADLSAFS EVCTIIGGGD 

       370        380        390        400 
SVAAVEKAGL AEKMSHISTG GGASLELLEG KTLPGVAALN DA 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV49832.1.
RefSeqYP_001483418.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G2K1.
SMRA8G2K1. Positions 1-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_02131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV49832; ABV49832; P9215_02131.
GeneID5616481.
KEGGpmh:P9215_02131.
PATRIC22989839. VBIProMar119824_0212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAVEDDKID.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycPMAR93060:GI08-218-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_PROM2
AccessionPrimary (citable) accession number: A8G2K1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 44 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