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Q7V390 (PGK_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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:PMM0195
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [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_0000145987

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
Q7V390 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0B2EA9934AE8AFB3

FASTA40242,964
        10         20         30         40         50         60 
MSKLSLSSLD KSKLEGKKVL VRVDFNVPLN DSGQITDDTR IRAAIPTIKY LINNSAKVIL 

        70         80         90        100        110        120 
AAHFGRPKGK VNEKMRLTPV AARLSDILEQ KVNLTESCIG EEALAKSNSL NNGEVLLLEN 

       130        140        150        160        170        180 
VRFYEEEEKN DLDFAKNLAS HADMYVNDAF GAAHRAHAST QGVTKFLEPA VAGFLLEKEL 

       190        200        210        220        230        240 
KYLQGAIDAP KRPLAAIVGG SKVSSKIGVL DSLLDKCDKI IIGGGMIFTF YKARGLDVGK 

       250        260        270        280        290        300 
SLVEEDKLEL ARNLEAKAKN KGVELLLPSD VLLANEFSPD AESKVSQIDA ISGDWMGLDI 

       310        320        330        340        350        360 
GPQSIKVFQN ALAECKTIIW NGPMGVFEFD KFAEGTNAIA TTLADLSSFS EVCTIIGGGD 

       370        380        390        400 
SVAAVEKAGL AEKMSHISTG GGASLELLEG KTLPGVAALK DA 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18654.1.
RefSeqNP_892316.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V390.
SMRQ7V390. Positions 1-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE18654; CAE18654; PMM0195.
GeneID1726439.
KEGGpmm:PMM0195.
PATRIC23031036. VBIProMar68066_0202.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAVEDDKID.
OrthoDBEOG64N9Z0.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-200-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_PROMP
AccessionPrimary (citable) accession number: Q7V390
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 63 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