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Q46HH8 (PGK_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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:PMN2A_1562
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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_1000058032

Regions

Nucleotide binding357 – 3604ATP 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
Q46HH8 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: A2EC9334AD508DBF

FASTA40142,359
        10         20         30         40         50         60 
MSKRSLSSLG AEDLCGKRVL VRVDFNVPLG DEGLITDDTR IRAALPTIND LLDKSARVIL 

        70         80         90        100        110        120 
SAHFGRPKGQ VNETMRLTAV AQRLSELLGK TVVKTESCIG AEAKSKVDAM SNGDVVLLEN 

       130        140        150        160        170        180 
VRFISGEEKN DTEFAKELAS LAEVYVNDAF GAAHRAHAST EGVTKFLSPC VAGYLMEKEL 

       190        200        210        220        230        240 
KYLQGAIDQP QSPLAAIVGG SKVSSKIGVL ESLIDKCDKI IVGGGMIFTF YKARGLSVGN 

       250        260        270        280        290        300 
SLVEEDKLEL ASALEKKAQE KGVEFLLPTD VVLADNFSPD ANSKLSKVDA ISEGWMGLDI 

       310        320        330        340        350        360 
GSESVELFQN ALKDCKTVIW NGPMGVFEFE KFANGTNAIA NTLAELSAQG CCTIIGGGDS 

       370        380        390        400 
VAAVEKAGLA KKMSHISTGG GASLELLEGK VLPGVSALDD A 

« 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: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59050.1.
RefSeqYP_292753.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46HH8.
SMRQ46HH8. Positions 1-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1562.

Proteomic databases

PRIDEQ46HH8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59050; AAZ59050; PMN2A_1562.
GeneID3606960.
KEGGpmn:PMN2A_1562.
PATRIC23022599. VBIProMar14922_0258.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227107.
KOK00927.
OMAWEALDIG.
OrthoDBEOG64N9Z0.
PhylomeDBQ46HH8.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-256-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_PROMT
AccessionPrimary (citable) accession number: Q46HH8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 60 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