Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoglycerate kinase

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoglycerate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglycerate kinase (EC:2.7.2.3)
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›20›20Phosphoglycerate kinasePRO_0000145901Add
BLAST

Expressioni

Inductioni

By heat shock.1 Publication

Interactioni

Subunit structurei

Monomer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphoglycerate kinase family.Curated

Sequencei

Sequence statusi: Fragment.

P83075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20
MNKKSIRNVN LKGKRVFDRV
Length:20
Mass (Da):2,403
Last modified:September 25, 2001 - v1
Checksum:iEDAD2CAF1155C353
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei20 – 201

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00185.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Heat and salt stress in the food pathogen Bacillus cereus."
    Browne N., Dowds B.C.A.
    J. Appl. Microbiol. 91:1085-1094(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, INDUCTION.
    Strain: NCIMB 11796 / DSM 626.

Entry informationi

Entry nameiPGK_BACCE
AccessioniPrimary (citable) accession number: P83075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 25, 2001
Last sequence update: September 25, 2001
Last modified: January 6, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.