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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: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase 2 (gap2), Glyceraldehyde-3-phosphate dehydrogenase 1 (gap1)
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_2), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase, Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk_1)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_2), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno), Enolase (eno_2), Enolase (eno), Enolase (eno_1), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (B4077_4482), Pyruvate kinase (pyk_3), Pyruvate kinase (TU62_03210), Pyruvate kinase (B4080_3619), Pyruvate kinase (B4077_3950), Pyruvate kinase (pyk_1), Pyruvate kinase (B4080_4928), Pyruvate kinase (TU62_18460), Pyruvate kinase (TU52_01675), Pyruvate kinase (pyk_2), Pyruvate kinase (TU52_29880), Pyruvate kinase (pyk_2), Pyruvate kinase (pyk_1), Pyruvate kinase (TU65_15370), Pyruvate kinase (TU65_15970), Pyruvate kinase (B4087_3378), Pyruvate kinase (TU58_10150), Pyruvate kinase (B4147_3784), Pyruvate kinase (pyk), Pyruvate kinase (TQ94_24925), Pyruvate kinase (TU68_07390), Pyruvate kinase (pyk), Pyruvate kinase (TQ94_03065), Pyruvate kinase (TU68_27375)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

GO - Molecular functioni

GO - Biological processi

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

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 26, 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(2001) [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 26, 2001
Last sequence update: September 26, 2001
Last modified: January 7, 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

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 one 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.