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B9J4M7 (PGK_BACCQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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:BCQ_4943
OrganismBacillus cereus (strain Q1) [Complete proteome] [HAMAP]
Taxonomic identifier361100 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length394 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
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

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 – 394394Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_1000192801

Regions

Nucleotide binding350 – 3534ATP By similarity
Region21 – 233Substrate binding By similarity
Region59 – 624Substrate binding By similarity

Sites

Binding site361Substrate By similarity
Binding site1181Substrate By similarity
Binding site1511Substrate By similarity
Binding site2011ATP By similarity
Binding site2921ATP; via carbonyl oxygen By similarity
Binding site3231ATP By similarity

Amino acid modifications

Modified residue1831Phosphoserine By similarity
Modified residue2991Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
B9J4M7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: FBE4C1BB4B427240

FASTA39442,299
        10         20         30         40         50         60 
MNKKSIRDVD LKGKRVFCRV DFNVPMKEGK ITDETRIRAA LPTIQYLVEQ GAKVILASHL 

        70         80         90        100        110        120 
GRPKGQVVEE LRLTPVAARL GELLGKDVKK ADEAFGPVAQ EMVAAMNEGD VLVLENVRFY 

       130        140        150        160        170        180 
AGEEKNDAEL AKEFAALADI FVNDAFGAAH RAHASTAGIA DYLPAVSGLL MEKELDVLGK 

       190        200        210        220        230        240 
ALSNPDRPFT AIIGGAKVKD KIGVIRHLLD KVDNLIIGGG LAYTFVKALG HEIGLSLCED 

       250        260        270        280        290        300 
DKIELAKEFM QLAKEKGVNF YMPVDVVITE EFSETATTKI VGIDSIPSNW EGVDIGPKTR 

       310        320        330        340        350        360 
EIYADVIKNS KLVVWNGPMG VFEMTPFSQG TKAVGQALAD AEGTYSVIGG GDSAAAVEKF 

       370        380        390 
GMADKMSHIS TGGGASLEFM EGKELPGVVC LNDK 

« Hide

References

[1]"Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Q1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000227 Genomic DNA. Translation: ACM15344.1.
RefSeqYP_002532633.1. NC_011969.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING361100.BCQ_4943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM15344; ACM15344; BCQ_4943.
GeneID7375195.
KEGGbcq:BCQ_4943.
PATRIC18917695. VBIBacCer120424_4987.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0126.
HOGENOMHOG000227108.
KOK00927.
OMAFGLADKM.
OrthoDBEOG64N9Z0.
ProtClustDBPRK00073.

Enzyme and pathway databases

BioCycBCER361100:GJ7M-4930-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_BACCQ
AccessionPrimary (citable) accession number: B9J4M7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 32 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