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Reviewed, UniProtKB/Swiss-Prot P18912 (PGK_BACST)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphoglycerate kinase
    EC=2.7.2.3
Gene names
Name: pgk
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

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Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. HAMAP MF_00145

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. HAMAP MF_00145

Subunit structure

Monomer. HAMAP MF_00145

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: 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: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Phosphoglycerate kinase HAMAP MF_00145
PRO_0000145904

Regions

Nucleotide binding350 – 3534ATP HAMAP MF_00145
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 HAMAP MF_00145
Binding site3161ATP HAMAP MF_00145
Binding site3231ATP HAMAP MF_00145

Amino acid modifications

Modified residue1831Phosphoserine By similarity
Modified residue2991Phosphothreonine By similarity

Secondary structure

1 ............................................................................. 394
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P18912-1 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 46BFA286F60E365A

FASTA39442,730
        10         20         30         40         50         60 
MNKKTIRDVD VRGKRVFCRV DFNVPMEQGA ITDDTRIRAA LPTIRYLIEH GAKVILASHL 

        70         80         90        100        110        120 
GRPKGKVVEE LRLDAVAKRL GELLERPVAK TNEAVGDEVK AAVDRLNEGD VLLLENVRFY 

       130        140        150        160        170        180 
PGEEKNDPEL AKAFAELADL YVNDAFGAAH RAHASTEGIA HYLPAVAGFL MEKELEVLGK 

       190        200        210        220        230        240 
ALSNPDRPFT AIIGGAKVKD KIGVIDNLLE KVDNLIIGGG LAYTFVKALG HDVGKSLLEE 

       250        260        270        280        290        300 
DKIELAKSFM EKAKEKGVRF YMPVDVVVAD RFANDANTKV VPIDAIPADW SALDIGPKTR 

       310        320        330        340        350        360 
ELYRDVIRES KLVVWNGPMG VFEMDAFAHG TKAIAEALAE ALDTYSVIGG GDSAAAVEKF 

       370        380        390 
GLADKMDHIS TGGGASLEFM EGKQLPGVVA LEDK

« Hide

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References

[1]"Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus."
Davies G.J., Littlechild J.A., Watson H.C., Hall L.
Gene 109:39-45(1991) [PubMed: 1756980] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli."
Branlant C., Oster T., Branlant G.
Gene 75:145-155(1989) [PubMed: 2656407] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
[3]"Purification, crystallization and preliminary X-ray analysis of the 3-phosphoglycerate kinase from Bacillus stearothermophilus."
Davies G.J., Gamblin S.J., Littlechild J.A., Watson H.C.
J. Mol. Biol. 227:1263-1264(1992) [PubMed: 1433299] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]"Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 A."
Davies G.J., Gamblin S.J., Littlechild J.A., Dauter Z., Wilson K.S., Watson H.C.
Acta Crystallogr. D 50:202-209(1994) [PubMed: 15299460] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[5]"Is the structure of the N-domain of phosphoglycerate kinase affected by isolation from the intact molecule?"
Hosszu L.L.P., Craven C.J., Spencer J., Parker M.J., Clarke A.R., Kelly M., Waltho J.P.
Biochemistry 36:333-340(1997) [PubMed: 9003185] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-174 IN COMPLEX WITH ADP.

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Cross-references

Sequence databases

X58059 Genomic DNA. Translation: CAA41093.1.
M24493 Genomic DNA. Translation: AAA22462.1. Different initiation.
PIRJQ1399.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PHPX-ray1.65A1-394[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.2.3. 266715.

Family and domain databases

HAMAPMF_00145.
[Tree]
InterProIPR001576. Phosphoglycerate_kinase.
IPR015901. Phosphoglycerate_kinase_C.
IPR015911. Phosphoglycerate_kinase_CS.
IPR015824. Phosphoglycerate_kinase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.1270. Phosphoglycerate_kinase_C. 1 hit.
G3DSA:3.40.50.1260. Phosphoglycerate_kinase_N. 1 hit.
PANTHERPTHR11406. PGK. 1 hit.
PfamPF00162. PGK. 1 hit.
[Graphical view]
PRINTSPR00477. PHGLYCKINASE.
PROSITEPS00111. PGLYCERATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePGK_BACST
AccessionPrimary (citable) accession number: P18912
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents