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P18912 (PGK_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm HAMAP-Rule MF_00145.

Sequence similarities

Belongs to the phosphoglycerate kinase family.

Sequence caution

The sequence AAA22462.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
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 – 394394Phosphoglycerate kinase HAMAP-Rule MF_00145
PRO_0000145904

Regions

Nucleotide binding350 – 3534ATP HAMAP-Rule 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
Binding site3161ATP
Binding site3231ATP

Amino acid modifications

Modified residue1831Phosphoserine By similarity
Modified residue2991Phosphothreonine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P18912 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-174 IN COMPLEX WITH ADP.

Cross-references

Sequence databases

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

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHPX-ray1.65A1-394[»]
ProteinModelPortalP18912.
SMRP18912. Positions 1-394.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP18912.
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...

Other

EvolutionaryTraceP18912.

Entry information

Entry namePGK_GEOSE
AccessionPrimary (citable) accession number: P18912
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 88 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways