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Q02499 (KPYK_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate kinase
Short name=PK
EC=2.7.1.40
Gene names
Name:pyk
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactor

Magnesium.

Potassium.

Enzyme regulation

Regulated by phosphoenolpyruvate substrate and is allosterically activated by ribose-5-phosphate, AMP and other nucleoside monophosphates but not by fructose-1,6-bisphosphate.

Pathway

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

Subunit structure

Homotetramer.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the pyruvate kinase family.

In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Sequence caution

The sequence CAA40994.1 differs from that shown. Reason: Frameshift at position 486.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Pyruvate kinase
PRO_0000112055

Sites

Metal binding351Potassium By similarity
Metal binding371Potassium By similarity
Metal binding671Potassium By similarity
Metal binding681Potassium; via carbonyl oxygen By similarity
Metal binding2231Magnesium By similarity
Metal binding2471Magnesium By similarity
Binding site331Substrate By similarity
Binding site2461Substrate; via amide nitrogen By similarity
Binding site2471Substrate; via amide nitrogen By similarity
Binding site2791Substrate By similarity
Site2211Transition state stabilizer By similarity

Amino acid modifications

Modified residue5411Phosphohistidine By similarity

Experimental info

Mutagenesis3081D → E: Reduced activity; when associated with Y-416.
Mutagenesis4161W → Y: Increased activity.

Secondary structure

1 .................................................................................................... 587
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02499 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 0794BA1A07BE0D5A

FASTA58762,318
        10         20         30         40         50         60 
MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN IREAAKRTGR 

        70         80         90        100        110        120 
TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG TPEKISVTYP SLIDDVSVGA 

       130        140        150        160        170        180 
KILLDDGLIS LEVNAVDKQA GEIVTTVLNG GVLKNKKGVN VPGVKVNLPG ITEKDRADIL 

       190        200        210        220        230        240 
FGIRQGIDFI AASFVRRASD VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG 

       250        260        270        280        290        300 
LMVARGDLGV EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA 

       310        320        330        340        350        360 
NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT KESQTTITDA 

       370        380        390        400        410        420 
IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII AVTSNEAVSR RLALVWGVYT 

       430        440        450        460        470        480 
KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD LVVITAGVPV GETGSTNLMK VHVISDLLAK 

       490        500        510        520        530        540 
GQGIGRKSAF GKAVVAKTAE EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS 

       550        560        570        580 
HAAVVGLSLG IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon."
Sakai H., Ohta T.
Eur. J. Biochem. 211:851-859(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 328-346 AND 393-396.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
[2]"Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis."
Walker D., Chia W.N., Muirhead H.
J. Mol. Biol. 228:265-276(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-51.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13095 Genomic DNA. Translation: BAA02406.1.
X57859 Genomic DNA. Translation: CAA40994.1. Frameshift.
PIRS27330.
S29783.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E28X-ray2.40A1-587[»]
ProteinModelPortalQ02499.
SMRQ02499. Positions 1-587.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR018209. Pyrv_Knase_AS.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF52009. PEP_mobile. 1 hit.
SSF50800. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01064. pyruv_kin. 1 hit.
PROSITEPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02499.

Entry information

Entry nameKPYK_GEOSE
AccessionPrimary (citable) accession number: Q02499
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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