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Protein

Pyruvate kinase

Gene

pyk

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331SubstrateBy similarity
Metal bindingi35 – 351PotassiumBy similarity
Metal bindingi37 – 371PotassiumBy similarity
Metal bindingi67 – 671PotassiumBy similarity
Metal bindingi68 – 681Potassium; via carbonyl oxygenBy similarity
Sitei221 – 2211Transition state stabilizerBy similarity
Metal bindingi223 – 2231MagnesiumBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
Binding sitei279 – 2791SubstrateBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

BRENDAi2.7.1.40. 623.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi308 – 3081D → E: Reduced activity; when associated with Y-416.
Mutagenesisi416 – 4161W → Y: Increased activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 587587Pyruvate kinasePRO_0000112055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei541 – 5411PhosphohistidineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Turni13 – 153Combined sources
Helixi18 – 2710Combined sources
Beta strandi29 – 357Combined sources
Helixi41 – 5717Combined sources
Beta strandi63 – 675Combined sources
Beta strandi90 – 967Combined sources
Beta strandi102 – 1087Combined sources
Turni113 – 1153Combined sources
Beta strandi121 – 1244Combined sources
Turni125 – 1284Combined sources
Beta strandi129 – 1379Combined sources
Turni138 – 1414Combined sources
Beta strandi142 – 1465Combined sources
Beta strandi158 – 1603Combined sources
Helixi173 – 18513Combined sources
Beta strandi188 – 1947Combined sources
Helixi198 – 21013Combined sources
Beta strandi216 – 2227Combined sources
Helixi225 – 2295Combined sources
Helixi231 – 2377Combined sources
Beta strandi238 – 2447Combined sources
Helixi245 – 2517Combined sources
Helixi254 – 2563Combined sources
Helixi257 – 27115Combined sources
Beta strandi275 – 2828Combined sources
Helixi283 – 2864Combined sources
Helixi293 – 30513Combined sources
Beta strandi308 – 3136Combined sources
Helixi314 – 3174Combined sources
Helixi322 – 33716Combined sources
Helixi342 – 3509Combined sources
Helixi357 – 37115Combined sources
Beta strandi375 – 3806Combined sources
Beta strandi382 – 3843Combined sources
Helixi385 – 3928Combined sources
Beta strandi399 – 4057Combined sources
Helixi406 – 4116Combined sources
Helixi412 – 4143Combined sources
Beta strandi418 – 4225Combined sources
Helixi429 – 44315Combined sources
Beta strandi451 – 4566Combined sources
Beta strandi468 – 4736Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi482 – 4865Combined sources
Beta strandi492 – 4954Combined sources
Helixi499 – 5057Combined sources
Beta strandi511 – 5155Combined sources
Helixi519 – 5213Combined sources
Helixi522 – 5254Combined sources
Beta strandi529 – 5357Combined sources
Helixi541 – 5499Combined sources
Beta strandi553 – 5553Combined sources
Helixi560 – 5634Combined sources
Beta strandi569 – 5735Combined sources
Turni574 – 5774Combined sources
Beta strandi578 – 5825Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E28X-ray2.40A1-587[»]
ProteinModelPortaliQ02499.
SMRiQ02499. Positions 1-587.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02499.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated
In the C-terminal section; belongs to the PEP-utilizing enzyme family.Curated

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN
60 70 80 90 100
IREAAKRTGR TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG
110 120 130 140 150
TPEKISVTYP SLIDDVSVGA KILLDDGLIS LEVNAVDKQA GEIVTTVLNG
160 170 180 190 200
GVLKNKKGVN VPGVKVNLPG ITEKDRADIL FGIRQGIDFI AASFVRRASD
210 220 230 240 250
VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG LMVARGDLGV
260 270 280 290 300
EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA
310 320 330 340 350
NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT
360 370 380 390 400
KESQTTITDA IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII
410 420 430 440 450
AVTSNEAVSR RLALVWGVYT KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD
460 470 480 490 500
LVVITAGVPV GETGSTNLMK VHVISDLLAK GQGIGRKSAF GKAVVAKTAE
510 520 530 540 550
EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS HAAVVGLSLG
560 570 580
IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL
Length:587
Mass (Da):62,318
Last modified:October 1, 1994 - v2
Checksum:i0794BA1A07BE0D5A
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13095 Genomic DNA. Translation: BAA02406.1.
X57859 Genomic DNA. Translation: CAA40994.1. Frameshift.
PIRiS27330.
S29783.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13095 Genomic DNA. Translation: BAA02406.1.
X57859 Genomic DNA. Translation: CAA40994.1. Frameshift.
PIRiS27330.
S29783.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E28X-ray2.40A1-587[»]
ProteinModelPortaliQ02499.
SMRiQ02499. Positions 1-587.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BRENDAi2.7.1.40. 623.

Miscellaneous databases

EvolutionaryTraceiQ02499.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
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]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1992) [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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-51.
    Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.

Entry informationi

Entry nameiKPYK_GEOSE
AccessioniPrimary (citable) accession number: Q02499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: April 1, 2015
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.