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Q02499

- KPYK_GEOSE

UniProt

Q02499 - KPYK_GEOSE

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

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

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 – 331Substrate By similarity
Metal bindingi35 – 351Potassium By similarity
Metal bindingi37 – 371Potassium By similarity
Metal bindingi67 – 671Potassium By similarity
Metal bindingi68 – 681Potassium; via carbonyl oxygen By similarity
Sitei221 – 2211Transition state stabilizer By similarity
Metal bindingi223 – 2231Magnesium By similarity
Binding sitei246 – 2461Substrate; via amide nitrogen By similarity
Metal bindingi247 – 2471Magnesium By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Binding sitei279 – 2791Substrate By 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
Complete GO annotation...

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

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 kinase
PRO_0000112055Add
BLAST

Amino acid modifications

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

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E28X-ray2.40A1-587[»]
ProteinModelPortaliQ02499.
SMRiQ02499. Positions 1-587.

Miscellaneous databases

EvolutionaryTraceiQ02499.

Family & Domainsi

Sequence similaritiesi

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

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

MKRKTKIVCT IGPASESVDK LVQLMEAGMN VARLNFSHGD HEEHGRRIAN    50
IREAAKRTGR TVAILLDTKG PEIRTHNMEN GAIELKEGSK LVISMSEVLG 100
TPEKISVTYP SLIDDVSVGA KILLDDGLIS LEVNAVDKQA GEIVTTVLNG 150
GVLKNKKGVN VPGVKVNLPG ITEKDRADIL FGIRQGIDFI AASFVRRASD 200
VLEIRELLEA HDALHIQIIA KIENEEGVAN IDEILEAADG LMVARGDLGV 250
EIPAEEVPLI QKLLIKKCNM LGKPVITATQ MLDSMQRNPR PTRAEASDVA 300
NAIFDGTDAV MLSGETAAGQ YPVEAVKTMH QIALRTEQAL EHRDILSQRT 350
KESQTTITDA IGQSVAHTAL NLDVAAIVTP TVSGKTPQMV AKYRPKAPII 400
AVTSNEAVSR RLALVWGVYT KEAPHVNTTD EMLDVAVDAA VRSGLVKHGD 450
LVVITAGVPV GETGSTNLMK VHVISDLLAK GQGIGRKSAF GKAVVAKTAE 500
EARQKMVDGG ILVTVSTDAD MMPAIEKAAA IITEEGGLTS HAAVVGLSLG 550
IPVIVGVENA TTLFKDGQEI TVDGGFGAVY RGHASVL 587
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D13095 Genomic DNA. Translation: BAA02406.1 .
X57859 Genomic DNA. Translation: CAA40994.1 . Frameshift.
PIRi S27330.
S29783.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E28 X-ray 2.40 A 1-587 [» ]
ProteinModelPortali Q02499.
SMRi Q02499. Positions 1-587.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Miscellaneous databases

EvolutionaryTracei Q02499.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProi IPR008279. 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52009. SSF52009. 1 hit.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

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: June 11, 2014
This is version 103 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

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