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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: glycolysis

This protein is involved in step 5 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk), Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI_1)
  4. Enolase (eno), Enolase (eno), Enolase (eno)
  5. Pyruvate kinase (pyk), Pyruvate kinase (AA904_05055), Pyruvate kinase (pyk), Pyruvate kinase (GT94_09925), Pyruvate kinase (B4114_2369)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33SubstrateBy similarity1
Metal bindingi35PotassiumBy similarity1
Metal bindingi37PotassiumBy similarity1
Metal bindingi67PotassiumBy similarity1
Metal bindingi68Potassium; via carbonyl oxygenBy similarity1
Sitei221Transition state stabilizerBy similarity1
Metal bindingi223MagnesiumBy similarity1
Binding sitei246Substrate; via amide nitrogenBy similarity1
Metal bindingi247MagnesiumBy similarity1
Binding sitei247Substrate; via amide nitrogenBy similarity1
Binding sitei279SubstrateBy similarity1

GO - Molecular functioni

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)DescriptionActionsGraphical viewLength
Mutagenesisi308D → E: Reduced activity; when associated with Y-416. 1
Mutagenesisi416W → Y: Increased activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120551 – 587Pyruvate kinaseAdd BLAST587

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei541PhosphohistidineBy similarity1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1587
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Turni13 – 15Combined sources3
Helixi18 – 27Combined sources10
Beta strandi29 – 35Combined sources7
Helixi41 – 57Combined sources17
Beta strandi63 – 67Combined sources5
Beta strandi90 – 96Combined sources7
Beta strandi102 – 108Combined sources7
Turni113 – 115Combined sources3
Beta strandi121 – 124Combined sources4
Turni125 – 128Combined sources4
Beta strandi129 – 137Combined sources9
Turni138 – 141Combined sources4
Beta strandi142 – 146Combined sources5
Beta strandi158 – 160Combined sources3
Helixi173 – 185Combined sources13
Beta strandi188 – 194Combined sources7
Helixi198 – 210Combined sources13
Beta strandi216 – 222Combined sources7
Helixi225 – 229Combined sources5
Helixi231 – 237Combined sources7
Beta strandi238 – 244Combined sources7
Helixi245 – 251Combined sources7
Helixi254 – 256Combined sources3
Helixi257 – 271Combined sources15
Beta strandi275 – 282Combined sources8
Helixi283 – 286Combined sources4
Helixi293 – 305Combined sources13
Beta strandi308 – 313Combined sources6
Helixi314 – 317Combined sources4
Helixi322 – 337Combined sources16
Helixi342 – 350Combined sources9
Helixi357 – 371Combined sources15
Beta strandi375 – 380Combined sources6
Beta strandi382 – 384Combined sources3
Helixi385 – 392Combined sources8
Beta strandi399 – 405Combined sources7
Helixi406 – 411Combined sources6
Helixi412 – 414Combined sources3
Beta strandi418 – 422Combined sources5
Helixi429 – 443Combined sources15
Beta strandi451 – 456Combined sources6
Beta strandi468 – 473Combined sources6
Beta strandi477 – 480Combined sources4
Beta strandi482 – 486Combined sources5
Beta strandi492 – 495Combined sources4
Helixi499 – 505Combined sources7
Beta strandi511 – 515Combined sources5
Helixi519 – 521Combined sources3
Helixi522 – 525Combined sources4
Beta strandi529 – 535Combined sources7
Helixi541 – 549Combined sources9
Beta strandi553 – 555Combined sources3
Helixi560 – 563Combined sources4
Beta strandi569 – 573Combined sources5
Turni574 – 577Combined sources4
Beta strandi578 – 582Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E28X-ray2.40A1-587[»]
ProteinModelPortaliQ02499.
SMRiQ02499.
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 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.
RefSeqiWP_033014443.1. NZ_LUCR01000070.1.

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.
RefSeqiWP_033014443.1. NZ_LUCR01000070.1.

3D structure databases

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

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: November 2, 2016
This is version 112 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

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 one 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.