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Protein

Pyruvate kinase

Gene

pyk

Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321SubstrateBy similarity
Metal bindingi34 – 341PotassiumBy similarity
Metal bindingi36 – 361PotassiumBy similarity
Metal bindingi66 – 661PotassiumBy similarity
Metal bindingi67 – 671Potassium; via carbonyl oxygenBy similarity
Sitei219 – 2191Transition state stabilizerBy similarity
Metal bindingi221 – 2211MagnesiumBy similarity
Binding sitei244 – 2441Substrate; via amide nitrogenBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Binding sitei277 – 2771SubstrateBy 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

BioCyciSAUR273036:GJVS-1578-MONOMER.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
Ordered Locus Names:SAB1556c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 585585Pyruvate kinasePRO_0000294128Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi273036.SAB1556c.

Structurei

3D structure databases

ProteinModelPortaliQ2YTE3.
SMRiQ2YTE3. Positions 2-585.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
KOiK00873.
OMAiKIVAYCD.
OrthoDBiEOG6GBMB0.

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.
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.

Sequencei

Sequence statusi: Complete.

Q2YTE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKTKIVCTI GPASESEEMI EKLINAGMNV ARLNFSHGSH EEHKGRIDTI
60 70 80 90 100
RKVAKRLDKI VAILLDTKGP EIRTHNMKDG IIELERGNEV IVSMNEVEGT
110 120 130 140 150
PEKFSVTYEN LINDVQVGSY ILLDDGLIEL QVKDIDHAKK EVKCDILNSG
160 170 180 190 200
ELKNKKGVNL PGVRVSLPGI TEKDAEDIRF GIKENVDFIA ASFVRRPSDV
210 220 230 240 250
LEIREILEEQ KANISVFPKI ENQEGIDNIA EILEVSDGLM VARGDMGVEI
260 270 280 290 300
PPEKVPMVQK DLIRQCNKLG KPVITATQML DSMQRNPRAT RAEASDVANA
310 320 330 340 350
IYDGTDAVML SGETAAGLYP EEAVKTMRNI AVSAEAAQDY KKLLSDRTKL
360 370 380 390 400
VETSLVNAIG ISVAHTALNL NVKAIVAATE SGSTARTISK YRPHSDIIAV
410 420 430 440 450
TPSEETARQC SIVWGVQPVV KKGRKSTDAL LNNAVATAVE TGRVTNGDLI
460 470 480 490 500
IITAGVPTGE TGTTNMMKIH LVGDEIANGQ GIGRGSVVGT TLVAETVKDL
510 520 530 540 550
EGKDLSDKVI VTNSIDETFV PYVEKALGLI TEENGITSPS AIVGLEKGIP
560 570 580
TVVGVEKAVK NISNNMLVTI DAAQGKIFEG YANVL
Length:585
Mass (Da):63,116
Last modified:December 20, 2005 - v1
Checksum:i4AB45ADE066401A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI81245.1.
RefSeqiYP_417026.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI81245; CAI81245; SAB1556c.
GeneIDi3794684.
KEGGisab:SAB1556c.
PATRICi19524009. VBIStaAur92441_1653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ938182 Genomic DNA. Translation: CAI81245.1.
RefSeqiYP_417026.1. NC_007622.1.

3D structure databases

ProteinModelPortaliQ2YTE3.
SMRiQ2YTE3. Positions 2-585.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273036.SAB1556c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI81245; CAI81245; SAB1556c.
GeneIDi3794684.
KEGGisab:SAB1556c.
PATRICi19524009. VBIStaAur92441_1653.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
KOiK00873.
OMAiKIVAYCD.
OrthoDBiEOG6GBMB0.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciSAUR273036:GJVS-1578-MONOMER.

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.
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.
ProtoNetiSearch...

Publicationsi

  1. "Molecular correlates of host specialization in Staphylococcus aureus."
    Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
    PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: bovine RF122 / ET3-1.

Entry informationi

Entry nameiKPYK_STAAB
AccessioniPrimary (citable) accession number: Q2YTE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.