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Protein

Pyruvate kinase

Gene

pyk

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity
  • K+By similarity

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 1 (gapA1), Glyceraldehyde-3-phosphate dehydrogenase 2 (gapA2)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
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 sitei32SubstrateBy similarity1
Metal bindingi34PotassiumBy similarity1
Metal bindingi36PotassiumBy similarity1
Metal bindingi66PotassiumBy similarity1
Metal bindingi67Potassium; via carbonyl oxygenBy similarity1
Sitei219Transition state stabilizerBy similarity1
Metal bindingi221MagnesiumBy similarity1
Binding sitei244Substrate; via amide nitrogenBy similarity1
Metal bindingi245MagnesiumBy similarity1
Binding sitei245Substrate; via amide nitrogenBy similarity1
Binding sitei277SubstrateBy 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. 3352.
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:SAR1776
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2189162.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002941301 – 585Pyruvate kinaseAdd BLAST585

Interactioni

Chemistry databases

BindingDBiQ6GG09.

Structurei

Secondary structure

1585
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 14Combined sources3
Helixi17 – 25Combined sources9
Beta strandi28 – 34Combined sources7
Helixi40 – 56Combined sources17
Beta strandi62 – 66Combined sources5
Beta strandi72 – 74Combined sources3
Beta strandi80 – 83Combined sources4
Beta strandi89 – 95Combined sources7
Beta strandi101 – 107Combined sources7
Helixi111 – 114Combined sources4
Beta strandi120 – 123Combined sources4
Turni124 – 127Combined sources4
Beta strandi128 – 136Combined sources9
Turni137 – 140Combined sources4
Beta strandi141 – 146Combined sources6
Beta strandi151 – 153Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi161 – 163Combined sources3
Helixi172 – 183Combined sources12
Beta strandi187 – 191Combined sources5
Helixi197 – 209Combined sources13
Beta strandi215 – 218Combined sources4
Helixi223 – 227Combined sources5
Helixi229 – 235Combined sources7
Beta strandi239 – 242Combined sources4
Helixi243 – 249Combined sources7
Helixi252 – 254Combined sources3
Helixi255 – 269Combined sources15
Beta strandi273 – 280Combined sources8
Helixi281 – 283Combined sources3
Beta strandi286 – 288Combined sources3
Helixi291 – 303Combined sources13
Beta strandi306 – 310Combined sources5
Helixi312 – 315Combined sources4
Helixi321 – 336Combined sources16
Helixi340 – 350Combined sources11
Helixi355 – 370Combined sources16
Beta strandi373 – 378Combined sources6
Beta strandi380 – 382Combined sources3
Helixi383 – 390Combined sources8
Beta strandi394 – 402Combined sources9
Helixi404 – 411Combined sources8
Beta strandi413 – 420Combined sources8
Helixi427 – 440Combined sources14
Beta strandi449 – 454Combined sources6
Turni458 – 460Combined sources3
Beta strandi466 – 471Combined sources6
Beta strandi476 – 478Combined sources3
Beta strandi480 – 484Combined sources5
Beta strandi486 – 493Combined sources8
Helixi497 – 500Combined sources4
Beta strandi501 – 503Combined sources3
Beta strandi506 – 513Combined sources8
Turni517 – 519Combined sources3
Helixi520 – 523Combined sources4
Beta strandi526 – 533Combined sources8
Beta strandi536 – 538Combined sources3
Helixi539 – 546Combined sources8
Beta strandi551 – 553Combined sources3
Helixi558 – 561Combined sources4
Beta strandi567 – 571Combined sources5
Turni572 – 575Combined sources4
Beta strandi576 – 580Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T05X-ray3.05A/B/C/D1-585[»]
3T07X-ray3.30A/B/C/D1-585[»]
3T0TX-ray3.10A/B/C/D1-585[»]
ProteinModelPortaliQ6GG09.
SMRiQ6GG09.
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

HOGENOMiHOG000021559.
KOiK00873.
OMAiGTHEEHK.

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.

Q6GG09-1 [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 ENQEGIDNIE 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 NISNNVLVTI DAAQGKIFEG YANVL
Length:585
Mass (Da):63,142
Last modified:July 19, 2004 - v1
Checksum:i87D790B356585362
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40767.1.
RefSeqiWP_001232655.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG40767; CAG40767; SAR1776.
KEGGisar:SAR1776.
PATRICi19547102. VBIStaAur71814_1780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG40767.1.
RefSeqiWP_001232655.1. NC_002952.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3T05X-ray3.05A/B/C/D1-585[»]
3T07X-ray3.30A/B/C/D1-585[»]
3T0TX-ray3.10A/B/C/D1-585[»]
ProteinModelPortaliQ6GG09.
SMRiQ6GG09.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ6GG09.
ChEMBLiCHEMBL2189162.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG40767; CAG40767; SAR1776.
KEGGisar:SAR1776.
PATRICi19547102. VBIStaAur71814_1780.

Phylogenomic databases

HOGENOMiHOG000021559.
KOiK00873.
OMAiGTHEEHK.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BRENDAi2.7.1.40. 3352.

Miscellaneous databases

PROiQ6GG09.

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...

Entry informationi

Entry nameiKPYK_STAAR
AccessioniPrimary (citable) accession number: Q6GG09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 85 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

3D-structure

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.