UniProtKB - Q7A0N4 (KPYK_STAAW)
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Protein
Pyruvate kinase
Gene
pyk
Organism
Staphylococcus aureus (strain MW2)
Status
Functioni
Catalytic activityi
ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactori
Protein has several cofactor binding sites:: glycolysis Pathwayi
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:
- Glyceraldehyde-3-phosphate dehydrogenase 1 (gapA1), Glyceraldehyde-3-phosphate dehydrogenase 2 (gapA2)
- Phosphoglycerate kinase (pgk)
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
- Enolase (eno)
- Pyruvate kinase (pyk)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 32 | SubstrateBy similarity | 1 | |
Metal bindingi | 34 | PotassiumBy similarity | 1 | |
Metal bindingi | 36 | PotassiumBy similarity | 1 | |
Metal bindingi | 66 | PotassiumBy similarity | 1 | |
Metal bindingi | 67 | Potassium; via carbonyl oxygenBy similarity | 1 | |
Sitei | 219 | Transition state stabilizerBy similarity | 1 | |
Metal bindingi | 221 | MagnesiumBy similarity | 1 | |
Binding sitei | 244 | Substrate; via amide nitrogenBy similarity | 1 | |
Metal bindingi | 245 | MagnesiumBy similarity | 1 | |
Binding sitei | 245 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 277 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- kinase activity Source: UniProtKB-KW
- magnesium ion binding Source: InterPro
- potassium ion binding Source: InterPro
- pyruvate kinase activity Source: UniProtKB-EC
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Glycolysis |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate |
Enzyme and pathway databases
UniPathwayi | UPA00109; UER00188. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pyk Ordered Locus Names:MW1641 |
Organismi | Staphylococcus aureus (strain MW2) |
Taxonomic identifieri | 196620 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000294133 | 1 – 585 | Pyruvate kinaseAdd BLAST | 585 |
Proteomic databases
PRIDEi | Q7A0N4. |
Structurei
3D structure databases
ProteinModelPortali | Q7A0N4. |
SMRi | Q7A0N4. |
ModBasei | Search... |
MobiDBi | Search... |
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
HOGENOMi | HOG000021559. |
KOi | K00873. |
OMAi | KHEAIEQ. |
Family and domain databases
Gene3Di | 2.40.33.10. 1 hit. 3.40.1380.20. 1 hit. |
InterProi | View protein in InterPro IPR008279. PEP-util_enz_mobile_dom. IPR036637. Phosphohistidine_dom_sf. IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase-like_dom. IPR011037. Pyrv_Knase-like_insert_dom_sf. IPR015793. Pyrv_Knase_brl. IPR015795. Pyrv_Knase_C. IPR036918. Pyrv_Knase_C_sf. IPR015806. Pyrv_Knase_insert_dom_sf. |
PANTHERi | PTHR11817. PTHR11817. 1 hit. |
Pfami | View protein in Pfam PF00391. PEP-utilizers. 1 hit. PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. |
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. |
i Sequence
Sequence statusi: Complete.
Q7A0N4-1 [UniParc]FASTAAdd to basket
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 TGRVSNGDLI
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000033 Genomic DNA. Translation: BAB95506.1. |
RefSeqi | WP_001232648.1. NC_003923.1. |
Genome annotation databases
EnsemblBacteriai | BAB95506; BAB95506; BAB95506. |
KEGGi | sam:MW1641. |
Similar proteinsi
Entry informationi
Entry namei | KPYK_STAAW | |
Accessioni | Q7A0N4Primary (citable) accession number: Q7A0N4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 10, 2007 |
Last sequence update: | July 5, 2004 | |
Last modified: | February 28, 2018 | |
This is version 88 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |