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Protein

Pyruvate kinase

Gene

pyk

Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
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:

Pathway: 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. no protein annotated in this organism
  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)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
Sitei220 – 2201Transition state stabilizerBy similarity
Metal bindingi222 – 2221MagnesiumBy similarity
Binding sitei245 – 2451Substrate; via amide nitrogenBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Binding sitei246 – 2461Substrate; via amide nitrogenBy similarity
Binding sitei278 – 2781SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

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

BioCyciSSAP342451:GKFA-1128-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:SSP1069
OrganismiStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Taxonomic identifieri342451 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000006371 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586Pyruvate kinasePRO_0000294140Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi342451.SSP1069.

Structurei

3D structure databases

ProteinModelPortaliQ49YC7.
SMRiQ49YC7. Positions 2-586.
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.
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.

Q49YC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKTKIVCTI GPASESEEML EKLIKAGMNV ARLNFSHGDQ AEHKARIDTI
60 70 80 90 100
RKVSKRLGKT VAILLDTKGP EIRTHNMKDG LIELEKGSEV TVSMTEVEGT
110 120 130 140 150
PEKFSVTYEN LINDVEEGSY ILLDDGLIEL QVKSIDKANG EVLCDVLNTG
160 170 180 190 200
ELKNKKGVNL PGVKVSLPGI TDKDADDINF GISEGVDFIA ASFVRRPSDV
210 220 230 240 250
LDIRKLLEAK QNKNISIIPK IENQEGIDNI KEILEVSDGL MVARGDMGVE
260 270 280 290 300
IPPESVPMVQ KDLIRQCNKL GKPVITATQM LDSMQRNPRA TRAEASDVAN
310 320 330 340 350
AIYDGTDAVM LSGETAAGQY PEEAVKTMRN IAVSAEAAQD YKKLLSDRTK
360 370 380 390 400
LVETSLVNAI GVSVAHTALN LNVKAIVAAT ESGSTARTIS KYRPQSDIIA
410 420 430 440 450
VTPNAETARQ CALVWGIFPV VKEGRKTTDA LLNNAVATAV ETERVQNGDL
460 470 480 490 500
IIITAGVPTG EKGTTNMMKL HLVGDELAKG QGIGRSSVVG KTLVVKDASE
510 520 530 540 550
LEGKDLSESI IVTSSVDETL VPYIENAIGL ITEENGITSP SAIIGLEKGI
560 570 580
PTVVGVENAT SEIQSDVLIT VDANQGKIFE GYANVL
Length:586
Mass (Da):62,853
Last modified:September 13, 2005 - v1
Checksum:iFE093F0E7D948CAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE18214.1.
RefSeqiWP_011302911.1. NC_007350.1.
YP_301159.1. NC_007350.1.

Genome annotation databases

EnsemblBacteriaiBAE18214; BAE18214; SSP1069.
GeneIDi23780396.
KEGGissp:SSP1069.
PATRICi19623722. VBIStaSap90642_1068.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE18214.1.
RefSeqiWP_011302911.1. NC_007350.1.
YP_301159.1. NC_007350.1.

3D structure databases

ProteinModelPortaliQ49YC7.
SMRiQ49YC7. Positions 2-586.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi342451.SSP1069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE18214; BAE18214; SSP1069.
GeneIDi23780396.
KEGGissp:SSP1069.
PATRICi19623722. VBIStaSap90642_1068.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
KOiK00873.
OMAiKIVAYCD.
OrthoDBiEOG6GBMB0.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciSSAP342451:GKFA-1128-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.
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...

Publicationsi

  1. "Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
    Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
    Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15305 / DSM 20229.

Entry informationi

Entry nameiKPYK_STAS1
AccessioniPrimary (citable) accession number: Q49YC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: September 13, 2005
Last modified: May 27, 2015
This is version 67 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, Reference 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.