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Protein

Pyruvate kinase I

Gene

pykF

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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:

Enzyme regulationi

Belongs to type I PK; fructose 1,6-bisphosphate-activated.

Pathway:iglycolysis

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 (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase I (pykF), Pyruvate kinase II (pykA)
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

BioCyciSENT99287:GCTI-1388-MONOMER.
UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase I (EC:2.7.1.40)
Alternative name(s):
PK-1
Gene namesi
Name:pykF
Ordered Locus Names:STM1378
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Pyruvate kinase IPRO_0000112072Add
BLAST

Proteomic databases

PaxDbiP77983.
PRIDEiP77983.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi99287.STM1378.

Structurei

3D structure databases

ProteinModelPortaliP77983.
SMRiP77983. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
KOiK00873.
OMAiKQHGGEH.
OrthoDBiEOG6GBMB0.
PhylomeDBiP77983.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKIVCTI GPKTESEEML SKMLDAGMNV MRLNFSHGDY AEHGQRIQNL
60 70 80 90 100
RNVMSKTGKK AAILLDTKGP EIRTIKLEGG NDVSLKAGQT FTFTTDKSVV
110 120 130 140 150
GNNEIVAVTY EGFTSDLSVG NTVLVDDGLI GMEVTAIEGN KVICKVLNNG
160 170 180 190 200
DLGENKGVNL PGVSIALPAL AEKDKQDLIF GCEQGVDFVA ASFIRKRSDV
210 220 230 240 250
VEIREHLKAH GGENIQIISK IENQEGLNNF DEILEASDGI MVARGDLGVE
260 270 280 290 300
IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
310 320 330 340 350
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLDYNNDSR
360 370 380 390 400
KLRITEAVCR GAVETAEKLE APLIVVATQG GKSARAVRKY FPDATILALT
410 420 430 440 450
TNEVTARQLV LSKGVVSQLV KEINSTDDFY RLGKDVALQS GLAQKGDVVV
460 470
MVSGALVPSG TTNTASVHVL
Length:470
Mass (Da):50,657
Last modified:January 23, 2002 - v2
Checksum:i116411A30C49AAC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421V → C in CAA68205 (PubMed:9023191).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99945 Genomic DNA. Translation: CAA68205.1.
AE006468 Genomic DNA. Translation: AAL20302.1.
RefSeqiNP_460343.1. NC_003197.1.
WP_000751447.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20302; AAL20302; STM1378.
GeneIDi1252896.
KEGGistm:STM1378.
PATRICi32381237. VBISalEnt20916_1461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99945 Genomic DNA. Translation: CAA68205.1.
AE006468 Genomic DNA. Translation: AAL20302.1.
RefSeqiNP_460343.1. NC_003197.1.
WP_000751447.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP77983.
SMRiP77983. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1378.

Proteomic databases

PaxDbiP77983.
PRIDEiP77983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20302; AAL20302; STM1378.
GeneIDi1252896.
KEGGistm:STM1378.
PATRICi32381237. VBISalEnt20916_1461.

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
KOiK00873.
OMAiKQHGGEH.
OrthoDBiEOG6GBMB0.
PhylomeDBiP77983.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciSENT99287:GCTI-1388-MONOMER.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProiIPR001697. 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.
PfamiPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.
PROSITEiPS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12."
    Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.
    J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiKPYK1_SALTY
AccessioniPrimary (citable) accession number: P77983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 106 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

Allosteric enzyme, 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.