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Protein

Pyruvate kinase I

Gene

pykF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

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. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
  2. Phosphoglycerate kinase (pgk)
  3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 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)DescriptionActionsGraphical viewLength
Binding sitei32SubstrateBy similarity1
Metal bindingi34PotassiumBy similarity1
Metal bindingi36PotassiumBy similarity1
Metal bindingi66PotassiumBy similarity1
Metal bindingi67Potassium; via carbonyl oxygenBy similarity1
Sitei220Transition state stabilizerBy similarity1
Metal bindingi222MagnesiumBy similarity1
Binding sitei245Substrate; via amide nitrogenBy similarity1
Metal bindingi246MagnesiumBy similarity1
Binding sitei246Substrate; via amide nitrogenBy similarity1
Binding sitei278SubstrateBy similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc
  • kinase activity Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro
  • potassium ion binding Source: InterPro
  • pyruvate kinase activity Source: EcoCyc

GO - Biological processi

  • protein homotetramerization Source: EcoCyc
  • response to heat Source: EcoCyc
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

BioCyciEcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RKP0AD61.
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:b1676, JW1666
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10804. pykF.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001120691 – 470Pyruvate kinase IAdd BLAST470

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei76N6-acetyllysine1 Publication1
Modified residuei319N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0AD61.
PaxDbiP0AD61.
PRIDEiP0AD61.

2D gel databases

SWISS-2DPAGEP0AD61.

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260275. 18 interactors.
DIPiDIP-36221N.
IntActiP0AD61. 21 interactors.
STRINGi511145.b1676.

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 14Combined sources3
Helixi17 – 26Combined sources10
Beta strandi28 – 34Combined sources7
Helixi40 – 57Combined sources18
Beta strandi62 – 66Combined sources5
Beta strandi72 – 74Combined sources3
Helixi78 – 80Combined sources3
Beta strandi83 – 85Combined sources3
Beta strandi90 – 95Combined sources6
Beta strandi105 – 109Combined sources5
Helixi113 – 116Combined sources4
Beta strandi122 – 125Combined sources4
Turni126 – 129Combined sources4
Beta strandi130 – 138Combined sources9
Beta strandi141 – 146Combined sources6
Beta strandi150 – 152Combined sources3
Beta strandi157 – 159Combined sources3
Helixi172 – 184Combined sources13
Beta strandi187 – 193Combined sources7
Helixi197 – 208Combined sources12
Turni209 – 211Combined sources3
Beta strandi216 – 221Combined sources6
Helixi224 – 228Combined sources5
Helixi230 – 236Combined sources7
Beta strandi237 – 243Combined sources7
Helixi244 – 250Combined sources7
Helixi253 – 270Combined sources18
Beta strandi273 – 277Combined sources5
Beta strandi278 – 281Combined sources4
Helixi282 – 285Combined sources4
Helixi292 – 304Combined sources13
Beta strandi307 – 311Combined sources5
Helixi313 – 316Combined sources4
Helixi322 – 336Combined sources15
Helixi355 – 368Combined sources14
Beta strandi372 – 377Combined sources6
Beta strandi379 – 381Combined sources3
Helixi382 – 388Combined sources7
Beta strandi393 – 401Combined sources9
Helixi403 – 408Combined sources6
Helixi409 – 411Combined sources3
Beta strandi415 – 419Combined sources5
Helixi426 – 439Combined sources14
Beta strandi441 – 443Combined sources3
Beta strandi448 – 453Combined sources6
Beta strandi455 – 457Combined sources3
Beta strandi464 – 469Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
4YNGX-ray2.28A/B/C/D/E/F/G/H1-470[»]
ProteinModelPortaliP0AD61.
SMRiP0AD61.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AD61.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105CA9. Bacteria.
COG0469. LUCA.
HOGENOMiHOG000021559.
InParanoidiP0AD61.
KOiK00873.
OMAiGTHEEHK.
PhylomeDBiP0AD61.

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.

P0AD61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL
60 70 80 90 100
RNVMSKTGKT AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI
110 120 130 140 150
GNSEMVAVTY EGFTTDLSVG NTVLVDDGLI GMEVTAIEGN KVICKVLNNG
160 170 180 190 200
DLGENKGVNL PGVSIALPAL AEKDKQDLIF GCEQGVDFVA ASFIRKRSDV
210 220 230 240 250
IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI MVARGDLGVE
260 270 280 290 300
IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
310 320 330 340 350
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR
360 370 380 390 400
KLRITEAVCR GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT
410 420 430 440 450
TNEKTAHQLV LSKGVVPQLV KEITSTDDFY RLGKELALQS GLAHKGDVVV
460 470
MVSGALVPSG TTNTASVHVL
Length:470
Mass (Da):50,729
Last modified:December 6, 2005 - v1
Checksum:iE29BF01B90327D8B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti44G → S AA sequence (PubMed:1859631).Curated1
Sequence conflicti379Q → N AA sequence (PubMed:2653362).Curated1
Sequence conflicti401T → D AA sequence (PubMed:2653362).Curated1
Sequence conflicti451 – 470MVSGA…SVHVL → YGFWCTGTERHY (PubMed:2674937).CuratedAdd BLAST20
Sequence conflicti451 – 470MVSGA…SVHVL → YGFWCTGTERHY (PubMed:9097039).CuratedAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.
PIRiD64925.
RefSeqiNP_416191.1. NC_000913.3.
WP_001295403.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneIDi946179.
KEGGiecj:JW1666.
eco:b1676.
PATRICi32118658. VBIEscCol129921_1747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.
PIRiD64925.
RefSeqiNP_416191.1. NC_000913.3.
WP_001295403.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
4YNGX-ray2.28A/B/C/D/E/F/G/H1-470[»]
ProteinModelPortaliP0AD61.
SMRiP0AD61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260275. 18 interactors.
DIPiDIP-36221N.
IntActiP0AD61. 21 interactors.
STRINGi511145.b1676.

2D gel databases

SWISS-2DPAGEP0AD61.

Proteomic databases

EPDiP0AD61.
PaxDbiP0AD61.
PRIDEiP0AD61.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneIDi946179.
KEGGiecj:JW1666.
eco:b1676.
PATRICi32118658. VBIEscCol129921_1747.

Organism-specific databases

EchoBASEiEB0797.
EcoGeneiEG10804. pykF.

Phylogenomic databases

eggNOGiENOG4105CA9. Bacteria.
COG0469. LUCA.
HOGENOMiHOG000021559.
InParanoidiP0AD61.
KOiK00873.
OMAiGTHEEHK.
PhylomeDBiP0AD61.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.
BioCyciEcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RKP0AD61.

Miscellaneous databases

EvolutionaryTraceiP0AD61.
PROiP0AD61.

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...

Entry informationi

Entry nameiKPYK1_ECOLI
AccessioniPrimary (citable) accession number: P0AD61
Secondary accession number(s): P14178
, P76921, P78165, P78231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 104 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.