Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0AD61

- KPYK1_ECOLI

UniProt

P0AD61 - KPYK1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyruvate kinase I

Gene

pykF

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

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

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

Pathwayi

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

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
  2. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10804. pykF.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Pyruvate kinase IPRO_0000112069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-acetyllysine1 Publication
Modified residuei319 – 3191N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0AD61.
PRIDEiP0AD61.

2D gel databases

SWISS-2DPAGEP0AD61.

PTM databases

PhosSiteiP0810429.

Expressioni

Gene expression databases

GenevestigatoriP0AD61.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-36221N.
IntActiP0AD61. 21 interactions.
STRINGi511145.b1676.

Structurei

Secondary structure

1
470
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Helixi12 – 143
Helixi17 – 2610
Beta strandi28 – 347
Helixi40 – 5718
Beta strandi62 – 665
Beta strandi72 – 743
Helixi78 – 803
Beta strandi83 – 853
Beta strandi90 – 956
Beta strandi105 – 1095
Helixi113 – 1164
Beta strandi122 – 1254
Turni126 – 1294
Beta strandi130 – 1389
Beta strandi141 – 1466
Beta strandi150 – 1523
Beta strandi157 – 1593
Helixi172 – 18413
Beta strandi187 – 1937
Helixi197 – 20812
Turni209 – 2113
Beta strandi216 – 2216
Helixi224 – 2285
Helixi230 – 2367
Beta strandi237 – 2437
Helixi244 – 2507
Helixi253 – 27018
Beta strandi273 – 2775
Beta strandi278 – 2814
Helixi282 – 2854
Helixi292 – 30413
Beta strandi307 – 3115
Helixi313 – 3164
Helixi322 – 33615
Helixi355 – 36814
Beta strandi372 – 3776
Beta strandi379 – 3813
Helixi382 – 3887
Beta strandi393 – 4019
Helixi403 – 4086
Helixi409 – 4113
Beta strandi415 – 4195
Helixi426 – 43914
Beta strandi441 – 4433
Beta strandi448 – 4536
Beta strandi455 – 4573
Beta strandi464 – 4696

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0TX-ray1.80A/B/C/D1-470[»]
1E0UX-ray2.80A/B/C/D1-470[»]
1PKYX-ray2.50A/B/C/D1-470[»]
ProteinModelPortaliP0AD61.
SMRiP0AD61. Positions 1-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AD61.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.Curated

Phylogenomic databases

eggNOGiCOG0469.
HOGENOMiHOG000021559.
InParanoidiP0AD61.
KOiK00873.
OMAiCIVENAG.
OrthoDBiEOG6GBMB0.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441G → S AA sequence (PubMed:1859631)Curated
Sequence conflicti379 – 3791Q → N AA sequence (PubMed:2653362)Curated
Sequence conflicti401 – 4011T → D AA sequence (PubMed:2653362)Curated
Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:2674937)CuratedAdd
BLAST
Sequence conflicti451 – 47020MVSGA…SVHVL → YGFWCTGTERHY(PubMed:9097039)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_489938.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.
GeneIDi12931281.
946179.
KEGGiecj:Y75_p1651.
eco:b1676.
PATRICi32118658. VBIEscCol129921_1747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi D64925.
RefSeqi NP_416191.1. NC_000913.3.
YP_489938.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E0T X-ray 1.80 A/B/C/D 1-470 [» ]
1E0U X-ray 2.80 A/B/C/D 1-470 [» ]
1PKY X-ray 2.50 A/B/C/D 1-470 [» ]
ProteinModelPortali P0AD61.
SMRi P0AD61. Positions 1-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36221N.
IntActi P0AD61. 21 interactions.
STRINGi 511145.b1676.

PTM databases

PhosSitei P0810429.

2D gel databases

SWISS-2DPAGE P0AD61.

Proteomic databases

PaxDbi P0AD61.
PRIDEi P0AD61.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74746 ; AAC74746 ; b1676 .
BAA15445 ; BAA15445 ; BAA15445 .
GeneIDi 12931281.
946179.
KEGGi ecj:Y75_p1651.
eco:b1676.
PATRICi 32118658. VBIEscCol129921_1747.

Organism-specific databases

EchoBASEi EB0797.
EcoGenei EG10804. pykF.

Phylogenomic databases

eggNOGi COG0469.
HOGENOMi HOG000021559.
InParanoidi P0AD61.
KOi K00873.
OMAi CIVENAG.
OrthoDBi EOG6GBMB0.
PhylomeDBi P0AD61.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .
BioCyci EcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.
SABIO-RK P0AD61.

Miscellaneous databases

EvolutionaryTracei P0AD61.
PROi P0AD61.

Gene expression databases

Genevestigatori P0AD61.

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
InterProi 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 ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
PROSITEi PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli."
    Ohara O., Dorit R.L., Gilbert W.
    Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 451-470.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Bacterial pyruvate kinases have a shorter N-terminal domain."
    Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.
    Biol. Chem. Hoppe-Seyler 372:91-93(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-48.
  7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
    Strain: K12 / EMG2.
  8. "Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli."
    Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., Ferri G.
    Biol. Chem. Hoppe-Seyler 370:211-216(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 293-319; 369-385 AND 389-404.
  9. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  10. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-319, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  11. "Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition."
    Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A.
    Structure 3:729-741(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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: October 29, 2014
This is version 91 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

External Data

Dasty 3