P0AD61 (KPYK1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate kinase I
EC=2.7.1.40

Alternative name(s):
PK-1

Gene names

Name:	pykF
Ordered Locus Names:	b1676, JW1666

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Belongs to type I PK; fructose 1,6-bisphosphate-activated.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the pyruvate kinase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium Pyruvate
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro potassium ion binding Inferred from electronic annotation. Source: InterPro pyruvate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 470

470

Pyruvate kinase I

PRO_0000112069

Sites

Metal binding

34

1

Potassium By similarity

Metal binding

36

1

Potassium By similarity

Metal binding

66

1

Potassium By similarity

Metal binding

67

1

Potassium; via carbonyl oxygen By similarity

Metal binding

222

1

Magnesium By similarity

Metal binding

246

1

Magnesium By similarity

Binding site

32

1

Substrate By similarity

Binding site

245

1

Substrate; via amide nitrogen By similarity

Binding site

246

1

Substrate; via amide nitrogen By similarity

Binding site

278

1

Substrate By similarity

Site

220

1

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

76

1

N6-acetyllysine Ref.10

Modified residue

319

1

N6-acetyllysine Ref.10

Experimental info

Sequence conflict

44

1

G → S AA sequence Ref.6

Sequence conflict

379

1

Q → N AA sequence Ref.8

Sequence conflict

401

1

T → D AA sequence Ref.8

Sequence conflict

451 – 470

20

MVSGA…SVHVL → YGFWCTGTERHY Ref.1

Sequence conflict

451 – 470

20

MVSGA…SVHVL → YGFWCTGTERHY Ref.3

Secondary structure

1

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470

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

12 – 14

3

Helix

17 – 26

10

Beta strand

28 – 34

7

Helix

40 – 57

18

Beta strand

62 – 66

5

Beta strand

72 – 74

3

Helix

78 – 80

3

Beta strand

83 – 85

3

Beta strand

90 – 95

6

Beta strand

105 – 109

5

Helix

113 – 116

4

Beta strand

122 – 125

4

Turn

126 – 129

4

Beta strand

130 – 138

9

Beta strand

141 – 146

6

Beta strand

150 – 152

3

Beta strand

157 – 159

3

Helix

172 – 184

13

Beta strand

187 – 193

7

Helix

197 – 208

12

Turn

209 – 211

3

Beta strand

216 – 221

6

Helix

224 – 228

5

Helix

230 – 236

7

Beta strand

237 – 243

7

Helix

244 – 250

7

Helix

253 – 270

18

Beta strand

273 – 277

5

Beta strand

278 – 281

4

Helix

282 – 285

4

Helix

292 – 304

13

Beta strand

307 – 311

5

Helix

313 – 316

4

Helix

322 – 336

15

Helix

355 – 368

14

Beta strand

372 – 377

6

Beta strand

379 – 381

3

Helix

382 – 388

7

Beta strand

393 – 401

9

Helix

403 – 408

6

Helix

409 – 411

3

Beta strand

415 – 419

5

Helix

426 – 439

14

Beta strand

441 – 443

3

Beta strand

448 – 453

6

Beta strand

455 – 457

3

Beta strand

464 – 469

6

Sequences

	Sequence		Length	Mass (Da)
	P0AD61 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: E29BF01B90327D8B	FASTA	470	50,729
	10 20 30 40 50 60 MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKT 70 80 90 100 110 120 AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI GNSEMVAVTY EGFTTDLSVG 130 140 150 160 170 180 NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF 190 200 210 220 230 240 GCEQGVDFVA ASFIRKRSDV IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI 250 260 270 280 290 300 MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN 310 320 330 340 350 360 AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR KLRITEAVCR 370 380 390 400 410 420 GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT TNEKTAHQLV LSKGVVPQLV 430 440 450 460 470 KEITSTDDFY RLGKELALQS GLAHKGDVVV MVSGALVPSG TTNTASVHVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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, 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]	"The allosteric regulation of pyruvate kinase." Valentini G., Chiarelli L., Fortin R., Speranza M.L., Galizzi A., Mattevi A. J. Biol. Chem. 275:18145-18152(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M24636 Genomic DNA. Translation: AAA24392.1.
U68703 Genomic DNA. Translation: AAB47952.1.
U00096 Genomic DNA. Translation: AAC74746.1.
AP009048 Genomic DNA. Translation: BAA15445.2.

PIR

D64925.

RefSeq

NP_416191.1. NC_000913.2.
YP_489938.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0AD61.

SMR

P0AD61. Positions 1-470.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36221N.

IntAct

P0AD61. 21 interactions.

STRING

511145.b1676.

PTM databases

PhosSite

P0810429.

2D gel databases

SWISS-2DPAGE

P0AD61.

Proteomic databases

PaxDb

P0AD61.

PRIDE

P0AD61.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74746; AAC74746; b1676.
BAA15445; BAA15445; BAA15445.

GeneID

12931281.
946179.

KEGG

ecj:Y75_p1651.
eco:b1676.

PATRIC

32118658. VBIEscCol129921_1747.

Organism-specific databases

EchoBASE

EB0797.

EcoGene

EG10804. pykF.

Phylogenomic databases

eggNOG

COG0469.

HOGENOM

HOG000021559.

KO

K00873.

OMA

NSGYTAR.

ProtClustDB

PRK09206.

Enzyme and pathway databases

BioCyc

EcoCyc:PKI-MONOMER.
ECOL316407:JW1666-MONOMER.
MetaCyc:PKI-MONOMER.

SABIO-RK

P0AD61.

UniPathway

UPA00109; UER00188.

Gene expression databases

Genevestigator

P0AD61.

Family and domain databases

Gene3D

2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.

InterPro

IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase.
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]

PANTHER

PTHR11817. PTHR11817. 1 hit.

Pfam

PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]

PRINTS

PR01050. PYRUVTKNASE.

SUPFAM

SSF50800. PK_B_barrel_like. 1 hit.
SSF52935. Pyruvate_kinase. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

TIGRFAMs

TIGR01064. pyruv_kin. 1 hit.

PROSITE

PS00110. PYRUVATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AD61.

Entry information

Entry name

KPYK1_ECOLI

Accession

Primary (citable) accession number: P0AD61
Secondary accession number(s): P14178 , P76921, P78165, P78231

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program