Reviewed, UniProtKB/Swiss-Prot P21599 (KPYK2_ECOLI)

Names and origin

Protein names

Recommended name:
    Pyruvate kinase II
    EC=2.7.1.40
Alternative name(s):
    PK-2

Gene names

Name:	pykA
Ordered Locus Names:	b1854, JW1843

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + pyruvate = ADP + phosphoenolpyruvate.
Cofactor	Magnesium. Potassium.
Enzyme regulation	Allosterically activated by AMP and by several sugar phosphates. Belongs to type II PK.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the pyruvate kinase family.
Sequence caution	The sequence AAA96707.1 differs from that shown. Reason: Frameshift at position 441.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Pyruvate
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 480	479	Pyruvate kinase II		PRO_0000112073
Sites
	Active site	223	1	By similarity
	Metal binding	225	1	Magnesium By similarity
	Metal binding	249	1	Magnesium By similarity
	Metal binding	250	1	Magnesium By similarity
Amino acid modifications
	Modified residue	351	1	N6-acetyllysine Ref.9
Experimental info
	Sequence conflict	20	1	R → C AA sequence Ref.7
	Sequence conflict	43	1	S → G AA sequence Ref.7
	Sequence conflict	442	1	Missing AA sequence Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P21599-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C37F004C374D27E9	FASTA	480	51,357
	10 20 30 40 50 60 MSRRLRRTKI VTTLGPATDR DNNLEKVIAA GANVVRMNFS HGSPEDHKMR ADKVREIAAK 70 80 90 100 110 120 LGRHVAILGD LQGPKIRVST FKEGKVFLNI GDKFLLDANL GKGEGDKEKV GIDYKGLPAD 130 140 150 160 170 180 VVPGDILLLD DGRVQLKVLE VQGMKVFTEV TVGGPLSNNK GINKLGGGLS AEALTEKDKA 190 200 210 220 230 240 DIKTAALIGV DYLAVSFPRC GEDLNYARRL ARDAGCDAKI VAKVERAEAV CSQDAMDDII 250 260 270 280 290 300 LASDVVMVAR GDLGVEIGDP ELVGIQKALI RRARQLNRAV ITATQMMESM ITNPMPTRAE 310 320 330 340 350 360 VMDVANAVLD GTDAVMLSAE TAAGQYPSET VAAMARVCLG AEKIPSINVS KHRLDVQFDN 370 380 390 400 410 420 VEEAIAMSAM YAANHLKGVT AIITMTESGR TALMTSRISS GLPIFAMSRH ERTLNLTALY 430 440 450 460 470 480 RGVTPVHFDS ANDGVAAASE AVNLLRDKGY LMSGDLVIVT QGDVMSTVGS TNTTRILTVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Bledig S.A., Fotheringham I.G., Hunter M.G. Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., 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., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB." Karow M.L., Georgopoulos C. J. Bacteriol. 174:702-710(1992) [PubMed: 1732206] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-480. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	Engel H., Smink A.J., Keck W. Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-480. Strain: K12.
[7]	"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: 1859631] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-44.
[8]	"Divergent binding sites in pyruvate kinases I and II from Escherichia coli." Valentini G., Stoppini M., Iadarola P., Malcovati M., Ferri G., Speranza M.L. Biol. Chem. Hoppe-Seyler 374:69-74(1993) [PubMed: 8439398] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-77; 83-107; 251-272 AND 337-353.
[9]	"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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-351, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M63703 Genomic DNA. Translation: AAA24473.1. U00096 Genomic DNA. Translation: AAC74924.1. AP009048 Genomic DNA. Translation: BAA15662.1. M77039 Genomic DNA. No translation available. M87660 Genomic DNA. Translation: AAA96707.1. Frameshift.
PIR	S29790.
RefSeq	AP_002474.1. NP_416368.1.
3D structure databases
HSSP	HSSP built from PDB template 1E0T based on UniProtKB P14178.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10622N.
Genome annotation databases
GeneID	946527.
GenomeReviews	Gene locus JW1843 in contig AP009048_GR. Gene locus b1854 in contig U00096_GR.
KEGG	ecj:JW1843. eco:b1854.
Organism-specific databases
EchoBASE	EB0796.
EcoGene	EG10803. pykA.
CMR	Search...
Phylogenomic databases
HOGENOM	P21599.
OMA	P21599. RMIKLAR.
Enzyme and pathway databases
BioCyc	EcoCyc:PKII-MON. MetaCyc:PKII-MON.
Family and domain databases
InterPro	IPR001697. Pyr_Knase. IPR015813. Pyrv/PenolPyrv_Kinase_cat. IPR015794. Pyrv_Knase_a/b. IPR018209. Pyrv_Knase_AS. IPR015793. Pyrv_Knase_brl. [Graphical view]
Gene3D	G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. G3DSA:3.40.1380.20. Pyrv_Knase_a/b. 1 hit.
PANTHER	PTHR11817. Pyruvate_kinase. 1 hit.
Pfam	PF00224. PK. 1 hit. PF02887. PK_C. 1 hit. [Graphical view]
PRINTS	PR01050. PYRUVTKNASE.
ProDom	PD001009. Pyruvate_kinase. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01064. pyruv_kin. 1 hit.
PROSITE	PS00110. PYRUVATE_KINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KPYK2_ECOLI

Accession

Primary (citable) accession number: P21599

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)