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UniProtKB/Swiss-Prot entry P21599


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPYK2_ECOLI
Primary accession number P21599
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 89)
Name and origin of the protein
Protein name Pyruvate kinase II
Synonyms EC 2.7.1.40
PK-2
Gene name
Name: pykA
OrderedLocusNames: b1854, JW1843
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Bledig S.A., Fotheringham I.G., Hunter M.G.;
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.379; PubMed=9097040 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-480.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=1732206 [NCBI, ExPASy, EBI, Israel, Japan]
Karow M.L., Georgopoulos C.;
"Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB.";
J. Bacteriol. 174:702-710(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-480.
STRAIN=K12;
Engel H., Smink A.J., Keck W.;
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 2-44.
PubMed=1859631 [NCBI, ExPASy, EBI, Israel, Japan]
Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.;
"Bacterial pyruvate kinases have a shorter N-terminal domain.";
Biol. Chem. Hoppe-Seyler 372:91-93(1991).
[8]
PROTEIN SEQUENCE OF 64-77; 83-107; 251-272 AND 337-353.
PubMed=8439398 [NCBI, ExPASy, EBI, Israel, Japan]
Valentini G., Stoppini M., Iadarola P., Malcovati M., Ferri G., Speranza M.L.;
"Divergent binding sites in pyruvate kinases I and II from Escherichia coli.";
Biol. Chem. Hoppe-Seyler 374:69-74(1993).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-351, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M63703; AAA24473.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74924.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15662.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77039; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
M87660; AAA96707.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S29790; S29790.
RefSeq AP_002474.1; -.
NP_416368.1; -.
3D structure databases
HSSP P14178; 1E0T. [HSSP ENTRY / PDB]
ModBase P21599.
Protein-protein interaction databases
DIP DIP:10622N; -.
Enzyme and pathway databases
BioCyc EcoCyc:PKII-MON; -.
MetaCyc:PKII-MON; -.
Organism-specific databases
EchoBASE EB0796; -.
EcoGene EG10803; pykA.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0030955; Molecular function: potassium ion binding (inferred from electronic annotation from InterPro).
GO:0004743; Molecular function: pyruvate kinase activity (inferred from electronic annotation from InterPro).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001697; Pyr_Knase.
IPR015813; Pyrv/PenolPyrv_Kinase_cat.
IPR015794; Pyrv_Knase_a/b.
IPR015793; Pyrv_Knase_brl.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
PANTHER PTHR11817; Pyruvate_kinase; 1.
Pfam PF00224; PK; 1.
PF02887; PK_C; 1.
Pfam graphical view of domain structure.
ProDom PD001009; Pyruvate_kinase; 2.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01064; pyruv_kin; 1.
PROSITE PS00110; PYRUVATE_KINASE; 1.
ProtoNet P21599.
Genome annotation databases
GeneID 946527; -.
GenomeReviews U00096_GR; b1854.
AP009048_GR; JW1843.
KEGG ecj:JW1843; -.
eco:b1854; -.
Phylogenomic databases
HOGENOM P21599; -.
Genome annotation databases
CMR P21599; b1854.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Allosteric enzyme; Complete proteome; Direct protein sequencing; Glycolysis; Kinase; Magnesium; Metal-binding; Pyruvate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   480  479     Pyruvate kinase II. PRO_0000112073
ACT_SITE   223   223        By similarity. 
METAL   225   225        Magnesium (By similarity). 
METAL   249   249        Magnesium (By similarity). 
METAL   250   250        Magnesium (By similarity). 
MOD_RES   351   351        N6-acetyllysine. 
CONFLICT   20    20        R -> C (in Ref. 7; AA sequence). 
CONFLICT   43    43        S -> G (in Ref. 7; AA sequence). 
CONFLICT   442   442        Missing (in Ref. 6; AA sequence). 
Sequence information
Length: 480 AA [This is the length of the unprocessed precursor] Molecular weight: 51357 Da [This is the MW of the unprocessed precursor] CRC64: C37F004C374D27E9 [This is a checksum on the sequence]
        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 

P21599 in FASTA format

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View entry in raw text format (no links)
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