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NiceProt View of Swiss-Prot: P14178

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

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Entry information
Entry name KPY1_ECOLI
Primary accession number P14178
Secondary accession numbers P76921 P78165 P78231
Entered in Swiss-Prot in Release 13, January 1990
Sequence was last modified in Release 35, November 1997
Annotations were last modified in    Release 42, October 2003
Name and origin of the protein
Protein name Pyruvate kinase I
Synonyms EC 2.7.1.40
PK-1
Gene name
PYKF or B1676 or Z2704 or ECS2383
From
Escherichia coli  [TaxID: 562]
Escherichia coli O157:H7  [TaxID: 83334]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]
SEQUENCE FROM NUCLEIC ACID.
MEDLINE=89386643; PubMed=2674937; [NCBI, ExPASy, EBI, Israel, Japan]
Ohara O., Dorit R.L., Gilbert W.;
"Direct genomic sequencing of bacterial DNA: the pyruvate kinase I gene of Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989).
[2]
SEQUENCE FROM NUCLEIC ACID.
STRAIN=K12 / MG1655;
MEDLINE=97426617; 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).
[3]
SEQUENCE FROM NUCLEIC ACID.
MEDLINE=97175536; PubMed=9023191; [NCBI, ExPASy, EBI, Israel, Japan]
Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.;
"Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12.";
J. Bacteriol. 179:1105-1111(1997).
[4]
SEQUENCE FROM NUCLEIC ACID.
STRAIN=K12;
MEDLINE=97251357; PubMed=9097039; [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
DNA Res. 3:363-377(1996).
[5]
SEQUENCE FROM NUCLEIC ACID.
STRAIN=O157:H7 / EDL933 / ATCC 700927;
MEDLINE=21074935; PubMed=11206551; [NCBI, ExPASy, EBI, Israel, Japan]
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[6]
SEQUENCE FROM NUCLEIC ACID.
STRAIN=O157:H7 / RIMD 0509952;
MEDLINE=21156231; PubMed=11258796; [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
[7]
SEQUENCE OF 293-319; 369-385 AND 389-404.
MEDLINE=89228557; PubMed=2653362; [NCBI, ExPASy, EBI, Israel, Japan]
Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., Ferri G.;
"Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli.";
Biol. Chem. Hoppe-Seyler 370:211-216(1989).
[8]
SEQUENCE OF 1-48.
MEDLINE=91315755; 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).
[9]
SEQUENCE OF 1-11.
STRAIN=K12 / EMG2;
MEDLINE=97443975; PubMed=9298646; [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[10]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
MEDLINE=96000862; PubMed=8591049; [NCBI, ExPASy, EBI, Israel, Japan]
Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A.;
"Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition.";
Structure 3:729-741(1995).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
MEDLINE=20309762; PubMed=10751408; [NCBI, ExPASy, EBI, Israel, Japan]
Valentini G., Chiarelli L., Fortin R., Speranza M.L., Galizzi A., Mattevi A.;
"The allosteric regulation of pyruvate kinase.";
J. Biol. Chem. 275:18145-18152(2000).
Comments
Copyright
This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/ or send an email to license@isb-sib.ch)
Cross-references
EMBL
M24636; AAA24392.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
AE000262; AAC74746.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
U68703; AAB47952.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
D90810; BAA15445.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
D90853; BAA16043.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
AE005390; AAG56663.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
AP002558; BAB35806.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C85775; C85775.
D64925; D64925.
G90926; G90926.
PDB
1PKY; 07-DEC-95. [ExPASy / RCSB]
1E0T; 20-JUL-00. [ExPASy / RCSB]
1E0U; 20-JUL-00. [ExPASy / RCSB]
Detailed list of linked structures.
SWISS-2DPAGE P14178; COLI.
ECO2DBASE G054.7; 6TH EDITION.
EcoGene EG10804; pykF.
EcoCyc EG10804; pykF.
CMR P14178; B1676.
InterPro IPR001697; Pyruvate_kinase.
Graphical view of domain structure.
Pfam PF00224; PK; 1.
PF02887; PK_C; 1.
PRINTS PR01050; PYRUVTKNASE.
ProDom PD001009; Pyruvate_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01064; pyruv_kin; 1.
PROSITE PS00110; PYRUVATE_KINASE; 1.
HOBACGEN [Family / Alignment / Tree]
BLOCKS P14178.
ProtoNet P14178.
ProtoMap P14178.
PRESAGE P14178.
DIP P14178.
ModBase P14178.
Keywords
Transferase; Kinase; Glycolysis; Allosteric enzyme; Multigene family; Magnesium; 3D-structure; Complete proteome.
Features
SEVIEWER logo Feature table viewer
Key From   To  Length   Description
ACT_SITE    220   220           BY SIMILARITY.  
METAL    222   222           MAGNESIUM (BY SIMILARITY).  
METAL    243   243           MAGNESIUM (BY SIMILARITY).  
METAL    244   244           MAGNESIUM (BY SIMILARITY).  
CONFLICT    44    44           G -> S (IN REF. 8).  
CONFLICT    379   379           Q -> N (IN REF. 7).  
CONFLICT    401   401           T -> D (IN REF. 7).  
CONFLICT    451   470           MVSGALVPSGTTNTASVHVL -> YGFWCTGTERHY (IN REF. 1 AND 4).  
STRAND    5     9   5        
HELIX    12    14   3        
HELIX    17    26   10        
TURN    27    27   1        
STRAND    28    34   7        
TURN    35    36   2        
HELIX    40    57   18        
TURN    58    58   1        
STRAND    62    66   5        
STRAND    72    74   3        
STRAND    77    77   1        
HELIX    78    80   3        
STRAND    83    85   3        
TURN    87    88   2        
STRAND    90    94   5        
TURN    97    98   2        
STRAND    101   102   2        
TURN    103   104   2        
STRAND    105   108   4        
TURN    111   112   2        
HELIX    113   116   4        
TURN    119   120   2        
STRAND    122   125   4        
TURN    126   129   4        
STRAND    130   138   9        
TURN    139   140   2        
STRAND    141   146   6        
STRAND    150   152   3        
STRAND    157   159   3        
HELIX    172   184   13        
TURN    185   185   1        
STRAND    188   191   4        
HELIX    197   208   12        
TURN    209   211   3        
TURN    213   214   2        
STRAND    216   221   6        
HELIX    224   228   5        
TURN    229   229   1        
HELIX    230   236   7        
STRAND    239   243   5        
HELIX    244   250   7        
HELIX    253   270   18        
TURN    271   271   1        
STRAND    273   277   5        
HELIX    292   304   13        
TURN    305   305   1        
STRAND    308   311   4        
HELIX    322   336   15        
TURN    337   338   2        
HELIX    355   368   14        
TURN    369   370   2        
STRAND    373   377   5        
HELIX    382   388   7        
TURN    389   390   2        
STRAND    395   400   6        
HELIX    403   408   6        
HELIX    409   411   3        
TURN    413   414   2        
STRAND    415   419   5        
HELIX    426   439   14        
TURN    440   440   1        
TURN    445   446   2        
STRAND    448   453   6        
TURN    459   460   2        
STRAND    464   470   7        
Sequence information
Length: 470 AA Molecular weight: 50729 Da CRC64: E29BF01B90327D8B [This is a checksum on the sequence]
        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 

P14178 in FASTA format

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