Swiss-Prot: P14178
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ID KPY1_ECOLI STANDARD; PRT; 470 AA.
AC P14178; P76921; P78165; P78231;
DT 01-JAN-1990 (Rel. 13, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 10-OCT-2003 (Rel. 42, Last annotation update)
DE Pyruvate kinase I (EC 2.7.1.40) (PK-1).
GN PYKF OR B1676 OR Z2704 OR ECS2383.
OS Escherichia coli, and
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562, 83334;
RN [1]
RP SEQUENCE FROM N.A.
RX MEDLINE=89386643; PubMed=2674937; [NCBI, ExPASy, EBI, Israel, Japan]
RA Ohara O., Dorit R.L., Gilbert W.;
RT "Direct genomic sequencing of bacterial DNA: the pyruvate kinase I
RT gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6883-6887(1989).
RN [2]
RP SEQUENCE FROM N.A.
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; [NCBI, ExPASy, EBI, Israel, Japan]
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=97175536; PubMed=9023191; [NCBI, ExPASy, EBI, Israel, Japan]
RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA Holden D.W.;
RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and
RT the corresponding chromosomal region of Escherichia coli K-12.";
RL J. Bacteriol. 179:1105-1111(1997).
RN [4]
RP SEQUENCE FROM N.A.
RC STRAIN=K12;
RX MEDLINE=97251357; PubMed=9097039; [NCBI, ExPASy, EBI, Israel, Japan]
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [5]
RP SEQUENCE FROM N.A.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927;
RX MEDLINE=21074935; PubMed=11206551; [NCBI, ExPASy, EBI, Israel, Japan]
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA Welch R.A., Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [6]
RP SEQUENCE FROM N.A.
RC STRAIN=O157:H7 / RIMD 0509952;
RX MEDLINE=21156231; PubMed=11258796; [NCBI, ExPASy, EBI, Israel, Japan]
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli
RT O157:H7 and genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [7]
RP SEQUENCE OF 293-319; 369-385 AND 389-404.
RX MEDLINE=89228557; PubMed=2653362; [NCBI, ExPASy, EBI, Israel, Japan]
RA Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M.,
RA Ferri G.;
RT "Primary structure of three peptides at the catalytic and allosteric
RT sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from
RT Escherichia coli.";
RL Biol. Chem. Hoppe-Seyler 370:211-216(1989).
RN [8]
RP SEQUENCE OF 1-48.
RX MEDLINE=91315755; PubMed=1859631; [NCBI, ExPASy, EBI, Israel, Japan]
RA Valentini G., Stoppini M., Speranza M.L., Malcovati M., Ferri G.;
RT "Bacterial pyruvate kinases have a shorter N-terminal domain.";
RL Biol. Chem. Hoppe-Seyler 372:91-93(1991).
RN [9]
RP SEQUENCE OF 1-11.
RC STRAIN=K12 / EMG2;
RX MEDLINE=97443975; PubMed=9298646; [NCBI, ExPASy, EBI, Israel, Japan]
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded
RT in the genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX MEDLINE=96000862; PubMed=8591049; [NCBI, ExPASy, EBI, Israel, Japan]
RA Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M.,
RA Coda A.;
RT "Crystal structure of Escherichia coli pyruvate kinase type I:
RT molecular basis of the allosteric transition.";
RL Structure 3:729-741(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX MEDLINE=20309762; PubMed=10751408; [NCBI, ExPASy, EBI, Israel, Japan]
RA Valentini G., Chiarelli L., Fortin R., Speranza M.L., Galizzi A.,
RA Mattevi A.;
RT "The allosteric regulation of pyruvate kinase.";
RL J. Biol. Chem. 275:18145-18152(2000).
CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC -!- COFACTOR: Requires magnesium and potassium.
CC -!- ENZYME REGULATION: BELONGS TO TYPE I PK; FRUCTOSE
CC 1,6-BISPHOSPHATE-ACTIVATED.
CC -!- PATHWAY: Glycolysis; final step.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
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DR EMBL; M24636; AAA24392.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AE000262; AAC74746.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U68703; AAB47952.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; D90810; BAA15445.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; D90853; BAA16043.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AE005390; AAG56663.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AP002558; BAB35806.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; C85775; C85775.
DR PIR; D64925; D64925.
DR PIR; G90926; G90926.
DR PDB; 1PKY; 07-DEC-95. [ExPASy / RCSB]
DR PDB; 1E0T; 20-JUL-00. [ExPASy / RCSB]
DR PDB; 1E0U; 20-JUL-00. [ExPASy / RCSB]
DR SWISS-2DPAGE; P14178; COLI.
DR ECO2DBASE; G054.7; 6TH EDITION.
DR EcoGene; EG10804; pykF.
DR ECOCYC; EG10804; pykF.
DR InterPro; IPR001697; Pyruvate_kinase.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR ProDom; PD001009; Pyruvate_kinase; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
DR CMR; P14178.
DR HOBACGEN [Family / Alignment / Tree]
DR BLOCKS; P14178.
DR ProtoNet; P14178.
DR ProtoMap; P14178.
DR PRESAGE; P14178.
DR DIP; P14178.
DR ModBase; P14178.
KW Transferase; Kinase; Glycolysis; Allosteric enzyme; Multigene family;
KW Magnesium; 3D-structure; Complete proteome.
FT ACT_SITE 220 220 BY SIMILARITY.
FT METAL 222 222 MAGNESIUM (BY SIMILARITY).
FT METAL 243 243 MAGNESIUM (BY SIMILARITY).
FT METAL 244 244 MAGNESIUM (BY SIMILARITY).
FT CONFLICT 44 44 G -> S (IN REF. 8).
FT CONFLICT 379 379 Q -> N (IN REF. 7).
FT CONFLICT 401 401 T -> D (IN REF. 7).
FT CONFLICT 451 470 MVSGALVPSGTTNTASVHVL -> YGFWCTGTERHY (IN
FT REF. 1 AND 4).
FT STRAND 5 9
FT HELIX 12 14
FT HELIX 17 26
FT TURN 27 27
FT STRAND 28 34
FT TURN 35 36
FT HELIX 40 57
FT TURN 58 58
FT STRAND 62 66
FT STRAND 72 74
FT STRAND 77 77
FT HELIX 78 80
FT STRAND 83 85
FT TURN 87 88
FT STRAND 90 94
FT TURN 97 98
FT STRAND 101 102
FT TURN 103 104
FT STRAND 105 108
FT TURN 111 112
FT HELIX 113 116
FT TURN 119 120
FT STRAND 122 125
FT TURN 126 129
FT STRAND 130 138
FT TURN 139 140
FT STRAND 141 146
FT STRAND 150 152
FT STRAND 157 159
FT HELIX 172 184
FT TURN 185 185
FT STRAND 188 191
FT HELIX 197 208
FT TURN 209 211
FT TURN 213 214
FT STRAND 216 221
FT HELIX 224 228
FT TURN 229 229
FT HELIX 230 236
FT STRAND 239 243
FT HELIX 244 250
FT HELIX 253 270
FT TURN 271 271
FT STRAND 273 277
FT HELIX 292 304
FT TURN 305 305
FT STRAND 308 311
FT HELIX 322 336
FT TURN 337 338
FT HELIX 355 368
FT TURN 369 370
FT STRAND 373 377
FT HELIX 382 388
FT TURN 389 390
FT STRAND 395 400
FT HELIX 403 408
FT HELIX 409 411
FT TURN 413 414
FT STRAND 415 419
FT HELIX 426 439
FT TURN 440 440
FT TURN 445 446
FT STRAND 448 453
FT TURN 459 460
FT STRAND 464 470
SQ SEQUENCE 470 AA; 50729 MW; E29BF01B90327D8B CRC64;
MKKTKIVCTI GPKTESEEML AKMLDAGMNV MRLNFSHGDY AEHGQRIQNL RNVMSKTGKT
AAILLDTKGP EIRTMKLEGG NDVSLKAGQT FTFTTDKSVI GNSEMVAVTY EGFTTDLSVG
NTVLVDDGLI GMEVTAIEGN KVICKVLNNG DLGENKGVNL PGVSIALPAL AEKDKQDLIF
GCEQGVDFVA ASFIRKRSDV IEIREHLKAH GGENIHIISK IENQEGLNNF DEILEASDGI
MVARGDLGVE IPVEEVIFAQ KMMIEKCIRA RKVVITATQM LDSMIKNPRP TRAEAGDVAN
AILDGTDAVM LSGESAKGKY PLEAVSIMAT ICERTDRVMN SRLEFNNDNR KLRITEAVCR
GAVETAEKLD APLIVVATQG GKSARAVRKY FPDATILALT TNEKTAHQLV LSKGVVPQLV
KEITSTDDFY RLGKELALQS GLAHKGDVVV MVSGALVPSG TTNTASVHVL
//
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