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ID THD1_ECOLI Reviewed; 514 AA.
AC P04968; Q2M881;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 12-DEC-2006, entry version 83.
DE Threonine dehydratase biosynthetic (EC 4.3.1.19) (Threonine
DE deaminase).
GN Name=ilvA; OrderedLocusNames=b3772, JW3745;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=88056322; PubMed=3315862; DOI=10.1016/0378-1119(87)90136-3;
RA Cox J.L., Cox B.J., Fidanza V., Calhoun D.H.;
RT "The complete nucleotide sequence of the ilvGMEDA cluster of
RT Escherichia coli K-12.";
RL Gene 56:185-198(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Garrison E., Harms E., Umbarger H.E.;
RL Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=87174741; PubMed=3550695;
RA Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E.,
RA Hatfield G.W.;
RT "The complete nucleotide sequence of the ilvGMEDA operon of
RT Escherichia coli K-12.";
RL Nucleic Acids Res. 15:2137-2155(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX MEDLINE=92358234; PubMed=1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region
RT from 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 439-514.
RC STRAIN=K12;
RX MEDLINE=86111952; PubMed=3003115;
RA Wek R.C., Hatfield G.W.;
RT "Nucleotide sequence and in vivo expression of the ilvY and ilvC genes
RT in Escherichia coli K12. Transcription from divergent overlapping
RT promoters.";
RL J. Biol. Chem. 261:2441-2450(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=K12;
RX MEDLINE=89326124; PubMed=2473940; DOI=10.1016/0378-1119(89)90166-2;
RA Lopes J.M., Lawther R.P.;
RT "Physical identification of an internal promoter, ilvAp, in the distal
RT portion of the ilvGMEDA operon.";
RL Gene 76:255-269(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX MEDLINE=98230745; PubMed=9562556; DOI=10.1016/S0969-2126(98)00048-3;
RA Gallagher D.T., Gilliland G.L., Xiao G., Zondlo J., Fisher K.E.,
RA Chinchilla D., Eisenstein E.;
RT "Structure and control of pyridoxal phosphate dependent allosteric
RT threonine deaminase.";
RL Structure 6:465-475(1998).
CC -!- FUNCTION: Catalyzes the formation of alpha-ketobutyrate from
CC threonine in a two-step reaction. The first step is a dehydration
CC of threonine, followed by rehydration and liberation of ammonia.
CC Deaminates L-threonine, but also L-serine to a lesser extent.
CC -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3).
CC -!- COFACTOR: Pyridoxal phosphate.
CC -!- ENZYME REGULATION: Isoleucine allosterically inhibits whereas
CC valine allosterically activates this enzyme.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: single step.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
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DR EMBL; X04890; CAA28577.1; -; Genomic_DNA.
DR EMBL; K03503; AAA24014.1; -; Genomic_DNA.
DR EMBL; M10313; AAB59054.1; -; Genomic_DNA.
DR EMBL; M11689; AAA24027.1; -; Genomic_DNA.
DR EMBL; M32253; AAA24024.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67575.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77492.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77525.1; -; Genomic_DNA.
DR EMBL; M25497; AAA24015.1; -; Genomic_DNA.
DR PIR; B27310; DWECTS.
DR PDB; 1TDJ; X-ray; @=1-514.
DR DIP; DIP:10018N; -.
DR IntAct; P04968; -.
DR ECO2DBASE; F050.1; 6TH EDITION.
DR GenomeReviews; U00096_GR; b3772.
DR GenomeReviews; AP009048_GR; JW3745.
DR KEGG; ecj:JW3745; -.
DR KEGG; eco:b3772; -.
DR EchoBASE; EB0488; -.
DR EcoGene; EG10493; ilvA.
DR BioCyc; EcoCyc:THREDEHYDSYN-MONOMER; -.
DR InterPro; IPR001926; B6_enzyme_beta.
DR InterPro; IPR000634; S_T_dehydrtse_BS.
DR InterPro; IPR005787; Thr_dehydrateI.
DR InterPro; IPR001721; ThrDh_C.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome;
KW Isoleucine biosynthesis; Lyase; Pyridoxal phosphate.
FT CHAIN 1 514 Threonine dehydratase biosynthetic.
FT /FTId=PRO_0000185573.
FT BINDING 62 62 Pyridoxal phosphate (covalent).
FT CONFLICT 120 120 A -> R (in Ref. 2).
FT CONFLICT 140 140 A -> R (in Ref. 2).
FT CONFLICT 195 195 G -> C (in Ref. 2).
FT CONFLICT 243 243 A -> G (in Ref. 3).
FT CONFLICT 334 334 G -> V (in Ref. 2).
FT TURN 6 7
FT HELIX 13 22
FT HELIX 25 27
FT TURN 28 28
FT STRAND 34 36
FT HELIX 38 43
FT TURN 44 45
FT STRAND 46 51
FT HELIX 53 55
FT TURN 57 58
FT STRAND 59 61
FT TURN 62 62
FT HELIX 63 71
FT TURN 72 75
FT STRAND 79 81
FT STRAND 83 86
FT STRAND 88 90
FT HELIX 91 100
FT TURN 101 102
FT STRAND 105 108
FT HELIX 115 124
FT STRAND 127 129
FT HELIX 135 149
FT HELIX 160 176
FT TURN 178 179
FT STRAND 182 186
FT STRAND 188 190
FT HELIX 191 203
FT TURN 205 206
FT STRAND 208 214
FT TURN 215 217
FT HELIX 219 226
FT TURN 227 227
FT STRAND 237 240
FT TURN 241 242
FT HELIX 250 255
FT TURN 256 257
FT STRAND 261 265
FT HELIX 267 279
FT TURN 280 281
FT HELIX 287 303
FT TURN 304 304
FT STRAND 309 313
FT TURN 321 322
FT HELIX 323 335
FT STRAND 338 344
FT STRAND 347 350
FT HELIX 353 357
FT TURN 358 359
FT STRAND 360 370
FT STRAND 374 376
FT STRAND 378 384
FT TURN 388 388
FT HELIX 389 399
FT TURN 400 400
FT STRAND 401 403
FT STRAND 405 407
FT TURN 408 409
FT HELIX 413 417
FT TURN 418 418
FT HELIX 419 421
FT TURN 422 422
FT STRAND 434 439
FT TURN 444 445
FT HELIX 446 454
FT STRAND 462 464
FT TURN 468 470
FT STRAND 475 479
FT STRAND 498 501
FT TURN 503 504
FT HELIX 506 511
FT TURN 512 512
SQ SEQUENCE 514 AA; 56195 MW; 9D389A0EDD8DE692 CRC64;
MADSQPLSGA PEGAEYLRAV LRAPVYEAAQ VTPLQKMEKL SSRLDNVILV KREDRQPVHS
FKLRGAYAMM AGLTEEQKAH GVITASAGNH AQGVAFSSAR LGVKALIVMP TATADIKVDA
VRGFGGEVLL HGANFDEAKA KAIELSQQQG FTWVPPFDHP MVIAGQGTLA LELLQQDAHL
DRVFVPVGGG GLAAGVAVLI KQLMPQIKVI AVEAEDSACL KAALDAGHPV DLPRVGLFAE
GVAVKRIGDE TFRLCQEYLD DIITVDSDAI CAAMKDLFED VRAVAEPSGA LALAGMKKYI
ALHNIRGERL AHILSGANVN FHGLRYVSER CELGEQREAL LAVTIPEEKG SFLKFCQLLG
GRSVTEFNYR FADAKNACIF VGVRLSRGLE ERKEILQMLN DGGYSVVDLS DDEMAKLHVR
YMVGGRPSHP LQERLYSFEF PESPGALLRF LNTLGTYWNI SLFHYRSHGT DYGRVLAAFE
LGDHEPDFET RLNELGYDCH DETNNPAFRF FLAG
//