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ID TRMD_ECOLI Reviewed; 255 AA.
AC P0A873; P07020;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 05-FEB-2008, entry version 27.
DE tRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.31) (M1G-
DE methyltransferase) (tRNA [GM37] methyltransferase).
GN Name=trmD; OrderedLocusNames=b2607, JW2588;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=84057772; PubMed=6357787;
RA Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.;
RT "The nucleotide sequence of an Escherichia coli operon containing
RT genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16
RT and L19 and a 21-K polypeptide.";
RL EMBO J. 2:899-905(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-10.
RX MEDLINE=83108856; PubMed=6337136;
RA Hjalmarsson K.J., Bystroem A.S., Bjoerk G.R.;
RT "Purification and characterization of transfer RNA (guanine-
RT 1)methyltransferase from Escherichia coli.";
RL J. Biol. Chem. 258:1343-1351(1983).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-59; GLY-91; ARG-114;
RP TYR-115; GLY-117; ASP-119; ARG-121; ASP-128; ASP-135; TYR-136;
RP GLY-141; ARG-154; ASP-169; PHE-171; PRO-184; VAL-192; PRO-193;
RP LEU-196; LEU-197; ILE-204; TRP-207 AND ARG-208.
RX MEDLINE=22945896; PubMed=14583191; DOI=10.1016/j.jmb.2003.09.011;
RA Elkins P.A., Watts J.M., Zalacain M., van Thiel A., Vitazka P.R.,
RA Redlak M., Andraos-Selim C., Rastinejad F., Holmes W.M.;
RT "Insights into catalysis by a knotted TrmD tRNA methyltransferase.";
RL J. Mol. Biol. 333:931-949(2003).
CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC homocysteine + tRNA containing N(1)-methylguanine.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- MISCELLANEOUS: The specific activity of this enzyme increases only
CC slightly with increased growth rate.
CC -!- MISCELLANEOUS: This enzyme is present at ca. 80 molecules/genome.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase trmD family.
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DR EMBL; X01818; CAA25959.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75656.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16492.1; -; Genomic_DNA.
DR PIR; A30380; XYECG1.
DR RefSeq; AP_003188.1; -.
DR RefSeq; NP_417098.1; -.
DR PDB; 1P9P; X-ray; 2.50 A; A=1-255.
DR PDBsum; 1P9P; -.
DR IntAct; P0A873; -.
DR GeneID; 947099; -.
DR GenomeReviews; U00096_GR; b2607.
DR GenomeReviews; AP009048_GR; JW2588.
DR KEGG; ecj:JW2588; -.
DR KEGG; eco:b2607; -.
DR EchoBASE; EB1016; -.
DR EcoGene; EG11023; trmD.
DR BioCyc; EcoCyc:EG11023-MON; -.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR HAMAP; MF_00605; -; 1.
DR InterPro; IPR002649; tRNA_m1G_mtfrase.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR ProDom; PD004978; tRNA_m1G_mtfrase; 1.
DR TIGRFAMs; TIGR00088; trmD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1 255 tRNA (guanine-N(1)-)-methyltransferase.
FT /FTId=PRO_0000060375.
FT REGION 133 138 S-adenosyl-L-methionine binding.
FT ACT_SITE 169 169 Proton acceptor (Potential).
FT BINDING 86 86 S-adenosyl-L-methionine.
FT BINDING 113 113 S-adenosyl-L-methionine; via amide
FT nitrogen (By similarity).
FT MUTAGEN 59 59 G->A: Loss of activity.
FT MUTAGEN 91 91 G->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 114 114 R->A: Loss of activity.
FT MUTAGEN 115 115 Y->A: Increases Km for S-adenosyl-L-
FT methionine 24-fold.
FT MUTAGEN 117 117 G->A: Loss of activity.
FT MUTAGEN 119 119 D->A: Loss of activity.
FT MUTAGEN 121 121 R->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 128 128 D->A: Loss of activity.
FT MUTAGEN 135 135 D->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 136 136 Y->A: Increases Km for S-adenosyl-L-
FT methionine 68-fold.
FT MUTAGEN 141 141 G->A: Increases Km for S-adenosyl-L-
FT methionine 82-fold.
FT MUTAGEN 154 154 R->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 169 169 D->A: Loss of activity.
FT MUTAGEN 171 171 F->A: Loss of activity.
FT MUTAGEN 184 184 P->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 192 192 V->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 193 193 P->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 196 196 L->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 197 197 L->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 204 204 I->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 207 207 W->A: Loss of activity; no effect on tRNA
FT binding.
FT MUTAGEN 207 207 W->F,H: Small decrease in activity.
FT MUTAGEN 208 208 R->A: Loss of activity; no effect on tRNA
FT binding.
FT STRAND 2 6
FT HELIX 10 13
FT HELIX 14 17
FT HELIX 20 27
FT STRAND 32 36
FT HELIX 38 41
FT HELIX 64 78
FT STRAND 83 87
FT STRAND 91 93
FT HELIX 96 103
FT STRAND 106 111
FT HELIX 120 126
FT STRAND 128 136
FT HELIX 142 153
FT TURN 157 159
FT STRAND 185 187
FT HELIX 194 197
FT HELIX 201 219
FT HELIX 221 225
FT HELIX 231 245
SQ SEQUENCE 255 AA; 28422 MW; B101087229B4CDBD CRC64;
MWIGIISLFP EMFRAITDYG VTGRAVKNGL LSIQSWSPRD FTHDRHRTVD DRPYGGGPGM
LMMVQPLRDA IHAAKAAAGE GAKVIYLSPQ GRKLDQAGVS ELATNQKLIL VCGRYEGIDE
RVIQTEIDEE WSIGDYVLSG GELPAMTLID SVSRFIPGVL GHEASATEDS FAEGLLDCPH
YTRPEVLEGM EVPPVLLSGN HAEIRRWRLK QSLGRTWLRR PELLENLALT EEQARLLAEF
KTEHAQQQHK HDGMA
//