GenomeNet

Database: UniProt
Entry: P00959
LinkDB: P00959
Original site: P00959 
ID   SYM_ECOLI               Reviewed;         677 AA.
AC   P00959; Q2MAW4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 206.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=b2114, JW2101;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6094501;
RA   Dardel F., Fayat G., Blanquet S.;
RT   "Molecular cloning and primary structure of the Escherichia coli methionyl-
RT   tRNA synthetase gene.";
RL   J. Bacteriol. 160:1115-1122(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2259334; DOI=10.1007/bf00315804;
RA   Dardel F., Panvert M., Fayat G.;
RT   "Transcription and regulation of expression of the Escherichia coli
RT   methionyl-tRNA synthetase gene.";
RL   Mol. Gen. Genet. 223:121-133(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-566, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=6756915;
RA   Barker D.G., Ebel J.-P., Jakes R., Bruton C.J.;
RT   "Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the
RT   active crystallised tryptic fragment.";
RL   Eur. J. Biochem. 127:449-457(1982).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=7042987; DOI=10.1016/0022-2836(82)90492-2;
RA   Zelwer C., Risler J.-L., Brunie S.;
RT   "Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5-A
RT   resolution.";
RL   J. Mol. Biol. 155:63-81(1982).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=2254937; DOI=10.1016/s0022-2836(05)80331-6;
RA   Brunie S., Zelwer C., Risler J.-L.;
RT   "Crystallographic study at 2.5-A resolution of the interaction of
RT   methionyl-tRNA synthetase from Escherichia coli with ATP.";
RL   J. Mol. Biol. 216:411-424(1990).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-553.
RX   PubMed=10600385; DOI=10.1006/jmbi.1999.3339;
RA   Mechulam Y., Schmitt E., Maveyraud L., Zelwer C., Nureki O., Yokoyama S.,
RA   Konno M., Blanquet S.;
RT   "Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights
RT   species-specific features.";
RL   J. Mol. Biol. 294:1287-1297(1999).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-552 IN COMPLEX WITH
RP   L-METHIONINE.
RX   PubMed=11243794; DOI=10.1006/jmbi.2001.4408;
RA   Serre L., Verdon G., Choinowski T., Hervouet N., Risler J.-L., Zelwer C.;
RT   "How methionyl-tRNA synthetase creates its amino acid recognition pocket
RT   upon L-methionine binding.";
RL   J. Mol. Biol. 306:863-876(2001).
RN   [12]
RP   STRUCTURE BY NMR OF 139-164.
RX   PubMed=8515466; DOI=10.1006/jmbi.1993.1353;
RA   Fourmy D., Dardel F., Blanquet S.;
RT   "Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure
RT   and homology with rubredoxin and gag retroviral proteins.";
RL   J. Mol. Biol. 231:1078-1089(1993).
RN   [13]
RP   MAPPING OF SUBSTRATE-BINDING SITES.
RX   PubMed=1702021; DOI=10.1021/bi00487a029;
RA   Hountondji C., Schmitter J.-M., Beauvallet C., Blanquet S.;
RT   "Mapping of the active site of Escherichia coli methionyl-tRNA synthetase:
RT   identification of amino acid residues labeled by periodate-oxidized
RT   tRNA(fMet) molecules having modified lengths at the 3'-acceptor end.";
RL   Biochemistry 29:8190-8198(1990).
RN   [14]
RP   REVIEW.
RX   PubMed=2126467; DOI=10.1016/0300-9084(90)90126-2;
RA   Meinnel T., Mechulam Y., Dardel F., Schmitter J.-M., Hountondji C.,
RA   Brunie S., Dessen P., Fayat G., Blanquet S.;
RT   "Methionyl-tRNA synthetase from E. coli -- a review.";
RL   Biochimie 72:625-632(1990).
RN   [15]
RP   MUTAGENESIS.
RX   PubMed=1959615; DOI=10.1016/0014-5793(91)80879-8;
RA   Fourmy D., Mechulam Y., Brunie S., Blanquet S., Fayat G.;
RT   "Identification of residues involved in the binding of methionine by
RT   Escherichia coli methionyl-tRNA synthetase.";
RL   FEBS Lett. 292:259-263(1991).
RN   [16]
RP   MUTAGENESIS OF ZINC LIGANDS.
RX   PubMed=8515465; DOI=10.1006/jmbi.1993.1352;
RA   Fourmy D., Meinnel T., Mechulam Y., Blanquet S.;
RT   "Mapping of the zinc binding domain of Escherichia coli methionyl-tRNA
RT   synthetase.";
RL   J. Mol. Biol. 231:1068-1077(1993).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11243794}.
CC   -!- INTERACTION:
CC       P60422:rplB; NbExp=2; IntAct=EBI-909268, EBI-543515;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA60526.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; K02671; AAA24161.1; -; Genomic_DNA.
DR   EMBL; X55791; CAA39315.1; -; Genomic_DNA.
DR   EMBL; U00007; AAA60526.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC75175.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76592.1; -; Genomic_DNA.
DR   PIR; S14427; SYECMT.
DR   RefSeq; NP_416617.1; NC_000913.3.
DR   RefSeq; WP_001350533.1; NZ_LN832404.1.
DR   PDB; 1F4L; X-ray; 1.85 A; A=1-551.
DR   PDB; 1MEA; NMR; -; A=139-164.
DR   PDB; 1MED; NMR; -; A=139-164.
DR   PDB; 1P7P; X-ray; 1.80 A; A=2-552.
DR   PDB; 1PFU; X-ray; 1.91 A; A=2-552.
DR   PDB; 1PFV; X-ray; 1.70 A; A=2-552.
DR   PDB; 1PFW; X-ray; 1.78 A; A=2-552.
DR   PDB; 1PFY; X-ray; 1.93 A; A=2-552.
DR   PDB; 1PG0; X-ray; 1.90 A; A=2-552.
DR   PDB; 1PG2; X-ray; 1.75 A; A=2-552.
DR   PDB; 1QQT; X-ray; 2.03 A; A=2-552.
DR   PDB; 3H97; X-ray; 1.70 A; A=1-548.
DR   PDB; 3H99; X-ray; 1.40 A; A=1-548.
DR   PDB; 3H9B; X-ray; 1.50 A; A=1-548.
DR   PDB; 3H9C; X-ray; 1.40 A; A=2-548.
DR   PDBsum; 1F4L; -.
DR   PDBsum; 1MEA; -.
DR   PDBsum; 1MED; -.
DR   PDBsum; 1P7P; -.
DR   PDBsum; 1PFU; -.
DR   PDBsum; 1PFV; -.
DR   PDBsum; 1PFW; -.
DR   PDBsum; 1PFY; -.
DR   PDBsum; 1PG0; -.
DR   PDBsum; 1PG2; -.
DR   PDBsum; 1QQT; -.
DR   PDBsum; 3H97; -.
DR   PDBsum; 3H99; -.
DR   PDBsum; 3H9B; -.
DR   PDBsum; 3H9C; -.
DR   SMR; P00959; -.
DR   BioGrid; 4259174; 16.
DR   BioGrid; 850988; 1.
DR   DIP; DIP-10194N; -.
DR   IntAct; P00959; 4.
DR   STRING; 511145.b2114; -.
DR   BindingDB; P00959; -.
DR   ChEMBL; CHEMBL3367; -.
DR   DrugBank; DB02229; 5'-O-[(L-methionyl)-sulphamoyl]adenosine.
DR   DrugBank; DB03816; Difluoromethionine.
DR   DrugBank; DB04015; Methionine Phosphinate.
DR   DrugBank; DB02151; Methionine Phosphonate.
DR   DrugBank; DB03799; Trifluoromethionine.
DR   SWISS-2DPAGE; P00959; -.
DR   EPD; P00959; -.
DR   jPOST; P00959; -.
DR   PaxDb; P00959; -.
DR   PRIDE; P00959; -.
DR   EnsemblBacteria; AAC75175; AAC75175; b2114.
DR   EnsemblBacteria; BAE76592; BAE76592; BAE76592.
DR   GeneID; 946643; -.
DR   KEGG; ecj:JW2101; -.
DR   KEGG; eco:b2114; -.
DR   PATRIC; fig|1411691.4.peg.133; -.
DR   EchoBASE; EB0581; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0073; LUCA.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200400; -.
DR   InParanoid; P00959; -.
DR   KO; K01874; -.
DR   PhylomeDB; P00959; -.
DR   BioCyc; EcoCyc:METG-MONOMER; -.
DR   BioCyc; ECOL316407:JW2101-MONOMER; -.
DR   BioCyc; MetaCyc:METG-MONOMER; -.
DR   BRENDA; 6.1.1.10; 2026.
DR   EvolutionaryTrace; P00959; -.
DR   PRO; PR:P00959; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IDA:EcoCyc.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IMP:EcoCyc.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..677
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139129"
FT   DOMAIN          575..677
FT                   /note="tRNA-binding"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   MOTIF           333..337
FT                   /note="'KMSKS' region"
FT   METAL           146
FT                   /note="Zinc"
FT   METAL           149
FT                   /note="Zinc"
FT   METAL           159
FT                   /note="Zinc"
FT   METAL           162
FT                   /note="Zinc"
FT   BINDING         336
FT                   /note="ATP"
FT   MUTAGEN         336
FT                   /note="K->Q,A,E,R: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1959615,
FT                   ECO:0000269|PubMed:8515465"
FT   STRAND          7..12
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          16..19
FT                   /evidence="ECO:0000244|PDB:1QQT"
FT   HELIX           23..41
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          45..53
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           57..66
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           70..87
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          93..100
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           101..116
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          120..130
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            131..134
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           139..141
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          142..145
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            147..149
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          152..155
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            160..162
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           168..170
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          172..176
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            177..179
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          184..193
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           195..198
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           199..207
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           213..225
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          233..237
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          249..251
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           253..272
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           277..282
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          288..295
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           296..298
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           299..303
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           305..312
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          319..324
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          327..329
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            336..339
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           344..350
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           353..363
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   STRAND          371..373
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           375..385
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           386..390
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           392..395
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           398..404
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           416..424
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           426..434
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           438..459
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           461..464
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           471..492
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   TURN            493..495
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           497..507
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           514..517
FT                   /evidence="ECO:0000244|PDB:3H99"
FT   HELIX           537..547
FT                   /evidence="ECO:0000244|PDB:3H99"
SQ   SEQUENCE   677 AA;  76255 MW;  363F3324AFD3202C CRC64;
     MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM
     LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS EENRQLSELI YSRLKENGFI
     KNRTISQLYD PEKGMFLPDR FVKGTCPKCK SPDQYGDNCE VCGATYSPTE LIEPKSVVSG
     ATPVMRDSEH FFFDLPSFSE MLQAWTRSGA LQEQVANKMQ EWFESGLQQW DISRDAPYFG
     FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDSVSFDE YWKKDSTAEL YHFIGKDIVY
     FHSLFWPAML EGSNFRKPSN LFVHGYVTVN GAKMSKSRGT FIKASTWLNH FDADSLRYYY
     TAKLSSRIDD IDLNLEDFVQ RVNADIVNKV VNLASRNAGF INKRFDGVLA SELADPQLYK
     TFTDAAEVIG EAWESREFGK AVREIMALAD LANRYVDEQA PWVVAKQEGR DADLQAICSM
     GINLFRVLMT YLKPVLPKLT ERAEAFLNTE LTWDGIQQPL LGHKVNPFKA LYNRIDMRQV
     EALVEASKEE VKAAAAPVTG PLADDPIQET ITFDDFAKVD LRVALIENAE FVEGSDKLLR
     LTLDLGGEKR NVFSGIRSAY PDPQALIGRH TIMVANLAPR KMRFGISEGM VMAAGPGGKD
     IFLLSPDAGA KPGHQVK
//
DBGET integrated database retrieval system