SYM_ECOLI
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 03-AUG-2022, entry version 218.
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; DOI=10.1128/jb.160.3.1115-1122.1984;
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 P00959; 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 6SPN; X-ray; 1.45 A; A=2-548.
DR PDB; 6SPO; X-ray; 1.20 A; A=2-548.
DR PDB; 6SPP; X-ray; 1.49 A; A=2-548.
DR PDB; 6SPQ; X-ray; 1.38 A; A=2-548.
DR PDB; 6SPR; X-ray; 1.48 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 PDBsum; 6SPN; -.
DR PDBsum; 6SPO; -.
DR PDBsum; 6SPP; -.
DR PDBsum; 6SPQ; -.
DR PDBsum; 6SPR; -.
DR AlphaFoldDB; P00959; -.
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 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; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_7_0_6; -.
DR InParanoid; P00959; -.
DR OMA; SDMHGTP; -.
DR PhylomeDB; P00959; -.
DR BioCyc; EcoCyc:METG-MON; -.
DR BioCyc; MetaCyc:METG-MON; -.
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; 2.40.50.140; -; 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 PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
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 BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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:0007829|PDB:6SPO"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1QQT"
FT HELIX 23..41
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 253..272
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 299..303
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:6SPO"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 438..459
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 471..492
FT /evidence="ECO:0007829|PDB:6SPO"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 497..507
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:6SPO"
FT HELIX 537..547
FT /evidence="ECO:0007829|PDB:6SPO"
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
