ID   SYM_BURO0               Reviewed;         716 AA.
AC   B1JWS3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 101.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_00098};
GN   OrderedLocusNames=Bcenmc03_2442;
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia;
OC   Burkholderia cepacia complex; Burkholderia orbicola.
OX   NCBI_TaxID=406425;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of L-methionine to tRNA(Met). Is
CC       required not only for elongation of protein synthesis but also for the
CC       initiation of all mRNA translation through initiator tRNA(fMet)
CC       aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Met) + L-methionine + ATP = L-methionyl-tRNA(Met) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-
CC         COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215;
CC         EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
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DR   EMBL; CP000958; ACA91603.1; -; Genomic_DNA.
DR   RefSeq; WP_012329008.1; NC_010508.1.
DR   AlphaFoldDB; B1JWS3; -.
DR   SMR; B1JWS3; -.
DR   KEGG; bcm:Bcenmc03_2442; -.
DR   HOGENOM; CLU_009710_7_0_4; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   FunFam; 2.20.28.20:FF:000001; Methionine--tRNA ligase; 1.
DR   FunFam; 2.40.50.140:FF:000042; Methionine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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   NCBIfam; TIGR00398; metG; 1.
DR   NCBIfam; TIGR00399; metG_C_term; 1.
DR   NCBIfam; NF001100; PRK00133.1; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..716
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_1000093701"
FT   DOMAIN          610..716
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           27..37
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           348..352
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         351
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   716 AA;  79073 MW;  90697D15301A2D43 CRC64;
     MSASDLTSVQ AAAPQGSRQI LVTSALPYAN GQIHIGHLVE YIQTDIWVRT LRMHGHEVYY
     IGADDTHGTP IMLRAEKEGL TPKQLIDRVW TEHKRDFDSF GVSFDNFYTT DSEENRVLSE
     NIYLALQEAG LIAEREIEQA YDPVKEMFLP DRFIKGECPK CHAKDQYGDS CEVCGSTYLP
     TELLNPYSVV SGATPVRKTS KHYFFRLSDP RCESFLREWV SGLAQPEATN KMREWLGDAG
     ESKLADWDIS RDAPYFGFEI PGAPGKYFYV WLDAPVGYYA SFKNLCERNG IDFDAWIRPG
     SKAEQYHFIG KDILYFHTLF WPAMLEFSGH RTPTNVFAHG FLTVDGAKMS KSRGTFITAQ
     SYIDTGLNPE WLRYYFAAKL NATMEDIDLN LDDFQARVNS DLVGKYVNIA SRAAGFLIKR
     FDGRVQDSAM NHPLVAKLRD AIAQIAASYE AREYGRALRH TMELADEVNA YVDGAKPWDL
     AKDPANAVAL HETCSVSLEA FRLLSLALKP VMPRVAEAVE AFFGIAPLAW ADAAKPLSSA
     QPIKAYQHLM TRVDAKQIEA LLAANRDSLQ AEAAGAAAAG ANAAKDAKSN AKAKPAAVNG
     ADDAPISIDD FAKIDLRIAK IVACQAVEGS DKLLQLTLDV GEEKTRNVFS GIKSAYQPEQ
     LVGKLTVMVA NLAPRKMKFG LSEGMVLAAS ATDEKAEPGL YILEPHSGAK PGMRVK
//