SYM_SYNY3
ID SYM_SYNY3 Reviewed; 532 AA.
AC Q55729;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; Synonyms=metS; OrderedLocusNames=slr0649;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2A subfamily. {ECO:0000305}.
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DR EMBL; BA000022; BAA10371.1; -; Genomic_DNA.
DR PIR; S76525; S76525.
DR AlphaFoldDB; Q55729; -.
DR SMR; Q55729; -.
DR IntAct; Q55729; 2.
DR STRING; 1148.1001640; -.
DR PaxDb; Q55729; -.
DR PRIDE; Q55729; -.
DR EnsemblBacteria; BAA10371; BAA10371; BAA10371.
DR KEGG; syn:slr0649; -.
DR eggNOG; COG0143; Bacteria.
DR InParanoid; Q55729; -.
DR OMA; SDMHGTP; -.
DR PhylomeDB; Q55729; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..532
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139256"
FT MOTIF 16..26
FT /note="'HIGH' region"
FT MOTIF 305..309
FT /note="'KMSKS' region"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 532 AA; 61442 MW; 8D97AE90D3F18A34 CRC64;
MLDSSVPTFS VTTPLYYVND VPHLGSAYTT VVADTLARFK RLQGYDVLMI TGTDEHGQKI
QRTAEAQELD PQTHCDRTVV KFKELWRSLN ILYDRFSRTT DPRHLAIVKD FFQRVWDKGD
IYLAQQQGWY CVACEEFKEK RDLLEDNHCP LHPNRKAEWR DEENYFFRLS RYQHPLEELY
AQRPEFIQPS SRRNEVLNFV AQGLQDFSIS RVNLDWGFPL PNDPNHTIYV WFDALLGYVT
ALLDEDEEPN LTNALVKWWP INLHLIGKDI LRFHAVYWPA MLMSAELAIP AQVFGHGFLT
KDGQKMGKSL GNTVDPLDLI NRYGEDAFRY YFLKEIEFGK DGDFNEQRFV NVLNADLAND
LGNLLNRTLG MVKKYCQGQG PQVMATDLAP DNPLKALGSH LGEEVSSAYE RLSFTDACEA
IFTLVRAGNK YIDDMAPWKL FKQGSQKEVE DVLYSVLESI RLSAYLLSPI VPRLSTKIYQ
QLGFTWDFDQ WRSPLEQAEE FNRHQSWGQL GANQNLPPAQ PIFTKLELPA EE
