SYM_MYCGE
ID SYM_MYCGE Reviewed; 512 AA.
AC P47267; Q49339; Q49473;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=MG021;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-508.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=1945886; DOI=10.1093/nar/19.21.6027;
RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A random sequencing approach for placing markers on the physical map of
RT Mycoplasma genitalium.";
RL Nucleic Acids Res. 19:6027-6031(1991).
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; L43967; AAC71237.1; -; Genomic_DNA.
DR EMBL; U02229; AAA03382.2; -; Genomic_DNA.
DR EMBL; X61513; CAA43727.1; -; Genomic_DNA.
DR PIR; C64202; C64202.
DR RefSeq; WP_009885919.1; NZ_AAGX01000010.1.
DR AlphaFoldDB; P47267; -.
DR SMR; P47267; -.
DR STRING; 243273.MG_021; -.
DR EnsemblBacteria; AAC71237; AAC71237; MG_021.
DR KEGG; mge:MG_021; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_14; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR BioCyc; MGEN243273:G1GJ2-21-MON; -.
DR Proteomes; UP000000807; 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; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
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; PF09334; tRNA-synt_1g; 2.
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..512
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139228"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT MOTIF 301..305
FT /note="'KMSKS' region"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 506..508
FT /note="VLF -> FYL (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 60007 MW; CA05EC9B4356F432 CRC64;
MKRCYITTPI YYASGKPHIG HAFTTILADV IKRFKIQNGY EAFLLVGSDE HGNKIESKAK
SLNLDPKTFV DINAQAFKLM WKTLNISFDH FIRTTDEIHK QQVQKTFQDL YDKKLIYQSE
WKGAYCVECE QNYFTFNKQT MLCEIGHNLS LVQEPCWFIS FSSTKNWIET TIGKNQLNII
PKSRASELKN NFINNGLNDL ALTRKNVTWG IKVPFDPNQT IYVWFDALFS YITNLGFRNG
DPNFIKWWNN DNKEREVIHL ISREITRFHC IYWPIFLHLL DIKLPTQFLS HGWIVDGEGR
KMSKSLNNVI SPEQLIDQFG VDGTRYCLLK EMRLDKDNRC SVSILKEIYN ADLANSFGNH
VSRTFGMIKK YLNGKLEYQI ITDNALQKIM ILIDESIVQF DHYFNSYEFY RAINLLLKIV
FELSKLIDDF KPWELFKNQE FSLLKQLLFT CVRCVQVCYV LLTPILVNTA SKVFHLFNFA
DDACRKDQLR DATLLKKIII SNSMEVLFKR VD
