SYM_MYCTU
ID SYM_MYCTU Reviewed; 519 AA.
AC P9WFU5; L0T8C8; O05593;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228, ECO:0000269|PubMed:9607323};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228, ECO:0000303|PubMed:9607323};
DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228, ECO:0000303|PubMed:9607323};
GN Name=metG {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metS;
GN OrderedLocusNames=Rv1007c; ORFNames=MTCI237.24;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DOMAIN.
RX PubMed=9607323; DOI=10.1016/s0014-5793(98)00417-7;
RA Kim S., Jo Y.J., Lee S.H., Motegi H., Shiba K., Sassanfar M.,
RA Martinis S.A.;
RT "Biochemical and phylogenetic analyses of methionyl-tRNA synthetase
RT isolated from a pathogenic microorganism, Mycobacterium tuberculosis.";
RL FEBS Lett. 427:259-262(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000255|HAMAP-Rule:MF_01228,
CC ECO:0000269|PubMed:9607323}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01228, ECO:0000269|PubMed:9607323};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
CC Evidence={ECO:0000269|PubMed:9607323};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for E.coli tRNAfMet {ECO:0000269|PubMed:9607323};
CC Note=kcat is 2.83 sec(-1) with E.coli tRNAfMet as substrate.
CC {ECO:0000269|PubMed:9607323};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01228,
CC ECO:0000269|PubMed:9607323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- DOMAIN: Lacks the Zn(2+) binding motif and the C-terminal dimerization
CC appendix that are found in MetRSs from several organisms including
CC E.coli MetRS. {ECO:0000269|PubMed:9607323}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR EMBL; AL123456; CCP43757.1; -; Genomic_DNA.
DR PIR; B70603; B70603.
DR RefSeq; NP_215523.1; NC_000962.3.
DR RefSeq; WP_003911321.1; NZ_NVQJ01000018.1.
DR PDB; 6AX8; X-ray; 2.60 A; A=1-519.
DR PDBsum; 6AX8; -.
DR AlphaFoldDB; P9WFU5; -.
DR SMR; P9WFU5; -.
DR STRING; 83332.Rv1007c; -.
DR PaxDb; P9WFU5; -.
DR DNASU; 886050; -.
DR GeneID; 886050; -.
DR KEGG; mtu:Rv1007c; -.
DR TubercuList; Rv1007c; -.
DR eggNOG; COG0143; Bacteria.
DR OMA; SDMHGTP; -.
DR PhylomeDB; P9WFU5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IDA:MTBBASE.
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; IPR001412; aa-tRNA-synth_I_CS.
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; PF09334; tRNA-synt_1g; 2.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..519
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139233"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT MOTIF 299..303
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT COMPBIAS 501..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 66..83
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 97..112
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:6AX8"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6AX8"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6AX8"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6AX8"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 356..369
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 407..428
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 439..463
FT /evidence="ECO:0007829|PDB:6AX8"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 468..477
FT /evidence="ECO:0007829|PDB:6AX8"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6AX8"
SQ SEQUENCE 519 AA; 58093 MW; B8DAE2553B5EFB49 CRC64;
MKPYYVTTAI AYPNAAPHVG HAYEYIATDA IARFKRLDRY DVRFLTGTDE HGLKVAQAAA
AAGVPTAALA RRNSDVFQRM QEALNISFDR FIRTTDADHH EASKELWRRM SAAGDIYLDN
YSGWYSVRDE RFFVESETQL VDGTRLTVET GTPVTWTEEQ TYFFRLSAYT DKLLAHYHAN
PDFIAPETRR NEVISFVSGG LDDLSISRTS FDWGVQVPEH PDHVMYVWVD ALTNYLTGAG
FPDTDSELFR RYWPADLHMI GKDIIRFHAV YWPAFLMSAG IELPRRIFAH GFLHNRGEKM
SKSVGNIVDP VALAEALGVD QVRYFLLREV PFGQDGSYSD EAIVTRINTD LANELGNLAQ
RSLSMVAKNL DGRVPNPGEF ADADAALLAT ADGLLERVRG HFDAQAMHLA LEAIWLMLGD
ANKYFSVQQP WVLRKSESEA DQARFRTTLY VTCEVVRIAA LLIQPVMPES AGKILDLLGQ
APNQRSFAAV GVRLTPGTAL PPPTGVFPRY QPPQPPEGK
