SYM_AQUAE
ID SYM_AQUAE Reviewed; 497 AA.
AC O67298;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=aq_1257;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed
RT with tRNA(met).";
RL Submitted (SEP-2005) to the PDB data bank.
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; AE000657; AAC07256.1; -; Genomic_DNA.
DR PIR; G70408; G70408.
DR RefSeq; NP_213862.1; NC_000918.1.
DR RefSeq; WP_010880800.1; NC_000918.1.
DR PDB; 2CSX; X-ray; 2.70 A; A/B=1-497.
DR PDB; 2CT8; X-ray; 2.70 A; A/B=1-497.
DR PDBsum; 2CSX; -.
DR PDBsum; 2CT8; -.
DR AlphaFoldDB; O67298; -.
DR SMR; O67298; -.
DR STRING; 224324.aq_1257; -.
DR PRIDE; O67298; -.
DR EnsemblBacteria; AAC07256; AAC07256; aq_1257.
DR KEGG; aae:aq_1257; -.
DR PATRIC; fig|224324.8.peg.980; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_0; -.
DR InParanoid; O67298; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR EvolutionaryTrace; O67298; -.
DR Proteomes; UP000000798; 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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..497
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139206"
FT MOTIF 14..24
FT /note="'HIGH' region"
FT MOTIF 295..299
FT /note="'KMSKS' region"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
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 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 22..40
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 100..115
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2CT8"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2CT8"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2CSX"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:2CSX"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2CSX"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:2CSX"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:2CSX"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 398..419
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 421..425
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 430..451
FT /evidence="ECO:0007829|PDB:2CSX"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2CSX"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:2CSX"
SQ SEQUENCE 497 AA; 58931 MW; 846C68E72AFEB4F7 CRC64;
MTLMKKFYVT TPIYYVNDVP HLGHAYTTIA ADTIARYYRL RDYDVFFLTG TDEHGLKIQK
KAEELGISPK ELVDRNAERF KKLWEFLKIE YTKFIRTTDP YHVKFVQKVF EECYKRGDIY
LGEYEGWYCV GCEEFKSEAE LAEDHTCPIH QKKCEYIKEP SYFFRLSKYQ DKLLELYEKN
PEFIQPDYRR NEIISFVKQG LKDLSVTRPR SRVKWGIPVP FDPEHTIYVW FDALFNYISA
LEDKVEIYWP ADLHLVGKDI LRFHTVYWPA FLMSLGYELP KKVFAHGWWT VEGKKMSKTL
GNVVDPYEVV QEYGLDEVRY FLLREVPFGQ DGDFSKKAIL NRINGELANE IGNLYSRVVN
MAHKFLGGEV SGARDEEYAK IAQESIKNYE NYMEKVNFYK AIEEILKFTS YLNKYVDEKQ
PWALNKERKK EELQKVLYAL VDGLFVLTHL LYPITPNKMK EALQMLGEKE FLKELKPYSK
NTYKLGERKI LFPKREG
