SYM_XANAC
ID SYM_XANAC Reviewed; 694 AA.
AC Q8PMP0;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
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}; Synonyms=metS;
GN OrderedLocusNames=XAC1386;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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_00098}.
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_00098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-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; AE008923; AAM36257.1; -; Genomic_DNA.
DR RefSeq; WP_011050884.1; NC_003919.1.
DR PDB; 6WQ6; X-ray; 1.70 A; A=1-694.
DR PDB; 6WQI; X-ray; 2.00 A; A/B=1-694.
DR PDB; 6WQS; X-ray; 2.00 A; A=1-563.
DR PDB; 6WQT; X-ray; 1.65 A; A=1-563.
DR PDBsum; 6WQ6; -.
DR PDBsum; 6WQI; -.
DR PDBsum; 6WQS; -.
DR PDBsum; 6WQT; -.
DR AlphaFoldDB; Q8PMP0; -.
DR SMR; Q8PMP0; -.
DR STRING; 190486.XAC1386; -.
DR PRIDE; Q8PMP0; -.
DR EnsemblBacteria; AAM36257; AAM36257; XAC1386.
DR GeneID; 66910553; -.
DR KEGG; xac:XAC1386; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_7_0_6; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000576; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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 Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 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; 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 PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR TIGRFAMs; TIGR00399; metG_C_term; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..694
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139175"
FT DOMAIN 591..694
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT REGION 550..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT MOTIF 330..334
FT /note="'KMSKS' region"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 252..271
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6WQT"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 388..403
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 414..432
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 436..457
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 469..490
FT /evidence="ECO:0007829|PDB:6WQT"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:6WQT"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:6WQT"
SQ SEQUENCE 694 AA; 75338 MW; C67052B9355A6D59 CRC64;
MTRTALVTTA LPYANGPLHL GHLVGYIQAD IWVRARRLRG DKTWFVCADD THGTPIMLAA
EKAGVTPEAF IANVQASHER DFAAFGVTFD HYDSTNSPVN RELTEAFYAK LEAAGHISRR
SVAQFYDTAK GMFLPDRYIK GICPNCGSPD QYGDNCEVCG ATYAPTELKE PKSVISGATP
ELRDSEHFFF EVGHFDGFLR EWLAGDVALP GVKAKLKEWL DAEGGLRAWD ISRDAPYFGF
QIPGQPGKYF YVWLDAPIGY LCSFKTLCAQ MGENFEAHLV AGTQTELHHF IGKDIVNFHG
LFWPAVLHGT GHRAPTRLHV NGYLTVDGAK MSKSRGTFVM ARTFLDVGLE PEALRYYFAA
KSSGGVDDLD LNLGDFIARV NADLVGKFVN LASRCAGFIG KRFDGKLADA LPDAAQYDRF
VAALAPIREA YERNDAASAI RQTMALADEA NKYIDDTKPW VIAKQDGADA QLQSVCTQGL
NLFRILVAAL KPILPRTCAE AEAFLSAPMT SWEDVIGPLT AHTIQPYTAL FTRIDPKLID
AMTDASKDTL AAPATPATAS KPAPAKADAK PAAAANPQSP IATPGFIGMD DFAKLDLRIG
KVLACEFVEG SDKLLRFELD AGELGTRQIF SGIRASYREP ETLVGRSVVF IANLAPRKMR
FGISEGMILS AGFDGGALAL LDADSGAQPG MPVR
