ID   SYV_MYCGE               Reviewed;         837 AA.
AC   P47576;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-JUN-2026, entry version 149.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=MG334;
OS   Mycoplasmoides genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 /
OS   G37) (Mycoplasma genitalium).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
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 801-837.
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).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; L43967; AAC71557.1; -; Genomic_DNA.
DR   EMBL; U02249; AAD12537.1; -; Genomic_DNA.
DR   PIR; I64236; I64236.
DR   RefSeq; WP_010869437.1; NC_000908.2.
DR   AlphaFoldDB; P47576; -.
DR   SMR; P47576; -.
DR   FunCoup; P47576; 201.
DR   STRING; 243273.MG_334; -.
DR   GeneID; 99647225; -.
DR   KEGG; mge:MG_334; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_14; -.
DR   InParanoid; P47576; -.
DR   OrthoDB; 9810365at2; -.
DR   BioCyc; MGEN243273:G1GJ2-416-MONOMER; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   NCBIfam; NF004349; PRK05729.1; 1.
DR   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..837
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106230"
FT   COILED          767..837
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           514..518
FT                   /note="'KMSKS' region"
FT   BINDING         517
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   837 AA;  97464 MW;  7F2FD1FE95D3D8C5 CRC64;
     MKDKFSFQKN YDFNLVSDGL YEIWNNAGFF KPKDKNNSFT AILPPPNLTG TLHIGHAFEV
     SITDQIMRFK KMQGFSINWI PGFDHAGIAT QTKYEKIALK ENQKYFDADD DKKSEMIMNW
     ALNQSEIIKN QLKSLGVCLN WSETKFTLSE QANKIVNNCF KNLYENGFIY QAYTLVNWDT
     KLNTAISNIE VINKPVNQHL HYVVYKLAND SKQELIVATT RPETIFADVC LLVNPKDKRY
     TNFWNKLVVN PLTGKQIPVV TDSYVDIKFG TGILKCTPAH DFNDYEINTK YKFDFLSCID
     SNGILNQNAS KFQGLSVLQA RNKIVKWLEK NKLLVKSIPL TSNVGFSERS GTVVEPMLSK
     QWFVDLPKLK DHLYLKKYPD FIPKRFNKQV SNWLNKLKPW CISRQLIWGH KIPVWFENNT
     GEIVVGEKPS KNLQNYTRSK DVLDTWFSSS LWPLICLNWE QDDSFHETEL LVTGYDILFF
     WVLRMLFNSF FETKKLPFKT VLIHGLVRDE QNRKMSKSLN NGIDPVDLIR NYGADAVRLF
     LCSNHTPGDD LIFSEQKIKS AWNFLNKLWN VTKFVIQLEN DQEISYDLDK LSLSETWILA
     KLDKVIQKIT KLLDKFQLAL ANQILVKFVW DDFCNTFIEA IKKEPNQLKP QLFYTAKSVL
     SNIAILLSIT VPFLSERIYQ QFNNKSVMQA TWPLATKIKI PKLFDLVLAA INDLRNYRKQ
     YMLNSQQKLV VILSGKNAVD VKQYFNFSWI ELKIETNKKV SFKYQIVDDT TQRLKSLQKQ
     QAFFESEVKR SQAIVKNKSF LEKAPKEKVK SEFLKLEEYQ KKLTETNQLI AKLTKAH
//