ID   SYV_ZYMMO               Reviewed;         884 AA.
AC   Q5NLA8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 3.
DT   03-AUG-2022, entry version 113.
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=ZMO1878;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=19816441; DOI=10.1038/nbt1009-893;
RA   Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA   Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA   Chang Y.J., Samatova N.F., Brown S.D.;
RT   "Improved genome annotation for Zymomonas mobilis.";
RL   Nat. Biotechnol. 27:893-894(2009).
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=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); 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; AE008692; AAV90502.2; -; Genomic_DNA.
DR   RefSeq; WP_011241606.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q5NLA8; -.
DR   SMR; Q5NLA8; -.
DR   STRING; 264203.ZMO1878; -.
DR   EnsemblBacteria; AAV90502; AAV90502; ZMO1878.
DR   GeneID; 58027583; -.
DR   KEGG; zmo:ZMO1878; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 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..884
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224605"
FT   COILED          817..884
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           530..534
FT                   /note="'KMSKS' region"
FT   BINDING         533
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   884 AA;  100416 MW;  536C61ED3F543654 CRC64;
     MTIDKTFDPA AIESRWYTHW EEEGLFHPER PGADPFTLVI PPPNVTGSLH IGHALDDTLQ
     DILVRHARLK GKDALWVVGT DHAGIATQMV VERNLAKIGQ KRTDMDRETF VNKVWEWKAE
     SGGTITRQLR RLGASCDWAH ERFTMDEGFS KAVIKVFVSL YNEGLIYRDK RLVNWDPHLG
     TAISDLEVEN REVQGHFWHF RYPLEDGSGE IIVATTRPET MLADMAVAVN PEDDRYKALI
     GKNIRLPITN RLIPIIADIH ADPELGSGAV KITPGHDFND FEVGKRAGIK PADMLNMLDS
     HARVIQTAEN DVPEELIGLD RFEARQIIVE KIDALGLLDK IEDRVIQAPY GDRSGVPIEP
     WLTDQWYVDA EKLAQPALEA VRSGKIKIIP ESWTKTYYNW LENIQPWCIS RQLWWGHQIP
     VWYTDDGQAI VAENEESAQE KAGQGVNLRR DPDVLDTWFS SALWPFATLG WPDTDPKALG
     RYPNDVLISG FDILFFWDAR MIMQGLHFMK DVPFPKLYLH GLVRAADGSK MSKSKGNTVD
     PLGLIDKYGA DALRFTLCAM ESQGRDIKLD EKRVEGYRNF ATKLWNAVRF AQNNNCAVNT
     SKQPPEATLT TNRWIIAETA KVARALDQHI EDMRYDELAN SLYHFVWNDF CDWYLELIKP
     ILTSTEDQNQ GELQETLAVL GWVIDQILIM LHPIMPFITE ELWHALGDRD HDLIVAAWPD
     YKNWSVDETA QNDIDWLIRL ITAIRATRSE LNVPPALKVP LHSHGIPEKA AHNLERFDPF
     IKRLARIESI HKEAAPKGAA AQIVVDEATF VLPLEGVIDL DAERGRLKKA IEAVEKEKTA
     TEKRLGNPNF VARAKAEVVA ENRERLNNFT GEITKLKAAL ERLM