ID   SYV_PSEPK               Reviewed;         948 AA.
AC   Q88P76;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PP_0977;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN66602.1; -; Genomic_DNA.
DR   RefSeq; NP_743138.1; NC_002947.4.
DR   RefSeq; WP_010952166.1; NC_002947.4.
DR   AlphaFoldDB; Q88P76; -.
DR   SMR; Q88P76; -.
DR   STRING; 160488.PP_0977; -.
DR   PRIDE; Q88P76; -.
DR   EnsemblBacteria; AAN66602; AAN66602; PP_0977.
DR   KEGG; ppu:PP_0977; -.
DR   PATRIC; fig|160488.4.peg.1038; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   PhylomeDB; Q88P76; -.
DR   BioCyc; PPUT160488:G1G01-1050-MON; -.
DR   Proteomes; UP000000556; 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; -; 2.
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..948
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224537"
FT   COILED          877..947
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           551..555
FT                   /note="'KMSKS' region"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   948 AA;  107496 MW;  B84AF923EA39306B CRC64;
     MDKTYQPHAI ETSWYNTWES ENYFAPQGAG ESYTIMIPPP NVTGSLHMGH GFNNAIMDAL
     IRFRRMQGRD TLWQPGTDHA GIATQMLVER QLEAKGQNRH DLGREKFLEK VWEWKDQSGG
     NISRQIRRLG SSVDWSRERF TMDDGLSEAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
     SDLEVENHDE KGHLWNLRYP LADGAKTAEG QDYLVVATTR PETLLGDAAV AVNPNDERYQ
     ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
     NAFVLSSAQA FNLDGSVNEQ VDTQLPAQYA NLDRFVARKQ IVADLDAQGL LVSIDDHALK
     VPKGDRSGTV IEPWLTDQWY VSTKPLAEPA IAAVEDGRIQ FVPKQYENMY FSWMRDIQDW
     CISRQLWWGH RIPAWYDEAG QVYVGRNEEE VRAKHKLGAD VVLRQDDDVL DTWFSSGLWT
     FSTLGWPEQT EFLKKFHSTD VLVTGFDIIF FWVARMIMLT MHLIKNEDGT PQVPFKTVYV
     HGLVRDGQGQ KMSKSKGNVL DPLDIVDGIT LDALLEKRTS GMMQPKLAEK IAKQTKAEFP
     EGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGYRNFCN KIWNAARYVL DKGEDCGQNG
     EAYELSLADR WIISQLQRTE AEVTRQLEQF RFDLASQALY EFIWNQYCDW YLELSKPVLW
     DENAPVERAR GTRRTLVRVL EVALRLAHPF MPFITEEIWQ RIAPLAGIDG KTIMLQPWPV
     ANEARIDAAA EGDIEWLKEL MVGLRNIRAE MNIGPGKPLP LFLKNANADD QRRLQENEAL
     LKKLAKVESF TVLGDADEAP LSATALVGDL QVLVPMAGLI DKDAELARLN KEIQRLQGEV
     QRVGGKLSNT AFVDKAPPAV IEKERAKLAE SEQALANFTE QHARIAAL