SYV_BACTN
ID SYV_BACTN Reviewed; 879 AA.
AC Q89ZM4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=BT_4353;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO79458.1; -; Genomic_DNA.
DR RefSeq; NP_813264.1; NC_004663.1.
DR RefSeq; WP_011109217.1; NC_004663.1.
DR AlphaFoldDB; Q89ZM4; -.
DR SMR; Q89ZM4; -.
DR STRING; 226186.BT_4353; -.
DR PaxDb; Q89ZM4; -.
DR PRIDE; Q89ZM4; -.
DR EnsemblBacteria; AAO79458; AAO79458; BT_4353.
DR GeneID; 60925530; -.
DR KEGG; bth:BT_4353; -.
DR PATRIC; fig|226186.12.peg.4430; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_10; -.
DR InParanoid; Q89ZM4; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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..879
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224439"
FT COILED 807..878
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 534..538
FT /note="'KMSKS' region"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 879 AA; 99939 MW; 1D527CDE2914662B CRC64;
MELASKYNPA DVEGKWYQYW LEHRLFSSKP DGREPYTIVI PPPNVTGVLH MGHMLNNTIQ
DILVRRARME GKNACWVPGT DHASIATEAK VVNKLAAQGI KKTDLTRDEF LKHAWDWTEE
HGGIILKQLR KLGASCDWDR TAFTMDEERS KSVLKVFVDL YNKGLIYRGV RMVNWDPKAL
TALSDEEVIY KEEHGKLFYL RYKVEGDPEG RYAVVATTRP ETIMGDTAMC INPNDPKNAW
LKGKKVIVPL VNRVIPVIED DYVDIEFGTG CLKVTPAHDV NDYMLGEKYN LPSIDIFNDN
GTLSEAAGLY IGMDRFDVRK QIEKDLDAAG LLEKTEAYTN KVGYSERTNV VIEPKLSMQW
FLKMQHFADM ALPPVMNDEL KFYPAKYKNT YRHWMENIKD WCISRQLWWG HRIPAYFLPE
GGYVVAATPE EALAKAKEKT GNAALTMDDL RQDEDCLDTW FSSWLWPISL FDGINHPGNE
EISYYYPTSD LVTGPDIIFF WVARMIMVGY EYEGKMPFKN VYFTGIVRDK LGRKMSKSLG
NSPDPLELID KYGADGVRMG MMLAAPAGND ILFDDALCEQ GRNFCSKIWN AFRLIKGWTV
DDNIQASDAA KLAVHWFESK QNEVAAEVAD LFSKYRLSEA LMAVYKLFWD EFSSWYLEMI
KPAYGQGIDR TTYSATLCFL DNLLHLLHPF MPFITEELWQ QMYERNAEEG ESLMVSALSM
DTYVDTAFVA QFEVVKGVIS NIRSIRLQKN IAQKEPLDLQ VLGENPVAEF NAVIQKMCNL
SSITVVESKA EGASSFMVGT TEYAVPLGNM IDVEAEIARM EAELKHKEGF LQGVLKKLSN
EKFINNAPAA VLEMERKKQA DAESIISSLK ESIAALKKA
