ID SYV_GLUOX Reviewed; 888 AA.
AC Q5FN28;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=GOX2489;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW62219.1; -; Genomic_DNA.
DR RefSeq; WP_011253986.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FN28; -.
DR SMR; Q5FN28; -.
DR STRING; 290633.GOX2489; -.
DR KEGG; gox:GOX2489; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR Proteomes; UP000006375; 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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
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 Pfam; PF10458; Val_tRNA-synt_C; 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..888
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224484"
FT COILED 821..888
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 538..542
FT /note="'KMSKS' region"
FT BINDING 541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 888 AA; 100683 MW; 3254DC17DC49362D CRC64;
MLEKSFVPAD HENALYDAWE KSGAFRAHPD QPGEPFSIMF PPPNVTGTLH LGHSLNFVLQ
DMLIRWKRQE GFNVLWQPGT DHAGIATQMV VERALDKEGT SRTALGREGF LERVWDWKQE
YGGTIVKQLR KLGASADWER ERFTMDDGLS RAVRKVFVTL YNEGLIYRDR RLVNWDPKFR
SAISDLEVEN HETKGSMWYI RYPLEDGRTI TVATTRPETM LGDVAVAVHP EDERYADMIG
KTVILPLTGR RIPVVADLHS DPEKGTGAVK ITPAHDFNDF EVGKRHDLPA PTVLDETACL
WIEEIRPELR DVEGLASVAF VETLNGLSRE EGRKQVVAEL ERLEWLEKIE PHKLQVPHAE
RGGAIVEPRL TLQWYCDAKT LSGPAVEAVE SGKIAFEPRQ WENTFHAWMR DIQPWCISRQ
LWWGHRIPAW YGADGKVYVA ENEQDAQVQA GEGVSLTQDE DVLDTWFSSA LWPFTTLGWP
DRTEELARYY PTSVLVTGFD IIFFWVARMM MMGLHFMDDV PFRTVLIHGL VRDEKGQKMS
KSKGNGLDPL DLVAEFGADA TRLAICAGTG PGRDIKLGRK RVEEHRAFVT KLWNAARFLE
MNGAKPTEDF DPASVKSALG RWILTEANDA ITEAGRALSV YRFDEYASCC YRFVWSRFCD
WFVEFSKPVF AAENEETAEL RAVSAHVLGL ILRLMQPVIP FVTATLWQEL GYPGKFEEIR
WPEIMTVTRA DEARAELDWV IRLIGDVRTV RSEMNIPPSQ KAPLLLRDAA PENLERAKTW
AEAIGRMARV SDVGVVGEDA PRNAAQLVLD EATVFIPLEG LIDLDAERAR LAKEITRIEG
EILKVTRKLD NADFVARAKP EVVEENHDRL ATFQSDLERL KAALGRLA
//
