ID V9UUT5_9PSED Unreviewed; 948 AA.
AC V9UUT5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN ORFNames=X970_03230 {ECO:0000313|EMBL:AHC86456.1};
OS Pseudomonas monteilii SB3101.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC86456.1, ECO:0000313|Proteomes:UP000018660};
RN [1] {ECO:0000313|EMBL:AHC86456.1, ECO:0000313|Proteomes:UP000018660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3101 {ECO:0000313|EMBL:AHC86456.1,
RC ECO:0000313|Proteomes:UP000018660};
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA Nielsen J.L.;
RT "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP006979; AHC86456.1; -; Genomic_DNA.
DR RefSeq; WP_013971095.1; NC_023076.1.
DR AlphaFoldDB; V9UUT5; -.
DR KEGG; pmot:X970_03230; -.
DR PATRIC; fig|1435058.3.peg.629; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR Proteomes; UP000018660; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}.
FT DOMAIN 14..628
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 669..821
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 883..944
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 879..941
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 551..555
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 948 AA; 107437 MW; B74ECE03440E7C7B CRC64;
MDKTYQPHAI ETSWYNTWES ENYFAPQGAG ESYTIMIPPP NVTGSLHMGH GFNNAIMDAL
IRFRRMQGRD TLWQPGTDHA GIATQMLVER QLEAKGQNRH DLGREKFLEK VWEWKDQSGG
NISRQIRRLG SSVDWSRERF TMDDGLSEAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
SDLEVENHDE KGHLWNLRYP LADGAKTAEG KDYLVVATTR PETLLGDAAV AVNPNDERYQ
ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
NAFVLASAQA FNLDGSVNEQ VDTRLPAQYA NLDRFVARKQ IVADLDAQGL LVSIDDHALK
VPKGDRSGTV IEPWLTDQWY VSTKPLAEPA IAAVEDGRIQ FVPKQYENMY FSWMRDIQDW
CISRQLWWGH RIPAWYDEAG QVYVGRNEEE VRAKHNLGAD 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 RIAPLAGIEG KTIMLQPWPV
ANESRIDAAA EGDIEWLKEL MVGLRNIRAE MNIGPGKPLP LFLKNANADD QRRLQENEAL
LKKLAKVESF TVLGDADEAP LSATALVGDL QVLVPMAGLI DKDAELARLN KEIQRLQGEV
ARVGGKLSNA AFVDKAPPAV IEKERAKLAE SEQALANFTE QHARIAAL
//
