SYV_PSEAE
ID SYV_PSEAE Reviewed; 950 AA.
AC Q9HXH0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PA3834;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG07221.1; -; Genomic_DNA.
DR PIR; G83167; G83167.
DR RefSeq; NP_252523.1; NC_002516.2.
DR RefSeq; WP_003113794.1; NZ_QZGE01000001.1.
DR PDB; 4XKZ; X-ray; 1.95 A; A=639-898.
DR PDBsum; 4XKZ; -.
DR AlphaFoldDB; Q9HXH0; -.
DR SMR; Q9HXH0; -.
DR STRING; 287.DR97_4032; -.
DR PaxDb; Q9HXH0; -.
DR PRIDE; Q9HXH0; -.
DR EnsemblBacteria; AAG07221; AAG07221; PA3834.
DR GeneID; 879905; -.
DR KEGG; pae:PA3834; -.
DR PATRIC; fig|208964.12.peg.4014; -.
DR PseudoCAP; PA3834; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR InParanoid; Q9HXH0; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q9HXH0; -.
DR BioCyc; PAER208964:G1FZ6-3906-MON; -.
DR Proteomes; UP000002438; 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; -; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil;
KW Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..950
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224535"
FT COILED 881..950
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"
FT HELIX 639..653
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 669..690
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 694..707
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 708..712
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 713..716
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 728..749
FT /evidence="ECO:0007829|PDB:4XKZ"
FT TURN 750..752
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 754..768
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 785..787
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 790..812
FT /evidence="ECO:0007829|PDB:4XKZ"
FT STRAND 821..827
FT /evidence="ECO:0007829|PDB:4XKZ"
FT HELIX 830..846
FT /evidence="ECO:0007829|PDB:4XKZ"
FT STRAND 849..854
FT /evidence="ECO:0007829|PDB:4XKZ"
FT STRAND 863..869
FT /evidence="ECO:0007829|PDB:4XKZ"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:4XKZ"
SQ SEQUENCE 950 AA; 107708 MW; 54992BE3655F5078 CRC64;
MDKTYQPHAI ETSWYETWES NDYFAPSGEG QPYTIMIPPP NVTGSLHMGH GFNNAIMDAL
IRYRRMQGRN TLWQPGTDHA GIATQMVVER QLGAQGVSRH DLGREKFLEK VWEWKEQSGG
NITRQIRRLG SSVDWSRERF TMDDGLSEAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
SDLEVENHDE KGHLWHLRYP LVNGAKTSEG LDYLVVATTR PETLLGDAAV AVHPEDERYA
KLIGQFAELP IVGRHIPIIA DEYVDREFGT GCVKITPAHD FNDYEVGKRH DLPLINIFDK
NAAVLAQAQV FHLDGSVNPN LDPSLPQSYA GMDRFAARKA IVAEFEAMGL LEKVDDHALK
VPKGDRSGTV IEPWLTDQWY VSTKPLAEDA IAAVEDGRIQ FVPKQYENMY FSWMRDIQDW
CISRQLWWGH RIPAWYDEAG NVYVGRDEVE VRTKHKLGNE AELRQDEDVL DTWFSSGLWT
FSTLGWPQQT EFLKTFHPTD VLVTGFDIIF FWVARMIMLT MHLVKNPDGT PQIPFKTVYV
HGLVRDGQGQ KMSKSKGNVL DPLDIVDGID LDTLLQKRTS GMMQPKLAEK IAKQTRAEFP
EGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGFRNFCN KIWNAANFVI ENTDGQDTGV
NGEPVELSSV DRWIISQLQR TEQEVTRQLD AFRFDLAAQA LYEFIWDEYC AWYLELVKPV
LWDENAPIER QRGTRRTLIR VLETALRLAH PFMPFITEEI WQRIKGQAGK EGPTLMLQPW
PVADEGRIDA AAEGDIEWVK ALMLGVRQIR GEMNISMAKR IDIILKNASP SDHRRLADNE
PLLMKLAKLE SIRVLEAGEE APMSATALVG DMEVLVPMAG LIDKSAELGR LDKEIQRLEG
EVKRVGGKLS NEGFVAKAPA DVIEKERAKL AEAEQALAKL AEQRQKIAAL
