ID A0A1W6L569_9BURK Unreviewed; 422 AA.
AC A0A1W6L569;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000256|HAMAP-Rule:MF_02007};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02007};
DE Short=TyrRS {ECO:0000256|HAMAP-Rule:MF_02007};
GN Name=tyrS {ECO:0000256|HAMAP-Rule:MF_02007,
GN ECO:0000313|EMBL:GLS93093.1};
GN ORFNames=A4W93_04820 {ECO:0000313|EMBL:ARN19288.1}, GCM10007918_03840
GN {ECO:0000313|EMBL:GLS93093.1};
OS Piscinibacter gummiphilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=946333 {ECO:0000313|EMBL:ARN19288.1, ECO:0000313|Proteomes:UP000193427};
RN [1] {ECO:0000313|EMBL:ARN19288.1, ECO:0000313|Proteomes:UP000193427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS21 {ECO:0000313|EMBL:ARN19288.1,
RC ECO:0000313|Proteomes:UP000193427};
RA Tabata M., Kasai D., Fukuda M.;
RT "Complete genome sequence of natural rubber-degrading, novel Gram-negative
RT bacterium, Rhizobacter gummiphilus strain NS21.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GLS93093.1, ECO:0000313|Proteomes:UP001157201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS93093.1,
RC ECO:0000313|Proteomes:UP001157201};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLS93093.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109400 {ECO:0000313|EMBL:GLS93093.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Rhizobacter gummiphilus strain NBRC 109400.";
RL Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). {ECO:0000256|HAMAP-
CC Rule:MF_02007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000069, ECO:0000256|HAMAP-
CC Rule:MF_02007};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02007}.
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DR EMBL; CP015118; ARN19288.1; -; Genomic_DNA.
DR EMBL; BSPR01000002; GLS93093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6L569; -.
DR STRING; 946333.A4W93_04820; -.
DR KEGG; rgu:A4W93_04820; -.
DR OrthoDB; 9804243at2; -.
DR Proteomes; UP000193427; Chromosome.
DR Proteomes; UP001157201; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024108; Tyr-tRNA-ligase_bac_2.
DR NCBIfam; TIGR00234; tyrS; 1.
DR PANTHER; PTHR11766:SF1; TYROSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11766; TYROSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02007};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02007};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02007};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02007}; Reference proteome {ECO:0000313|Proteomes:UP000193427};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT MOTIF 68..77
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT MOTIF 252..256
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02007"
SQ SEQUENCE 422 AA; 45839 MW; EDD9C1E2E9307007 CRC64;
MPASEISATA VNDTAAADKF PVTDRVRQAL DVTRRGVDEL LPESEWTTKL ARSEATGVPL
RIKLGLDPTA PDIHLGHTVV LNKMRQLQDL GHQVIFLIGD FTSTIGDPSG RNTTRPPLSR
EQIEANATTY LNQANLVLDP GRTEVRYNSE WCDALGARGM IQLASRYTVA RMMERDDFTK
RFKAGTPISV HEFLYPLMQG YDSVALKADL ELGGTDQKFN LLVGRALQSE YGQEPQCVLT
MPLLEGLDGV EKMSKSKGNY IGITEPANTM FAKLLSISDV MMWRYFTLLS FLSEAEIAKL
KAEVEGGRNP KDAKVLLAKE ITTRFHSAAA ADAAEADFNN RSKGGIPDEI PEVSLTGAPL
GIGALLRSAN LAASSSEGLR LIDGGGVRVD SVVISDKGLK LEAGTYVVQV GRRKFARVTL
TA
//
