SYY1_PSEAE
ID SYY1_PSEAE Reviewed; 412 AA.
AC Q9HWP3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Tyrosine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS 1 {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS1 {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=PA4138;
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 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:0000255|HAMAP-
CC Rule:MF_02006}.
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:0000255|HAMAP-Rule:MF_02006};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR EMBL; AE004091; AAG07525.1; -; Genomic_DNA.
DR PIR; A83129; A83129.
DR RefSeq; NP_252827.1; NC_002516.2.
DR RefSeq; WP_003113003.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWP3; -.
DR SMR; Q9HWP3; -.
DR STRING; 208964.PA4138; -.
DR PaxDb; Q9HWP3; -.
DR PRIDE; Q9HWP3; -.
DR EnsemblBacteria; AAG07525; AAG07525; PA4138.
DR GeneID; 880105; -.
DR KEGG; pae:PA4138; -.
DR PATRIC; fig|208964.12.peg.4336; -.
DR PseudoCAP; PA4138; -.
DR HOGENOM; CLU_024003_0_3_6; -.
DR InParanoid; Q9HWP3; -.
DR OMA; YHSSVQA; -.
DR PhylomeDB; Q9HWP3; -.
DR BioCyc; PAER208964:G1FZ6-4211-MON; -.
DR BRENDA; 6.1.1.1; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..412
FT /note="Tyrosine--tRNA ligase 1"
FT /id="PRO_0000234753"
FT DOMAIN 348..411
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 46..55
FT /note="'HIGH' region"
FT MOTIF 234..238
FT /note="'KMSKS' region"
FT BINDING 41
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 174
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 178
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ SEQUENCE 412 AA; 45177 MW; A3B49DAD41B7A980 CRC64;
MSVPTHQQDL IALLEERGFV HQCTDRDGLA AHLAAGPATA YLGFDATADS LHVGHLQGLM
LMRWLQKAGH RPLLLIGGAT TRIGDPSFRD SSRPILTEAQ IQANIDGIAR VFSRYVELHD
DSLVNNAEWL DGVGYLEFLD RVGRHFSINR LLTFDAIRQR LDREHSLSFL EFGYTLLQAY
DFVELSRRRG CTLQLGGADQ WANIINGVEL SRRQGGAQLF GLTMPLLATS DGRKMGKSAQ
GAVWLNAERL APFDFWQFWR NCDDRDVGRF LALFSELPMD EVRRLGALQG AELNEAKVVL
ANAATALAHG EHAARSAADA ARGVFADGTR DSGLPVMKLS RARLAQGLSL TDLLLEHAIQ
PSRSAVRRLA AGGGLRLDGT PVSDPDTPLA GEVDGLRLSL GKKQHLHLRL ED
