SYY_ACIFR
ID SYY_ACIFR Reviewed; 407 AA.
AC P41256;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02007};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02007, ECO:0000269|PubMed:11240138, ECO:0000269|PubMed:7517395};
DE AltName: Full=TyrRZ {ECO:0000303|PubMed:7517395};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02007, ECO:0000303|PubMed:7517395};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02007, ECO:0000303|PubMed:7517395};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02007};
GN Synonyms=tyrZ {ECO:0000303|PubMed:7517395};
OS Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=920;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=Torma;
RX PubMed=7517395; DOI=10.1128/jb.176.14.4409-4415.1994;
RA Salazar O., Sagredo B., Jedlicki E., Soell D., Weygand-Durasevic I.,
RA Orellana O.;
RT "Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in
RT Escherichia coli.";
RL J. Bacteriol. 176:4409-4415(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP HIS-53; HIS-306; SER-356 AND LYS-395, AND SUBUNIT.
RX PubMed=11240138; DOI=10.1016/s0014-5793(01)02214-1;
RA Salazar J.C., Zuniga R., Lefimil C., Soell D., Orellana O.;
RT "Conserved amino acids near the carboxy terminus of bacterial tyrosyl-tRNA
RT synthetase are involved in tRNA and Tyr-AMP binding.";
RL FEBS Lett. 491:257-260(2001).
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_02007, ECO:0000269|PubMed:11240138}.
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_02007,
CC ECO:0000269|PubMed:11240138, ECO:0000269|PubMed:7517395};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for ATP {ECO:0000269|PubMed:11240138};
CC KM=26.8 uM for tyrosine {ECO:0000269|PubMed:11240138};
CC KM=2.54 uM for tRNA(Tyr) {ECO:0000269|PubMed:11240138};
CC Note=kcat is 7.7 sec(-1). {ECO:0000269|PubMed:11240138};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02007,
CC ECO:0000269|PubMed:11240138}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02007}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02007, ECO:0000305}.
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DR EMBL; X79010; CAA55643.1; -; Genomic_DNA.
DR PIR; A55515; A55515.
DR AlphaFoldDB; P41256; -.
DR SMR; P41256; -.
DR STRING; 380394.Lferr_2686; -.
DR PRIDE; P41256; -.
DR SABIO-RK; P41256; -.
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; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02007; Tyr_tRNA_synth_type2; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002942; S4_RNA-bd.
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 PANTHER; PTHR11766; PTHR11766; 1.
DR PANTHER; PTHR11766:SF1; PTHR11766:SF1; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT CHAIN 1..407
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055666"
FT DOMAIN 342..403
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 47..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MOTIF 231..235
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02007"
FT MUTAGEN 53
FT /note="H->A: Does not complement the tyrS mutation in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:11240138"
FT MUTAGEN 306
FT /note="H->A: Does not complement the tyrS mutation in
FT E.coli. 3-fold decrease in kcat for amino acid activation,
FT without effect on Km for tyrosine or ATP."
FT /evidence="ECO:0000269|PubMed:11240138"
FT MUTAGEN 306
FT /note="H->D: Does not complement the tyrS mutation in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:11240138"
FT MUTAGEN 356
FT /note="S->A: Does not complement the tyrS mutation in
FT E.coli. 7-fold increase in Km for E.coli tRNA, without
FT effect on other kinetic parameters."
FT /evidence="ECO:0000269|PubMed:11240138"
FT MUTAGEN 395
FT /note="K->N: Complements the tyrS mutation in E. coli very
FT poorly. 17-fold increase in Km for E.coli tRNA, without
FT effect on Km for ATP or tyrosine."
FT /evidence="ECO:0000269|PubMed:11240138"
SQ SEQUENCE 407 AA; 45860 MW; 7B73FBA2252A2C6B CRC64;
MTMKHQDAFE QIAFGTVDML PEGEMLARLA AAQRDNRPLR IKLGMDPTAP DLHLGAYVLL
HKARQFQDLG HRLLFVIGDF TAMIGDPTGK SVTRKALSRE EVVANAATYR PQVFKILDPE
RTEVMFNSEW LGALRPEELI QIAACYTVAR MLERDDFNKR YSANQPIAIH EFLYPLLQGY
DSVAIKADVE LGGTDQRFNL LVGRELQREY GQKPQLVLTM PILEGLDGVQ KMSKSLGNFI
AVEDPPAEMF GKIMSISDFL MWRYYALLSR VPAVEQTRLQ KEAASGARNP RDIKLDLAGE
LVRRFHGTAA AQEAHIAFLA RFQRHETPED LPLQAIKLSE APRLSQLLVQ VHLAASTSEA
MRKMKEGAVR VDWRRVVDPA TILALDAVYL LQFGKRHFAR VALQKGE
