SYY_MYCTU
ID SYY_MYCTU Reviewed; 424 AA.
AC P9WFT1; L0TA47; O33191; P67611;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=Rv1689;
GN ORFNames=MTCI125.11;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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; AL123456; CCP44454.1; -; Genomic_DNA.
DR PIR; H70501; H70501.
DR RefSeq; NP_216205.1; NC_000962.3.
DR RefSeq; WP_003408375.1; NZ_NVQJ01000010.1.
DR PDB; 2JAN; X-ray; 2.90 A; A/B/C/D=1-424.
DR PDBsum; 2JAN; -.
DR AlphaFoldDB; P9WFT1; -.
DR SMR; P9WFT1; -.
DR STRING; 83332.Rv1689; -.
DR PaxDb; P9WFT1; -.
DR DNASU; 885668; -.
DR GeneID; 45425658; -.
DR GeneID; 885668; -.
DR KEGG; mtu:Rv1689; -.
DR PATRIC; fig|83332.111.peg.1876; -.
DR TubercuList; Rv1689; -.
DR eggNOG; COG0162; Bacteria.
DR OMA; YMMAKDS; -.
DR PhylomeDB; P9WFT1; -.
DR BRENDA; 6.1.1.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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_02006; Tyr_tRNA_synth_type1; 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; 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; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..424
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055660"
FT DOMAIN 356..413
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 41..50
FT /note="'HIGH' region"
FT MOTIF 231..235
FT /note="'KMSKS' region"
FT BINDING 36
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 171
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 175
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2JAN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 91..109
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 166..186
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2JAN"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 250..258
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 295..323
FT /evidence="ECO:0007829|PDB:2JAN"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 335..344
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:2JAN"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:2JAN"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:2JAN"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 407..415
FT /evidence="ECO:0007829|PDB:2JAN"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:2JAN"
SQ SEQUENCE 424 AA; 46330 MW; A8DAFEC1085CB491 CRC64;
MSGMILDELS WRGLIAQSTD LDTLAAEAQR GPMTVYAGFD PTAPSLHAGH LVPLLTLRRF
QRAGHRPIVL AGGATGMIGD PRDVGERSLN EADTVAEWTE RIRGQLERFV DFDDSPMGAI
VENNLEWTGS LSAIEFLRDI GKHFSVNVML ARDTIRRRLA GEGISYTEFS YLLLQANDYV
ELHRRHGCTL QIGGADQWGN IIAGVRLVRQ KLGATVHALT VPLVTAADGT KFGKSTGGGS
LWLDPQMTSP YAWYQYFVNT ADADVIRYLR WFTFLSADEL AELEQATAQR PQQRAAQRRL
ASELTVLVHG EAATAAVEHA SRALFGRGEL ARLDEATLAA ALRETTVAEL KPGSPDGIVD
LLVASGLSAS KGAARRTIHE GGVSVNNIRV DNEEWVPQSS DFLHGRWLVL RRGKRSIAGV
ERIG
