SYT_FLAJ1
ID SYT_FLAJ1 Reviewed; 648 AA.
AC A5FP01;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=Fjoh_0024;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC Rule:MF_00184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; CP000685; ABQ03062.1; -; Genomic_DNA.
DR RefSeq; WP_011921543.1; NZ_MUGZ01000005.1.
DR AlphaFoldDB; A5FP01; -.
DR SMR; A5FP01; -.
DR STRING; 376686.Fjoh_0024; -.
DR PRIDE; A5FP01; -.
DR EnsemblBacteria; ABQ03062; ABQ03062; Fjoh_0024.
DR KEGG; fjo:Fjoh_0024; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_10; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 900765at2; -.
DR Proteomes; UP000006694; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..648
FT /note="Threonine--tRNA ligase"
FT /id="PRO_1000077358"
FT DOMAIN 1..61
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 240..539
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 648 AA; 74040 MW; 9C1DC457BEC41BF2 CRC64;
MIKITLPDGS IREFAQGVTP MEVAKNISEG FARNVISASF NGTTIETETP LTTDGNLILY
TWNDAEGKKA FWHSTSHVMA QALEELYPGI KLTLGPAIAN GFYYDVDFED QKISEADFKK
IEDRILEIAR GKFDFKMRPV TKAEALEMYK DNVYKTELIS NLEDGTITFC DHATFTDLCR
GGHIPNTGII KAVKIMSVAG AYWRGDEKNK QLTRVYGTSF PKQKDLTEYL ELLEEAKRRD
HRKLGKELEL FAFSQKVGQG LPLWLPKGAA LRDRLEQFLK RAQKKAGYEQ VVSPHIGQKE
LYVTSGHYAK YGADSFQPIH TPAEGEEFLL KPMNCPHHCE IYNVRPWSYK DLPKRYAEFG
TVYRYEQSGE LHGLTRVRGF TQDDAHIFCT PEQLDEEFKK VIDLVLYVFG SLGFENFTAQ
ISLRDQEDRE KYIGTDENWE KAENAIINAA KDKGLNTVVE YGEAAFYGPK LDFMVKDALG
RQWQLGTIQV DYNLPERFEL TYKGADNELH RPVMIHRAPF GSMERFIAIL LEHTAGNFPL
WLMPEQAIIL SLSEKYENYA KKVLDLLENH EIRALIDNRN ETIGKKIRDA EMQKIPFMLI
VGEEEEKNGT ISIRRHGQEG KGNITVSIEE FASIVDEEIK KTLKVFTV
