SYT_STRMK
ID SYT_STRMK Reviewed; 633 AA.
AC B2FN79;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Smlt3378;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM743169; CAQ46806.1; -; Genomic_DNA.
DR RefSeq; WP_005414065.1; NC_010943.1.
DR PDB; 6VU9; X-ray; 2.20 A; A=1-633.
DR PDBsum; 6VU9; -.
DR AlphaFoldDB; B2FN79; -.
DR SMR; B2FN79; -.
DR STRING; 522373.Smlt3378; -.
DR PRIDE; B2FN79; -.
DR EnsemblBacteria; CAQ46806; CAQ46806; Smlt3378.
DR KEGG; sml:Smlt3378; -.
DR PATRIC; fig|522373.3.peg.3167; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_6; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 900765at2; -.
DR Proteomes; UP000008840; 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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..633
FT /note="Threonine--tRNA ligase"
FT /id="PRO_1000098617"
FT DOMAIN 1..61
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 243..534
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 65..86
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 268..287
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:6VU9"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:6VU9"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 377..388
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 393..410
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 431..447
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 477..488
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 508..515
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:6VU9"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:6VU9"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 552..564
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 598..603
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 605..612
FT /evidence="ECO:0007829|PDB:6VU9"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:6VU9"
FT HELIX 621..630
FT /evidence="ECO:0007829|PDB:6VU9"
SQ SEQUENCE 633 AA; 71912 MW; 87AD2FE47F7DBAEC CRC64;
MINITLPDGS RREFENPVSV MEVAQSIGAG LAKATIAGAV DGVLVDASDV IDHDASLRII
TAKDEEGVEI IRHSCAHLVG HAVKQLYPDV KMVIGPVIAE GFYYDIYSER PFTPDDMAAI
EKRMGELIAQ DYDVIKKMTP RAEVIEIFKA RGEDYKLRLI EDMSEDIQAM GMYYHQEYVD
MCRGPHVPNT RFLKAFKLTR ISGAYWRGDA QNEQLQRIYG TAWADKKQLE AYIKRIEEAE
MRDHRRIGKQ QDLFHLQEEA PGLVFWHPKG WALWQVVEQY MRKVYRNSGY GEVRCPQILD
VSLWKKSGHW DNYQDNMFFT ESEKRTYAVK PMNCPGHIQV FNQGLHSYRD LPIRYGEFGS
CHRNEPSGAL HGILRVRGFT QDDGHVFCTE NQIESEVTAF HQQALAVYQH FGFDEIQIKI
ALRPESRLGD DATWDKAEGA LRSALTACGV EWQELPGEGA FYGPKIEYHL KDAIGRTWQL
GTMQVDFMMP GRLGAEYVDE NSQKKHPVML HRAIVGSMER FLGILIEHHA GQFPAWLAPT
QVVVANITDA QADYVSGVTK TLAEQGFRVS SDLRNEKIGY KIREHTLQRV PYLLVIGDRE
KENGAVAVRT RSGEDLGSMS LQAFIERLHA EGA
