ID A0A077DC98_9BURK Unreviewed; 643 AA.
AC A0A077DC98;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000256|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000256|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000256|HAMAP-Rule:MF_00184};
GN ORFNames=IX83_03655 {ECO:0000313|EMBL:AIL32520.1};
OS Basilea psittacipulmonis DSM 24701.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Basilea.
OX NCBI_TaxID=1072685 {ECO:0000313|EMBL:AIL32520.1, ECO:0000313|Proteomes:UP000028945};
RN [1] {ECO:0000313|EMBL:AIL32520.1, ECO:0000313|Proteomes:UP000028945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24701 {ECO:0000313|EMBL:AIL32520.1,
RC ECO:0000313|Proteomes:UP000028945};
RX PubMed=24581117; DOI=10.1186/1471-2164-15-169;
RA Whiteson K.L., Hernandez D., Lazarevic V., Gaia N., Farinelli L.,
RA Francois P., Pilo P., Frey J., Schrenzel J.;
RT "A genomic perspective on a new bacterial genus and species from the
RT Alcaligenaceae family, Basilea psittacipulmonis.";
RL BMC Genomics 15:169-169(2014).
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:0000256|ARBA:ARBA00000070, ECO:0000256|HAMAP-
CC Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00184}.
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DR EMBL; CP009238; AIL32520.1; -; Genomic_DNA.
DR RefSeq; WP_038499258.1; NZ_CP009238.1.
DR AlphaFoldDB; A0A077DC98; -.
DR STRING; 1072685.IX83_03655; -.
DR KEGG; bpsi:IX83_03655; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_4; -.
DR OrthoDB; 9802304at2; -.
DR Proteomes; UP000028945; 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; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 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; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00184};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00184};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00184};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00184}; Reference proteome {ECO:0000313|Proteomes:UP000028945};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00184};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00184}.
FT DOMAIN 1..66
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 247..539
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 247..538
FT /note="Catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ SEQUENCE 643 AA; 73993 MW; 09876650EADF95B8 CRC64;
MIQITLPDGS KREYDKPVSV ADVAHDIAPS LAKVALAGKV VLTNQEEKLV DTSYLITEHV
KLSIITGKDP EGLDLIRHST AHLLAYAVKE LFPDAQVTIG PVIENGFYYD FSYKRPFTPE
DLQKIEKKMQ ELAKKNETVT REEWTRDEAV AFFLEQGEKY KAEIIASIPT NETISLYREG
NFIDLCRGPH VPSTGKLKVF KLMKVAGAYW RGDSKNEMLQ RIYGTAWATK EEQDHYLHML
EEAEKRDHRK LGRELDLFHM QEEAPGLVFW HPRGWTMWQQ IESYIRRVYV ENGYQEVRSP
QIMDISLWKR TGHWDNYKEN MFTTESENRL YGLKPMNCPG HIQIYNSNLH SYRELPIRYG
EFGACHRNEP SGSLHGIMRV RGFTQDDGHI FCTEDQLQEE CANFTKLLQK VYQDFGFTDI
LYKVATRPEH RIGEDSIWDK AESALMDSLR HGGYDFEISE GEGAFYGPKI EYTLKDALGR
HWQCGTLQVD FSMPVRLGAE YVDANDQRRI PVMLHRAILG SLERFLGMLI EHYAGAMPPW
LSPVQVAVCN ISDAQKEYVE EVVSKLKQQG IRVIADLRGE KITRKIREQS MQKIPYILVV
GDKEKEDGSV AVRARGNQDL GVMPLEKFIE CLQDNVKNLK TNV
//
