ID A0A0P0GJ87_9BACE Unreviewed; 646 AA.
AC A0A0P0GJ87;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ECO:0000313|EMBL:ALJ58138.1};
GN ORFNames=BcellWH2_00876 {ECO:0000313|EMBL:ALJ58138.1}, DWW88_21785
GN {ECO:0000313|EMBL:RGU21994.1}, DWX97_21375
GN {ECO:0000313|EMBL:RGS33717.1}, F2Y70_14775
GN {ECO:0000313|EMBL:KAA5425270.1}, F2Y81_15765
GN {ECO:0000313|EMBL:KAA5416607.1}, F2Y86_27285
GN {ECO:0000313|EMBL:KAA5401783.1}, F2Y87_24030
GN {ECO:0000313|EMBL:KAA5414396.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:ALJ58138.1, ECO:0000313|Proteomes:UP000061809};
RN [1] {ECO:0000313|EMBL:ALJ58138.1, ECO:0000313|Proteomes:UP000061809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH2 {ECO:0000313|EMBL:ALJ58138.1,
RC ECO:0000313|Proteomes:UP000061809};
RX PubMed=26430127;
RA Wu M., McNulty N.P., Rodionov D.A., Khoroshkin M.S., Griffin N.W.,
RA Cheng J., Latreille P., Kerstetter R.A., Terrapon N., Henrissat B.,
RA Osterman A.L., Gordon J.I.;
RT "Genetic determinants of in vivo fitness and diet responsiveness in
RT multiple human gut Bacteroides.";
RL Science 350:AAC5992-AAC5992(2015).
RN [2] {ECO:0000313|Proteomes:UP000283341, ECO:0000313|Proteomes:UP000285677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF17-25 {ECO:0000313|EMBL:RGU21994.1,
RC ECO:0000313|Proteomes:UP000285677}, and AF22-3AC
RC {ECO:0000313|EMBL:RGS33717.1, ECO:0000313|Proteomes:UP000283341};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000325055, ECO:0000313|Proteomes:UP000448877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A3 {ECO:0000313|EMBL:KAA5425270.1,
RC ECO:0000313|Proteomes:UP000475645}, BIOML-A6
RC {ECO:0000313|EMBL:KAA5416607.1, ECO:0000313|Proteomes:UP000448877},
RC BIOML-A7 {ECO:0000313|EMBL:KAA5401783.1,
RC ECO:0000313|Proteomes:UP000325055}, and BIOML-A8
RC {ECO:0000313|EMBL:KAA5414396.1, ECO:0000313|Proteomes:UP000482653};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00184}.
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DR EMBL; CP012801; ALJ58138.1; -; Genomic_DNA.
DR EMBL; VVYW01000049; KAA5401783.1; -; Genomic_DNA.
DR EMBL; VVYX01000039; KAA5414396.1; -; Genomic_DNA.
DR EMBL; VVYV01000026; KAA5416607.1; -; Genomic_DNA.
DR EMBL; VVYT01000044; KAA5425270.1; -; Genomic_DNA.
DR EMBL; QRVJ01000027; RGS33717.1; -; Genomic_DNA.
DR EMBL; QRXS01000016; RGU21994.1; -; Genomic_DNA.
DR RefSeq; WP_007217788.1; NZ_VVYX01000039.1.
DR AlphaFoldDB; A0A0P0GJ87; -.
DR STRING; 246787.BcellWH2_00876; -.
DR GeneID; 66307788; -.
DR KEGG; bcel:BcellWH2_00876; -.
DR PATRIC; fig|246787.4.peg.905; -.
DR eggNOG; COG0441; Bacteria.
DR Proteomes; UP000061809; Chromosome.
DR Proteomes; UP000283341; Unassembled WGS sequence.
DR Proteomes; UP000285677; Unassembled WGS sequence.
DR Proteomes; UP000325055; Unassembled WGS sequence.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR Proteomes; UP000475645; Unassembled WGS sequence.
DR Proteomes; UP000482653; Unassembled WGS sequence.
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};
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..61
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 242..541
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ SEQUENCE 646 AA; 74512 MW; B861D86E94D6EED5 CRC64;
MIKITFPDGS VREYNEGVTG LQIAESISSR LAQEVLACGV NGEIYDLGRP INEDAEFVLY
KWEDEQGKHA FWHTSAHLLA EALQELYPGI QFGIGPAIEN GFYYDVDPGE AVIKESDLPA
IEAKMAELVA KKEAVVRESI SKTDALKKFG DRGENYKCEL ISELEDGRIT TYTQGAFTDL
CRGPHLMTTA PIKAIKLMSV AGAYWRGHED RKMMTRIYGI TFPKKKMLDE YLAMLEEAKK
RDHRKIGKEM DLFMFSDTVG KGLPMWLPKG TALRLRLQEF LRRIQARYDY QEVITPPIGN
KLLYITSGHY AKYGKDSFQP IHTPEEGEEY FLKPMNCPHH CMIYKNSPRS YKDLPLRLAE
FGTVCRYEQS GELHGLTRVR SFTQDDAHIF CRPDQVKDEF LRVMDIISIV FRSMDFANVE
AQISLRDKVN REKYIGSDEN WERAEQSIIE ACEEKGLSAR IEYGEAAFYG PKLDFMVKDA
IGRRWQLGTI QVDYNLPERF ELEYTGADNQ KHRPVMIHRA PFGSMERFVA VLIEHTAGKF
PLWLTPEQVA ILPISEKFND YAQEVKKFLK QYDIRAIVDE RNEKIGRKIR DNELKRIPYM
LIVGEKEAEN REVSVRKQGE GDKGTMKFEE FAKILNEEVQ NMINKW
//
