ID D1AYY1_SULD5 Unreviewed; 605 AA.
AC D1AYY1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=Sdel_0081 {ECO:0000313|EMBL:ACZ11119.1};
OS Sulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=525898 {ECO:0000313|EMBL:ACZ11119.1, ECO:0000313|Proteomes:UP000002222};
RN [1] {ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Munk A.C., Lu M., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Aumann P., Schneider S., Lang E.,
RA Spring S., Klenk H.P., Eisen J.A.;
RT "The complete genome of Sulfurospirillum deleyianum DSM 6946.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ11119.1, ECO:0000313|Proteomes:UP000002222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51133 / DSM 6946 / 5175
RC {ECO:0000313|Proteomes:UP000002222};
RX PubMed=21304697; DOI=10.4056/sigs.671209;
RA Sikorski J., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., Goodwin L.,
RA Pitluck S., Ovchinnikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Detter J.C., Han C., Rohde M., Lang E., Spring S., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Sulfurospirillum deleyianum type strain
RT (5175).";
RL Stand. Genomic Sci. 2:149-157(2010).
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; CP001816; ACZ11119.1; -; Genomic_DNA.
DR AlphaFoldDB; D1AYY1; -.
DR STRING; 525898.Sdel_0081; -.
DR KEGG; sdl:Sdel_0081; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_7; -.
DR Proteomes; UP000002222; 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; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 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; 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; 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; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 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}; Cytoplasm {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:UP000002222};
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 237..502
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 211..502
FT /note="Catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00184"
SQ SEQUENCE 605 AA; 69272 MW; 11FBC44DA62FAA0F CRC64;
MMNDVIAYKE GSTLIDTQTA LASSKTYEDK ILFNNSKDAL EVIRHSCAHL MAQAIKALYK
DAQFFVGPVI EDGFYYDFRV NEKIGDADLK EIEKKMAELA NAKLPIEKIY TTKAEALKHF
AHDDLKQEVM LRIPDGEVSI YKQGDFEDLC RGPHVPNTKY LRFFKLIKVA GAYLGGDEKR
EMLTRIYGIA FADKESLKDY VTMIEEAKKR DHRKIGNELK LFTFDDEVGA GLPIWLPQGG
KLRAKLEKLL FTAHRKRGYQ PVRGPEILKS DAWKISGHYQ NYGENMYFTV IDEAEYGIKP
MNCLGHIKVF QSEVRSYRDL PLKFFEYGVV HRHEKSGVLH GLFRVREFTQ DDAHIFCTPD
QIKENVLEIL SFVDSIMKTF GFHYEMEIST RPEKSIGDER YWEAATQGLK NALDENGITY
GIDEGGGAFY GPKIDIKITD ALKRKWQCGT IQVDFNLPER FDISYVDANN EHARPVMLHR
AILGSFERFI GILIEHTSGE FPFFLAPTQV VIVPISDAHL EYAKSVANAL MAEEIDVEVS
SKNESLNKRI RNAETMRVPM ILVIGDAEVE NQSVAVRDRR ERTQYNLSKV ELIKTLKEKL
SEVHF
//
