ID SYT_BURCM Reviewed; 635 AA. AC Q0BG06; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Threonyl-tRNA synthetase; DE EC=6.1.1.3; DE AltName: Full=Threonine--tRNA ligase; DE Short=ThrRS; GN Name=thrS; OrderedLocusNames=Bamb_1359; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000440; ABI86917.1; -; Genomic_DNA. DR RefSeq; YP_773251.1; -. DR GeneID; 4311276; -. DR GenomeReviews; CP000440_GR; Bamb_1359. DR KEGG; bam:Bamb_1359; -. DR NMPDR; fig|339670.3.peg.2188; -. DR OMA; Q0BG06; ELELFMF. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00184; -; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-reg. DR InterPro; IPR006195; aa-tRNA-synth_II_cons-reg. DR InterPro; IPR004154; Anticodon_bd. DR InterPro; IPR012675; b-grasp_ferredoxin-like. DR InterPro; IPR004095; TGS. DR InterPro; IPR002320; Thr-tRNA-synth_IIa. DR InterPro; IPR018158; Thr-tRNA-synth_IIa_cons-reg. DR InterPro; IPR012947; tRNA_SAD. DR Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1. DR Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 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 TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc. FT CHAIN 1 635 Threonyl-tRNA synthetase. FT /FTId=PRO_1000020351. FT REGION 242 533 Catalytic. FT METAL 333 333 Zinc; catalytic (By similarity). FT METAL 384 384 Zinc; catalytic (By similarity). FT METAL 510 510 Zinc; catalytic (By similarity). SQ SEQUENCE 635 AA; 72306 MW; 7C27EA357756C0EA CRC64; MVSIRLPDGS VRQYEHPVTV AEVAASIGPG LAKAALGGKL DGELVDTSTV IDRDAALAII TDKDADGLDI IRHSTAHLLA YAVKELYPDA QVTIGPVIDN GFYYDFSYNR PFTPEDLEKI EKRMQEIAKK DEPVTRRVVS RDEAAGYFRS IGEKYKAEII ESIPQTDEIK LYSHGGFTDL CRGPHVPSTG KLKVFKLMKV AGAYWRGDSK NEQLQRIYGT AWTKKEDQDQ YLHMLEEAEK RDHRKLGKQL DLFHMQEESP GMVFWHPKGW ALWQQVEQYM RRRVNDAGYL EIKTPMIMDR SLWEASGHWQ NYRENMFTTE SEKRDYAIKP MNCPGHVQVF KHGLRSYRDL PLRYAEFGSC HRNEASGALH GLMRVRGFVQ DDAHIFCTEE QFIAESIAFN TLAMSVYKDF GFEHIDIKLS LRPEQRAGTD ETWDRAEQGL RDALTACGLS WEELPGEGAF YGPKIEYHIK DALGRSWQCG TLQLDMVLPE RLGAEYVAED NSRRRPVMLH RAIVGSMERF LGILIEHHAG AMPAWLAPFQ AVVLNIAESQ VEYAHSLTQT LQKQGVRVAG DLRNEKISYK IREHTLEKVP YLLVVGDKER DAQTVAVRAR GGVDLGVMPI EAFVERLQED LRSFK //