(data stored in ACNUC7421 zone)

SWISSPROT: TSAC_PSEAB

ID   TSAC_PSEAB              Reviewed;         185 AA.
AC   Q02V59;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
GN   Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN;
GN   OrderedLocusNames=PA14_00240;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine. Catalyzes the conversion of L-threonine,
CC       HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as
CC       the acyladenylate intermediate, with the release of diphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L-
CC       threonylcarbamoyladenylate + diphosphate + H(2)O.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
DR   EMBL; CP000438; ABJ14978.1; -; Genomic_DNA.
DR   RefSeq; WP_003097300.1; NC_008463.1.
DR   ProteinModelPortal; Q02V59; -.
DR   EnsemblBacteria; ABJ14978; ABJ14978; PA14_00240.
DR   KEGG; pau:PA14_00240; -.
DR   HOGENOM; HOG000076163; -.
DR   KO; K07566; -.
DR   OMA; FGLGCNP; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR   Gene3D; 3.90.870.10; -; 1.
DR   HAMAP; MF_01852; TsaC; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR023535; TC-AMP_synthase.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02V59.
DR   SWISS-2DPAGE; Q02V59.
KW   ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding;
KW   Nucleotidyltransferase; Transferase; tRNA processing.
FT   CHAIN         1    185       Threonylcarbamoyl-AMP synthase.
FT                                /FTId=PRO_0000352950.
FT   DOMAIN        4    185       YrdC-like. {ECO:0000255|HAMAP-
FT                                Rule:MF_01852}.
SQ   SEQUENCE   185 AA;  20371 MW;  9DCCE860C2D7E979 CRC64;
     MISSFRAQCA ARVVREGGVI AYPTEAVWGL GCDPWNEDAV YRLLALKARP VEKGLIVVAA
     NIHQLDFLLE DLPDVWLDRL AGTWPGPNTW LVPHQERLPE WVTGVHDSVA VRVTDHPLVQ
     ELCHLTGPLI STSANPAGRP AARTRLRVEQ YFHDELDAIL GGALGGRRNP SLIRDLVTGQ
     VIRPA
//

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