(data stored in ACNUC29543 zone)

SWISSPROT: TSAC_ACIBT

ID   TSAC_ACIBT              Reviewed;         189 AA.
AC   A3M154;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAY-2019, entry version 70.
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=A1S_0165;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O
CC         + L-threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:73682;
CC         EC=2.7.7.87; Evidence={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; CP000521; ABO10648.2; -; Genomic_DNA.
DR   EnsemblBacteria; ABO10648; ABO10648; A1S_0165.
DR   KEGG; acb:A1S_0165; -.
DR   HOGENOM; HOG000076163; -.
DR   KO; K07566; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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   PANTHER; PTHR17490:SF8; PTHR17490:SF8; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A3M154.
DR   SWISS-2DPAGE; A3M154.
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN         1    189       Threonylcarbamoyl-AMP synthase.
FT                                /FTId=PRO_0000352887.
FT   DOMAIN        3    189       YrdC-like. {ECO:0000255|HAMAP-
FT                                Rule:MF_01852}.
SQ   SEQUENCE   189 AA;  20786 MW;  8E8E42558601FCD1 CRC64;
     MITTSVTEAA ECLQQGQVLA YPTEAVWGLG CDPFNEQAFQ KILELKQRPI EKGVILLAGH
     ISQVEHLLTS LPQTTQQEII DCWTNHQPSE RATTWLLPAD QHIPSWIKGE HPLVAVRVTT
     HPLCVALCNA FHGFIVSTSA NPSGQEPAHS LQDACQYFGS QLNYLNGDLG QSQQPSRIIN
     ALTGEVIRP
//

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