ID TSAC_PSYIN Reviewed; 191 AA.
AC A1SR31;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Ping_0072;
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17664 / CCUG 51855 / 37;
RX PubMed=18460197; DOI=10.1186/1471-2164-9-210;
RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J.,
RA Land M.L., Thompson L.S.;
RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii.";
RL BMC Genomics 9:210-210(2008).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2)
CC and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate
CC intermediate, with the release of diphosphate. {ECO:0000255|HAMAP-
CC Rule:MF_01852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC 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}.
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DR EMBL; CP000510; ABM01946.1; -; Genomic_DNA.
DR AlphaFoldDB; A1SR31; -.
DR SMR; A1SR31; -.
DR STRING; 357804.Ping_0072; -.
DR KEGG; pin:Ping_0072; -.
DR eggNOG; COG0009; Bacteria.
DR HOGENOM; CLU_031397_6_0_6; -.
DR OrthoDB; 9814580at2; -.
DR Proteomes; UP000000639; Chromosome.
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 Gene3D; 3.90.870.10; DHBP synthase; 1.
DR HAMAP; MF_01852; TsaC; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR023535; TC-AMP_synthase.
DR NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1.
DR PANTHER; PTHR17490; SUA5; 1.
DR PANTHER; PTHR17490:SF18; THREONYLCARBAMOYL-AMP SYNTHASE; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..191
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000352965"
FT DOMAIN 7..191
FT /note="YrdC-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ SEQUENCE 191 AA; 20772 MW; C9FF56BA7EF56480 CRC64;
MLLLLKQSEL NDALKILKSQ GVIAYPTESV FGLGCDPDCE AAIQKILLLK QRPAYKGLIL
IAASIEQLEK YADFSLLTAA QLTVIKKTWP GPITWIVPSQ KNLSKLISGD FESVAVRVTA
HPIVRQICLA FDKPIISTSA NLSSLEAALS SQQVNKMFKS NTLLNLVIDA PVSGLSTPTQ
IFHASTGKRL R
//
