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TSAC_SHEAM
ID   TSAC_SHEAM              Reviewed;         187 AA.
AC   A1S1K5;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 69.
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=Sama_0049;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=326297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1098 / SB2B;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella amazonensis SB2B.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL98261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000507; ABL98261.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041409559.1; NC_008700.1.
DR   AlphaFoldDB; A1S1K5; -.
DR   SMR; A1S1K5; -.
DR   STRING; 326297.Sama_0049; -.
DR   EnsemblBacteria; ABL98261; ABL98261; Sama_0049.
DR   KEGG; saz:Sama_0049; -.
DR   eggNOG; COG0009; Bacteria.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   OrthoDB; 1913202at2; -.
DR   Proteomes; UP000009175; 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   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   TIGRFAMs; TIGR00057; TIGR00057; 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..187
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000352974"
FT   DOMAIN          3..187
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ   SEQUENCE   187 AA;  20044 MW;  D2A00866ED9AD162 CRC64;
     MLQVTPSQIS GIIESGGVVA YPTEAVYGLG CDPDNDTAIQ KLLAVKQRPW EKGLILIASS
     FDQLKPYIDL SRVTEAQLQA AFDKWPGPFT FVIPAKADVS PMLRGCFDTI AVRVSAHQDV
     RAMCYACQKP LVSTSANLAG EQPALTLAEV QTQLGDKIDA VVLGALGQSC QPSTIIDIQT
     GHIFRQG
 
 
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