ID A0A0G0DYC8_9BACT Unreviewed; 350 AA.
AC A0A0G0DYC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|ARBA:ARBA00012584};
DE EC=2.7.7.87 {ECO:0000256|ARBA:ARBA00012584};
DE AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|ARBA:ARBA00029774};
GN ORFNames=UR54_C0018G0006 {ECO:0000313|EMBL:KKP60137.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWA2_34_18.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618477 {ECO:0000313|EMBL:KKP60137.1, ECO:0000313|Proteomes:UP000034688};
RN [1] {ECO:0000313|EMBL:KKP60137.1, ECO:0000313|Proteomes:UP000034688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:0000256|ARBA:ARBA00001803};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the SUA5 family.
CC {ECO:0000256|ARBA:ARBA00007663}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKP60137.1}.
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DR EMBL; LBPP01000018; KKP60137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DYC8; -.
DR STRING; 1618477.UR54_C0018G0006; -.
DR PATRIC; fig|1618477.3.peg.324; -.
DR Proteomes; UP000034688; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR003442; T6A_TsaE.
DR NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1.
DR NCBIfam; TIGR00150; T6A_YjeE; 1.
DR PANTHER; PTHR17490; SUA5; 1.
DR PANTHER; PTHR17490:SF16; THREONYLCARBAMOYL-AMP SYNTHASE; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..200
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
SQ SEQUENCE 350 AA; 39778 MW; AC60802C8C40D307 CRC64;
MKIIKSKNKN TNLIINQTIK ILNLNGLVVF PSDTVYGLLC DATNKTAVKK LIAFKNRPPG
KAISVFCNFE LIDELVKINK QQKKIVKEIL PGPFTVILPS KHKVDKLLES EKRSLGIRIP
MYRYIEILVN KFKKPITATS ANLAGRSAHY SVNTLLDKTS EKQKKLIDLV VDSGTLPKNK
PSTVVDLTEY NVKILRQGDV NFSNKSKIFL SKSASKTKDI ASRVISSEAR NLAKRKLRKP
LIFIIEGELG VGKTVFVKGL GESLGINNIV SPTFVIYYQY ENFYHFDLYR IEEKEELKHL
GIEKLLIPGN ILCFEWGEKA GEIINLLKEK DIKYLIFVIQ LLFKFCYLLL
//
