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Database: UniProt
Entry: A0A0G1IIM5_9BACT
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Original site: A0A0G1IIM5_9BACT 
ID   A0A0G1IIM5_9BACT        Unreviewed;       353 AA.
AC   A0A0G1IIM5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=UW18_C0003G0276 {ECO:0000313|EMBL:KKT31692.1};
OS   Microgenomates group bacterium GW2011_GWF1_44_10.
OC   Bacteria.
OX   NCBI_TaxID=1618537 {ECO:0000313|EMBL:KKT31692.1, ECO:0000313|Proteomes:UP000034538};
RN   [1] {ECO:0000313|EMBL:KKT31692.1, ECO:0000313|Proteomes:UP000034538}
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:KKT31692.1}.
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DR   EMBL; LCHI01000003; KKT31692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1IIM5; -.
DR   Proteomes; UP000034538; 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          9..198
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
SQ   SEQUENCE   353 AA;  39120 MW;  2AE1C7D949D687BA CRC64;
     MNVLIPSSID FLSQVVHILS SGGMIIYPTE TTYGLGVDAT NERAVQKLLQ YKKRRDGKPL
     SIAVADIQMA EKYVVLNNVA RNVYKQFLPG PVTVISSGKH RVATFVESNH GTLGIRISSY
     PLVNEIVYAF GKPITATGAN ASDQKRPYSI VDVFSFLDDT QQNLIDAVID VGELPHVEPS
     TIIDTTLDNP IILRQGASPV HAKNEFISHS VDRTKELGEL CALQQKNHFG HKPIIFALRG
     EMGAGKTQFV KGIASALKIA RTISSPTYVL CKEYQFEAEG KIIPCIHIDA WRLSEEHELF
     SLGFEKMLQE NAVIAIEWAD RTMSALERIE REAVVVWVNI AVGSCENDRV ISW
//
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