ID A0A1F5DVP6_9BACT Unreviewed; 349 AA.
AC A0A1F5DVP6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=A3I57_03445 {ECO:0000313|EMBL:OGD59165.1};
OS Candidatus Beckwithbacteria bacterium RIFCSPLOWO2_02_FULL_47_23.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1797463 {ECO:0000313|EMBL:OGD59165.1, ECO:0000313|Proteomes:UP000176364};
RN [1] {ECO:0000313|EMBL:OGD59165.1, ECO:0000313|Proteomes:UP000176364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD59165.1}.
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DR EMBL; MEZQ01000040; OGD59165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5DVP6; -.
DR Proteomes; UP000176364; 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 1..190
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
SQ SEQUENCE 349 AA; 38786 MW; D91F8F6A8E2B8B57 CRC64;
MDPVAQAVKV LRSGGLIIYP TETCYGAGAD AANQSAVDKL LRYKSRREGR PLSIAVTDQT
MASKYIIMNT TAKNLYNKFL PGPLTIVSAG RHKLAKGVES ETGTLGVRIP DHPVALELVR
RLGRPITATS ANVSYKPRPY SIKQLLTQTS KKQQGLIDYI IDAGALPKRP VSTIVDTTLD
DPLVIRQGKI NIPPRGGIIS KSPEETKKLA QTLCLKYWKD LQTKPLMFLL IGELGAGKTQ
FAKGIGAWLK IKQPITSPTF TIAKEYDWVR YGIKGRFLHL DTWRLQHLEE FEALGLKKQL
LPKTIMAIEW ADRSFDYLLK IARKAKVVIL SLQTEGAASP THRRITFGR
//
