ID A0A124FY18_9BACT Unreviewed; 362 AA.
AC A0A124FY18;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=XD95_0096 {ECO:0000313|EMBL:KUK79810.1};
OS Microgenomates bacterium 39_7.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1641390 {ECO:0000313|EMBL:KUK79810.1, ECO:0000313|Proteomes:UP000054437};
RN [1] {ECO:0000313|Proteomes:UP000054437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK79810.1}.
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DR EMBL; LGGQ01000006; KUK79810.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FY18; -.
DR PATRIC; fig|1641390.4.peg.592; -.
DR Proteomes; UP000054437; 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..201
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
SQ SEQUENCE 362 AA; 40227 MW; B935F811BBF70132 CRC64;
MEIIKLNQKN CQQTAKHAAE VLKKGGLVIF PTETVYGIGA DATNQQAILK LLSYKSRREG
KPLSIAVTDQ LMAEQFVELN EQAKNLYQRF LPGPYTIVSR YKNGLADGVA SEFNTLGVRI
PDHKLALDIV RNLKQPITAT SANASGKKRP YAVTDILKNL SNKQKALIDL IIDAGELPPN
EPSVVIDTTL STPLTLRSSG SPQDKSSKKS IKLISHSEKE TQEIAGKLLL KHWDQLTQQG
LIIGLDGELG AGKTVFAKGV GNFLRISSTI TSPTYSYIRE YDFTRYQTEG KLFHIDVWKV
DDPQVLEKLQ IPALLAPNHL IVIEWWTQLK DSLAQFQANL NVRLELISEN ERSLTIIENP
SS
//
