ID A0A0G0TPJ8_9BACT Unreviewed; 326 AA.
AC A0A0G0TPJ8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000313|EMBL:KKR78919.1};
DE Flags: Fragment;
GN ORFNames=UU25_C0027G0001 {ECO:0000313|EMBL:KKR78919.1};
OS Microgenomates group bacterium GW2011_GWB1_40_9.
OC Bacteria.
OX NCBI_TaxID=1618504 {ECO:0000313|EMBL:KKR78919.1, ECO:0000313|Proteomes:UP000034379};
RN [1] {ECO:0000313|EMBL:KKR78919.1, ECO:0000313|Proteomes:UP000034379}
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 -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC presence of glutamine and ATP through an activated phospho-Asp-
CC tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000256|ARBA:ARBA00024799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00000924};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000256|ARBA:ARBA00005306}.
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:KKR78919.1}.
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DR EMBL; LBZX01000027; KKR78919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0TPJ8; -.
DR PATRIC; fig|1618504.3.peg.429; -.
DR Proteomes; UP000034379; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR004413; GatB.
DR InterPro; IPR042114; GatB_C_1.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR NCBIfam; TIGR00133; gatB; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS01234; GATB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Transferase {ECO:0000313|EMBL:KKR78919.1}.
FT DOMAIN 8..289
FT /note="Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit
FT B/E catalytic"
FT /evidence="ECO:0000259|Pfam:PF02934"
FT NON_TER 326
FT /evidence="ECO:0000313|EMBL:KKR78919.1"
SQ SEQUENCE 326 AA; 37881 MW; 48D6EBFDC268292F CRC64;
MKKIYEPVIG LEVHVELKTN SKMFCGCPAD HFGKEPNTQT CPVCLGLPGA LPVPNKKAIE
WCIKLGLALH CTVPAESKFD RKNYFYPDLP KGYQISQYDK PLCENGWIQI NDRKIRIRRV
HQEEDTGKLQ HIEAEGQQVT LVDFNRSGVP LVEIVTEPDF HTIDEVDQYV KQIRRIIRYL
DISNADMEKG SMRLEPSISL RVSGSDELPN YRVELKNINS FRFVRKAIEF EIKRQSEILD
LGETIVQQTR GWNESKQVTL PQREKEEAHD YRYFPEPDIP PMRFTNVFVE GIRKQIPELP
DAKKSRFMKT YNMNESVADI LIQEKE
//
