ID A0A1W9JAC6_9PROT Unreviewed; 223 AA.
AC A0A1W9JAC6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Aspartyl/glutamyl-tRNA amidotransferase subunit B {ECO:0000313|EMBL:OQW68858.1};
GN Name=gatB {ECO:0000313|EMBL:OQW68858.1};
GN ORFNames=BVN35_19610 {ECO:0000313|EMBL:OQW68858.1};
OS Proteobacteria bacterium ST_bin11.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978759 {ECO:0000313|EMBL:OQW68858.1, ECO:0000313|Proteomes:UP000192691};
RN [1] {ECO:0000313|EMBL:OQW68858.1, ECO:0000313|Proteomes:UP000192691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin11 {ECO:0000313|EMBL:OQW68858.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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-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 -!- 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:OQW68858.1}.
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DR EMBL; MSXO01000056; OQW68858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9JAC6; -.
DR STRING; 1978759.BVN35_19610; -.
DR Proteomes; UP000192691; 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:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.410; -; 1.
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; IPR018027; Asn/Gln_amidotransferase.
DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR InterPro; IPR042114; GatB_C_1.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
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 Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 4: Predicted;
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}.
FT DOMAIN 73..221
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQW68858.1"
SQ SEQUENCE 223 AA; 24401 MW; 16963A48670BBF86 CRC64;
DETRSMRSKE EANDYRYFPD PDLLPVLIED SLKDEIRATL PELPDAKKQR FIDQYALDNE
SATTLTSSRE LADFYETVVK QSGGEAKLAG NWLTGDVLGA LNKAGLEISD CPVSAERLAG
LIKRIADNTI SGKTAKQVFD KLWNGSDSAD EIIEKEGLVQ ITDMSAIEAI VDKVIAANPV
PVEQYRAGKD KALMALVGQI MKETQGKANP GEVNKMLIAK LKS
//