ID A0A1C2FX31_9GAMM Unreviewed; 477 AA.
AC A0A1C2FX31;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000256|HAMAP-Rule:MF_00121};
DE Short=Asp/Glu-ADT subunit B {ECO:0000256|HAMAP-Rule:MF_00121};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00121};
GN Name=gatB {ECO:0000256|HAMAP-Rule:MF_00121,
GN ECO:0000313|EMBL:OCX43819.1};
GN ORFNames=A9R16_05600 {ECO:0000313|EMBL:OCX43819.1}, C4900_01280
GN {ECO:0000313|EMBL:RCN58458.1};
OS Acidiferrobacter thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Acidiferrobacterales;
OC Acidiferrobacteraceae; Acidiferrobacter.
OX NCBI_TaxID=163359 {ECO:0000313|EMBL:OCX43819.1};
RN [1] {ECO:0000313|EMBL:OCX43819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZJ {ECO:0000313|EMBL:OCX43819.1};
RA Ma L.;
RT "Draft Genome Sequence of Acidiferrobacter thiooxydans ZJ, a Distinctive
RT Species of Ectothiorhodospiraceae.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RCN58458.1, ECO:0000313|Proteomes:UP000253250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M-1 {ECO:0000313|EMBL:RCN58458.1}, and m-1
RC {ECO:0000313|Proteomes:UP000253250};
RA Issotta F., Thyssen C., Mena C., Moya A., Bellenberg S., Sproer C.,
RA Covarrubias P.C., Sand W., Quatrini R., Vera M.;
RT "Insights into the biology of acidophilic members of the
RT Acidiferrobacteraceae family derived from comparative genomic analyses.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|HAMAP-Rule:MF_00121}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00121};
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, ECO:0000256|HAMAP-
CC Rule:MF_00121};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC {ECO:0000256|ARBA:ARBA00011123, ECO:0000256|HAMAP-Rule:MF_00121}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000256|ARBA:ARBA00005306, ECO:0000256|HAMAP-Rule:MF_00121}.
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:OCX43819.1}.
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DR EMBL; MDCF01000252; OCX43819.1; -; Genomic_DNA.
DR EMBL; PSYR01000001; RCN58458.1; -; Genomic_DNA.
DR RefSeq; WP_065972319.1; NZ_PSYR01000001.1.
DR STRING; 163359.A9R16_05600; -.
DR OrthoDB; 9804078at2; -.
DR Proteomes; UP000253250; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.410; -; 1.
DR Gene3D; 1.10.150.380; GatB domain, N-terminal subdomain; 1.
DR HAMAP; MF_00121; GatB; 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; IPR004413; GatB.
DR InterPro; IPR042114; GatB_C_1.
DR InterPro; IPR023168; GatB_Yqey_C_2.
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 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.
DR PROSITE; PS01234; GATB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00121};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00121};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00121};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00121}; Transferase {ECO:0000313|EMBL:OCX43819.1}.
FT DOMAIN 327..475
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 477 AA; 52168 MW; E9AF643F6608EB00 CRC64;
MEWETVIGLE VHAQLKTQSK IFSASPTAYG AAPNTQANVV DAAFPGVLPV LNGEAVRMAA
RFGVAIGATV HRRSVFARKN YFYPDLPKGY QISQYEHPIV ERGRLVITTP TGEKTIGITR
AHLEEDAGKS LHEDMGGFTG IDLNRAGTPL LEIVSEPDMR SAAEAVAYLK TLHTLVRYLD
ICDGNMQEGS FRCDANVSVR PLGQARLGTR AELKNINSFR FVERAIDYEV RRQIALISAG
GEVRQETRLY DSARDETRSM RSKEEANDYR YFPDPDLPAL VLTEAFLAEV KDAMPELPDA
KRQRFGVQYG LSAYDAGVLT ASRELAQYYE DAVAAAGVEP KLVANWVTGE LAARLNEDGL
DIVDSRVRAA ALAGLLRRIA DGTVSGKAAK DVFEAMWAGE GDADAVIAAR GLRQISDDSA
IEEVVRQVIA ANPKQLAQYR AGEEKVFTFF VGQTMKASRG KANPAKVNEI LKRLLAS
//
