ID A0A161GW94_9RHOB Unreviewed; 503 AA.
AC A0A161GW94;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-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 ORFNames=AKL17_1223 {ECO:0000313|EMBL:AMY68479.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY68479.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY68479.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) 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}.
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DR EMBL; CP012661; AMY68479.1; -; Genomic_DNA.
DR RefSeq; WP_066811575.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A161GW94; -.
DR STRING; 1335048.AKL17_1223; -.
DR KEGG; daa:AKL17_1223; -.
DR PATRIC; fig|1335048.3.peg.1267; -.
DR OrthoDB; 9804078at2; -.
DR Proteomes; UP000076128; Chromosome.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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:AMY68479.1}.
FT DOMAIN 356..501
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 503 AA; 54683 MW; E042BF02CFA1022E CRC64;
MLDLTFTAPQ PKVISGAKAD WELVIGLEVH AQVASNAKLF SGASTSFGAE PNANVAFVDA
AMPGMLPVVN EFCVAQAVRT GLGLKAQINL RSAFDRKNYF YPDLPQGYQI SQLYHPIVGE
GEVIVDMGPG IARRVRIERI HLEQDAGKSI HDMDPNMSFV DLNRTGVALM EIVSRPDIRG
PEEAAAYVAK LRQILRYLGT CDGNMQNGNL RADVNVSVCK PGQYEKYQAT QDFSHLGTRC
EIKNMNSLRF IQAAIDYEAR RQIAILEDGG SIVQETRLYD PDKGETRSMR SKEEAHDYRY
FPDPDLLPLE IEQAWVDDIA ATMPELPDAR KARYMGDFGL TDYDASVLTA EKENAVFFEA
VATGRDGKTA ANWVINELFG RLNKEGLGIA ESPVSAAQLG GVLDLIGSGE ISGKMAKDLF
EILWTEGGEP AEIAAARGMK QVTDTGAIEA AVDEIIAANP AQVEKARANA KLAGWFTGQV
LKATGGKANP AVVNEMVARK LGL
//
