ID A0A086Y1T6_9RHOB Unreviewed; 504 AA.
AC A0A086Y1T6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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:KFI28236.1};
GN ORFNames=CG50_15240 {ECO:0000313|EMBL:KFI28236.1};
OS Paenirhodobacter enshiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paenirhodobacter.
OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI28236.1, ECO:0000313|Proteomes:UP000028824};
RN [1] {ECO:0000313|EMBL:KFI28236.1, ECO:0000313|Proteomes:UP000028824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI28236.1,
RC ECO:0000313|Proteomes:UP000028824};
RA Wang D., Wang G.;
RT "Genome of Paenirhodobacter enshiensis DW2-9.";
RL Submitted (MAR-2014) 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:KFI28236.1}.
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DR EMBL; JFZB01000007; KFI28236.1; -; Genomic_DNA.
DR RefSeq; WP_036636279.1; NZ_JFZB01000007.1.
DR AlphaFoldDB; A0A086Y1T6; -.
DR STRING; 1105367.CG50_15240; -.
DR eggNOG; COG0064; Bacteria.
DR OrthoDB; 9804078at2; -.
DR Proteomes; UP000028824; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028824};
KW Transferase {ECO:0000313|EMBL:KFI28236.1}.
FT DOMAIN 356..502
FT /note="Asn/Gln amidotransferase"
FT /evidence="ECO:0000259|SMART:SM00845"
SQ SEQUENCE 504 AA; 55484 MW; B61699010474945A CRC64;
MLDLSTKAPE PKVIAGAKGD WELVIGMEIH AQVSSNAKLF SGASTGFGAE PNSHVAFVDA
AMPGMLPVIN EYCIAQAVRS GLGLKAAINL RSAFDRKNYF YPDLPQGYQI SQLYHPIVGE
GEVIVEMEPG IERRVRIERI HLEQDAGKSI HDMDPTMSFV DLNRTGVALM EIVSRPDIRG
PEEAAAYVVK LRQILRYLGT CDGNMQNGNL RCDVNVSVCK PGQYEKYQET QDFSHLGTRC
ELKNMNSMRF IQAAIDYEAR RQIAILEDGG SVDQETRLYD PDKNETRSMR SKEEAHDYRY
FPCPDLLPLE IEQGWVDEIA ANMPELPDAK KRRFIEELGL SDYDASVLTA ELEHADYFEA
VVAACGDGKQ AANWVINDLF GRLKKDGTEF DACPVSPAQL GAIIALIRKG DISGKIAKDL
FEIVFTEGGE PAEIVEARGM KQVTDTGAIE KVVDEIIAKS PSEVEKARAN PKLIGWFVGQ
VMKASGGKAN PAAVNKIVAE KLGL
//
