UniProt/TrEMBL: A0A1B4NVJ5

Database: UniProt/TrEMBL
Entry: A0A1B4NVJ5_9BURK

LinkDB:  A0A1B4NVJ5_9BURK 
Original site:  A0A1B4NVJ5_9BURK

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Ontology (5)   
   GO (5)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (13)   
   InterPro (9)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (22)   

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ID   A0A1B4NVJ5_9BURK        Unreviewed;       491 AA.
AC   A0A1B4NVJ5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:AOK05677.1};
GN   ORFNames=K6W21_16475 {ECO:0000313|EMBL:MBY4695666.1}, WK25_15080
GN   {ECO:0000313|EMBL:AOK05677.1};
OS   Burkholderia latens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=488446 {ECO:0000313|EMBL:AOK05677.1, ECO:0000313|Proteomes:UP000094509};
RN   [1] {ECO:0000313|EMBL:AOK05677.1, ECO:0000313|Proteomes:UP000094509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17928 {ECO:0000313|EMBL:AOK05677.1,
RC   ECO:0000313|Proteomes:UP000094509};
RA   Sahl J., Wagner D., Keim P.;
RT   "Diversity of Burkholderia near neighbor genomes.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBY4695666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AU41890 {ECO:0000313|EMBL:MBY4695666.1};
RA   Spilker T., Lipuma J.;
RT   "A collection of bacterial strains from the Burkholderia cepacia Research
RT   Laboratory and Repository.";
RL   Submitted (AUG-2021) 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; CP013435; AOK05677.1; -; Genomic_DNA.
DR   EMBL; JAIMCT010000010; MBY4695666.1; -; Genomic_DNA.
DR   RefSeq; WP_069241868.1; NZ_JAIMCT010000010.1.
DR   AlphaFoldDB; A0A1B4NVJ5; -.
DR   KEGG; blat:WK25_15080; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000094509; Chromosome 1.
DR   Proteomes; UP000713854; 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}; Transferase {ECO:0000313|EMBL:AOK05677.1}.
FT   DOMAIN          337..490
FT                   /note="Asn/Gln amidotransferase"
FT                   /evidence="ECO:0000259|SMART:SM00845"
SQ   SEQUENCE   491 AA;  53415 MW;  A7C9E9011FF324D7 CRC64;
     MATQWEVVIG LETHAQLSTV SKIFSGASTQ FGAEPNTQAC PVDLALPGVL PVLNRGAVER
     AIRFGLAIGS TIAPRSIFAR KNYFYPDLPK GYQISQYEIP VVQGGRITIQ VPANEKAGKA
     AYEKTVNLTR AHLEEDAGKS LHEDFAGMTG IDLNRAGTPL LEIVTEPEMR SAAEAVAYAK
     ALHALVVWLG ICDGNMQEGS FRCDANVSVR PLGQEKFGTR AEIKNLNSFR FLEEAINYEV
     RRQIELIEDG GEVVQETRLY DPDKRETRSM RSKEDAHDYR YFPDPDLMPL VIGQDWIERV
     QAGMPELPAA MQQRFAEQYG VSAYDAGVLT SSKAMAAYFE AVVAKAGAAN AKIAANWLMG
     DVSSQLNRDG IEIDAIPVSA AQLALVLQRI ADGTISNKIA KEIFATIWDE KAADEGAADR
     IIDAKGLKQI SDTGALEAII DEVLAANAKS VEEFRAGKEK AFNALIGQAM KATKGKANPQ
     QVNELLKKKL G
//

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