(data stored in SCRATCH9089 zone)

SWISSPROT: GATB_BURP1

ID   GATB_BURP1              Reviewed;         490 AA.
AC   Q3JXC0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   11-DEC-2019, entry version 75.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121};
GN   OrderedLocusNames=BURPS1710b_0369;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) 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:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_00121};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00121}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
DR   EMBL; CP000124; ABA47986.1; -; Genomic_DNA.
DR   RefSeq; WP_004523090.1; NC_007434.1.
DR   SMR; Q3JXC0; -.
DR   EnsemblBacteria; ABA47986; ABA47986; BURPS1710b_0369.
DR   KEGG; bpm:BURPS1710b_0369; -.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; ARKWWMG; -.
DR   OrthoDB; 497127at2; -.
DR   BioCyc; BPSE320372:G1G58-426-MONOMER; -.
DR   Proteomes; UP000002700; Chromosome I.
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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 1.
DR   HAMAP; MF_00121; GatB; 1.
DR   InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3JXC0.
DR   SWISS-2DPAGE; Q3JXC0.
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..490
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_0000241204"
SQ   SEQUENCE   490 AA;  53323 MW;  DC36ECFADCDA910A CRC64;
     MTQWEVVIGL ETHAQLSTVS KIFSGASTQF GAQPNTQACP VDLALPGVLP VLNRGAVERA
     IRFGLAIGAT VAPRSVFARK NYFYPDLPKG YQISQYEIPV VQGGQITIQV PANEKAGKQA
     YSKTVNLTRA HLEEDAGKSL HEDFAGMTGI DLNRAGTPLL EIVTEPEMRS AAEAVAYAKA
     LHGLVMWLGI CDGNMQEGSF RCDANVSVRP VGQEKFGTRA EIKNLNSFRF LEDAINYEVR
     RQIELIEDGG EVVQETRLYD PDKRETRSMR SKEDAHDYRY FPDPDLMPLV IGADWIARVK
     GEMPELPAAM QQRFVEQYGV SAYDAGVLTS TKAMAEYFEA LVAKAGAANA KLAANWLMGD
     VSSQLNRDGI DIDACPVSAA QLALVLQRIA DGTISNKIAK EIFVTIWDEK AADEGAADRI
     IEAKGLKQIS DTGALEAIID EVLAANAKSV EEFRAGKDKA FNALVGQAMK ATKGKANPQQ
     VNELLKKKLG
//

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