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Database: UniProt/SWISS-PROT
Entry: GATB_RHIE6
LinkDB: GATB_RHIE6
Original site: GATB_RHIE6 
ID   GATB_RHIE6              Reviewed;         500 AA.
AC   B3PXX8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=RHECIAT_CH0001948;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn)
CC       or Gln-tRNA(Gln) through the transamidation of misacylated Asp-
CC       tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both
CC       of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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
CC         H(+) + 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; CP001074; ACE90914.1; -; Genomic_DNA.
DR   RefSeq; WP_012483630.1; NC_010994.1.
DR   SMR; B3PXX8; -.
DR   STRING; 491916.RHECIAT_CH0001948; -.
DR   PRIDE; B3PXX8; -.
DR   EnsemblBacteria; ACE90914; ACE90914; RHECIAT_CH0001948.
DR   KEGG; rec:RHECIAT_CH0001948; -.
DR   eggNOG; ENOG4105CHT; Bacteria.
DR   eggNOG; COG0064; LUCA.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; SDGNMQE; -.
DR   BioCyc; RETL491916:G1GBZ-1932-MONOMER; -.
DR   Proteomes; UP000008817; Chromosome.
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;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    500       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit B.
FT                                /FTId=PRO_1000095236.
SQ   SEQUENCE   500 AA;  54739 MW;  95C3E4A40D8471E9 CRC64;
     MTLVDVRTPD PKRFIPGATG DWEVIVGMEV HAQVLSNSKL FSGASTEFGK PQNSNVSLVD
     AAMPGMLPVI NEECVKQAVR TGLGLKAQIN KRSLFDRKNY FYPDLPQGYQ ISQFKDPIVG
     EGKIVISLGP DRQGQFEDIE IGIERLHLEQ DAGKSMHDQH ATMSYVDLNR SGVALMEIVS
     KPDMRSSDEA KAYMTKLRSI VRYLGTCDGN MDEGSMRADV NVSVRRPGEA FGTRCEIKNV
     NSIRFIGQAI EYEARRQIGI LEDGGTIEQE TRLFDPNKGE TRSMRSKEDA HDYRYFPDPD
     LLPLEFDDAF VTALAADLPE LPDDKKERFV RELGLSVYDA SVLVSEKAIA DYFEAVAAGR
     DGKTAANWVI NDLLGALNRT GKDIEQTPVS PAQLGAIIDL IKAGTISGKI AKDLFEIVLT
     EGGDPAEIVE SRGMKQVTDT GAIEKAVDEI IAANPDQVEK VKAKPTMAAW FVGQVMKATG
     GKANPQAVQA LVKAKLGIEE
//
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