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Database: UniProt/SWISS-PROT
Entry: GATB_OCHA4
LinkDB: GATB_OCHA4
Original site: GATB_OCHA4 
ID   GATB_OCHA4              Reviewed;         500 AA.
AC   A6X191;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   11-DEC-2019, entry version 71.
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}; OrderedLocusNames=Oant_2279;
OS   Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC
OS   15819 / NCTC 12168).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae;
OC   Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS14995.1; -; Genomic_DNA.
DR   RefSeq; WP_012092152.1; NC_009667.1.
DR   SMR; A6X191; -.
DR   STRING; 439375.Oant_2279; -.
DR   EnsemblBacteria; ABS14995; ABS14995; Oant_2279.
DR   GeneID; 5379808; -.
DR   KEGG; oan:Oant_2279; -.
DR   PATRIC; fig|439375.7.peg.2399; -.
DR   eggNOG; ENOG4105CHT; Bacteria.
DR   eggNOG; COG0064; LUCA.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; ARKWWMG; -.
DR   OrthoDB; 497127at2; -.
DR   BioCyc; OANT439375:G1G9F-2421-MONOMER; -.
DR   Proteomes; UP000002301; Chromosome 1.
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; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_1000016011"
SQ   SEQUENCE   500 AA;  54775 MW;  340A09E64392BF35 CRC64;
     MSLIDTRIPE PKRFISGATG DWEVVIGMEV HAQVTSESKL FSGASTSFGA EPNSNVSLVD
     AAMPGMLPVI NLECVKQAVR TGIGLNAQIN LKSVFDRKNY FYPDLPQGYQ ISQFKQPIVG
     EGKIMISVGP DNKGQFEDVE IGIERLHLEQ DAGKSMHDQH PTMSYVDLNR SGVALMEIVS
     KPDLRSSDEA RAYLTKLRTI VRYLGTCDGN MDEGSMRADV NVSVRRPGGE FGTRCEIKNV
     NSIRFVGQAI EYEARRQIAI LEDGGSIDQE TRLFDPVKGE TRSMRSKEEA HDYRYFPDPD
     LLPLEFDQAF VDALAVDLPE LPDVKKQRLV EKQGISIYDA SILVTEKAIA DYYESVAAGR
     DGKAAANWVI NDLLGALNKA GKDIEESPVS PEQLGAVIDL IKEGTISGKI AKDLFEIVWN
     EGGDPKKLVE ERGMKQVTDT GAIEKAVDDV IAANPEKVEQ AKAKPTLAGW FVGQVMKATG
     GKANPQSVNE LVKAKLGIEE
//
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