GenomeNet

Database: UniProt/SWISS-PROT
Entry: GATB_AGRVS
LinkDB: GATB_AGRVS
Original site: GATB_AGRVS 
ID   GATB_AGRVS              Reviewed;         500 AA.
AC   B9JVJ7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=Avi_1781;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis
OS   (strain S4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/JB.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I.,
RA   Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T.,
RA   Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J.,
RA   Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V.,
RA   Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L.,
RA   Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000633; ACM36277.1; -; Genomic_DNA.
DR   RefSeq; WP_015915700.1; NC_011989.1.
DR   SMR; B9JVJ7; -.
DR   STRING; 311402.Avi_1781; -.
DR   EnsemblBacteria; ACM36277; ACM36277; Avi_1781.
DR   GeneID; 31495099; -.
DR   KEGG; avi:Avi_1781; -.
DR   eggNOG; ENOG4105CHT; Bacteria.
DR   eggNOG; COG0064; LUCA.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; SDGNMQE; -.
DR   OrthoDB; 497127at2; -.
DR   Proteomes; UP000001596; 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; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    500       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit B.
FT                                /FTId=PRO_1000122500.
SQ   SEQUENCE   500 AA;  54460 MW;  4704CC183798A70C CRC64;
     MTLVDTRTPD PKRLIPGATG DWEIVIGMEV HAQVLSQSKL FSGASTTFGN APNDNVSLVD
     AAMPGMLPVI NEECVRQAVR TGLGLKAKIN KRSIFDRKNY FYPDLPQGYQ ISQFKDPIVG
     EGKIIISLGP DRQGNFEDIE IGIERLHLEQ DAGKSMHDQH PTMSYVDLNR SGVALMEIVS
     KPDMRSSDEA KAYMTKLRSI VRYLGTCDGN MDEGSMRADV NVSVRKPGGE FGTRCEIKNV
     NSIRFIGQAI EYEARRQIAI LEDGGSIDQE TRLFDPGKGE TRSMRSKEDA HDYRYFPDPD
     LLPLEFDDAF VQALKKDLPE LPDDKKARFV ASLGLSVYDA SVLVSEKAIA DYYEAVAAGR
     DGKIAANWVI NDLLGALNKA GKGIEETPVS PAQLGGIIDL IKAETISGKI AKDLFEIVFN
     EGGDPADIVE SRGMKQVTDT GAIEKAVDEI IAANPDQVAK VLAKPTLAGW FVGQVMKATG
     GKANPQAVQA LVKAKLGLEE
//
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