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Database: UniProt/SWISS-PROT
Entry: GATB_ERYLH
LinkDB: GATB_ERYLH
Original site: GATB_ERYLH 
ID   GATB_ERYLH              Reviewed;         498 AA.
AC   Q2ND71;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
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=ELI_01390;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594;
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(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; CP000157; ABC62370.1; -; Genomic_DNA.
DR   RefSeq; WP_011413246.1; NC_007722.1.
DR   SMR; Q2ND71; -.
DR   STRING; 314225.ELI_01390; -.
DR   PRIDE; Q2ND71; -.
DR   EnsemblBacteria; ABC62370; ABC62370; ELI_01390.
DR   KEGG; eli:ELI_01390; -.
DR   eggNOG; ENOG4105CHT; Bacteria.
DR   eggNOG; COG0064; LUCA.
DR   HOGENOM; HOG000223742; -.
DR   KO; K02434; -.
DR   OMA; SDGNMQE; -.
DR   OrthoDB; 497127at2; -.
DR   BioCyc; ELIT314225:G1G5F-280-MONOMER; -.
DR   Proteomes; UP000008808; 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; 2.
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    498       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit B.
FT                                /FTId=PRO_1000015965.
SQ   SEQUENCE   498 AA;  54845 MW;  3EE2BA904DBB5EA9 CRC64;
     MSTYRIQGAT GEWEVVIGLE VHAQVTSNAK LFSGASTEFG AEPNAQVSLV DAAMPGMLPV
     PNRECIRQAV RTGMAIEAQI NTWSRFDRKN YFYADLPQGY QISQLYHPLV GEGQLLIEAD
     EKAGISEDKV IGIERIHVEQ DAGKLMHDQH PTMSYVDLNR CGVALMEIVS RPDMRSPAEA
     GAYVRKLRAI LRYVGSCDGN MEEGSMRADV NVSVRRPGEE FGTRTETKNV NSVRFVMQVI
     EYEANRQVDL IESGGAVEQE TRLFDPGTGT TRTMRSKEDA HDYRYFPDPD LLPLELEDSF
     LDECRASLPE LPDAKRQRYE NELGLTPYNA RELTAEVETF ARFETLLAAT AKAIGEDEKK
     VATQVANWAL SVAPGVIKSL GDEAHVENAT AERQAAILKM QDAGEISGGQ AKEIFEIVLK
     EGGDPATIAD EKGLKQVSDT GAIEAAIDEI LANNEDKVEQ YKCGKDKLFG FFVGQTMKAM
     QGKANPAVVN QILKDKLG
//
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