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Database: UniProt/SWISS-PROT
Entry: GATB_METRJ
LinkDB: GATB_METRJ
Original site: GATB_METRJ 
ID   GATB_METRJ              Reviewed;         490 AA.
AC   B1LUB2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
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=Mrad2831_0481;
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM
OS   2831 / NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC   0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-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; CP001001; ACB22492.1; -; Genomic_DNA.
DR   RefSeq; WP_012317488.1; NC_010505.1.
DR   SMR; B1LUB2; -.
DR   STRING; 426355.Mrad2831_0481; -.
DR   EnsemblBacteria; ACB22492; ACB22492; Mrad2831_0481.
DR   GeneID; 6136494; -.
DR   KEGG; mrd:Mrad2831_0481; -.
DR   eggNOG; ENOG4105CHT; Bacteria.
DR   eggNOG; COG0064; LUCA.
DR   HOGENOM; HOG000223743; -.
DR   KO; K02434; -.
DR   OMA; SDGNMQE; -.
DR   OrthoDB; 497127at2; -.
DR   Proteomes; UP000006589; 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; Reference proteome.
FT   CHAIN         1    490       Aspartyl/glutamyl-tRNA(Asn/Gln)
FT                                amidotransferase subunit B.
FT                                /FTId=PRO_1000095224.
SQ   SEQUENCE   490 AA;  53117 MW;  A3958582AA17DE9D CRC64;
     MNAPVDPKKL IKGGLHDWEV IVGMEIHAQV SSRAKLFSGA STEFGAEPND HVSLVDAAMP
     GMLPVINAEC VAQAVRTGLG LKAKINLRSV FDRKNYFYPD LPQGYQISQY KDPIVGEGEV
     LVDLADGASI TVGIERLHLE QDAGKSLHDQ DPTRSFVDLN RSGVALMEIV SRPDLRSSEE
     AKAYVTKLRT ILRYLGTCDG DMEKGSLRAD VNVSVRRPGE PLGTRCEIKN VNSIRFIGQA
     IETEARRQIA ILEDGGTIDQ ETRLFDPTKG ETRSMRSKEE AHDYRYFPDP DLLPLEFDQA
     YVDALAEGLP ELPDAKKARF VSAFGLSPYD AGVLVAERAS ADYYEAVAKG RDGKAAANWV
     INELFGRLNK EGLSIEATPV SADQLGTIID LIGEGVISGK IAKDLFEIVW TEGGDPRVVV
     ESRGMKQVTD TGAIEAAVDQ IIAANPDKVA QAKEKPTLLG WFVGQTMKAT GGKANPAAVN
     ALLKAKLGIE
//
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