GATB_METJA
ID GATB_METJA Reviewed; 472 AA.
AC Q57624;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE Short=Asp/Glu-ADT subunit B;
DE EC=6.3.5.-;
GN Name=gatB; OrderedLocusNames=MJ0160;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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) (By similarity). {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98144.1; -; Genomic_DNA.
DR PIR; A64320; A64320.
DR AlphaFoldDB; Q57624; -.
DR SMR; Q57624; -.
DR STRING; 243232.MJ_0160; -.
DR EnsemblBacteria; AAB98144; AAB98144; MJ_0160.
DR KEGG; mja:MJ_0160; -.
DR eggNOG; arCOG01718; Archaea.
DR HOGENOM; CLU_019240_0_0_2; -.
DR InParanoid; Q57624; -.
DR OMA; ARKWWMG; -.
DR PhylomeDB; Q57624; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
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..472
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148871"
SQ SEQUENCE 472 AA; 53736 MW; 2C14856409CBF03A CRC64;
MGGNMEDVKM KCGLEIHVQI DTKSKLFCNC STNYLDAEPN TNVCPVCLGL PGAKPLPPNK
KAVEVAIMVA KMLGCKIVVD EDIYFQRKHY DYPDLPSGYQ RTSTPIGVDG EFMGIGIHEV
HLEEDPGQYN PSFGIVDYNR SGTPLIEIVT KPDIKSPEEA REFLKQLMTL FRYLGCLRGE
GTMRADVNIS IEYMGVQGNR VEVKNVNSIK GVYKVLKYEL IRQKNIIKRG GEVKRETRAF
LESQMITKAM RSKETAEDYR YIPDPDIQPI VISEKWVKEI EEKMPETPLA KKKRFVEEYG
IDEEDAKVLV SDLDMAEMFE EVVKSLGVNK ENVDLAVTWI RNELRRSLQY HKVDLYESGV
KAEHIVELIK LIKEGVISQK IAKEIVDLLV INRGKKMPKE LVEELGLTVI RDEDALVKAV
EEAIKNNPKA VEDYLNGKKE ALNFLMGQVM RLTRGRADPK RVIELLKERL DK