ID GATB_HALSA Reviewed; 495 AA.
AC Q9HS93;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=VNG_0345G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
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DR EMBL; AE004437; AAG18915.1; -; Genomic_DNA.
DR PIR; G84193; G84193.
DR RefSeq; WP_010902210.1; NC_002607.1.
DR AlphaFoldDB; Q9HS93; -.
DR SMR; Q9HS93; -.
DR STRING; 64091.VNG_0345G; -.
DR PaxDb; 64091-VNG_0345G; -.
DR GeneID; 68693284; -.
DR KEGG; hal:VNG_0345G; -.
DR PATRIC; fig|64091.14.peg.256; -.
DR HOGENOM; CLU_019240_0_0_2; -.
DR InParanoid; Q9HS93; -.
DR OrthoDB; 52755at2157; -.
DR PhylomeDB; Q9HS93; -.
DR Proteomes; UP000000554; 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; GatB domain, N-terminal subdomain; 1.
DR HAMAP; MF_00121; GatB; 1.
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; IPR004413; GatB.
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 NCBIfam; TIGR00133; gatB; 1.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF89095; GatB/YqeY motif; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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..495
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148869"
SQ SEQUENCE 495 AA; 54267 MW; 46F15547DF1E2825 CRC64;
MSAQAAERDL TAIIGLEVHV QLETDTKIFC GCSTDTDDAD PNTHTCPVCL GLPGALPTLN
EGAVEAAVKL GKAIDADIPE RTRFHRKNYF YPDLPKGFQI TQYDAPICQD GELEVGTADD
RRAIGIERAH LEEDPGSLQH VGGSIEDADY TLVDYNRAGT PLMEIVTRPD FRAAEEVRSF
LAKLTSVLEY LGVFDAERDG SLRVDANISM VDSAELAGEG GPSDDVLEAA NRTEVKNISS
HRAAQKALAY ETTRQRNQLE RGMAVAQETR HWDEARGVTV SMRSKEEEKD YRYFREADIP
PLEVSDWKDE IPIPELPDAR RERFRTEYGV GDETASKLTS RKAVADLFEE LADEYDAALA
ATWVADNVLG ELNYRDLSLD DVADRDDEFE RLVELVAEDE ITAKNAEEVV LRTMLDEDRA
PDEIVDAEGL GKTSGDAVAD AVAEAIAENP DAVADYHDGE GDALNFLVGQ VMAKTGGSAD
PGQVNELLRD ELAQA
//
