ID   GATB_CALS4              Reviewed;         475 AA.
AC   Q8RC39;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 109.
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=6.3.5.6 {ECO:0000255|HAMAP-Rule:MF_00121};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00121};
DE   AltName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE            Short=Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
GN   Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121};
GN   OrderedLocusNames=TTE0608;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Catalytic subunit of the Asp/Glu-tRNA(Asn/Gln)
CC       amidotransferase complex GatCAB. GatCAB allows the formation of
CC       correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step
CC       transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in
CC       organisms which lack either or both of asparaginyl-tRNA or glutaminyl-
CC       tRNA synthetases. The reaction takes place in the presence of glutamine
CC       and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-
CC       tRNA(Gln). This subunit specifically recognizes tRNA(Gln) and
CC       tRNA(Asn), and mediates the transamidation of misloaded Glu and Asp
CC       respectively by catalyzing formation of the activated gamma-phospho-
CC       intermediate and its subsequent aminolysis using ammonia produced by
CC       the gatA subunit. Recognizes the first base pair and the D-loop of its
CC       specific tRNA substrates. {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl-
CC         tRNA(Gln) + L-glutamate + ADP + phosphate + H(+);
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; EC=6.3.5.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L-
CC         asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+);
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; EC=6.3.5.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) +
CC         ADP; Xref=Rhea:RHEA:57908, Rhea:RHEA-COMP:9684, Rhea:RHEA-COMP:15032,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:78520, ChEBI:CHEBI:142449,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartyl-tRNA(Asn) + ATP = 4-phospho-L-aspartyl-tRNA(Asn) +
CC         ADP + H(+); Xref=Rhea:RHEA:57916, Rhea:RHEA-COMP:9677, Rhea:RHEA-
CC         COMP:15033, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:142450, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl-
CC         tRNA(Gln) + phosphate + H(+); Xref=Rhea:RHEA:57912, Rhea:RHEA-
CC         COMP:9681, Rhea:RHEA-COMP:15032, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:78521,
CC         ChEBI:CHEBI:142449; Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-phospho-L-aspartyl-tRNA(Asn) + NH4(+) = L-asparaginyl-
CC         tRNA(Asn) + phosphate + H(+); Xref=Rhea:RHEA:57920, Rhea:RHEA-
CC         COMP:9674, Rhea:RHEA-COMP:15033, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:78515,
CC         ChEBI:CHEBI:142450; Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00121};
CC       Note=Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning
CC       of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a
CC       secondary transient Mg(2+) ion that participates in phosphoryl transfer
CC       by polarizing the gamma-phosphate group of ATP. {ECO:0000255|HAMAP-
CC       Rule:MF_00121};
CC   -!- SUBUNIT: Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln)
CC       amidotransferase complex composed of GatA, GatB and GatC.
CC       {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- DOMAIN: The N-terminal cradle domain recognizes the first base of the
CC       acceptor tRNA stem. {ECO:0000255|HAMAP-Rule:MF_00121}.
CC   -!- DOMAIN: The C-terminal tail domain, an anti-parallel amphiphilic helix
CC       bundle, is involved in discriminating and binding specific tRNAs.
CC       Probably recognizes the tRNA(Gln)-specific D-loop structure.
CC       {ECO:0000255|HAMAP-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; AE008691; AAM23878.1; -; Genomic_DNA.
DR   RefSeq; WP_011025023.1; NC_003869.1.
DR   AlphaFoldDB; Q8RC39; -.
DR   SMR; Q8RC39; -.
DR   STRING; 273068.TTE0608; -.
DR   KEGG; tte:TTE0608; -.
DR   eggNOG; COG0064; Bacteria.
DR   HOGENOM; CLU_019240_0_0_9; -.
DR   OrthoDB; 9804078at2; -.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:TreeGrafter.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   FunFam; 1.10.10.410:FF:000001; Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 1.
DR   FunFam; 1.10.150.380:FF:000001; Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; 1.
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   NCBIfam; NF004012; PRK05477.1-2; 1.
DR   NCBIfam; NF004014; PRK05477.1-4; 1.
DR   NCBIfam; NF004015; PRK05477.1-5; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_0000148859"
FT   REGION          1..295
FT                   /note="Cradle"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   REGION          413..475
FT                   /note="Tail"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00121"
SQ   SEQUENCE   475 AA;  53803 MW;  D24D52CE1C4F49F7 CRC64;
     MKYEAVIGLE VHAELLTDSK IFCGCSTKFG SEPNTQVCPV CLGLPGTLPV LNKKVVEYAV
     RAGLALNCTI ANFSKMDRKN YFYPDLPKAY QISQYDLPLC SNGYIEIEVE GGTKRIGIKR
     IHIEEDAGKL LHEGTDGSLV DYNRAGVPLI EIVSEPDIST PEEAYQYLVK LKSILEYTEV
     SDCKMQEGSL RVDTNVSVRP VGTTELGTKI ELKNLNSFKA VQKALEYEIK RQIKVLEEGG
     TIVQETRRWN EAKGITEPMR TKEEAHDYRY FPEPDLVPII VTEEWKEEIR KTLPEMPDAK
     RERFITQYGL PEYDAKVITS SKKMADFFEK CASNYHSPKI VSNWLMGEFA RLLNDTGKEI
     DEVPITPDML IELLKLVDDN VISGSIAKTV FEEMFFTGKN PQIIVEEKGL RQIADEGELR
     RIVRKVIEEN PKSVEDYKKG KEKALGFLVG QVMKETKGKA NPQLTNQLLR EELSK
//