ID GATB_THET8 Reviewed; 469 AA.
AC Q9LCX2; Q5SLC7;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=TTHA0366;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=10913601; DOI=10.1016/s0014-5793(00)01697-5;
RA Becker H.D., Min B., Jacobi C., Raczniak G., Pelaschier J., Roy H.,
RA Klein S., Kern D., Soell D.;
RT "The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can
RT also generate Gln-tRNA(Gln).";
RL FEBS Lett. 476:140-144(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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).
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; AF202448; AAF91177.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70189.1; -; Genomic_DNA.
DR RefSeq; WP_011227883.1; NC_006461.1.
DR RefSeq; YP_143632.1; NC_006461.1.
DR PDB; 3KFU; X-ray; 3.00 A; F/I=1-396.
DR PDBsum; 3KFU; -.
DR AlphaFoldDB; Q9LCX2; -.
DR SMR; Q9LCX2; -.
DR EnsemblBacteria; BAD70189; BAD70189; BAD70189.
DR GeneID; 3169083; -.
DR KEGG; ttj:TTHA0366; -.
DR PATRIC; fig|300852.9.peg.366; -.
DR eggNOG; COG0064; Bacteria.
DR HOGENOM; CLU_019240_0_0_0; -.
DR PhylomeDB; Q9LCX2; -.
DR EvolutionaryTrace; Q9LCX2; -.
DR Proteomes; UP000000532; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.410; -; 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; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..469
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148858"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 39..43
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 110..121
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 156..173
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3KFU"
SQ SEQUENCE 469 AA; 52236 MW; 10D01DFF9C9B0625 CRC64;
MYEAVIGLEV HLHLKTRTKM FCGCRADYFG AEPNTHTCPV CLGLPGALPV PNRVAVEHGL
RLALALGAEV PERLVFHRKN YFYPDLPKNY QISQYDLPLG RGGSLPLGER RVRIKRLHLE
EDAGKSLHLE GRTLLDLNRA GSPLIELVTE PDLKTPEEAR LFLQRIQALV QTLGISDASP
EEGKLRADVN VSVRRVGEPL GTKVEIKNLN SFKSVQRALE YEIRRQTEIL RRGEKVKQAT
MGFEEGSGKT YPMRTKEEEA DYRYFPEPDL PPVAIPRDWL EEVRRSLPEL PWEKEARYRA
LGIKEKDAEV LAYTPSLARF LDQALPLGLA SPQALANWLL ADVAGLLHER GLRLEETRLS
PEGLARLVGL FERGEVTSRV AKSLLPEVLE GQDPEALVRE RGLKVVADEG ALKALVAEAI
AAMPEAAESV RQGKVKALDA LVGQVMRKTR GQARPDLVRR LLLEALGVG
//
