GATD_THEAC
ID GATD_THEAC Reviewed; 409 AA.
AC Q9HJJ5;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D {ECO:0000255|HAMAP-Rule:MF_00586};
DE Short=Glu-ADT subunit D {ECO:0000255|HAMAP-Rule:MF_00586};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00586};
GN Name=gatD {ECO:0000255|HAMAP-Rule:MF_00586}; OrderedLocusNames=Ta0972;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC tRNA(Gln). The GatDE system is specific for glutamate and does not act
CC on aspartate. {ECO:0000255|HAMAP-Rule:MF_00586}.
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_00586};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP-
CC Rule:MF_00586}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00586}.
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DR EMBL; AL445066; CAC12101.1; -; Genomic_DNA.
DR RefSeq; WP_010901383.1; NC_002578.1.
DR AlphaFoldDB; Q9HJJ5; -.
DR SMR; Q9HJJ5; -.
DR STRING; 273075.Ta0972; -.
DR EnsemblBacteria; CAC12101; CAC12101; CAC12101.
DR GeneID; 1456499; -.
DR KEGG; tac:Ta0972; -.
DR eggNOG; arCOG01924; Archaea.
DR HOGENOM; CLU_019134_2_1_2; -.
DR OMA; RKNHTSR; -.
DR OrthoDB; 61613at2157; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0004067; F:asparaginase activity; IEA:InterPro.
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:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR HAMAP; MF_00586; GatD; 1.
DR InterPro; IPR006033; AsnA_fam.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR011878; GatD.
DR InterPro; IPR037222; GatD_N_sf.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF500175; Glu_ADT_D; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF141300; SSF141300; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00519; asnASE_I; 1.
DR TIGRFAMs; TIGR02153; gatD_arch; 1.
DR PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..409
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140066"
FT DOMAIN 68..390
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 78
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 152
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 153
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 230
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ SEQUENCE 409 AA; 45005 MW; FFBDC4AB39BB53E1 CRC64;
MERAVLRYKN SVISGLIINE SNGLITLKAS NGYNMTFDRS EVEFIERKKE ESPERKSIEA
VEKGQGDRKI SVLATGGTIA SRVDYETGAV SPVSDPELIF GGSDILTRFT VAVKPILNEF
SENLKPADWI RIGQAVADES SEADGVVVAH GTDTMAYTSS ALAFMFERMR VPVVFVGAQR
SSDRPSSDSR ENMQAAINFA GTDLGEVGIS MHASTSDGHV SLLRSVRSRK MHTSRRDAFE
SIGIPPLAEY DGSVKFLIDY RRVSDTVEFR PDLDDRVSMI YFHPGLNAGD LENMIAEKHA
VVILGTGLGH MAKDLIPVVK KYTADGNYAI MASQCIYGST DLNVYSTGRE LLAAGVIEAG
NMVPEVAYVK AMYLLGQYPH DLFRDLFRKN MRGEIVERDL PVEIIKLGR
