ID   GATD_HALWD              Reviewed;         442 AA.
AC   Q18GL3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=HQ_2776A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ52884.1; -; Genomic_DNA.
DR   RefSeq; WP_011571998.1; NC_008212.1.
DR   AlphaFoldDB; Q18GL3; -.
DR   SMR; Q18GL3; -.
DR   STRING; 362976.HQ_2776A; -.
DR   EnsemblBacteria; CAJ52884; CAJ52884; HQ_2776A.
DR   GeneID; 4194013; -.
DR   KEGG; hwa:HQ_2776A; -.
DR   eggNOG; arCOG01924; Archaea.
DR   HOGENOM; CLU_019134_2_1_2; -.
DR   OMA; RKNHTSR; -.
DR   Proteomes; UP000001975; 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   CDD; cd08962; GatD; 1.
DR   Gene3D; 2.30.30.520; -; 1.
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; IPR040918; GatD_N.
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   Pfam; PF18195; GatD_N; 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..442
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT                   /id="PRO_1000025454"
FT   DOMAIN          102..429
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   REGION          63..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ   SEQUENCE   442 AA;  46773 MW;  76D6A196B669CAA2 CRC64;
     MSPHPGDRVR VERADVTNEG ILMPSSTSDH LVIKLDGGYN VGIDRADASI DLVTSDAYDI
     GGTQTDIGSS AGAGADTEAD KTESDITSKS AASAVAFDES LPTVSLISTG GTIASTVDYR
     TGAVTAQFDA EDVLRAVPDL AGRANYRGRV VRNILSENMT PAVWQDLAAA VADEIRAGAD
     GVVVMHGTDT MQYSASALSY MLDTPVPVVF TGSQRSADRP SSDNVMNAVC AVEAATADIS
     GVFVCMHAST ADDTCALHRG TRVRKNHTSR RDAFKTVGAT PIGKIEYDTE TVSFHRDHAA
     RESTELNLTS ELNEDVMLLT FTPGMNIDRQ TAFLTDSTPD GLIIAGTGLG HVHTEFIPTV
     AELVADGVVV AMTSQCIEGR VCDRVYDTGR DLLEAGVVEA GDTLPGTAKV KLMWALANHP
     DPTNAMRKSL AGELQHRSVP WE