ID   GATD_SULIN              Reviewed;         445 AA.
AC   C3NHQ2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=YN1551_1574;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP48662.1; -; Genomic_DNA.
DR   RefSeq; WP_012711295.1; NC_012623.1.
DR   AlphaFoldDB; C3NHQ2; -.
DR   SMR; C3NHQ2; -.
DR   EnsemblBacteria; ACP48662; ACP48662; YN1551_1574.
DR   GeneID; 7809167; -.
DR   GeneID; 7941020; -.
DR   GeneID; 8761218; -.
DR   KEGG; sin:YN1551_1574; -.
DR   HOGENOM; CLU_019134_2_1_2; -.
DR   OMA; RKNHTSR; -.
DR   Proteomes; UP000006818; 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; 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; 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.
FT   CHAIN           1..445
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT                   /id="PRO_1000212153"
FT   DOMAIN          93..425
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ   SEQUENCE   445 AA;  49813 MW;  0AA21AD803DDC3CE CRC64;
     MQENYKAKAY DILKNLNIEE GDLIEIKKGD LRIRGILLPS YSKDERIFVI KLDNGYNIGI
     SIDNISEIKL ITKNSSKAQE SERKEVSRNG AKSEIKIIST GGTIVSKVEY ETGAVRPALT
     TEEIVQFLPE INEIAKVDAE VLFSILSENM KPEYWVKIAE SVKKAFDEGN TGVVIAHGTD
     TMAYTASALA FSLRSLQGPV VLVGSQRSSD RPSSDSAINL LSAVTTAKYA PFGEVVVNMH
     ADSSDTYALV HRGVKVRKMH SSRRDAFQSV NDKPLAKVLW KERKLVMLDK SYMSKKGETT
     LDAKFDNRAF LLYYYPGLDR DFLEHILTNT KIRGLIIAGT GLGHTSSDYV ELFRKATKDG
     IFIGMTTQCL FGRVNMNVYT TGRQLLDAGV TPLEDMLPEV ALVKLMWVLA HEQDLEKIRS
     LMISNLVGEI NPRHTLDLFP RWSYE