ID   GATD_NANEQ              Reviewed;         392 AA.
AC   P61401;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D;
DE            Short=Glu-ADT subunit D;
DE            EC=6.3.5.-;
GN   Name=gatD; OrderedLocusNames=NEQ126;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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 (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE017199; AAR38981.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61401; -.
DR   SMR; P61401; -.
DR   STRING; 228908.NEQ126; -.
DR   EnsemblBacteria; AAR38981; AAR38981; NEQ126.
DR   KEGG; neq:NEQ126; -.
DR   PATRIC; fig|228908.8.peg.131; -.
DR   HOGENOM; CLU_019134_2_1_2; -.
DR   OMA; RKNHTSR; -.
DR   Proteomes; UP000000578; 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;
KW   Reference proteome.
FT   CHAIN           1..392
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT                   /id="PRO_0000140057"
FT   DOMAIN          68..391
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
FT   ACT_SITE        229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
SQ   SEQUENCE   392 AA;  44210 MW;  EC636D58AB540E9C CRC64;
     MVGELYRFIT DFGVIEGYII KEEPNYYLIK LKNGYNIGIK KSQIKEMENL NEKIKVGQFP
     KRKPKGIGNL GFIYTGGTIG SKVDYLTGGV SAIMDIEELL AIADLPYDIK IIDSPFVKFS
     EDLNPKDWVE IVKSIERTYK KGAEGIIVAH GTDTMHFSSA YAYYALENPI PIAFTGAQRS
     SDRASTDAVI NLFASSIYAN SNIGEVAIVM HETINDDTAI AIRGISARKM HSTRRDAFKS
     INEEPLARIY YPSGKLEIIN KKYRKRSDKE MVAKPYLDTK GALIWVYPGF DPSILEYYRN
     YRGIIIAGTG MGHTSKELIP MLKELSKDLF IGITTQCIYG ITHPYVYSRG RELSKFATYL
     QGTPEKNYVK LLYVLGKESD LDGIKKEMKR LP