ID   GATD_PYRAE              Reviewed;         417 AA.
AC   Q8ZY04;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=PAE1003;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL63192.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZY04; -.
DR   SMR; Q8ZY04; -.
DR   STRING; 178306.PAE1003; -.
DR   EnsemblBacteria; AAL63192; AAL63192; PAE1003.
DR   KEGG; pai:PAE1003; -.
DR   PATRIC; fig|178306.9.peg.747; -.
DR   eggNOG; arCOG01924; Archaea.
DR   HOGENOM; CLU_019134_2_1_2; -.
DR   InParanoid; Q8ZY04; -.
DR   OMA; RKNHTSR; -.
DR   Proteomes; UP000002439; 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..417
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT                   /id="PRO_0000140059"
FT   DOMAIN          73..400
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ   SEQUENCE   417 AA;  45459 MW;  5D22FFC48D33A03D CRC64;
     MYKKVRVVLE NGDVFEGVML PPTQFSDSDI VVLKLKNGYN VGFKKGRIKE IVELGEVQTA
     PLSAKPMPKI EGEKVWLLAT GGTILSRVDY VTGGVYPTLS VDYLFEVLGG LEAPIEAEEV
     TAKFSEDMTP ALWGVIAERV AEAFKKGARG VVVLHGTDTM QYTAAALAFA FKSAPGPIAL
     VGAQRSSDRP STDAVLNLKA AIAVTARAPF AESVVVMHKT SGDTVVAVHR GTRVRKMHTS
     RRDTFQSINT TPIAEYYPEK ELLQVLTDVY KERGGLDYTA KFEEAVALVK FYPGMHPRLL
     EALLEVGMKG VVIEGTGFGH VGEGVLPAVK KLIDAGVIVA MTSQTLYGRV NLYVYRRGRE
     LLSMGVIPLE DMLPETAYAK MSWALANFKR EEVPRVLTTP IAYEMSPRSD PLVFGGL