GATD_THEKO
ID GATD_THEKO Reviewed; 440 AA.
AC Q5JI77;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, 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=TK0908;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85097.1; -; Genomic_DNA.
DR RefSeq; WP_011249859.1; NC_006624.1.
DR AlphaFoldDB; Q5JI77; -.
DR SMR; Q5JI77; -.
DR STRING; 69014.TK0908; -.
DR EnsemblBacteria; BAD85097; BAD85097; TK0908.
DR GeneID; 3235851; -.
DR KEGG; tko:TK0908; -.
DR PATRIC; fig|69014.16.peg.887; -.
DR eggNOG; arCOG01924; Archaea.
DR HOGENOM; CLU_019134_2_1_2; -.
DR InParanoid; Q5JI77; -.
DR OMA; RKNHTSR; -.
DR OrthoDB; 61613at2157; -.
DR PhylomeDB; Q5JI77; -.
DR Proteomes; UP000000536; 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..440
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140062"
FT DOMAIN 94..424
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 104
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 180
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 181
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 258
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ SEQUENCE 440 AA; 48941 MW; 8C0259558E783308 CRC64;
MKRKVDEFME RHGLGVGDLV RVVKREGDER ITFEGLVMPP YELSPGETLT IKLDNGYNIG
ILIDAIEGIE ILEKAKEAPK MEFREVLPRK EGLPSVTILG TGGTIASRID YKTGAVHAAF
TAEELAKAVP EIFDIANITP KLLFNIMSED MKPEYWKKIA HEAAKALNSD EDGVVIAHGT
DTMGYTAAAL SFMLRNLTKP VVLVGSQRSS DRPSSDAAMN LICATRMAVS DAAEVMVVMH
GETSDTYCLA HRGTKVRKMH TSRRDTFRSI NDVPIAKVWP DGKIEYLRDD YRKRGEGEVE
VDDKFEEKVA ILKIYPGVTS ELLEFLVDRG YKGIVIEGTG LGHTPNDMIP AIERAVENGV
AVCMTSQCLY GRVNLNVYST GRRLLKAGVI PCEDMLPETA YVKLGWVLGH TDDLKEVRRM
MLTNYAGEIT PYTRFDTFLR
