GATD_PYRHO
ID GATD_PYRHO Reviewed; 438 AA.
AC O59132;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=PH1463;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30570.1; -; Genomic_DNA.
DR PIR; B71021; B71021.
DR RefSeq; WP_010885545.1; NC_000961.1.
DR AlphaFoldDB; O59132; -.
DR SMR; O59132; -.
DR STRING; 70601.3257887; -.
DR PRIDE; O59132; -.
DR EnsemblBacteria; BAA30570; BAA30570; BAA30570.
DR GeneID; 1443783; -.
DR KEGG; pho:PH1463; -.
DR eggNOG; arCOG01924; Archaea.
DR OMA; RKNHTSR; -.
DR OrthoDB; 61613at2157; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..438
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140061"
FT DOMAIN 92..422
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 102
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 178
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 179
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ SEQUENCE 438 AA; 49115 MW; 50A2FC5F377E8FBF CRC64;
MRVEEFLKEK NINIGDFIRV IKEEDGEEVI YEGYVMPPYE LSPGDTLVLK LENGYNIGIA
LSKIRRVEVI ERAKVKPEIH FEAFIEGKPH LPDVTIIGTG GTIASRIDYE TGAVYPAFTA
EELAKAVPEI FEIANIKPKL LFNIFSEDMK PKHWIKIAHE VAKSLNSGDS GVVVAHGTDT
MGYTAAALSF MLRDLGKPVI LVGAQRSSDR PSSDAAMNLI CSVRMSTSDV AEVMVVMHGE
TGDTYCLAHR GTKVRKMHTS RRDAFRSIND VPIAKVWPNG KIEFLRDDYR RRSDSEVWVD
DKLEEKVALV KVYPGISSEI IEFFIDKGYR GIVIEGTGLG HTPNDIIPSI QRATEEGIAV
CMTSQCIYGR VNLNVYATGR RLLKAGVIPC EDMLPETAYV KLMWVLGHTQ DLEEVRRMML
TNYAGEITPY TRFDTYLR
