GATD_METS5
ID GATD_METS5 Reviewed; 439 AA.
AC A4YHH3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Msed_1720;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP95875.1; -; Genomic_DNA.
DR RefSeq; WP_012021662.1; NC_009440.1.
DR AlphaFoldDB; A4YHH3; -.
DR SMR; A4YHH3; -.
DR STRING; 399549.Msed_1720; -.
DR EnsemblBacteria; ABP95875; ABP95875; Msed_1720.
DR GeneID; 5105083; -.
DR GeneID; 59457162; -.
DR KEGG; mse:Msed_1720; -.
DR eggNOG; arCOG01924; Archaea.
DR HOGENOM; CLU_019134_2_1_2; -.
DR OMA; RKNHTSR; -.
DR Proteomes; UP000000242; 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..439
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_1000072590"
FT DOMAIN 88..419
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 98
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 174
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 253
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ SEQUENCE 439 AA; 48733 MW; 666B8275B5E3EB9E CRC64;
MLEGYRGKAL ELLSSLGAEI GDVLQVYNDK VSVKGILMPS YSRDDSVIVL KLDNGYNAGF
SVNKVKVSLL EKGNRPQERS EHRELLPGKV KIISTGGTIV SKVEYETGAV RPALSTEEII
RFVPEIQEIT SISAEILFSI LSENMKPEFW VKIAEAVKRA FDEGSEGVVV AHGTDTMSYT
AAALAFSIQR LPGPVVLVGS QRSSDRPSSD SGINLVSSVL LAKEAPFGEV VVNMHGESSD
TYTLAHRGVK VRKMHTSRRD AFQSINDHPL AKVLWKERTV KVLRNDYLRR SDGVELNPKF
ENRVFLLKFY PGLRPDIVDI LLSSGYRGII VEGTGLGHTS SDFQEAFKRA VKEGLFVGMT
SQCLFGRVNM NVYQTGRLLQ QSGVVPLGDM LPEVALVKLM WALGQTSDLE EVKRIMLTNL
VGEYNPRHSL DHFPRWKHE
