ID A0A4E0QAN4_9EURY Unreviewed; 426 AA.
AC A0A4E0QAN4;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D {ECO:0000256|HAMAP-Rule:MF_00586, ECO:0000256|RuleBase:RU004457};
DE Short=Glu-ADT subunit D {ECO:0000256|HAMAP-Rule:MF_00586};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_00586, ECO:0000256|RuleBase:RU004457};
GN Name=gatD {ECO:0000256|HAMAP-Rule:MF_00586};
GN ORFNames=CUN85_06720 {ECO:0000313|EMBL:TGC09517.1};
OS Methanolobus halotolerans.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=2052935 {ECO:0000313|EMBL:TGC09517.1, ECO:0000313|Proteomes:UP000297295};
RN [1] {ECO:0000313|EMBL:TGC09517.1, ECO:0000313|Proteomes:UP000297295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY-01 {ECO:0000313|EMBL:TGC09517.1,
RC ECO:0000313|Proteomes:UP000297295};
RA Shen Y., Huang H.-H., Lai M.-C., Chen S.-C.;
RT "Isolation and Characterization of Methanogenic Archaea from Saline
RT Meromictic Lake at Siberia.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00586,
CC ECO:0000256|RuleBase:RU004457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl-
CC tRNA(Gln) + L-glutamate + ADP + phosphate + H(+);
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:0000256|HAMAP-Rule:MF_00586,
CC ECO:0000256|RuleBase:RU004457};
CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000256|HAMAP-
CC Rule:MF_00586, ECO:0000256|RuleBase:RU004457}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00586, ECO:0000256|RuleBase:RU004457}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TGC09517.1}.
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DR EMBL; PGGK01000005; TGC09517.1; -; Genomic_DNA.
DR RefSeq; WP_135389555.1; NZ_PGGK01000005.1.
DR AlphaFoldDB; A0A4E0QAN4; -.
DR OrthoDB; 371959at2157; -.
DR Proteomes; UP000297295; Unassembled WGS sequence.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-UniRule.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P: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; 3.40.50.40; -; 1.
DR Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 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 NCBIfam; TIGR00519; asnASE_I; 1.
DR NCBIfam; TIGR02153; gatD_arch; 1.
DR NCBIfam; NF003217; PRK04183.1; 1.
DR PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR PANTHER; PTHR11707; L-ASPARAGINASE; 1.
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; GatD N-terminal domain-like; 1.
DR SUPFAM; SSF53774; Glutaminase/Asparaginase; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00586};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00586};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00586};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00586}; Reference proteome {ECO:0000313|Proteomes:UP000297295};
KW Transferase {ECO:0000313|EMBL:TGC09517.1}.
FT DOMAIN 3..52
FT /note="GatD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18195"
FT DOMAIN 80..268
FT /note="L-asparaginase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00710"
FT DOMAIN 294..405
FT /note="Asparaginase/glutaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17763"
FT ACT_SITE 89
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00586,
FT ECO:0000256|PROSITE-ProRule:PRU10099"
FT ACT_SITE 165
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00586,
FT ECO:0000256|PROSITE-ProRule:PRU10100"
FT ACT_SITE 166
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00586"
FT ACT_SITE 242
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00586"
SQ SEQUENCE 426 AA; 45956 MW; 6B7DDDB5F46AF451 CRC64;
MEFEEGDRIK IEKDGVEYEG VVMPSTTRHI VIKMISGYNA GIDPENASIK VVQKKKAANN
TLVAARGPDI SVERPASLPK VSILSTGGTI ASKIDYRTGA VTASFSADDI LQAIPELKEI
ADFSGRAIYN ILSENMKADY WQVLAKAIAE EIGKGADGII VAHGTDTMMY SAAALSFMIE
TPVPIVFVGS QRSADRPSSD NAMNAICAAL VAVSDIAEVT VVMHDDESDG RCAVHRGTKV
RKMHTSRRDA FRSVNADPIA YVDYTGRELH ATSTYTKRGA RQLELNDSLE PRCALVKFTP
GASPEILSYF TDAGYRGLVI EGTGLGHVST EWIPHIENVI RSGIPVVVTS QCISGRVCNR
VYDTGRDILK AGAIEGEDML PEVALVKLMW ALGQSDDIDT VAEIMTNAIA GEISERTLVS
ACECHE
//
