ID   GATD_METMA              Reviewed;         425 AA.
AC   Q8PUM7;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 1.
DT   01-MAY-2013, entry version 63.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D;
DE            Short=Glu-ADT subunit D;
DE            EC=6.3.5.-;
GN   Name=gatD; OrderedLocusNames=MM_2306;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in
CC       organisms which lack glutaminyl-tRNA synthetase. The reaction
CC       takes place in the presence of glutamine and ATP through an
CC       activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is
CC       specific for glutamate and does not act on aspartate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP
CC       + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
CC   -!- SUBUNIT: Heterodimer of GatD and GatE (By similarity).
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily.
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DR   EMBL; AE008384; AAM32002.1; -; Genomic_DNA.
DR   RefSeq; NP_634330.1; NC_003901.1.
DR   ProteinModelPortal; Q8PUM7; -.
DR   STRING; 192952.MM_2306; -.
DR   EnsemblBacteria; AAM32002; AAM32002; MM_2306.
DR   GeneID; 1480648; -.
DR   KEGG; mma:MM_2306; -.
DR   eggNOG; COG0252; -.
DR   HOGENOM; HOG000227975; -.
DR   KO; K09482; -.
DR   OMA; KKEHASN; -.
DR   ProtClustDB; PRK04183; -.
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:HAMAP.
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:HAMAP.
DR   HAMAP; MF_00586; GatD; 1; -.
DR   InterPro; IPR006033; AsnASEI.
DR   InterPro; IPR006034; Asparaginase/glutaminase.
DR   InterPro; IPR020827; Asparaginase/glutaminase_CS.
DR   InterPro; IPR011878; GatD.
DR   Pfam; PF00710; Asparaginase; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; Asp/Glutamnse; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    425       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit D.
FT                                /FTId=PRO_0000140054.
FT   ACT_SITE     95     95       By similarity.
FT   ACT_SITE    171    171       By similarity.
FT   ACT_SITE    172    172       By similarity.
FT   ACT_SITE    248    248       By similarity.
SQ   SEQUENCE   425 AA;  45845 MW;  C96DEF778096625D CRC64;
     MEFKQGDRVR IEKNGTVYEG KVMPSMEGYI TIKMKSGYNA GFSIDKVSIT PLENNGEAAN
     GGNGGKNGQK EPEPAKEKVS KPGLPKVSIL STGGTIASKI DYRTGAVTSQ FTADDILAAI
     PELKEIADFK GRAISSILSE NMDPDSWQNL ARAVVEEIEA GADGIIVTHG TDTMMYSAAA
     LSFMIETPVP IVFVGSQRSA DRPSSDNAMN AICAARVAIS DIAEVVVVMH GTSSDDYCEI
     HRGTKVRKMH TSRRDAFKSV NSLPIGTVDY DTGEIKTFIE YTGRGEKSLK FKPGMEPKCA
     IVKFTPGADP SVLDCYVDGG YKGLVLEGTG LGHVSTKWIP FIRRAVDAKM PVIVTSQCLN
     GRVCDRVYDT GRDMLKAGAI EGEDTLPETA LVKLMWVLGQ TDEFEKAVSM LGENLSGEIN
     ECTLR
//