GATD_METAC
ID GATD_METAC Reviewed; 424 AA.
AC Q8TR66;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 106.
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}; Synonyms=ansA;
GN OrderedLocusNames=MA_1317;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04734.1; -; Genomic_DNA.
DR RefSeq; WP_011021336.1; NC_003552.1.
DR AlphaFoldDB; Q8TR66; -.
DR SMR; Q8TR66; -.
DR STRING; 188937.MA_1317; -.
DR EnsemblBacteria; AAM04734; AAM04734; MA_1317.
DR GeneID; 1473205; -.
DR KEGG; mac:MA_1317; -.
DR HOGENOM; CLU_019134_2_1_2; -.
DR InParanoid; Q8TR66; -.
DR OMA; RKNHTSR; -.
DR OrthoDB; 61613at2157; -.
DR PhylomeDB; Q8TR66; -.
DR Proteomes; UP000002487; 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..424
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT /id="PRO_0000140051"
FT DOMAIN 84..413
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT REGION 56..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 171
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT ACT_SITE 247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ SEQUENCE 424 AA; 46108 MW; B4D6F03C17E3771A CRC64;
MEFKQGDWVR IERNGTVYEG KVMPSMEGYI TIKMKSGYNA GFSIDKVRIT LLENNGETAN
GSRNGGKGCK TNEEELPEPG KKLPKIAILS TGGTIASKID YRTGAVTSQF TADDILAAIP
ELKEIADFKG RVISSILSEN MDSDSWQNLS KAVVEEIEAG ADGVIVTHGT DTMMYSAAAL
SFMIKTPVPI VFVGSQRSAD RPSSDNAMNA ICAARVAISD IAEVVVVMHG TTSDDFCEIH
RGTKVRKLHT SRRDAFKSVN SLPVGTVDYG TGEIKTFIDY TRRGEKALKF KPGMEPKCAL
VKFTPGADPT VLDYYISNGY KGLVVEGTGL GHISTKWIPL LRKATDAKMP VIVTSQCLNG
RICDRVYDTG RDMLKAGAIE GEDTLPETAL VKLMWVLGQT DDFEKAAGML REDLSGEITE
CTQR
