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GATD_THEPD
ID   GATD_THEPD              Reviewed;         451 AA.
AC   A1RX40;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Tpen_0361;
OS   Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC   Thermofilum.
OX   NCBI_TaxID=368408;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2475 / Hrk 5;
RX   PubMed=18263724; DOI=10.1128/jb.01949-07;
RA   Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA   Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA   Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA   Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT   "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT   biosynthetic pathways without genome reduction.";
RL   J. Bacteriol. 190:2957-2965(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; CP000505; ABL77770.1; -; Genomic_DNA.
DR   RefSeq; WP_011752035.1; NC_008698.1.
DR   AlphaFoldDB; A1RX40; -.
DR   SMR; A1RX40; -.
DR   STRING; 368408.Tpen_0361; -.
DR   EnsemblBacteria; ABL77770; ABL77770; Tpen_0361.
DR   GeneID; 4601490; -.
DR   KEGG; tpe:Tpen_0361; -.
DR   eggNOG; arCOG01924; Archaea.
DR   HOGENOM; CLU_019134_2_1_2; -.
DR   OMA; RKNHTSR; -.
DR   OrthoDB; 61613at2157; -.
DR   Proteomes; UP000000641; 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..451
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit D"
FT                   /id="PRO_1000082414"
FT   DOMAIN          99..432
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   REGION          78..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00586"
SQ   SEQUENCE   451 AA;  49356 MW;  38B02BF3C1901C72 CRC64;
     MSQGYSEKVK ELLDSVGAAF FDRVKIKLAD GLVLEGLLMP RPAFGDPDVV VLKLDNGYNI
     GISLQRIVSV ELLEKFSPRE APTPGEEEGS QEDFGQPEPR VFFVGTGGTI ASRVDYVTGA
     VYPYFTAEEL YSMIPELKRL ARISSETLFS IFSEDMTPSH WQQLASKIGE IFRRESDVKG
     VVVAHGTDTL HYSAAAMAFA VQEAPGPIVF VGAQRSSDRP SSDAALNVIG ATVVAVHAPF
     AESVIAMHGS VNDDTILVHR GVRARKMHTS RRDAFMSINS KPIAEVDPLR GSLKLSTSTY
     KGRGDDVVVQ ASFSDKVALV KFYPGMSPDI FDFYLEKGFK GLVIEGTGLG HVSTALIDSV
     RRLVREGVFV AMASQCIFGR VNMNVYRTGV ELIKAGVVPA GDMIPETAYV KLSWILGQTE
     DPEEIQRLFT ANLAFEISER SEFDHYPGAR W
 
 
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