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Database: UniProt/SWISS-PROT
Entry: GATA_CAUSK
LinkDB: GATA_CAUSK
Original site: GATA_CAUSK 
ID   GATA_CAUSK              Reviewed;         490 AA.
AC   B0T193;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120};
GN   OrderedLocusNames=Caul_1520;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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
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). {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP +
CC         H(+) + 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         EC=6.3.5.7; Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00120}.
DR   EMBL; CP000927; ABZ70650.1; -; Genomic_DNA.
DR   RefSeq; WP_012285575.1; NC_010338.1.
DR   SMR; B0T193; -.
DR   STRING; 366602.Caul_1520; -.
DR   EnsemblBacteria; ABZ70650; ABZ70650; Caul_1520.
DR   KEGG; cak:Caul_1520; -.
DR   eggNOG; ENOG4105C3P; Bacteria.
DR   eggNOG; COG0154; LUCA.
DR   HOGENOM; HOG000116699; -.
DR   KO; K02433; -.
DR   OMA; MYLSDIF; -.
DR   OrthoDB; 1239251at2; -.
DR   Proteomes; UP000001316; Chromosome.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0004040; F:amidase 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   TIGRFAMs; TIGR00132; gatA; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN         1    490       Glutamyl-tRNA(Gln) amidotransferase
FT                                subunit A.
FT                                /FTId=PRO_1000076124.
FT   ACT_SITE     78     78       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    158    158       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00120}.
FT   ACT_SITE    182    182       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00120}.
SQ   SEQUENCE   490 AA;  51709 MW;  87DF70ABB00FAAFB CRC64;
     MSSLTSLTLK GALDGLEKGD FTSVELTRAH IDAIEAARGL NAFLLETPEQ ALSMAAASDA
     RRALDAARPL DGIPLGIKDL FCTQGVRTTA ASKILEPFVP QYESTVTSQL WRDGAVMLGK
     LNLDEFAMGS SNETSAYGPV VNPWRKAGSN QALTPGGSSG GSAAAVAADL CLGATATDTG
     GSIRQPAAFT GTVGIKPTYG RCSRWGVVAF ASSLDQAGPI AKTVTDAALL LTSMSGHDPK
     DSTSLDVPVP DFSAFVGKSI KGLRIGVPQE YRVDGMPAEI EKLWADGIAW LKDAGCEIVE
     ISLPHTKYAL PAYYIVAPAE ASSNLARYDG MRYGLRAEGS NLTEVYENTR AEGFGDEVKR
     RILIGTYVLS AGYYDAYYLK ALKVRRRIAE DFDNAWERCD AILTPTAPSA AFGLGENSSD
     PIAMYLNDVF TVTTNLAGLP GLSLPAGLDA NGLPLGLQII GKPLDEGTVF SVAGVLEKAA
     GFTAKATKWW
//
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