GATA_LACP7
ID GATA_LACP7 Reviewed; 494 AA.
AC A9KJ26;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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}; OrderedLocusNames=Cphy_0638;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) 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). {ECO:0000255|HAMAP-Rule:MF_00120}.
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; EC=6.3.5.7;
CC 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}.
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DR EMBL; CP000885; ABX41025.1; -; Genomic_DNA.
DR AlphaFoldDB; A9KJ26; -.
DR SMR; A9KJ26; -.
DR STRING; 357809.Cphy_0638; -.
DR EnsemblBacteria; ABX41025; ABX41025; Cphy_0638.
DR KEGG; cpy:Cphy_0638; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000000370; Chromosome.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; 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; Ligase; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..494
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000076125"
FT ACT_SITE 80
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 179
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 494 AA; 53426 MW; 638CD933AEA1F9EA CRC64;
MEITKLTAIE LSKKIKQKEL SVEEAVKATF SAIKKREPYY HSYITVNEEE ALEQASKIQI
AIEAGKFADS PLAGVPIAIK DNICVKGMRT TCASKILEDF IPPYNASVIE RLKDAGAIIL
GKTNMDEFAM GSTTETSYFG ATKNPWNIEC IPGGSSGGSA AAVAAEEAFI ALGTDTGGSI
RQPSAFCGVT GIKPTYGTVS RYGLVAYASS LDQIGPIARS VSDCAATLQV ISGADDKDST
CVKAASYDYV SALRSDVRGL RIGIPRGYFS EGLDAEVKKH VLEAAAFFKE QGAIVEEFDL
EAVDYATPAY YVIASAEASS NLSRYDGVKY GYRTADFDGL QELYKKTRSE GFGEEVKRRM
MIGSFVLSSG YYDAYYNKAL KVRALIKQSF DRAFERFDII LGPTTPAAAR KLGQSLFNPV
KMFLGDIYTV SVNLAGLPAI SLPCGLSEES SSDKSAGMPI GLQLIGKPFG EKDIIRAAYT
LEQTKIYQRP KLID
