GATA_XANP2
ID GATA_XANP2 Reviewed; 494 AA.
AC A7IMA7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, 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=Xaut_3926;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-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; CP000781; ABS69150.1; -; Genomic_DNA.
DR RefSeq; WP_012115898.1; NC_009720.1.
DR AlphaFoldDB; A7IMA7; -.
DR SMR; A7IMA7; -.
DR STRING; 78245.Xaut_3926; -.
DR EnsemblBacteria; ABS69150; ABS69150; Xaut_3926.
DR KEGG; xau:Xaut_3926; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1239251at2; -.
DR PhylomeDB; A7IMA7; -.
DR Proteomes; UP000002417; 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_1000095179"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 182
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
SQ SEQUENCE 494 AA; 53088 MW; 0422CE53821CEF84 CRC64;
MTKLTQLTLT QAREGLAQGE FTSVELTEAY LKAMEQARPL NAYVLETPEI ALEMAKESDR
RIASGETGPL EGIPLGIKDM FATEGVRTTA CAKILDNFIP QYESTVTSHL WRDGAVLLGK
LNNDEFAMGS SNETSAFGPV VSPWRRDGDE TPLVPGGSSG GSAAAVAAFL CAGATGTDTG
GSIRQPAAFT GTVGIKPTYG RCSRWGIVAF ASSLDQAGPF ARTVNDAAVL LKSMAGYDPK
DSTCVNRPVP DYEEAVGASI KGKKIGIPRE YRMDGMSDEI DALWTEGARF LKDAGAEIVD
ISLPHTQYAL PAYYIVAPAE ASSNLARYDG VRFGERVPGR DVVEMYENTR AAGFGPEVRR
RIMIGTYVLS AGYYDAYYLR AQKVRSLIKR DFDQVFAQGV DAVLTPATPS PAFGIGEKLK
ADPVEMYLND VFTVTVNMAG LPGIAVPAGL SADGLPLGLQ LIGRPFEEET LFSLAEVIEE
AAGRFPVDKQ WWRG