ID GATA_LACLA Reviewed; 486 AA.
AC Q9CJ43;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.7;
GN Name=gatA; OrderedLocusNames=LL0163; ORFNames=L0473;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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) (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005176; AAK04261.1; -; Genomic_DNA.
DR PIR; C86645; C86645.
DR RefSeq; NP_266319.1; NC_002662.1.
DR RefSeq; WP_010905164.1; NC_002662.1.
DR AlphaFoldDB; Q9CJ43; -.
DR SMR; Q9CJ43; -.
DR PaxDb; 272623-L0473; -.
DR EnsemblBacteria; AAK04261; AAK04261; L0473.
DR KEGG; lla:L0473; -.
DR PATRIC; fig|272623.7.peg.181; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000002196; 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; Amidase signature (AS) domain; 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 NCBIfam; TIGR00132; gatA; 1.
DR PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 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..486
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105168"
FT REGION 130..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 176
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 486 AA; 52071 MW; 52FC956059F05EF9 CRC64;
MSYNNKSIKE LHELLVNKEI SALELTKATL SDISAREPQI DAFLKITEEK ALQDAAAIDA
RGINPDVVTD GISIAVKDNI VTEGIETTAA SKILGGWIPP YNATVANKLS ESGLITIGKL
NMDEFAMGGS GENSSVKPTK NAWDQTKVPG GSSSGSAASV ASGQVRLSLG SDTGGSIRQP
AAFNGIVGLK PTYGRVSRFG LIAFASSLDQ IGPLAPTVEE NAQLLNVISG FDKNDSTSSN
VAVPDFTSKI GQDIKGMKIA LPKEYFGEGI DEKVKEQILA AAKHLEKLGA IVEEVSLPHS
KYGVAVYYII ASSEASSNLQ RFDGIRYGYR AQDIKNLEDL YVKSRSEGFG PEVQRRIMLG
TFSLSAGSYD KHFKKAGQVR TLIINDFAKV FEKYDLILGP TTPTPAWDLG ARVDDPLSMY
LADLLTIPVN LAGLPGISIP AGFADGLPVG MQLIGKRYDE ETIYKVAAAF EATTDFHKKQ
PIIFGK
//
