GATA_HELPY
ID GATA_HELPY Reviewed; 453 AA.
AC P56114;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, 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=HP_0830;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07880.1; -; Genomic_DNA.
DR PIR; F64623; F64623.
DR RefSeq; NP_207623.1; NC_000915.1.
DR RefSeq; WP_000631468.1; NC_018939.1.
DR AlphaFoldDB; P56114; -.
DR SMR; P56114; -.
DR DIP; DIP-3178N; -.
DR IntAct; P56114; 8.
DR MINT; P56114; -.
DR STRING; 85962.C694_04255; -.
DR PaxDb; P56114; -.
DR EnsemblBacteria; AAD07880; AAD07880; HP_0830.
DR KEGG; hpy:HP_0830; -.
DR PATRIC; fig|85962.47.peg.885; -.
DR eggNOG; COG0154; Bacteria.
DR OMA; EVSCPHF; -.
DR PhylomeDB; P56114; -.
DR Proteomes; UP000000429; 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..453
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105166"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 152
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 49653 MW; A35814B32F1AE13A CRC64;
MITLKQALSL SQDELETLKN EIDAKVRASD LNAYIKAPSL NGASAKGVPI LIKDNISVKG
WEITCSSKIL EGYVAPYHAS VMENLHQNSM AGFGLSNMDE FAMGSTTESS CYGITKNPRD
KNRVPGGSSG GSAAAVAGGL AVAALGSDTG GSIRQPASYC GCVGLKPTYG RVSRYGLIAY
CSSFDQIGPI TQNVEDASIL FDAISGYDSK DSTSANLKPT QTFKNLNRDK RFKIAVLMDH
IKDASNEVQL AYENTLKALK EMGHEIVEKK MLDSHYQISI YYIISMAEAS SNLARFDGVR
YGRRAQNIKD LKELYLKSRS EGFGDEVKRR IMLGNFVLSS GYYDAYYLKA QQMRLIIKEQ
YNKIFEEVDL IFTPVAPTSA HLFNYHASPL EMYLSDIYTI GANLSGLPAL SLPVAKDPLG
LPIGMQFIAK AFDEQSLLDV SYALEQELDL KLD
