ID GATA_RHOPB Reviewed; 492 AA.
AC Q215W8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=RPC_2264;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; CP000301; ABD87818.1; -; Genomic_DNA.
DR AlphaFoldDB; Q215W8; -.
DR SMR; Q215W8; -.
DR STRING; 316056.RPC_2264; -.
DR KEGG; rpc:RPC_2264; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_5; -.
DR OrthoDB; 9811471at2; -.
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.
FT CHAIN 1..492
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000241145"
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 492 AA; 52024 MW; C2AE025E289266AB CRC64;
MTDLTSLTLA EARDGLAAKS FSSLQLTDAH LAAIEAARVL NAFVLETPDQ ARSMAKAADA
KIAKGEGGPL EGLPLGIKDL FATSGVRTTA CSKILDDFTP PYESTVTSQL WRDGAVLLGK
LNNDEFAMGS SNETSCFGPV VNPWRREGSD AKLVPGGSSG GSASAVAAGL CLGATATDTG
GSIRQPAAFT GTVGIKPTYG RCSRWGIVAF ASSLDQAGPI ARTVRDSAIL LRSMAGYDAK
DTTSVDRAVP DYEAAVGRSV KGMKIGIPKE YRIGGMPAEI EALWKQGADW LKAAGAELVE
VSLPHTKYAL PAYYIVAPAE ASSNLARYDG VRYGARVNGR NITEMYENTR AQGFGAEVIR
RIMIGTYVLS AGYYDAYYLR AQKVRTLIKR DFEECFAKGV SAILTPATPS AAFGIGEKGG
ADPVEMYLND IFTVTVNMAG LPGIAVPAGR DSQGLPLGLQ LIGRPFDEET LFSLGEVIEQ
AAGRFTAAKW WI
//
