GATA_GEOSW
ID GATA_GEOSW Reviewed; 486 AA.
AC C5D4K6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=GWCH70_0287;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) 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; CP001638; ACS23214.1; -; Genomic_DNA.
DR RefSeq; WP_012749031.1; NC_012793.1.
DR AlphaFoldDB; C5D4K6; -.
DR SMR; C5D4K6; -.
DR STRING; 471223.GWCH70_0287; -.
DR EnsemblBacteria; ACS23214; ACS23214; GWCH70_0287.
DR KEGG; gwc:GWCH70_0287; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1239251at2; -.
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.
FT CHAIN 1..486
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_1000203038"
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 486 AA; 53043 MW; 7B59C1C61B93A7C8 CRC64;
MSLFDHKISE LHTLLQKKEI SVSDLVDESF RRIGEVEEQV QAFLTLNEEN ARAKAKELDD
KLAKEGNDFG VLFGMPIGIK DNIVTKGLRT TCASKILYNF DPIYDATVME RLNEAGAITI
GKLNMDEFAM GSSTENSGFQ LTRNPWDLER VPGGSSGGSA AAVAAGEVPF ALGSDTGGSI
RQPAAFCGVV GLKPTYGRVS RFGLVAFASS LDQIGPITRT VEDNAYLLQV IAGLDPMDST
SANVEVPNYV EALTGDIKGL KIAVPKEYLG EGVAEEVRQS VLDALKVLEK LGATWEEVSL
PHSKYALATY YLLASSEASA NLARFDGVRY GYRTDNAKNL IDMYKQTRSE GFGNEVKRRI
MLGTFALSAG YYDAYYKKAQ QVRTLIKQDF EKVFEKYDVI IGPTTPTPAF KIGEKTHDPL
TMYANDILTI PVNLAGVPGI SVPCGFVNGL PVGLQIIGKH FDESTIYRVA HAFEQATDYH
KQKPAL