ID A0A0F7DBU0_9EURY Unreviewed; 455 AA.
AC A0A0F7DBU0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|ARBA:ARBA00014428, ECO:0000256|HAMAP-Rule:MF_00120};
DE Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE EC=6.3.5.7 {ECO:0000256|ARBA:ARBA00012739, ECO:0000256|HAMAP-Rule:MF_00120};
GN Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120};
GN ORFNames=GAH_00999 {ECO:0000313|EMBL:AKG91676.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG91676.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG91676.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG91676.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) 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:0000256|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:0000256|ARBA:ARBA00001243, ECO:0000256|HAMAP-
CC Rule:MF_00120};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC Rule:MF_00120}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000256|ARBA:ARBA00008069, ECO:0000256|HAMAP-Rule:MF_00120}.
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DR EMBL; CP011267; AKG91676.1; -; Genomic_DNA.
DR RefSeq; WP_048095037.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7DBU0; -.
DR STRING; 113653.GAH_00999; -.
DR GeneID; 24803575; -.
DR KEGG; gah:GAH_00999; -.
DR PATRIC; fig|113653.22.peg.997; -.
DR HOGENOM; CLU_009600_0_3_2; -.
DR InParanoid; A0A0F7DBU0; -.
DR OrthoDB; 7931at2157; -.
DR Proteomes; UP000034723; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF7; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A, MITOCHONDRIAL; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00120};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00120};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00120};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00120}; Reference proteome {ECO:0000313|Proteomes:UP000034723};
KW Transferase {ECO:0000313|EMBL:AKG91676.1}.
FT DOMAIN 18..444
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 67
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 166
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 455 AA; 50537 MW; 96F4322D739466D4 CRC64;
MITVREWKER LEEEKAYDLV SELIEKIEKS RLNAYVTVTK EEALKKAEEY DRGRRDGRLA
GIPVAIKDNI STEGIRTTCG SRMLENYIPP YDAHVVERLK QEGAIIIGKT NMDEFGMGTT
TETSYFGVVR NPHDLKRVAG GSSGGSAAAI AGDETVLSLG TDTGGSIRCP SSFTGVYGLK
PTYGLVSRFG LIAYANSLEQ IGPMAASIDD LGFLLEIIAG RDDRDSTNSG REFSYRPVSK
RFRVGVVEEM QANPEVQQVF EEFVERLRKI ADVETVSLPS LKYALPAYYV IAMSEASSNL
ARYDGVRYGY ALENLDSWNR YFSRVRAEGF GAEVKRRIMM GSYALSAGYY GKYYLKALKV
RTLVINDFRR AFEKFDVLIS PTMPSTAFKI GELTDPVTMY KADVNTTPIN LAGLPALSMP
VRELDGLPVG LQVIGNHFEE NTILGFAKQV EEHEV
//
