ID A0A3N6N0Y5_9EURY Unreviewed; 426 AA.
AC A0A3N6N0Y5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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 ECO:0000313|EMBL:RQG91592.1};
GN ORFNames=EA462_06465 {ECO:0000313|EMBL:RQG91592.1};
OS Natrarchaeobius halalkaliphilus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobius.
OX NCBI_TaxID=1679091 {ECO:0000313|EMBL:RQG91592.1, ECO:0000313|Proteomes:UP000273828};
RN [1] {ECO:0000313|EMBL:RQG91592.1, ECO:0000313|Proteomes:UP000273828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArcht-Sl {ECO:0000313|EMBL:RQG91592.1,
RC ECO:0000313|Proteomes:UP000273828};
RA Sorokin D.Y., Elcheninov A.G., Kostrikina N.A., Bale N.J.,
RA Sinninghe Damste J.S., Khijniak T.V., Kublanov I.V., Toshchakov S.V.;
RT "Natrarchaeobius chitinivorans gen. nov., sp. nov., and Natrarchaeobius
RT haloalkaliphilus sp. nov., alkaliphilic, chitin-utilizing haloarchaea from
RT hypersaline alkaline lakes.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQG91592.1}.
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DR EMBL; REFY01000002; RQG91592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6N0Y5; -.
DR OrthoDB; 7931at2157; -.
DR Proteomes; UP000273828; Unassembled WGS sequence.
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:UP000273828};
KW Transferase {ECO:0000313|EMBL:RQG91592.1}.
FT DOMAIN 13..418
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 82..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 28
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 103
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 127
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 426 AA; 44355 MW; A78F23855C0924F3 CRC64;
MMSNIFITEE TIEGAADGPL AGRTVAVKDN ISTADVRTTC GSTMLEEYVP PYDATVVSRI
KDAGATIVGK ANMDEFGMGT TTETSAFGAT DNPTAPGHVP GGSSGGSAAA VAADEADLAL
GSDTGGSVRC PAAFCGVVGI KPTYGLVSRY GLVAYANSLE QIGPFGETVE DAAALLDVIA
GPDDRDGTTR EPPGSSERPT SYADAATGDV DGLSIGVPTE LLEGADDGVL ETFWDAIGEL
ETRGAKYHEV SLPSVEHAVE AYYVIAMSEA SSNLARFDGV RYGHSGGYDG NWNEAFAAAR
REGFGDEVKR RILLGTYALS AGYHDKYYKK AQDARAWVKQ DFDEALSEAD VLASPTMPVP
PFELGESLDD PLQMYLADAN TVPVNLADLP AISVPAGETD GLPVGLQLVG PSFGEERLVR
VASALS
//
