ID A0A3Q0QP55_AMPCI Unreviewed; 491 AA.
AC A0A3Q0QP55;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000256|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_03150};
DE AltName: Full=Glutaminyl-tRNA synthase-like protein 1 {ECO:0000256|HAMAP-Rule:MF_03150};
GN Name=QRSL1 {ECO:0000256|HAMAP-Rule:MF_03150};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000000774.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000000774.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000256|HAMAP-Rule:MF_03150}.
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|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC {ECO:0000256|HAMAP-Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03150}.
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DR AlphaFoldDB; A0A3Q0QP55; -.
DR STRING; 61819.ENSACIP00000000774; -.
DR Ensembl; ENSACIT00000000811.1; ENSACIP00000000774.1; ENSACIG00000000661.1.
DR GeneTree; ENSGT00550000074866; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial 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; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03150};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03150};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03150};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03150}.
FT DOMAIN 2..459
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 167
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ SEQUENCE 491 AA; 53434 MW; 186A638F4F4914E9 CRC64;
CRKCLNRIKK TQHLNAYITV TEERALEQAQ QSESRLLQGV PKGPLDGIPF AIKDNFCTEN
IRTTCASRML KDYTPPYNAT VVQKLLEQGA VLVGKTNMDE FAMGAGSTDG AFGPVKNPWS
YAAPYREQTG EDPDSDWVIA GGSSGGSAAA VASLTSYLAL GSDTGGSTRN PGALCGVVAL
KPTYGLLSRH GLIPLVNSMD VPGIMTRSVN DAAVILGVLQ GLDVRDSTTV PAPSSLTEFP
EDFDVRNICV GIPKEYHAPG LSDETLAQWS HVADLFEKAG ARVEQVSLPH TQYSIVCYHV
LCHAEVASNM ARFDGLEYGH RSKMDSSTEV MYASTRHEGF NDVVRGRILS GNYFLLKQNY
QHYFVKAQKV RRLIANDFHH VFNSGVDVLL TPTTLTDAAR YRDFTQEDNR TRSAQEDVFT
QPANMAGLPA VSVPTALSRR GLPIGLQLLA PALQDKKLLC VAQWIEQRVG FPSVSDCEDL
GMTKQEQTGA A
//