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Database: UniProt
Entry: A0A3Q0QP55_AMPCI
LinkDB: A0A3Q0QP55_AMPCI
Original site: A0A3Q0QP55_AMPCI 
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
//
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