ID A0A482WXC6_LAOST Unreviewed; 506 AA.
AC A0A482WXC6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-NOV-2023, entry version 13.
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};
GN Name=GatA {ECO:0000256|HAMAP-Rule:MF_03150};
GN ORFNames=LSTR_LSTR005580 {ECO:0000313|EMBL:RZF38219.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF38219.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF38219.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF38219.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF38219.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
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, B and C subunits. {ECO:0000256|HAMAP-
CC 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}.
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:RZF38219.1}.
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DR EMBL; QKKF02022802; RZF38219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482WXC6; -.
DR STRING; 195883.A0A482WXC6; -.
DR InParanoid; A0A482WXC6; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000291343}.
FT DOMAIN 23..144
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT DOMAIN 167..488
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
FT ACT_SITE 197
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03150"
SQ SEQUENCE 506 AA; 54777 MW; 63797C2C628F56EC CRC64;
MLKLSISEVA STLRDGKISP IDLCEKCLSR ADKVKKLNAF VRILKNESLN CASESQIKFQ
HGKVRSKIEG VAIAVKDNFC TKGITTTCSS KMLNDFVPTY NATVVQRLKD AGSILIGKTN
MDEFAMGSGT VDSIHGVTKN IWGSDIPYML GNKSVNDGIP SKGGTFERVA GGSSGGSAVA
VATGSCFAAL GSDTGGSTRN PAAYCGIVGL KPTYGSVSRF GLIPLVNSMD VPGIMARSVS
DVADVFNVIS GFDENDSTTL ERDKSAVVLN DSFNISSIKV GIPKEYHCPG MSPVVIDAWK
RVANLLEEAG ATVSQVSLPH TGYSIACYSV LNQCEVASNM ARYDGLEYGL RPEQTKSTEQ
LYADSRKHGF NDVVRGRILA GNYFLIQSNY EKYFMKAMKV RRLIANDFKN VWSKVDVLLT
PVTLSEPPLL KEFIKLDNRE QCSTQDYCTQ PANMSGCPAI SIPVCLSASS LPISLQLMAP
NFQEQSLLSA SHWLENQLNF PKLEVL
//
