GATA_ASHGO
ID GATA_ASHGO Reviewed; 463 AA.
AC Q75D84;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
GN Name=HER2 {ECO:0000255|HAMAP-Rule:MF_03150}; OrderedLocusNames=ABR140C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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:0000255|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:0000255|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatFAB amidotransferase (AdT)
CC complex, composed of A, B and F subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; AE016815; AAS50911.2; -; Genomic_DNA.
DR RefSeq; NP_983087.2; NM_208440.2.
DR AlphaFoldDB; Q75D84; -.
DR SMR; Q75D84; -.
DR STRING; 33169.AAS50911; -.
DR EnsemblFungi; AAS50911; AAS50911; AGOS_ABR140C.
DR GeneID; 4619197; -.
DR KEGG; ago:AGOS_ABR140C; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; Q75D84; -.
DR OMA; EVSCPHF; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:EnsemblFungi.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR Gene3D; 3.90.1300.10; -; 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 PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..463
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000413347"
FT ACT_SITE 47
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 148
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 463 AA; 49718 MW; B8E0B021E9F7B99E CRC64;
MKRALERLRQ LPRANERFNI FNSVNLSAAQ QVMPSEKPLG NLVVGIKDNI VTKKLPTTCS
SGVLAGYMSP YDATVVELLD EAGAVTAGKT NMDEFGMGSG GIHSFFGPTL NPAFPERPTV
AGGSSSGSAA AVAAGVVDFA LGTDTGGSVR MPAAYTSTVG FKPSYGRVSR HGVIAYAQSL
DTVGIGARDV GLVRRVFEVL DRHDPKDPTS LPDELRQQAA ALRREKKHLK IGIPAELLHG
SVAAEIRERL LVVLDKLQAQ GHELYPVSVP AVKNSLLVYY MLAPAEAASN LARYDGIRYG
CRDEDLDMSD EVLFAPTRGK FGKEVKNRIV LGNYNLCSGA FKNNYMKAQK LRVELINQFD
SIFAFENICT GNKPNPAGVD VLLSLTCMAP PPSLEAFTSK ENKSPVNSYI NDVFTVPMSL
AGLPCISVPL AGMKGVGIQL TAQFADDYGL LDAAEDVMQE QLN
