GATA_PEDHC
ID GATA_PEDHC Reviewed; 496 AA.
AC E0VSP9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=gatA {ECO:0000255|HAMAP-Rule:MF_03150}; ORFNames=PHUM422010;
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA;
RX PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., Clark J.M.,
RA Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., Gerlach D.,
RA Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., Veenstra J.A.,
RA Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., Johnston J.S., Reese J.T.,
RA Popadic A., Tojo M., Raoult D., Reed D.L., Tomoyasu Y., Krause E.,
RA Mittapalli O., Margam V.M., Li H.M., Meyer J.M., Johnson R.M.,
RA Romero-Severson J., Vanzee J.P., Alvarez-Ponce D., Vieira F.G., Aguade M.,
RA Guirao-Rico S., Anzola J.M., Yoon K.S., Strycharz J.P., Unger M.F.,
RA Christley S., Lobo N.F., Seufferheld M.J., Wang N., Dasch G.A.,
RA Struchiner C.J., Madey G., Hannick L.I., Bidwell S., Joardar V., Caler E.,
RA Shao R., Barker S.C., Cameron S., Bruggner R.V., Regier A., Johnson J.,
RA Viswanathan L., Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M.,
RA Venter J.C., Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA Pittendrigh B.R.;
RT "Genome sequences of the human body louse and its primary endosymbiont
RT provide insights into the permanent parasitic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
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 GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C 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; DS235755; EEB16405.1; -; Genomic_DNA.
DR RefSeq; XP_002429143.1; XM_002429098.1.
DR AlphaFoldDB; E0VSP9; -.
DR SMR; E0VSP9; -.
DR STRING; 121225.PHUM422010-PA; -.
DR EnsemblMetazoa; PHUM422010-RA; PHUM422010-PA; PHUM422010.
DR GeneID; 8234523; -.
DR KEGG; phu:Phum_PHUM422010; -.
DR CTD; 8234523; -.
DR VEuPathDB; VectorBase:PHUM422010; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; E0VSP9; -.
DR OMA; EVSCPHF; -.
DR PhylomeDB; E0VSP9; -.
DR Proteomes; UP000009046; 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; -; 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; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..496
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000413339"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 186
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 496 AA; 54152 MW; A8EE25888FB73BB0 CRC64;
MLQTSIKKIH GKLKGSNLNT AEVIVNSFKR AEQVLELNSF ISMNNNAGLQ VESSNEYFKN
GKPRSLLEGI PIAVKDNFCV KDTLTTCGSK MLQNFRPKYT ATVVQKLLDS GAILVGKTNM
DEFAMGSGTT TSIFGPTKNI WGSRFSNLCI QEKNDWFIPG GSSGGSAVAV ASGICLGALG
SDTGGSCRNP ASYCGIVGLK PTYGLLSRYG LIPLVNSMDV PAIMALNVED TACLLGIMMG
RDENDSTTVS KNLNLALNYS SSSVKGLKIG IPAEYNCQGL SDEIRSAWND IAKVLYQGGA
SIVPVSMPHT KYSIVCYSIL NQCEVASNMA RYDGIEFGLR SKEKGNRKNS YVTTRYSGFN
EVVRSRIIAG NFFLLSSNSN KYYEKALKVR RLIADDFNNA WRKGINILLT PTTLTDAPKY
SEYIKKDERE QSAIQDYCTQ PANMAGCPAI SIPIELSKKG FPISLQLMAP KFEEKTLLGC
ALYIENAVNF KNMNEQ
