GATA_MAIZE
ID GATA_MAIZE Reviewed; 543 AA.
AC B6U151;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/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};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts
CC and mitochondria. The reaction takes place in the presence of glutamine
CC and 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 Plastid, chloroplast stroma {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC 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; EU970966; ACG43084.1; -; mRNA.
DR EMBL; BT055492; ACL54099.1; -; mRNA.
DR RefSeq; NP_001146476.1; NM_001153004.1.
DR AlphaFoldDB; B6U151; -.
DR SMR; B6U151; -.
DR STRING; 4577.GRMZM2G022192_P01; -.
DR PaxDb; B6U151; -.
DR EnsemblPlants; Zm00001eb068770_T002; Zm00001eb068770_P002; Zm00001eb068770.
DR GeneID; 100280064; -.
DR Gramene; Zm00001eb068770_T002; Zm00001eb068770_P002; Zm00001eb068770.
DR KEGG; zma:100280064; -.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_3_1; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; B6U151; baseline and differential.
DR Genevisible; B6U151; ZM.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
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:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProt.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Plastid; Protein biosynthesis; Reference proteome.
FT CHAIN 1..543
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413345"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 220
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ SEQUENCE 543 AA; 57125 MW; 0BCAA1466E163211 CRC64;
MPPPLQAHRL LISHRRLPTP ARRRFTAASS VQSAPATTLA PGPATSSILS IRESLLSGER
TAADITSEYL SRLRRTEPTL RSFIHVADAA AEREAEELDR RIASGEKDAV GPLAGVLVGV
KDNLCTANMP STGGSRILDG YRPAYDATAV RRLREAGAIV LGKTNLDEFG MGSTTEGSAF
QVTTNPWDDS RVPGGSSGGS AAAVSARQCV VSLGSDTGGS VRQPASFCGV VGLKPTYGRV
SRFGLMAYAS SLDVVGCFGS SVFDTATILS VVAGHDKMDA TSSSQVVPEY ASELVSLDLL
ESKPLNGVRI GIIQETLGEG VASGVVSSIK GAASHLEQLG SVVEEVSLPS FSLGLPAYYI
LASSEASSNL SRYDGIRYGG QVSADDLNEL YGESRANGFG HEVKMRILMG TYALSAGYYD
AYYKRAQQVR TLVKQSFKDA LERYDILISP AAPSAAYKIG EKINDPLAMY AGDIMTVNVN
LAGLPALVVP CGFVEGGAAG LPVGLQMMGS PFCEGNLLRV GHIFEQTLQN LSFVPPLLAE
GQL
