GATA_ARATH
ID GATA_ARATH Reviewed; 537 AA.
AC Q9LI77; Q9FVA6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
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}; OrderedLocusNames=At3g25660;
GN ORFNames=T5M7.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chang W., Soll D.;
RT "Cloning and characterization of Glu-ADT from Arabidopsis thaliana.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18441100; DOI=10.1073/pnas.0712299105;
RA Pujol C., Bailly M., Kern D., Marechal-Drouard L., Becker H.,
RA Duchene A.-M.;
RT "Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial
RT and chloroplastic Gln-tRNAGln synthesis in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6481-6485(2008).
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, ECO:0000269|PubMed:18441100}.
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. Plastid, chloroplast stroma.
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; AF224745; AAG29095.1; -; mRNA.
DR EMBL; AP001313; BAB03086.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77048.1; -; Genomic_DNA.
DR EMBL; AY045664; AAK74022.1; -; mRNA.
DR EMBL; BT000644; AAN18210.1; -; mRNA.
DR EMBL; AK226499; BAE98641.1; -; mRNA.
DR RefSeq; NP_189194.1; NM_113465.4.
DR AlphaFoldDB; Q9LI77; -.
DR SMR; Q9LI77; -.
DR BioGRID; 7485; 3.
DR STRING; 3702.AT3G25660.1; -.
DR PaxDb; Q9LI77; -.
DR PRIDE; Q9LI77; -.
DR ProteomicsDB; 248608; -.
DR EnsemblPlants; AT3G25660.1; AT3G25660.1; AT3G25660.
DR GeneID; 822154; -.
DR Gramene; AT3G25660.1; AT3G25660.1; AT3G25660.
DR KEGG; ath:AT3G25660; -.
DR Araport; AT3G25660; -.
DR TAIR; locus:2102380; AT3G25660.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_0_3_1; -.
DR InParanoid; Q9LI77; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR PhylomeDB; Q9LI77; -.
DR BioCyc; ARA:AT3G25660-MON; -.
DR PRO; PR:Q9LI77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LI77; baseline and differential.
DR Genevisible; Q9LI77; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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..537
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413340"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 215
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT CONFLICT 286
FT /note="Q -> R (in Ref. 1; AAG29095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 57181 MW; 0CA842224D367DAD CRC64;
MLSTLQPPRS LSLLPLRRFQ ISKTIVSAAS SKTIDTSVIS PPQSQILTTR RSLLSGETTA
VEIAKSYLSR IRLTEPQLKC FLHVSENVLK DAQEIDQRIA KGEELGPLAG VLIGVKDNIC
TQGMPSTAAS RILEHYRPPF DATAVKKIKE LGGIVVGKTN MDEFGMGSTT EASAFQVTAN
PWDLSRVPGG SSGGSAAAVA ARQCMVSLGS DTGGSVRQPA SFCGVVGLKP TYGRVSRFGL
MAYASSLDVI GCFGSTVADA GMLLHAISGY DRFDSTSSKQ DVPEFQSQFL SVDHFESKPL
NGVKVGIIRE TLEDGVDSGV RSATQEAASH LEALGCILTE VSLPSFSLGL PAYYVIASSE
SSSNLSRYDG VRYGNQVMAE ELNKLYECSR GEGFGGEVKM RILMGTYALS AGYYDAYYKR
AQQVRTLIRK DFKAALEQND ILISPAAPSA AYKIGEKKDD PLAMYAGDIM TVNVNLAGLP
AMVLPCGLVE GGPSGLPVGL QMIGAAFDEE KLLKVGHIFE QTLKGSSFVP PLLANVA