GATC_ARATH
ID GATC_ARATH Reviewed; 155 AA.
AC F4JV80; O82634; Q8LAD3; Q9FV80;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03149};
DE Short=Glu-AdT subunit C {ECO:0000255|HAMAP-Rule:MF_03149};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149};
DE Flags: Precursor;
GN Name=GATC {ECO:0000255|HAMAP-Rule:MF_03149}; OrderedLocusNames=At4g32915;
GN ORFNames=F26P21;
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 "Arabidopsis thaliana Glu-tRNA(Gln) amidotransferase c subunit (gat c).";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-52.
RX PubMed=25862457; DOI=10.1104/pp.15.00300;
RA Huang S., Nelson C.J., Li L., Taylor N.L., Stroeher E., Peteriet J.,
RA Millar A.H.;
RT "INTERMEDIATE CLEAVAGE PEPTIDASE55 modifies enzyme amino termini and alters
RT protein stability in Arabidopsis mitochondria.";
RL Plant Physiol. 168:415-427(2015).
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_03149, 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03149};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149,
CC ECO:0000269|PubMed:18441100, ECO:0000305|PubMed:25862457}. Plastid,
CC chloroplast {ECO:0000255|HAMAP-Rule:MF_03149,
CC ECO:0000269|PubMed:18441100}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA21200.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g32910 has been split into 2 genes: At4g32910 and At4g32915.; Evidence={ECO:0000305};
CC Sequence=CAB80008.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g32910 has been split into 2 genes: At4g32910 and At4g32915.; Evidence={ECO:0000305};
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DR EMBL; AF240465; AAG29097.1; -; mRNA.
DR EMBL; AL031804; CAA21200.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161582; CAB80008.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86143.1; -; Genomic_DNA.
DR EMBL; AY087891; AAM65443.1; -; mRNA.
DR PIR; T05299; T05299.
DR RefSeq; NP_567909.1; NM_119445.4.
DR AlphaFoldDB; F4JV80; -.
DR SMR; F4JV80; -.
DR STRING; 3702.AT4G32915.1; -.
DR iPTMnet; F4JV80; -.
DR PaxDb; F4JV80; -.
DR PRIDE; F4JV80; -.
DR ProteomicsDB; 228966; -.
DR EnsemblPlants; AT4G32915.1; AT4G32915.1; AT4G32915.
DR GeneID; 829428; -.
DR Gramene; AT4G32915.1; AT4G32915.1; AT4G32915.
DR KEGG; ath:AT4G32915; -.
DR Araport; AT4G32915; -.
DR TAIR; locus:505006545; AT4G32915.
DR eggNOG; KOG2271; Eukaryota.
DR HOGENOM; CLU_105899_5_0_1; -.
DR InParanoid; F4JV80; -.
DR OMA; NAVWHRR; -.
DR OrthoDB; 1457819at2759; -.
DR PRO; PR:F4JV80; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JV80; baseline and differential.
DR Genevisible; F4JV80; AT.
DR GO; GO:0009507; C:chloroplast; 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; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR PANTHER; PTHR15004; PTHR15004; 1.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Plastid; Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000269|PubMed:25862457"
FT CHAIN 53..155
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000413317"
FT CONFLICT 4
FT /note="R -> I (in Ref. 5; AAM65443)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="Q -> L (in Ref. 1; AAG29097)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="K -> R (in Ref. 1; AAG29097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17519 MW; BE5C74DCDA61048A CRC64;
MATRALLAVI YASPNRCYIS PSRIKIQSLT CSSSSHYYQR QSRKNHRIAR SYSSDSDSSV
LQPPDVARLA QTARISLTPA EIEECETKIR RVIDWFGQLQ QVDVNSVEPA IRAEMDGGNL
REDAPETFDN RDSIRASIPS FEDAYLKVPK ILNKE
