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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
 
 
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