GLNA2_ARATH
ID GLNA2_ARATH Reviewed; 430 AA.
AC Q43127;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glutamine synthetase, chloroplastic/mitochondrial;
DE EC=6.3.1.2;
DE AltName: Full=GS2;
DE AltName: Full=Glutamate--ammonia ligase;
DE Flags: Precursor;
GN Name=GLN2; Synonyms=GSLI; OrderedLocusNames=At5g35630; ORFNames=MJE4.9;
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].
RX PubMed=1684022; DOI=10.1007/bf00290662;
RA Peterman T.K., Goodman H.M.;
RT "The glutamine synthetase gene family of Arabidopsis thaliana: light-
RT regulation and differential expression in leaves, roots and seeds.";
RL Mol. Gen. Genet. 230:145-154(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Arimura G., Fujii M., Takahashi M., Goshima N., Morikawa H.;
RT "Nucleotide sequences of genes for cytosolic and chloroplastic glutamine
RT synthetase from Arabidopsis thaliana.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP INDUCTION.
RX PubMed=10482686; DOI=10.1104/pp.121.1.301;
RA Oliveira I.C., Coruzzi G.M.;
RT "Carbon and amino acids reciprocally modulate the expression of glutamine
RT synthetase in Arabidopsis.";
RL Plant Physiol. 121:301-310(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15273293; DOI=10.1105/tpc.104.022046;
RA Taira M., Valtersson U., Burkhardt B., Ludwig R.A.;
RT "Arabidopsis thaliana GLN2-encoded glutamine synthetase is dual targeted to
RT leaf mitochondria and chloroplasts.";
RL Plant Cell 16:2048-2058(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: The light-modulated chloroplast/mitochondrial enzyme, encoded
CC by a nuclear gene and expressed primarily in leaves, is responsible for
CC the reassimilation of the ammonia generated by photorespiration.
CC {ECO:0000269|PubMed:15273293}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15273293}. Mitochondrion
CC {ECO:0000269|PubMed:15273293}.
CC -!- TISSUE SPECIFICITY: Expressed in mesophyll and epidermal cells of
CC leaves. {ECO:0000269|PubMed:15273293}.
CC -!- INDUCTION: By light, sucrose, glucose and fructose.
CC {ECO:0000269|PubMed:10482686}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S69727; AAB20558.1; -; mRNA.
DR EMBL; AB015045; BAA88761.1; -; Genomic_DNA.
DR EMBL; AB013393; BAB09304.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93993.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93994.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93995.1; -; Genomic_DNA.
DR EMBL; AF428319; AAL16249.1; -; mRNA.
DR EMBL; AF428461; AAL16230.1; -; mRNA.
DR EMBL; AY081252; AAL91141.1; -; mRNA.
DR EMBL; AY091114; AAM14064.1; -; mRNA.
DR EMBL; AY122977; AAM67510.1; -; mRNA.
DR EMBL; AY088222; AAM65763.1; -; mRNA.
DR PIR; S18600; S18600.
DR RefSeq; NP_001031969.1; NM_001036892.1.
DR RefSeq; NP_001078639.1; NM_001085170.1.
DR RefSeq; NP_198413.1; NM_122954.4.
DR AlphaFoldDB; Q43127; -.
DR SMR; Q43127; -.
DR BioGRID; 18788; 9.
DR DIP; DIP-32735N; -.
DR IntAct; Q43127; 3.
DR MINT; Q43127; -.
DR STRING; 3702.AT5G35630.1; -.
DR iPTMnet; Q43127; -.
DR MetOSite; Q43127; -.
DR SWISS-2DPAGE; Q43127; -.
DR PaxDb; Q43127; -.
DR PRIDE; Q43127; -.
DR ProteomicsDB; 248575; -.
DR EnsemblPlants; AT5G35630.1; AT5G35630.1; AT5G35630.
DR EnsemblPlants; AT5G35630.2; AT5G35630.2; AT5G35630.
DR EnsemblPlants; AT5G35630.3; AT5G35630.3; AT5G35630.
DR GeneID; 833535; -.
DR Gramene; AT5G35630.1; AT5G35630.1; AT5G35630.
DR Gramene; AT5G35630.2; AT5G35630.2; AT5G35630.
DR Gramene; AT5G35630.3; AT5G35630.3; AT5G35630.
DR KEGG; ath:AT5G35630; -.
DR Araport; AT5G35630; -.
DR TAIR; locus:2165897; AT5G35630.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; Q43127; -.
DR OMA; LVICDTW; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; Q43127; -.
DR BioCyc; ARA:AT5G35630-MON; -.
DR BioCyc; MetaCyc:AT5G35630-MON; -.
DR BRENDA; 6.3.1.2; 399.
DR PRO; PR:Q43127; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q43127; baseline and differential.
DR Genevisible; Q43127; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0007568; P:aging; TAS:TAIR.
DR GO; GO:0019676; P:ammonia assimilation cycle; TAS:TAIR.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Ligase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..430
FT /note="Glutamine synthetase, chloroplastic/mitochondrial"
FT /id="PRO_0000011174"
FT DOMAIN 77..157
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 161..430
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 97..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 430 AA; 47411 MW; 664029BC06572295 CRC64;
MAQILAASPT CQMRVPKHSS VIASSSKLWS SVVLKQKKQS NNKVRGFRVL ALQSDNSTVN
RVETLLNLDT KPYSDRIIAE YIWIGGSGID LRSKSRTIEK PVEDPSELPK WNYDGSSTGQ
APGEDSEVIL YPQAIFRDPF RGGNNILVIC DTWTPAGEPI PTNKRAKAAE IFSNKKVSGE
VPWFGIEQEY TLLQQNVKWP LGWPVGAFPG PQGPYYCGVG ADKIWGRDIS DAHYKACLYA
GINISGTNGE VMPGQWEFQV GPSVGIDAGD HVWCARYLLE RITEQAGVVL TLDPKPIEGD
WNGAGCHTNY STKSMREEGG FEVIKKAILN LSLRHKEHIS AYGEGNERRL TGKHETASID
QFSWGVANRG CSIRVGRDTE AKGKGYLEDR RPASNMDPYI VTSLLAETTL LWEPTLEAEA
LAAQKLSLNV
