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   16-JUN-2009, entry version 77.
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;
GN   ORFNames=MJE4.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92079889; 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
RT   glutamine 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   MEDLINE=98403884; 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.
RT   Sequence features of the regions of 1,367,185 bp covered by 19
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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   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
RT   glutamine synthetase in Arabidopsis.";
RL   Plant Physiol. 121:301-310(1999).
RN   [7]
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
RT   targeted to leaf mitochondria and chloroplasts.";
RL   Plant Cell 16:2048-2058(2004).
CC   -!- FUNCTION: The light-modulated chloroplast/mitochondrial enzyme,
CC       encoded by a nuclear gene and expressed primarily in leaves, is
CC       responsible for the reassimilation of the ammonia generated by
CC       photorespiration.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- INTERACTION:
CC       Q42403:TRX3; NbExp=1; IntAct=EBI-449283, EBI-449157;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Expressed in mesophyll and epidermal cells of
CC       leaves.
CC   -!- INDUCTION: By light, sucrose, glucose and fructose.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR   EMBL; S69727; AAB20558.1; -; mRNA.
DR   EMBL; AB015045; BAA88761.1; -; Genomic_DNA.
DR   EMBL; AB013393; BAB09304.1; -; 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   IPI; IPI00534852; -.
DR   PIR; S18600; S18600.
DR   RefSeq; NP_001031969.1; -.
DR   RefSeq; NP_001078639.1; -.
DR   RefSeq; NP_198413.1; -.
DR   UniGene; At.24218; -.
DR   SMR; Q43127; 65-413.
DR   IntAct; Q43127; 1.
DR   SWISS-2DPAGE; Q43127; -.
DR   PRIDE; Q43127; -.
DR   GeneID; 833535; -.
DR   GenomeReviews; BA000015_GR; AT5G35630.
DR   KEGG; ath:AT5G35630; -.
DR   NMPDR; fig|3702.1.peg.25264; -.
DR   TAIR; At5g35630; -.
DR   OMA; Q43127; RIPRQVG.
DR   BRENDA; 6.3.1.2; 302.
DR   ArrayExpress; Q43127; -.
DR   GermOnline; AT5G35630; Arabidopsis thaliana.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA: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:0005515; F:protein binding; IPI:IntAct.
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; IEA:InterPro.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   InterPro; IPR008146; Gln_synth_cat.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   ProDom; PD001057; Gln_synt_C; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chloroplast; Complete proteome; Ligase; Mitochondrion;
KW   Nucleotide-binding; Plastid; Transit peptide.
FT   TRANSIT       1     45       Chloroplast and mitochondrion
FT                                (Potential).
FT   CHAIN        46    430       Glutamine synthetase,
FT                                chloroplastic/mitochondrial.
FT                                /FTId=PRO_0000011174.
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
//