ID   GLNAC_BRANA             Reviewed;         428 AA.
AC   Q42624; Q9M429;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Glutamine synthetase, chloroplastic;
DE            EC=6.3.1.2;
DE   AltName: Full=GS2;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   Flags: Precursor;
GN   Name=GLN2; Synonyms=GLN;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   MEDLINE=94269200; PubMed=7911583; DOI=10.1104/pp.103.1.303;
RA   Ochs G., Schock G., Wild A.;
RT   "Chloroplastic glutamine synthetase from Brassica napus.";
RL   Plant Physiol. 103:303-304(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Drakkar; TISSUE=Leaf;
RA   Wojtyna S., Ochs G., Wild A.;
RT   "Cloning and Sequencing of genomic fragments coding for glutamine
RT   synthetase of Brassica napus.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The light-modulated chloroplast enzyme, encoded by a
CC       nuclear gene and expressed primarily in leaves, is responsible for
CC       the reassimilation of the ammonia generated by photorespiration
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR   EMBL; X72751; CAA51280.1; -; mRNA.
DR   EMBL; AJ271909; CAB72423.1; -; Genomic_DNA.
DR   PIR; S32228; S32228.
DR   SMR; Q42624; 63-411.
DR   BRENDA; 6.3.1.2; 393.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT       1     49       Chloroplast (Potential).
FT   CHAIN        50    428       Glutamine synthetase, chloroplastic.
FT                                /FTId=PRO_0000011175.
FT   CONFLICT     50     50       L -> I (in Ref. 2; CAB72423).
FT   CONFLICT     82     82       I -> Y (in Ref. 2; CAB72423).
FT   CONFLICT    263    263       G -> R (in Ref. 2; CAB72423).
FT   CONFLICT    338    338       S -> I (in Ref. 2; CAB72423).
SQ   SEQUENCE   428 AA;  47345 MW;  A0B558C64FD9B18A CRC64;
     MAQILAASPT CQMRLTKPSS IASSKLWNSV VLKQKKQSSS KVRSFKVMAL QSDNSTINRV
     ESLLNLDTKP FTDRIIAEYI WIGGSGIDLR SKSRTLEKPV EDPSELPKWN YDGSSTGQAP
     GEDSEVILYP QAIFRDPFRG GNNILVICDT YTPAGEPIPT NKRARAAEIF SNKKVNEEIP
     WFGIEQEYTL LQPNVNWPLG WPVGAYPGPQ GPYYCGVGAE KSWGRDISDA HYKACLYAGI
     NISGTNGEVM PGQWEFQVGP SVGIEAGDHV WCARYLLERI TEQAGVVLTL DPKPIEGDWN
     GAGCHTNYST KSMREDGGFE VIKKAILNLS LRHMEHISAY GEGNERRLTG KHETASIDQF
     SWGVANRGCS IRVGRDTEKK GKGYLEDRRP ASNMDPYIVT SLLAETTLLW EPTLEAEALA
     AQKLSLKV
//