GLNAC_BRANA
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 25-MAY-2022, entry version 103.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX 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 nuclear
CC gene and expressed primarily in leaves, is responsible for the
CC reassimilation of the ammonia generated by photorespiration.
CC {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X72751; CAA51280.1; -; mRNA.
DR EMBL; AJ271909; CAB72423.1; -; Genomic_DNA.
DR PIR; S32228; S32228.
DR RefSeq; NP_001302944.1; NM_001316015.1.
DR AlphaFoldDB; Q42624; -.
DR SMR; Q42624; -.
DR EnsemblPlants; CDX74644; CDX74644; GSBRNA2T00114639001.
DR GeneID; 106424972; -.
DR Gramene; CDX74644; CDX74644; GSBRNA2T00114639001.
DR KEGG; bna:106424972; -.
DR OMA; LVICDTW; -.
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:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Phosphoprotein;
KW Plastid; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..428
FT /note="Glutamine synthetase, chloroplastic"
FT /id="PRO_0000011175"
FT DOMAIN 75..155
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 159..428
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 94..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q43127"
FT CONFLICT 50
FT /note="L -> I (in Ref. 2; CAB72423)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="I -> Y (in Ref. 2; CAB72423)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="G -> R (in Ref. 2; CAB72423)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="S -> I (in Ref. 2; CAB72423)"
FT /evidence="ECO:0000305"
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
