ID GLNA2_PEA Reviewed; 430 AA.
AC P08281;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 01-MAY-2013, entry version 78.
DE RecName: Full=Glutamine synthetase leaf isozyme, chloroplastic;
DE EC=6.3.1.2;
DE AltName: Full=GS2;
DE AltName: Full=Glutamate--ammonia ligase;
DE Flags: Precursor;
GN Name=GS2;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2898472;
RA Tingey S.V., Tsai F., Edwards J., Walker E.L., Coruzzi G.M.;
RT "Chloroplast and cytosolic glutamine synthetase are encoded by
RT homologous nuclear genes which are differentially expressed in vivo.";
RL J. Biol. Chem. 263:9651-9657(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-430.
RC STRAIN=cv. Sparkle;
RX PubMed=2884100;
RA Tingey S.V., Walker E.L., Coruzzi G.M.;
RT "Glutamine synthetase genes of pea encode distinct polypeptides which
RT are differentially expressed in leaves, roots and nodules.";
RL EMBO J. 6:1-9(1987).
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 -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC L-glutamine.
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: In pea there are distinct isozymes in leaves, roots
CC and nodules.
CC -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC phosphinothricin (PPT).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR EMBL; M20664; AAA33653.1; -; mRNA.
DR EMBL; X05514; CAA29057.1; -; mRNA.
DR PIR; A28089; AJPMQ2.
DR ProteinModelPortal; P08281; -.
DR SMR; P08281; 64-413.
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 GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR008147; Gln_synt_beta.
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 SUPFAM; SSF54368; Gln_synt_beta; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Ligase; Nitrogen fixation;
KW Nucleotide-binding; Plastid; Transit peptide.
FT TRANSIT 1 49 Chloroplast.
FT CHAIN 50 430 Glutamine synthetase leaf isozyme,
FT chloroplastic.
FT /FTId=PRO_0000011182.
SQ SEQUENCE 430 AA; 47346 MW; AB7EFA4F53970D7E CRC64;
MAQILAPSTQ WQMRITKTSP CATPITSKMW SSLVMKQTKK VAHSAKFRVM AVNSENGTIN
RVEDLLNLDI TPFTDSIIAE YIWIGGTGID VRSKSRTISK PVSHPSEVPK WNYDGSSTGQ
APGEDSEVIL YPQAIFKDPF RGGNNILVVC DAYTPAGEPI PTNKRHRAAE IFSNPKVEAE
IPWYGIEQEY TLLQTNVKWP LGWPVGGYPG PQGPYYCAAG ADKSFGRDIS DAHYKACIYA
GINISGTNGE VMPGQWEYQV GPSVGIEAGD HIWASRYILE RITEQAGVVL TLDPKPIEGD
WNGAGCHTNY STKSMREDGG FEVIKKAILN LSLRHKIHIE AYGEGNERRL TGKHETASIN
DFSWGVANRG CSIRVGRDTE KNGKGYLEDR RPASNMDPYV VTALLAESTL LWEPTLEAEA
LAAQKIALKV
//
