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Glutamine synthetase leaf isozyme, chloroplastic (EC 6.3.1.2) (Glutamate--ammonia ligase) (Isozyme delta)

 GLNA4_PHAVU             Reviewed;         429 AA.
P15102;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-APR-2017, entry version 90.
RecName: Full=Glutamine synthetase leaf isozyme, chloroplastic;
EC=6.3.1.2;
AltName: Full=Glutamate--ammonia ligase;
AltName: Full=Isozyme delta;
Flags: Precursor;
Phaseolus vulgaris (Kidney bean) (French bean).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Tendergreen; TISSUE=Leaf;
AGRICOLA=IND92000070; DOI=10.1007/BF00015671;
Lightfoot D.A., Green N.K., Cullimore J.V.;
"The chloroplast-located glutamine synthetase of Phaseolus vulgaris
L.: nucleotide sequence, expression in different organs and uptake
into isolated chloroplasts.";
Plant Mol. Biol. 11:191-202(1988).
-!- FUNCTION: The light-modulated chloroplast enzyme, encoded by a
nuclear gene and expressed primarily in leaves, is responsible for
the reassimilation of the ammonia generated by photorespiration.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
L-glutamine.
-!- SUBUNIT: Homooctamer.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast.
-!- TISSUE SPECIFICITY: Expressed in leaves and stems. Low levels
detected in roots and nodules. {ECO:0000269|Ref.1}.
-!- MISCELLANEOUS: There are at least four isozymes of this enzyme in
P.vulgaris.
-!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
phosphinothricin (PPT).
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
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EMBL; X12738; CAA31234.1; -; mRNA.
PIR; S04031; AJFBQD.
RefSeq; XP_007147796.1; XM_007147734.1.
RefSeq; XP_007147797.1; XM_007147735.1.
ProteinModelPortal; P15102; -.
SMR; P15102; -.
PRIDE; P15102; -.
ProMEX; P15102; -.
GeneID; 18628920; -.
KEGG; pvu:PHAVU_006G155800g; -.
KO; K01915; -.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR008147; Gln_synt_b-grasp.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR008146; Gln_synth_cat_dom.
InterPro; IPR027303; Gln_synth_gly_rich_site.
InterPro; IPR027302; Gln_synth_N_conserv_site.
Pfam; PF00120; Gln-synt_C; 1.
Pfam; PF03951; Gln-synt_N; 1.
SMART; SM01230; Gln-synt_C; 1.
SUPFAM; SSF54368; SSF54368; 1.
PROSITE; PS00180; GLNA_1; 1.
PROSITE; PS00181; GLNA_ATP; 1.
2: Evidence at transcript level;
ATP-binding; Chloroplast; Ligase; Nitrogen fixation;
Nucleotide-binding; Plastid; Transit peptide.
TRANSIT 1 50 Chloroplast. {ECO:0000250}.
CHAIN 51 429 Glutamine synthetase leaf isozyme,
chloroplastic.
/FTId=PRO_0000011183.
SEQUENCE 429 AA; 47246 MW; 0CA55624B1118AF8 CRC64;
MAQILAPSTQ WQMRFTKSSR HASPITSNTW SSLLMKQNKK TSSAKFRVLA VKSDGSTINR
LEGLLNLDIT PFTDKIIAEY IWIGGTGIDV RSKSRTISKP VEHPSELPKW NYDGSSTGQA
PGEDSEVILY PQAIFKDPFR GGNNILVICD AYTPAGEPIP TNKRHRAAEV FSNPRVIAEV
PWFGIEQEYT LLQTNVNWPL GWPVGGYPGP QGPYYCSAGA DKSFGRDISD AHYKACLFAG
INISGTNGEV MPGQWEYQVG PSVGIEAGDH IWASRYILER ITEQAGVVLS LDPKPIEGDW
NGAGCHTNYS TKSMREDGGF EVIKKAILNL SLRHKEHISA YGEGNERRLT GKHETASINT
FSWGVANRGC SIRVGRDTEK NGKGYLEDRR PASNMDPYVV TSLLAESTLL WEPTLEAEAL
AAQKLALKV


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