GLNA3_PHAVU
ID GLNA3_PHAVU Reviewed; 356 AA.
AC P00965; Q9SAT5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Glutamine synthetase N-1;
DE EC=6.3.1.2;
DE AltName: Full=Gln isozyme gamma;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=Gln-gamma;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Root nodule;
RA Bennett M.J., Lightfoot D.A., Cullimore J.V.;
RT "cDNA sequence and differential expression of the gene encoding the
RT glutamine synthetase and polypeptide of Phaseolus vulgaris L.";
RL Plant Mol. Biol. 12:553-565(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 216-356.
RX PubMed=6152282;
RA Cullimore J.V., Gebhardt C., Saarelainen R., Miflin B.J., Idler K.B.,
RA Barker R.F.;
RT "Glutamine synthetase of Phaseolus vulgaris L.: organ-specific expression
RT of a multigene family.";
RL J. Mol. Appl. Genet. 2:589-599(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-38.
RX PubMed=1983793; DOI=10.2307/3869328;
RA Forde B.G., Freeman J., Oliver J.E., Pineda M.;
RT "Nuclear factors interact with conserved A/T-rich elements upstream of a
RT nodule-enhanced glutamine synthetase gene from French bean.";
RL Plant Cell 2:925-939(1990).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: This is a nodule isozyme.
CC -!- MISCELLANEOUS: There are at least four isozymes of this enzyme in
CC P.vulgaris.
CC -!- MISCELLANEOUS: Irreversibly inhibited by the herbicide L-
CC phosphinothricin (PPT).
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X14605; CAA32759.1; -; mRNA.
DR EMBL; M10159; AAA33762.1; -; mRNA.
DR EMBL; M92095; AAA33761.1; -; Genomic_DNA.
DR PIR; S04727; AJFBQ.
DR RefSeq; XP_007141923.1; XM_007141861.1.
DR AlphaFoldDB; P00965; -.
DR SMR; P00965; -.
DR STRING; 3885.XP_007141923.1; -.
DR PRIDE; P00965; -.
DR ProMEX; P00965; -.
DR EnsemblPlants; ESW13917; ESW13917; PHAVU_008G237400g.
DR GeneID; 18623838; -.
DR Gramene; ESW13917; ESW13917; PHAVU_008G237400g.
DR KEGG; pvu:PHAVU_008G237400g; -.
DR eggNOG; KOG0683; Eukaryota.
DR OMA; QTIFRDP; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; P00965; -.
DR GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT CHAIN 1..356
FT /note="Glutamine synthetase N-1"
FT /id="PRO_0000153193"
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..356
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 356 AA; 39341 MW; 3C88504756A452DC CRC64;
MSSISDLVNL NLSDSTERVI AEYIWVGGSG MDMRSKARTL SGPVKDPSKL PKWNYDGSST
GQAPGQDSEV ILYPQTIFRD PFRRGNNILV MCDAYTPAGE PIPTNKRHNA AKIFSNPEVV
AEEPWYGIEQ EYTLLQKDVQ WPVGWPLGGF PGPQGPYYCG IGANKAFGRD IVDSHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISA ADELWVARYI LERITEIAGV VLSFDPKPIQ
GDWNGAGAHT NYSTKSMRND GGYEVIKKAI TKLEKRHKEH IAAYGEGNER RLTGKHETAD
MNTFIWGVAN RGASIRVGRD TEKAGKGYFE DRRPASNMDP YVVTSMIAET TLLWKP
