GLNA1_PHAVU
ID GLNA1_PHAVU Reviewed; 356 AA.
AC P04770;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Glutamine synthetase PR-1;
DE EC=6.3.1.2;
DE AltName: Full=Gln isozyme beta;
DE AltName: Full=Glutamate--ammonia ligase;
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 [MRNA].
RX PubMed=16453687; DOI=10.1002/j.1460-2075.1986.tb04379.x;
RA Gebhardt C., Oliver J.E., Forde B.G., Saarelainen R., Miflin B.J.;
RT "Primary structure and differential expression of glutamine synthetase
RT genes in nodules, roots and leaves of Phaseolus vulgaris.";
RL EMBO J. 5:1429-1435(1986).
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: Roots.
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; X04001; CAA27631.1; -; mRNA.
DR PIR; A26308; AJFBQB.
DR AlphaFoldDB; P04770; -.
DR SMR; P04770; -.
DR STRING; 3885.XP_007163376.1; -.
DR ProMEX; P04770; -.
DR eggNOG; KOG0683; Eukaryota.
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 PR-1"
FT /id="PRO_0000153191"
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"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 39118 MW; E050631D3DBB8675 CRC64;
MSLLSDLINL NLSDTTEKVI AEYIWIGGSG LDLRSKARTL PGPVKNPSEL PKWNYDGSST
GQAPGQDSEV IIYPQAIFKD PFRRGNNILV ICDAYTPAGE PIPTNKRHNA AKIFSNPDVV
AEEPWYGIEQ EYTLLQKEVN WPVGWPVGGF PGPQGPYYCG VGADKAFGRD IVDAHYKACV
YAGINISGIN GEVMPGQWEF QVGPAVGISA GDELWVARYI LERITEVAGV VLSFDPKPIK
GDWNGAGAHT NYSTKTMRND GGYEEIKSAI QKLGKRHKEH IAAYGEGNER RLTGRHETAD
INTFLWGVAN RGASIRVGRD TEKAGKGYFE DRRPASNMDP YVVTSMIADT TILWKP
