ID   GLNA4_PEA               Reviewed;         357 AA.
AC   Q43066;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glutamine synthetase root isozyme B;
DE            EC=6.3.1.2;
DE   AltName: Full=Cytosolic GS3 B;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=GS3B;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Feltham First;
RX   PubMed=8616212; DOI=10.1007/bf00020456;
RA   Walker E.L., Weeden N.F., Taylor C.B., Green P., Coruzzi G.M.;
RT   "Molecular evolution of duplicate copies of genes encoding cytosolic
RT   glutamine synthetase in Pisum sativum.";
RL   Plant Mol. Biol. 29:1111-1125(1995).
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   -!- MISCELLANEOUS: In pea there are distinct isozymes in leaves, roots and
CC       nodules.
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; U28925; AAB03493.1; -; Genomic_DNA.
DR   PIR; S62712; S62712.
DR   AlphaFoldDB; Q43066; -.
DR   SMR; Q43066; -.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN           1..357
FT                   /note="Glutamine synthetase root isozyme B"
FT                   /id="PRO_0000153190"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..357
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   357 AA;  39295 MW;  F5F09B4BD96912CA CRC64;
     MSSLSDLINF NLSDSTEKII AEYIWVGGSG IDIRSKARTL PGPVSDPAKL PKWNYDGSST
     DQAPGKDSEV ILYPQAIFKD PFRRGNNILV ICDVYTPAGE PLPTNKRYNA AKIFSHPDVA
     AEVPWYGIEQ EYTLLQKDIN WPLGWPIGGY PGKQGPYYCG IGADKAYGRD IVDAHYKACL
     FAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWAARYI LERITEISGV VVSFDPKPIP
     GDWNGAGAHA NFSTKSMREN GGYEVIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETAD
     INVFSWGVAN RGSSIRVGRD TEKDGKGYFE DRRPASNMDP YVVTSMIAET TILWKKS