GLNA3_MEDSA
ID GLNA3_MEDSA Reviewed; 356 AA.
AC Q43785;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Glutamine synthetase nodule isozyme;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GS1;
OS Medicago sativa (Alfalfa).
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; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Iroquois; TISSUE=Root nodule;
RX PubMed=7756692; DOI=10.1094/mpmi-8-0218;
RA Temple S.J., Heard J., Ganter G., Dunn K., Sengupta-Gopalan C.;
RT "Characterization of a nodule-enhanced glutamine synthetase from alfalfa:
RT nucleotide sequence, in situ localization, and transcript analysis.";
RL Mol. Plant Microbe Interact. 8:218-227(1995).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Iroquois; TISSUE=Root nodule;
RX PubMed=2908768; DOI=10.1094/mpmi-1-066;
RA Dunn K., Dickstein R., Feinbaum R., Burnett B.K., Peterman T.K.,
RA Thoidis G., Goodman H.M., Ausubel F.M.;
RT "Developmental regulation of nodule-specific genes in alfalfa root
RT nodules.";
RL Mol. Plant Microbe Interact. 1:66-74(1988).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Found at highest levels in root nodules.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; U15591; AAB41554.1; -; mRNA.
DR AlphaFoldDB; Q43785; -.
DR SMR; Q43785; -.
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 nodule isozyme"
FT /id="PRO_0000153184"
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; 39152 MW; 5368C4BD10C96ECB CRC64;
MSLLSDLINL NLSESSEKII AEYIWVGGSG MDLRSKARTL PGPVSDPAKL PKWNYDGSST
NQAPGQDSEV ILYPQAIFKD PFRQGNNILV ICDVYTPAGE PLPTNKRHNA AKIFSHPDVA
AEVPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGADKAYGRD IVDAHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWAARYI LERITEIAGV VVSFDPKPIP
GDWNGAGAHT NYSTKSMRED GGYEIIKKAI EKLGLRHKEH IAAYGEGNER RLTGKHETTD
INTFSWGVAN RGASVRVGRD TEKDGKGYFE DRRPSSNMDP YVVTSMIAET TLLWKP