GLNA5_MAIZE
ID GLNA5_MAIZE Reviewed; 357 AA.
AC P38563;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glutamine synthetase root isozyme 5;
DE EC=6.3.1.2;
DE AltName: Full=GS117;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GS1-5;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Golden cross Bantam T51; TISSUE=Leaf;
RA Sakakibara H., Kawabata S., Takahashi H., Hase T., Sugiyama T.;
RT "Molecular cloning of the family of glutamine synthetase genes from maize:
RT expression of genes for glutamine synthetase and ferredoxin-dependent
RT glutamate synthase in photosynthetic and non-photosynthetic tissues.";
RL Plant Cell Physiol. 33:49-58(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 113-357.
RC STRAIN=cv. A188; TISSUE=Seedling;
RX PubMed=8106013; DOI=10.1007/bf00029015;
RA Li M.-G., Villemur R., Hussey P.J., Silflow C.D., Gantt J.S., Snustad D.P.;
RT "Differential expression of six glutamine synthetase genes in Zea mays.";
RL Plant Mol. Biol. 23:401-407(1993).
CC -!- FUNCTION: Plays a role in the flow of nitrogen into nitrogenous organic
CC compounds.
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: Found mainly in the cortical tissues of seedling
CC roots, stem and seedling shoot.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; D14578; BAA03432.1; ALT_SEQ; mRNA.
DR EMBL; X65930; CAA46723.1; -; mRNA.
DR PIR; S39481; S39481.
DR AlphaFoldDB; P38563; -.
DR SMR; P38563; -.
DR PRIDE; P38563; -.
DR MaizeGDB; 17151; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P38563; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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; Nucleotide-binding; Reference proteome.
FT CHAIN 1..357
FT /note="Glutamine synthetase root isozyme 5"
FT /id="PRO_0000153182"
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"
FT CONFLICT 139
FT /note="L -> V (in Ref. 2; CAA46723)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="R -> K (in Ref. 2; CAA46723)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..286
FT /note="GE -> DG (in Ref. 2; CAA46723)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> G (in Ref. 2; CAA46723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 39259 MW; 183F9C15F2FF33A6 CRC64;
MASLTDLVNL DLSDCTDKII AEYIWVGGSG IDLRSKARTV KGPITDPSQL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRKGNNILV MCDCYTPQGE PIPSNKRYKA ATVFSHPDVA
AEVPWYGIEQ EYTLLQKDLS WPLGWPVGGY PGPQGPYYCA AGADKAFGRD VVDAHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISA GDEIWVARYI LERITEMAGI VLSLDPKPIK
GDWNGAGAHT NYSTKSMREA GGYEVIKEAI EKLGRRHREH IAAYGEGNER RLTGRHETAD
INTFKWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTGMIADT TILWKGN