GLNA4_MAIZE
ID GLNA4_MAIZE Reviewed; 355 AA.
AC P38562;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutamine synthetase root isozyme 4;
DE EC=6.3.1.2;
DE AltName: Full=GS107;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GLN5; Synonyms=GS1-4;
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. 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).
RN [2]
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).
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 in all the tissues examined with higher
CC expression found in tissues of the root, stem and seedling shoot.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X65929; CAA46722.1; -; mRNA.
DR EMBL; D14576; BAA03430.1; -; mRNA.
DR PIR; S39480; S39480.
DR AlphaFoldDB; P38562; -.
DR SMR; P38562; -.
DR PRIDE; P38562; -.
DR MaizeGDB; 17151; -.
DR BRENDA; 6.3.1.2; 6752.
DR SABIO-RK; P38562; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P38562; 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..355
FT /note="Glutamine synthetase root isozyme 4"
FT /id="PRO_0000153181"
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..355
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 37..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 316
FT /note="A -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> RE (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 38981 MW; 02F891F1209C50E5 CRC64;
MACLTDLVNL NLSDTTEKII AEYIWIGGSG MDLRSKARTL PGPVTDPSKL PKWNYDGSST
GQAPGEDSEV ILYPQAIFKD PFRRGNNILV MCDCYTPAGE PIPTNKRYSA AKIFSSPEVA
AEEPWYGIEQ EYTLLQKDTN WPLGWPIGGF PGPQGPYYCG IGAEKSFGRD IVDAHYKACL
YAGINISGIN GEVMPGQWEF QVGPSVGISS GDQVWVARYI LERITEIAGV VVTFDPKPIP
GDWNGAGAHT NYSTESMRKE GGYEVIKAAI EKLKLRHKEH IAAYGEGNER RLTGRHETAD
INTFSWGVAN RGASVAVGQT EQNGKGYFED RRPASNMDPY VVTSMIAETT IVWKP