GLNA2_MAIZE
ID GLNA2_MAIZE Reviewed; 368 AA.
AC P38560;
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 2;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GLN2; Synonyms=GS1-2;
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).
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 vascular tissues of seedling
CC roots.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X65927; CAA46720.1; -; mRNA.
DR PIR; S39478; S39478.
DR AlphaFoldDB; P38560; -.
DR SMR; P38560; -.
DR STRING; 4577.GRMZM2G024104_P01; -.
DR PaxDb; P38560; -.
DR PRIDE; P38560; -.
DR MaizeGDB; 17151; -.
DR eggNOG; KOG0683; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P38560; 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..368
FT /note="Glutamine synthetase root isozyme 2"
FT /id="PRO_0000153179"
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..368
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT REGION 38..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40094 MW; 32F1E1AE109AEA0D CRC64;
MALLSDLINL DLSGRTGKII AEYIWVGGSG MDVRSKARTL SGPVDDPSKL PKWNFDGSST
GQAPGDDSEV ILCPRAIFRD PFRKGQNILV MCDCYEPNGE PIPSNKRHGA AKIFSHPDVK
AEEPWFGIEQ EYTLLQKDTK WPLGWPLAYP GPQGPYYCAA GADKSYGRDI VDCAYKACLY
AGIDISGING EVMPGQWEFQ VAPAVGVSAG DQLWVARYIL ERITEIAGVV VSFDPKPIPG
DWNGAGAHTN YSTKSMRSDG GYEVIKKAIG KLGLRHREHI AAYGDGNERP LTGRHETADI
NTFVWGVPNR GASVRVGRDT EKEGKGYFED RRPASNMDPY VVTCLIAETT MLWEPSHSNG
DGKGAAAP
