ID A0A5C2STG0_9APHY Unreviewed; 354 AA.
AC A0A5C2STG0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN ORFNames=L227DRAFT_569367 {ECO:0000313|EMBL:RPD67185.1};
OS Lentinus tigrinus ALCF2SS1-6.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Lentinus.
OX NCBI_TaxID=1328759 {ECO:0000313|EMBL:RPD67185.1, ECO:0000313|Proteomes:UP000313359};
RN [1] {ECO:0000313|EMBL:RPD67185.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALCF2SS1-6 {ECO:0000313|EMBL:RPD67185.1};
RX PubMed=30398645;
RA Wu B., Xu Z., Knudson A., Carlson A., Chen N., Kovaka S., LaButti K.,
RA Lipzen A., Pennachio C., Riley R., Schakwitz W., Umezawa K., Ohm R.A.,
RA Grigoriev I.V., Nagy L.G., Gibbons J., Hibbett D.;
RT "Genomics and development of Lentinus tigrinus, a white-rot wood-decaying
RT mushroom with dimorphic fruiting bodies.";
RL Genome Biol. Evol. 0:0-0(2018).
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 Evidence={ECO:0000256|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
CC -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; ML122250; RPD67185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C2STG0; -.
DR STRING; 1328759.A0A5C2STG0; -.
DR Proteomes; UP000313359; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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 PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356};
KW Reference proteome {ECO:0000313|Proteomes:UP000313359}.
FT DOMAIN 22..101
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 108..354
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 354 AA; 39234 MW; 43E50344FA3FA4D2 CRC64;
MSHQYRPDLL APYLALPQGD KIQAEYVWID GDGGLRSKTT TVTKKVTDIG TLRIWDFDGS
STNQAPGGDS DVYLRPAAIF KDPFRGGDNI LVLAECYNND GTPNRTNYRH HAAKVMELAK
DEIPWFGIEQ EYTLFDMDGT PYGWPKGGFP GPQGPYYCGA GAGKVFARDL IEAHYRACLY
AGVNISGINA EVMPSQWEFQ VGPCEGISMG DHLWMARYLL IRLAEQWGIK VSFHPKPLQG
DWNGAGCHTN YSTKAMREPG GMKHIEDAIA KLAKRHNEHI AVYGEDNDLR LTGRHETGHI
GTFSSGVANR GASIRIPRHV GAQGYGYLED RRPASNIDPY RVTGIIIETT CLDK
//
