GenomeNet

Database: UniProt
Entry: A0A401GC52_9APHY
LinkDB: A0A401GC52_9APHY
Original site: A0A401GC52_9APHY 
ID   A0A401GC52_9APHY        Unreviewed;       352 AA.
AC   A0A401GC52;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=SCP_0209220 {ECO:0000313|EMBL:GBE79721.1};
OS   Sparassis crispa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Sparassidaceae; Sparassis.
OX   NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE79721.1, ECO:0000313|Proteomes:UP000287166};
RN   [1] {ECO:0000313|EMBL:GBE79721.1, ECO:0000313|Proteomes:UP000287166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA   Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT   "Genome sequence of the cauliflower mushroom Sparassis crispa
RT   (Hanabiratake) and its association with beneficial usage.";
RL   Sci. Rep. 8:16053-16053(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBE79721.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BFAD01000002; GBE79721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401GC52; -.
DR   STRING; 139825.A0A401GC52; -.
DR   InParanoid; A0A401GC52; -.
DR   OrthoDB; 1115057at2759; -.
DR   Proteomes; UP000287166; 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:UP000287166}.
FT   DOMAIN          20..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          106..352
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   352 AA;  38937 MW;  39B9337768C9FB23 CRC64;
     MSYRPELLAP FLALPQGDKV QAEYVWIDGD GGLRSKTTTV TKKVTDIGQL RIWDFDGSST
     NQAPGTDSDV YLRPAAIFKD PFRGGDNILV LAECYNNDGT PNKTNYRHHA KKVMDLAKEQ
     VPWFGLEQEY TLFDTDGTPY GWPKGGFPGP QGPYYCGAGA GKVFARDLIE AHYRACLYAG
     VNISGINAEV MPSQWEFQVG PCEGISMGDH LWMARYLLVR AAQQWNITVS FHPKPLAGDW
     NGAGCHTNFS TKAMREPGGM AYIEAAIEKL SKRHNEHIAV YGEDNDLRLT GRHETGHIGT
     FTSGVANRGA SIRIPRHVGA QGYGYLEDRR PASNIDPYRV TSIIVETTCL DK
//
DBGET integrated database retrieval system