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Database: UniProt
Entry: A0A1S9D4S8_ASPOZ
LinkDB: A0A1S9D4S8_ASPOZ
Original site: A0A1S9D4S8_ASPOZ 
ID   A0A1S9D4S8_ASPOZ        Unreviewed;       487 AA.
AC   A0A1S9D4S8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=OAory_01049070 {ECO:0000313|EMBL:OOO04060.1};
OS   Aspergillus oryzae (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO04060.1, ECO:0000313|Proteomes:UP000190312};
RN   [1] {ECO:0000313|EMBL:OOO04060.1, ECO:0000313|Proteomes:UP000190312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC7051 {ECO:0000313|EMBL:OOO04060.1,
RC   ECO:0000313|Proteomes:UP000190312};
RA   Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA   Jeennor S., Laoteng K.;
RT   "Genome sequencing of Aspergillus oryzae BCC7051.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01330, 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:OOO04060.1}.
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DR   EMBL; MKZY01000011; OOO04060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9D4S8; -.
DR   VEuPathDB; FungiDB:AO090009000558; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   OMA; MFCDILM; -.
DR   Proteomes; UP000190312; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR   Pfam; PF00120; Gln-synt_C; 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; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190312}.
FT   DOMAIN          16..115
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          123..487
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   487 AA;  53808 MW;  376134652643D715 CRC64;
     MGSVSSPEVT LDNVAEILQR DTRVKLAGVD VDGMLRGKLV SKKKFLSIVS EGFGFCSVIF
     GWDMHDQTYF KELAISNKEN GYRDIVAIPD LSSFRRIPWE NNVPFFLVSF HDPDTREPVC
     ACPRGLVRTA LGKAEAAGYR AMAGAEYEFY QFRVPESHPS PERSASSTAT FLRENPVEAL
     PSLTEGMFGY SLTRPIHNQD YYYGIFDACE QFKCDIEGWH TESGPGVFEA ALQFGEAKEM
     ADKAGLFKYV VKSIGTKHGI TPTFMAKPRQ GLPGNSGHMH ISLVTSDGKN AFLRDTPDPS
     PPYPDVAYLS DLGRYFLAGV LTGLPDIMPM FAPTVNSYKR LVENFWAPVT VSWGLEHRAA
     SIRLITPPTG SPKATRLEVR VPGADANPHY VLAAIVALGW RGVEKKLEIP VPPLSKGEEM
     GGGSDQGVRL AKSLKEAVAA FTRKGSVARE VFGDAFVDHF GGTREHEVRL WEEAVTDWEV
     RRYIETV
//
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