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
//