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Database: UniProt
Entry: A0A166E4W3_9AGAM
LinkDB: A0A166E4W3_9AGAM
Original site: A0A166E4W3_9AGAM 
ID   A0A166E4W3_9AGAM        Unreviewed;       479 AA.
AC   A0A166E4W3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=PENSPDRAFT_653267 {ECO:0000313|EMBL:KZV68337.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV68337.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV68337.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV68337.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; KV424559; KZV68337.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166E4W3; -.
DR   STRING; 1314672.A0A166E4W3; -.
DR   InParanoid; A0A166E4W3; -.
DR   OrthoDB; 2534858at2759; -.
DR   Proteomes; UP000077086; 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; 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:SF2; TYPE-1 GLUTAMINE SYNTHETASE 1; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086}.
FT   DOMAIN          137..479
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   REGION          279..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  51273 MW;  D19F06A9D0878A92 CRC64;
     MGTPNSEPYG QVFTPSTISL PSFSAKDVSA LATSGVRYIR FTWVDLTNIV RCRVIPIGAF
     QALLAARRPG ISVATVALGL VGPTCAPGFT GTGEYLYVPD LSSLRKCGYA PGHANLLGYL
     EQKVPASGES LEVGLCPRTL LRRVVEDARA AGFEFLVGIE TEFILLRSVD PIEAVNDYPW
     STTAALPTGA KETLCMEEIA DALLASGIEL LMYHAEAAPG QFEFVTGPLP PLEAADAVVL
     TRETIYNIAA KHGLRATLAP RVYMDNCGSS AHAHISVHRS SVPATKTPKP SPNTNSSTTM
     APHERSFLQS LLDSITDIAA ITLPTQASYA RVADGIWSGG TYAAWGTENR ETLVRLTGPP
     GSHHFEIRSH DNTANPYLSL AAILGAGLQG IKQGVELTIG DCPGQAVDLS ENERAARNIT
     GQMPKSLKEA REKMRGNAAV KEVFGETFVE RYLSVNEAME KFMSTGTPES DAKKMVLTY
//
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