ID   A0A1Q5UEP3_9EURO        Unreviewed;       267 AA.
AC   A0A1Q5UEP3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   ORFNames=PENSUB_3761 {ECO:0000313|EMBL:OKP10941.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP10941.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKP10941.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP10941.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062};
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000256|ARBA:ARBA00008345}.
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:OKP10941.1}.
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DR   EMBL; MNBE01000310; OKP10941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5UEP3; -.
DR   STRING; 1316194.A0A1Q5UEP3; -.
DR   OrthoDB; 842at2759; -.
DR   Proteomes; UP000186955; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01749; GATase1_PB; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   HAMAP; MF_01615; PdxT; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002161; PdxT/SNO.
DR   InterPro; IPR021196; PdxT/SNO_CS.
DR   NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR   PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR   PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR   Pfam; PF01174; SNO; 2.
DR   PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS01236; PDXT_SNO_1; 1.
DR   PROSITE; PS51130; PDXT_SNO_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186955}.
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        238
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        240
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT   BINDING         55..57
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT   BINDING         118
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT   BINDING         149..150
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
SQ   SEQUENCE   267 AA;  29037 MW;  26C1A486E47E35CF CRC64;
     MPVTVGVLAL QGAFIEHVQL LKKAAEQEAL PDWDFIEVRT PQELDRCDGL VLPGGESTTM
     SLVAARSNLL EPLRDFVKVH RKPTWGTCAG LILLAESANK TKKGGQELIG GLDVRVNRNH
     FGRQTESFQG PLGLPFLGED AHPFPAVFIR APIVECILPH REGIQVGEAK REDTVIAPSR
     KVKDSVAEAA TADHVEVLAT LSGAAARSAT QGRNINPDQE VGDVVAVRQG NVFGTSFHPE
     LTGDARIHAW WLHQVQADVN RRKKLGH
//