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Database: UniProt
Entry: A0A1G4BB41_9PEZI
LinkDB: A0A1G4BB41_9PEZI
Original site: A0A1G4BB41_9PEZI 
ID   A0A1G4BB41_9PEZI        Unreviewed;       297 AA.
AC   A0A1G4BB41;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   ORFNames=CORC01_06049 {ECO:0000313|EMBL:OHE98598.1};
OS   Colletotrichum orchidophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE98598.1, ECO:0000313|Proteomes:UP000176998};
RN   [1] {ECO:0000313|EMBL:OHE98598.1, ECO:0000313|Proteomes:UP000176998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE98598.1,
RC   ECO:0000313|Proteomes:UP000176998};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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:OHE98598.1}.
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DR   EMBL; MJBS01000044; OHE98598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4BB41; -.
DR   STRING; 1209926.A0A1G4BB41; -.
DR   OrthoDB; 842at2759; -.
DR   Proteomes; UP000176998; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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   ECO:0000313|EMBL:OHE98598.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW   Transferase {ECO:0000313|EMBL:OHE98598.1}.
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   297 AA;  31758 MW;  6D57659BB9EBB8EB CRC64;
     MTQTRHLEPF ATLPIILKNS AERHQLQLPQ PHNLFLKMSP LTVGVLALQG GFHEHVELVR
     KAAAYLATAQ SSSPSPGPDI AAIEVRTEAE LRSCGALIIP GGESTTISFI AVQSGLMEPL
     KEFVKVDRKP VWGTCAGAIL LADEANATKK GGQELIGGLG VRVHRNHFGR QIESFVADLD
     LPFLTQGDGN TKTASSPYPG VFIRAPIVEE ILYMESEAAG KPSSSAVEVL AVLPGRKSKA
     AAGVSQSTAD DSVGDIVAVR QQNIFATSFH PELTDDVRIH VWWLEQVMQA VAPTSSA
//
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