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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//