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Database: UniProt
Entry: A0A135ULP0_9PEZI
LinkDB: A0A135ULP0_9PEZI
Original site: A0A135ULP0_9PEZI 
ID   A0A135ULP0_9PEZI        Unreviewed;       465 AA.
AC   A0A135ULP0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   ORFNames=CSAL01_13441 {ECO:0000313|EMBL:KXH61298.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH61298.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH61298.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH61298.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) 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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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:KXH61298.1}.
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DR   EMBL; JFFI01001299; KXH61298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135ULP0; -.
DR   STRING; 1209931.A0A135ULP0; -.
DR   OrthoDB; 537490at2759; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.30.750.24; STAS domain; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   InterPro; IPR002645; STAS_dom.
DR   InterPro; IPR036513; STAS_dom_sf.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT   DOMAIN          340..424
FT                   /note="STAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50801"
SQ   SEQUENCE   465 AA;  49691 MW;  4151DAE433EA944E CRC64;
     MKSPIPDYLN RVLENARPNE AGAPAGYIDV LAKADTSKMA VALAMVDGNL YSAGDDRVEF
     SIQSISKAFV YALAIEDAGL PAVLEKIGVE PSGDAFNRLS LERGSNRPMN PMINAGAITA
     HSLVVSPSAT LEQRTERILS ALSRLAGRQL HVDEEVYEAE LKDADRNMGI GYMLKAAGII
     TCDPREAVKG YIRQCSISVN VRDLAVMAAT LSNGGVQPLT GESVIPQTSV RQVLSVMTTC
     GMYDAAGDWV SNVGIPAKSG VAGGIIGALP GQVGLASFSP KLDERGNSVR GVAMCEQLSR
     DMGLHMMDVS QIASATVRTS VATIVAGAHE PHNPNCQREV VIFSLRGAVR FAGSERLTRA
     LARELGSPDP EDPGSGRHEK ACAVVFSFRD AYSLNAIARR IVHEDIRRLL LDERSVVVVD
     PNGVLGMEVD VDGEKPFPHV FTSETEARDF IGGVGCQTVF KENNW
//
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