ID A0A0D1ZBT4_9EURO Unreviewed; 274 AA.
AC A0A0D1ZBT4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=PV07_08399 {ECO:0000313|EMBL:KIW25201.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW25201.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW25201.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW25201.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847044; KIW25201.1; -; Genomic_DNA.
DR RefSeq; XP_016245417.1; XM_016395561.1.
DR AlphaFoldDB; A0A0D1ZBT4; -.
DR STRING; 569365.A0A0D1ZBT4; -.
DR GeneID; 27347593; -.
DR VEuPathDB; FungiDB:PV07_08399; -.
DR HOGENOM; CLU_069674_0_0_1; -.
DR OrthoDB; 842at2759; -.
DR Proteomes; UP000054466; 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 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:UP000054466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..274
FT /note="glutaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012045578"
FT ACT_SITE 92
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 274 AA; 29563 MW; AE59D81E3BC6EEF7 CRC64;
MTITVGVLAL QGAFLEHLVL LQRAADYLRR EDTAASFEFT EVRNAKDLAR CDALIIPGGE
STTISLVAAQ SGLLEPLREF VKVNRKPTWG TCAGLILLAE AANATKKGGQ DLIGGLDVRV
NRNHFGRQVE SFQADLDLPF LQNNGAVDKT PFPGVFIRAP VVEKILPNVE GIQKGEQQLA
ETVVAPYKSA KDDHARQAMS SHVDIMGKLP GRLKKAAGMG PEVHAGEEVG DIIAVKQGNV
FGTSFHPELT SDIRIHVWWL RQVLDAVGTA NGVS
//