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Database: UniProt
Entry: A0A1Y3NC87_PIRSE
LinkDB: A0A1Y3NC87_PIRSE
Original site: A0A1Y3NC87_PIRSE 
ID   A0A1Y3NC87_PIRSE        Unreviewed;       248 AA.
AC   A0A1Y3NC87;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
GN   ORFNames=PIROE2DRAFT_7587 {ECO:0000313|EMBL:OUM65380.1};
OS   Piromyces sp. (strain E2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM65380.1, ECO:0000313|Proteomes:UP000195826};
RN   [1] {ECO:0000313|EMBL:OUM65380.1, ECO:0000313|Proteomes:UP000195826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2 {ECO:0000313|EMBL:OUM65380.1,
RC   ECO:0000313|Proteomes:UP000195826};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; KZ150835; OUM65380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3NC87; -.
DR   STRING; 73868.A0A1Y3NC87; -.
DR   Proteomes; UP000195826; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195826}.
SQ   SEQUENCE   248 AA;  28381 MW;  43429033D2B723C5 CRC64;
     MNTILNFSSK YNSKKHPKLN STTKKKRQSI LNNDFYKDEF SNSQKNGSEI VSLAYGSRFS
     TENLPKYVIP QKSSEPKVIS QLIEDQIKIE ANPSQNMATF VSTWMEPECE NLMTQTWSKN
     FADQDCYPMI QNIHKRCIGM LGHLFHAPDD QEVIGTATTG SSEAVMLGGL ALKWRWRKAR
     MEKNLDCSKP NIVFGSNAQV ALEKFARYFD VEMRMVPVNE KTNFCLSPKR ALKYIDENTI
     GVMVKLKK
//
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