ID   E3RP31_PYRTT            Unreviewed;       518 AA.
AC   E3RP31;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Glutamate decarboxylase 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTT_10362 {ECO:0000313|EMBL:EFQ92522.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ92522.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ92522.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GL534277; EFQ92522.1; -; Genomic_DNA.
DR   RefSeq; XP_003299386.1; XM_003299338.1.
DR   AlphaFoldDB; E3RP31; -.
DR   STRING; 861557.E3RP31; -.
DR   EnsemblFungi; EFQ92522; EFQ92522; PTT_10362.
DR   KEGG; pte:PTT_10362; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   MOD_RES         332
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   518 AA;  55774 MW;  7A8EC0F0020076E4 CRC64;
     MASESATQSP LNRADEVQDL LTAIQHLIVP FIRAADEDAL TKPTGHGLQV SGGGPRTVLV
     EHHPPQKLES LLAQELEISN AGTEKQGEDQ GKEGLVKLVS SILKYSVNTW DQGFLDKLYA
     STNAVGVVSE LLLAVLNTNA HVYAVSPVLT LIEKRTTTYL ASLFSLPPST SGGLTLPGGS
     ASNSTAITLA RNTLYPLTKT EGNASFKFTL FTSEHGHYSI EKAANILGLG TKNVITVPVD
     ENGCMIPSAL EQKINESRQR GETPLFLNAT AGTTVHGSFD PFTALAAICK TENIWFHIDG
     SWGGSVVFSP KYRASRLAGA ELADSITINP HKMLGTPVTC SFLLARDMNQ MHKALTLPAG
     YLFHGSTGSV DARDVYDLGD LSPQCGRRAD SLKLFLALKY YGPEHFARLV ETAYEGAEYL
     LSKVKESGNF VAISPEPLPC LQVCFYYAKG GVLREDKELN SRTTTEIAQR LVSRGFMVDF
     APGEKGKFFR VVVNGGTLVG TLDGLVKAIE ETGEELGF
//