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Database: UniProt
Entry: A0A135SCS8_9PEZI
LinkDB: A0A135SCS8_9PEZI
Original site: A0A135SCS8_9PEZI 
ID   A0A135SCS8_9PEZI        Unreviewed;       506 AA.
AC   A0A135SCS8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CNYM01_07434 {ECO:0000313|EMBL:KXH33631.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH33631.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH33631.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH33631.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) 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|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:KXH33631.1}.
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DR   EMBL; JEMN01001553; KXH33631.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135SCS8; -.
DR   Proteomes; UP000070054; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon 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   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.
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}.
FT   MOD_RES         323
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   506 AA;  54596 MW;  8C994156A0F4A3A7 CRC64;
     MNGTNGTNGH HAVPQTLKRA EEVEDGLIVP YIRAADEAAG QKANGYTSVN IEGVPSNVLV
     DTQKPEALVE KLKLSLPEGD GLGKEGLLDV VQKILRYSVN TWDQGFMDKL YASNTPVGVV
     SDLVLSVLNT NLHVYQVSPA LSVIEKITAR KFANLFGFNG PRAGGVTCQG GSASNLTSLV
     VARSALYPET KASGNGSHDF VIFTSAHGHY SVEKSALACG LGASSVWAVP IDAAGRMIPE
     ALRELVVRAK AEGKTPLYVN STAGTTVMGS YDPFEEISSI CKEFGLWFHI DASWGGSAIF
     SEKQKAKLKG SHLADSLTVN PHKMMNVPVT CSFLLTPDEK VFHKANTLPA GYLFHNVDEA
     EDVWDLADLT LQCGRRGDSL KLALAWIYYG AGGFEQQIDH AFSLAEHLAT LVQKSDNFVL
     VSSNPPPCLQ VCFYYTPNGQ LAEEPEANTR RTSEMVHKLI QRGFMIDYAP GERGSFFRVV
     VNCQTLQGTV DGLVKALEEV GKEIAA
//
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