ID   S3BXH6_OPHP1            Unreviewed;       540 AA.
AC   S3BXH6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:EPE05222.1};
GN   ORFNames=F503_03827 {ECO:0000313|EMBL:EPE05222.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05222.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE05222.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05222.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(2013).
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}.
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DR   EMBL; KE148157; EPE05222.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3BXH6; -.
DR   STRING; 1262450.S3BXH6; -.
DR   VEuPathDB; FungiDB:F503_03827; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000016923; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923}.
FT   MOD_RES         348
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   540 AA;  57248 MW;  2187AE70D9457C37 CRC64;
     MAANGTHLTA TNGAVTNGAA EASAPVSVNS TPSRAAELSE LIDAVKALVV PFVDNADQAF
     AEREQGGPAG ASTASLPVRT ALVETLTPKQ VISRLDLNLS KGEGGGRTAA LETIQRILEL
     SVNTWDQGFL DKLYASTTPI GVAAELLLSV LNTNLHVFQV SPALTVIEKT TARELAHLFG
     FTGPRAGGIT VAGGSASNFT SVIVARNTLY PETKIDGNGV GRRFALFTSA HGHYSVEKAA
     QAAGLGSGAV WTVPIDAAGR MIPAELEKRI GEAKEAGQTP LYVNATAGTT VLGSYDPFEE
     ISAVCKRNGG LWMHIDGSWG GPAIFSAQQR HKLAGSHLAD SLTVNPHKMM NVPVTCSFLL
     GPDLGIFHKA NTLPAGYLFH SAGSDEETES GYQEVWDLAD LTLQCGRHGD SLKLALAWVY
     EGAAGFERQT DHAFAMAALL ADQVASRPDL FSLVSSNPPP CLQVCFYYAG ETSGQPHTND
     EVNSQRTRDA VQLLIRRGYM IDFAPGDHGG FFRVVVNWQT RPGTVEGLVR ALEIVRKEVN
//