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Database: UniProt
Entry: S0DYP5_GIBF5
LinkDB: S0DYP5_GIBF5
Original site: S0DYP5_GIBF5 
ID   S0DYP5_GIBF5            Unreviewed;       297 AA.
AC   S0DYP5;
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=Related to glutamic acid decarboxylase {ECO:0000313|EMBL:CCT65568.1};
GN   ORFNames=FFUJ_02523 {ECO:0000313|EMBL:CCT65568.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT65568.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679025; CCT65568.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0DYP5; -.
DR   STRING; 1279085.S0DYP5; -.
DR   EnsemblFungi; CCT65568; CCT65568; FFUJ_02523.
DR   VEuPathDB; FungiDB:FFUJ_02523; -.
DR   HOGENOM; CLU_937043_0_0_1; -.
DR   OrthoDB; 2606018at2759; -.
DR   Proteomes; UP000016800; Chromosome 3.
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; 3.40.640.10; 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|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  32823 MW;  FDF73AFAC00A28B2 CRC64;
     MRNPSPPPFE EHPRTTRDEG EGRTKRLFDE VVRWGVLFRT HRPDHAEARS IVPRQISFDS
     MSESGLTDEQ LIPELRSIIT KSTNLTSRDF LGFPDVTMCP AAVGAAPLIP LLNQNMVNPE
     TCPPEATFVE MEVIHWLREA LGYPVLGAYT KAMDVGGVFT PGGCLSNFVA LLAAREKCFP
     GSCSNGIPVL PSKIRVLVPD IAENRSIRSA MAMMSLGENN IVPVPVDAEF HMDQEALRRI
     ISQEKGLGNI VMACVAYAGD PTCLRIDDLY GLSQILKEKD IWFHVDACRG SQLAFLE
//
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