ID Q0U7M3_PHANO Unreviewed; 499 AA.
AC Q0U7M3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_12241 {ECO:0000313|EMBL:EAT80653.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80653.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
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; CH445345; EAT80653.1; -; Genomic_DNA.
DR RefSeq; XP_001802467.1; XM_001802415.1.
DR AlphaFoldDB; Q0U7M3; -.
DR STRING; 321614.Q0U7M3; -.
DR EnsemblFungi; SNOT_12241; SNOT_12241; SNOG_12241.
DR GeneID; 5979377; -.
DR KEGG; pno:SNOG_12241; -.
DR VEuPathDB; FungiDB:JI435_122410; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_6_2_1; -.
DR InParanoid; Q0U7M3; -.
DR OMA; WVIGGSH; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11999:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE 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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT MOD_RES 320
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 499 AA; 54955 MW; FA84FF27A0FC7346 CRC64;
MESARSEYQE LLRSAIAGLQ LEPSPTHVLP NQKAVEHARK TLANQLREDG LGLSETIRHL
QEDLKPAFNA SSRSPNYYGF VTGGVTPAAS IADNFVTAYD QNVSVHLPDE SIATDVEDHA
LSLLCELLNF QPDQWPHRIF TTGATASNVV GLACGREYVI AEASAHRTHT ENSVGEYGIM
EAMHRAGLDN IQILTTVPHS SLSKAASVLG MGRASIKHVG REDAPHRFDF KLLKSLMEQP
SSASIVAVSA SEVNTGLFAT SVLEEMEELR RLCDMHGAWI HVDGAFGILG RLLDSPRYQT
ITQACAGLEL ADSITGDGHK LLNVPYDCGF FLSRHRHIAE RVFQNPNAAY LATSNGPDSI
MSPLNVGLEN SRRFRALPVY ASLIAYGKSG YRDMLERQID LSRGIAKFIL ESETYELLPE
SDKSMEERLS TIYIIVLFRA KDGDLNKNLV DKIKATKKIY VSGTAWDGKP ACRFAVSNWQ
TDVTRDLPII EEVLQSVAE
//
