ID   A0A024TXH8_9STRA        Unreviewed;       464 AA.
AC   A0A024TXH8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=H310_08807 {ECO:0000313|EMBL:ETV98728.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV98728.1};
RN   [1] {ECO:0000313|EMBL:ETV98728.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV98728.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; KI913969; ETV98728.1; -; Genomic_DNA.
DR   RefSeq; XP_008872925.1; XM_008874703.1.
DR   AlphaFoldDB; A0A024TXH8; -.
DR   STRING; 157072.A0A024TXH8; -.
DR   EnsemblFungi; H310_08807-t26_1; H310_08807-t26_1-p1; H310_08807.
DR   EnsemblProtists; ETV98728; ETV98728; H310_08807.
DR   GeneID; 20085857; -.
DR   VEuPathDB; FungiDB:H310_08807; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   OrthoDB; 51460at2759; -.
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; 3.90.1150.10; 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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 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}.
FT   MOD_RES         295
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   464 AA;  49852 MW;  2307ED6A1EC55CB7 CRC64;
     MHPTLARDLE TLPDIASAAQ ALAVDYLCNV DAVPAARTPS RQRNAVEADD VSVGVGAVGA
     LERFRTQWLP HLSGSAGPRY LGFVTGGSTP ASLVGDWITS TVDQNPTSNW DSEAPSLERE
     TVASLAKWFN LPSHTGVFVT GATMSNFVGL AIAREWVGER RGVHVSTDGL AALGPVRIFA
     GTPHSSVSKA ASMLGLGRSA VHRVATLAGR EAMDIDALDV AMTSFNGTCI VVASAGTVNT
     GDFDDLVQLA ALKKRHDFWL HVDGAFGAFA ALDATLAPLV AGMDDADSVC IDCHKWMNVP
     YDSALQFTKR QDLQVAVFQN AAAYLGNVAS NVTPNFVHLT PENSRRWRAL AAWFSVVAYG
     RDGHAEIVSR NVECARLLAT RLGEFKDLVA VVAPVRLNVV LFTVQGVDDE TKMLVWLQRL
     TDTHQVFLTP TTYQGQWGVR AAFSNWRTTS HDVDVVVDAI KSVL
//