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Database: UniProt
Entry: A0A067CMH6_SAPPC
LinkDB: A0A067CMH6_SAPPC
Original site: A0A067CMH6_SAPPC 
ID   A0A067CMH6_SAPPC        Unreviewed;       489 AA.
AC   A0A067CMH6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SPRG_04347 {ECO:0000313|EMBL:KDO30445.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO30445.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO30445.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO30445.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583201; KDO30445.1; -; Genomic_DNA.
DR   RefSeq; XP_012198667.1; XM_012343277.1.
DR   AlphaFoldDB; A0A067CMH6; -.
DR   STRING; 695850.A0A067CMH6; -.
DR   EnsemblProtists; KDO30445; KDO30445; SPRG_04347.
DR   GeneID; 24126796; -.
DR   KEGG; spar:SPRG_04347; -.
DR   VEuPathDB; FungiDB:SPRG_04347; -.
DR   OMA; NWQPLMV; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000030745; 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; 3.90.1150.10; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745}.
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   489 AA;  52118 MW;  AF185B0E335EBFA3 CRC64;
     MASPLHLDPA VVEAAAIASV KLGLAHHKTF ANEPADARGD LTLSAASPLV QASLAFDERS
     APARGTDITS LLSFLQTNLV GVASGFNANT DTFLAYVLGG VLPQANVLDF YINAVDPTTI
     SWSKAPLIQR LEMNVVHWFC DLVGYARDSS LGIFTQGASG ANFDAAVIAR VKKFPRNRDI
     ARGTVYVSSG AHFCNARGAR MAGILPEHVR QLPVDATGRL RLDALAAALA ADVANGLVPF
     LMVASLGTTS LGAVDDLNGM ADLADSYGCH LHCDGALGGF FCSRSRAHSV SLDFHKGMAL
     PYATSMLLVK DKNDLINGFS ANDDMEYLKK TEVNSRFGIG TQDEFDLDLI TFADCSPDLS
     RACKGLKVWW LLKLHGLDAW KAHFDHLLNV ADAARRAIAT IRGLELAPGD LNVVNFRANV
     PGDADTVNAA TDALLAAVNA RRAVFLSMAT YTTTDGVKYA TARACFMNHN VTLATVQTLV
     DELRAVLLP
//
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