ID A0A2K0WAJ6_GIBNY Unreviewed; 493 AA.
AC A0A2K0WAJ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FNYG_07381 {ECO:0000313|EMBL:PNP79305.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP79305.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP79305.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP79305.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNP79305.1}.
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DR EMBL; MTQA01000092; PNP79305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WAJ6; -.
DR STRING; 42673.A0A2K0WAJ6; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000236664; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
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 InterPro; IPR021115; Pyridoxal-P_BS.
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 PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000236664}.
FT MOD_RES 310
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 493 AA; 54712 MW; 91D3D5CEA1571D3A CRC64;
MDSAEFREAA RTAIDEITDY YDNVSSQRVV SDVKPGYLRP LLPSSAPLEG ESWSDIHADI
ESKILPGITH WANPRFMAFF PCSSSYPAAL AEMYSNTFNG AHFNWICSPA VTELETIVMD
WLAKALGLPE CYLSGGSTHG GGVIHGSASE AILTVMCAAR DKYLAAVTKD MDEDAVWAVR
SKLVALGSSG SHSSTKKAAQ ILGVRFVAIP VTEEDGFAMT GRAVAKTVAE LRARGLEPFY
LTATMGTTDV CAVDDFAGIV EALSPTAGTE RDIWVHVDAA YAGSALLLEE NQPLTTPMAD
FHSFNFNPHK WMLTTFDCSA VWVRSRAWLI QSLSIKPPYL RNQFSDNELV TDYRDWQIPL
GRRFRSLKLW FVLRSFGIRG LQAHIRNGVT LGESLQSKLA SRPDLFTIFT SARFGLVTFR
VKGADEAEIN ARTEELYEWV NRTGEFYLTS TVVNDKFAIR VCTGVERVRE EHVQRIFDVL
VERTEADLGK TKQ
//
