ID A0A498J094_MALDO Unreviewed; 243 AA.
AC A0A498J094;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Aromatic amino acid beta-eliminating lyase/threonine aldolase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_022244 {ECO:0000313|EMBL:RXH86971.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH86971.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH86971.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH86971.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) 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:RXH86971.1}.
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DR EMBL; RDQH01000336; RXH86971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498J094; -.
DR STRING; 3750.A0A498J094; -.
DR Proteomes; UP000290289; Chromosome 10.
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; 3.40.640.10; 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; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF96; TYROSINE 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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:UP000290289}.
FT MOD_RES 166
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 243 AA; 26726 MW; C3E3F558B9C1CD5F CRC64;
MNGPRHNSVL HGSTHESVVC TMVAARDQIL SQIGKENIGN LVVYGSDQTH SALQKVSQIV
GIHSKIFWAI ETTRSSSFAL SPELLQLVIC SDVKSGLVPF YLCATVGTTA TAAVDPLGPL
CNVAKDYGMW VHVDAAYAGN ACICPEFRHF IDGIECANSF SLSAHKWFFT TLNCCCLWVK
NPSALTNSMS VNLEGLRNKA TDSKQMVDNK DWQIALTRGF PATKLWLVLR NYGVENLRNF
IRI
//
