ID   D2SSN7_DROPU            Unreviewed;       282 AA.
AC   D2SSN7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Alpha methyldopa hypersensitive {ECO:0000313|EMBL:ACV70023.1};
DE   Flags: Fragment;
GN   Name=amd {ECO:0000313|EMBL:ACV70023.1};
OS   Drosophila paulistorum (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46793 {ECO:0000313|EMBL:ACV70023.1};
RN   [1] {ECO:0000313|EMBL:ACV70023.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Llanos {ECO:0000313|EMBL:ACV70023.1};
RX   PubMed=20049511; DOI=10.1007/s10709-009-9432-5;
RA   Robe L.J., Cordeiro J., Loreto E.L., Valente V.L.;
RT   "Taxonomic boundaries, phylogenetic relationships and biogeography of the
RT   Drosophila willistoni subgroup (Diptera: Drosophilidae).";
RL   Genetica 0:0-0(2010).
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}.
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DR   EMBL; FJ664502; ACV70023.1; -; Genomic_DNA.
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; 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:SF60; 3,4-DIHYDROXYPHENYLACETALDEHYDE SYNTHASE; 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}.
FT   MOD_RES         170
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACV70023.1"
FT   NON_TER         282
FT                   /evidence="ECO:0000313|EMBL:ACV70023.1"
SQ   SEQUENCE   282 AA;  31182 MW;  FD42C6C19C8FB694 CRC64;
     HATEGPGGGA IQGSASEAVL VAVLAAREQA VVKYRELHPE LSESEIRGKL IAYSSDQSNS
     CIEKAGVIAA MPIKLLPAGE DLILRGEALK KAIEEDVQEG RIPVICIATL GTTGTCAYDD
     IESLATVCED HNVWLHVDAA YAGGAFALDE CADLRRGIDR VXSLNXNLHK FMLVNFDCSA
     MWLKDANKVV DSFNVDRIYL KHKYEGQSQI PDFRHWQIPL GRRFRALKVW ITFRTLGAEG
     LRAHVRXHIS LAEQFEKLVK DDKRFELVAP RALGLVCFRP KG
//