ID   F4YFL4_9MUSC            Unreviewed;       301 AA.
AC   F4YFL4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alpha methyldopa hypersensitive {ECO:0000313|EMBL:ADE08578.1};
DE   Flags: Fragment;
GN   Name=amd {ECO:0000313|EMBL:ADE08578.1};
OS   Drosophila acutilabella.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=133978 {ECO:0000313|EMBL:ADE08578.1};
RN   [1] {ECO:0000313|EMBL:ADE08578.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cenzi de Re F., Loreto E.L.S., Robe L.J.;
RT   "Gene and species trees reveal mitochondrial and nuclear discordance in the
RT   Drosophila cardini group (Diptera: Drosophilidae).";
RL   Invertebr. Biol. 129:353-367(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; HM006861; ADE08578.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4YFL4; -.
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         177
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADE08578.1"
FT   NON_TER         301
FT                   /evidence="ECO:0000313|EMBL:ADE08578.1"
SQ   SEQUENCE   301 AA;  33431 MW;  B00DED6F24E288F2 CRC64;
     KLPSHFLHET EGPGGGVIQG SASEAVLVAV LAAREQVVRR ERENHPEMSE SDIRGKLIAY
     SSDQSNSCIE KAGVLAAMPI KLLPASEDLV LRGPALKAAI ERDVAAGYIP VICIATLGTT
     GTCAYDEIES LASVCKEHQV WIHVDAAYAG AALALEECAE LRRGLDRVDS LNFNLHKFML
     VNFDCAAMWL RDANKVVDSF NVDRIYLKHK YEGHTQIPDF RHWQIPLGRR FRALKVWITF
     RTLGAEGLRA HVRKHIDLAA QFESLVRSDP RFELIAPRAL GLVCFRAKGD NEITSQLLLR
     L
//