ID   Q3ZQJ5_9MUSC            Unreviewed;       212 AA.
AC   Q3ZQJ5;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Alpha methyldopa hypersensitive protein {ECO:0000313|EMBL:AAW28055.1};
DE   Flags: Fragment;
GN   Name=amd {ECO:0000313|FlyBase:FBgn0083346};
GN   Synonyms=Amd {ECO:0000313|EMBL:AAW28055.1};
OS   Drosophila viracochi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=306030 {ECO:0000313|EMBL:AAW28055.1};
RN   [1] {ECO:0000313|EMBL:AAW28055.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15970444; DOI=10.1016/j.ympev.2005.05.005;
RA   Robe L.J., Valente V.L., Budnik M., Loreto E.L.;
RT   "Molecular phylogeny of the subgenus Drosophila (Diptera, Drosophilidae)
RT   with an emphasis on Neotropical species and groups: a nuclear versus
RT   mitochondrial gene approach.";
RL   Mol. Phylogenet. Evol. 36:623-640(2005).
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; AY699244; AAW28055.1; -; Genomic_DNA.
DR   FlyBase; FBgn0083346; Dvra\amd.
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: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         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAW28055.1"
FT   NON_TER         212
FT                   /evidence="ECO:0000313|EMBL:AAW28055.1"
SQ   SEQUENCE   212 AA;  23737 MW;  28914FCC936AACC3 CRC64;
     CIEKAGVLAA MPIKLLPAGE DLVLRGDTLK QAXERDVATG LIPVIXVATL GTTGTCAYDD
     IESLASICEE NSVWLHVDSA YAGGAFALEE CSELRRGLER VDSLNFNLHK FMLVNFDCAA
     MWLRDANKVI DSFNVDRIYL KHKHEGQTQI PDFRHWQIPL GRRFRALKVW ITFRTLGAEG
     LRAHIRKHIS LAGQFADLVK ADERFELIAP RA
//