ID   Q964L1_DRORO            Unreviewed;       344 AA.
AC   Q964L1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Alpha methyldopa hypersensitive {ECO:0000313|EMBL:AAK94697.1};
DE   Flags: Fragment;
GN   Name=amd {ECO:0000313|EMBL:AAK94697.1,
GN   ECO:0000313|FlyBase:FBgn0046145};
OS   Drosophila robusta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7257 {ECO:0000313|EMBL:AAK94697.1};
RN   [1] {ECO:0000313|EMBL:AAK94697.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tatarenkov A.N., Zurovcova M., Ayala F.J.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAK94697.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11476641; DOI=10.1006/mpev.2001.0967;
RA   Tatarenkov A., Zurovcova M., Ayala F.J.;
RT   "Ddc and amd sequences resolve phylogenetic relationships of Drosophila.";
RL   Mol. Phylogenet. Evol. 20:321-325(2001).
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; AF293724; AAK94697.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q964L1; -.
DR   FlyBase; FBgn0046145; Drob\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; 3.90.1150.10; 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         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK94697.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:AAK94697.1"
SQ   SEQUENCE   344 AA;  38024 MW;  5C7EE19EB52EAC37 CRC64;
     VSYPSIVGEM LASGFGIIGF SWICSPACTE LEVVVMDWLA KFLNLPEHFL HETEGPGGGV
     IQGSASEAVL VAVLAAREQA VRRERECHPE LSESEIRGKL IAYSSDQSNS CIEKAGVLAA
     MPIKLLPAGE DLVLRGATLS EAIERDVAAG LIPVICIATL GTTGTCAYDD IESLAGICER
     RQVWLHVDAA YAGGAFALDE CAQLRRGLDR VDSLNFNLHK FMLVNFDCSA MWLRDANKVV
     DSFNVDRIYL KHKYEGQTQL PDFRHWQIPL GRRFRALKVW ITFRTLGAEG LRAHMRKHID
     LAAQFEALVK ADERFELVAP RALGLVCFRA KGDNEITAQL LQRL
//