ID   DHAPP_DROLE             Reviewed;         439 AA.
AC   O96569; Q964M1;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=3,4-dihydroxyphenylacetaldehyde synthase 2;
DE            Short=DHPAA synthase;
DE            EC=4.1.1.107 {ECO:0000250|UniProtKB:P18486};
DE   AltName: Full=Alpha-methyldopa hypersensitive protein;
DE   Flags: Fragment;
GN   Name=amd; Synonyms=l(2)amd;
OS   Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Scaptodrosophila.
OX   NCBI_TaxID=7225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Beirut;
RX   PubMed=10231575; DOI=10.1016/s0378-1119(99)00096-7;
RA   Tatarenkov A., Saez A.G., Ayala F.J.;
RT   "A compact gene cluster in Drosophila: the unrelated Cs gene is compressed
RT   between duplicated amd and Ddc.";
RL   Gene 231:111-120(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-356.
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   -!- FUNCTION: Catalyzes both the decarboxylation and deamination of L-dopa
CC       to 3,4-dihydroxylphenylacetaldehyde (DHPAA) (By similarity). Probably
CC       responsible for the protein cross-linking during the development of
CC       flexible cuticles (By similarity). Participates in catecholamine
CC       catabolism (By similarity). {ECO:0000250|UniProtKB:P18486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + L-dopa + O2 = 3,4-dihydroxyphenylacetaldehyde +
CC         CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55524, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57504; EC=4.1.1.107;
CC         Evidence={ECO:0000250|UniProtKB:P18486};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55525;
CC         Evidence={ECO:0000250|UniProtKB:P18486};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P18486};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF091329; AAC67583.1; -; Genomic_DNA.
DR   EMBL; AF293714; AAK94687.1; -; Genomic_DNA.
DR   AlphaFoldDB; O96569; -.
DR   SMR; O96569; -.
DR   FlyBase; FBgn0025670; Dleb\amd.
DR   Proteomes; UP000504634; Unplaced.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR   GO; GO:0006584; P:catecholamine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0040003; P:chitin-based cuticle development; ISS:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Catecholamine metabolism; Cuticle; Decarboxylase; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           <1..439
FT                   /note="3,4-dihydroxyphenylacetaldehyde synthase 2"
FT                   /id="PRO_0000147009"
FT   MOD_RES         232
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   439 AA;  48494 MW;  CFB8E419E688260D CRC64;
     VPPHMHGYYP TSVSYPSIVG EMLASGFSII GFSWICSPAC TELEVVVMDW LAKFLKLPEH
     FLHATEGPGG GVIQGSASEA VLVAVLAARE QAVCRVRASH PELSESDIRG KLVAYSSDQS
     NSCIEKAGVL AAMPIKLLPA GEDLILRGAA LRSAIEQDVT AGLIPVICIA TLGTTGTCAY
     DDVDSLATVC EQYNVWLHVD AAYAGGAFAL DECSELRRGL ERVDSLNFNL HKFMLVNFDC
     SAMWLRDANK VVDSFNVDRI YLKHKYEGQT QIPDFRHWQI PLGRRFRALK VWITFRTLGA
     EGLRAHVRKH IELAKKFEVF VLADARFELV APRALGLVCF RAKGENEITA QLLQRLMERK
     KIYMVKAEHR GQLFLRFAVC GMDPKPSDIE FAWTEIGTQL TALLAEQEHL AAVGKAGDVT
     ELTQQFGLQL TNGTNEKSQ