ID   DHAPP_DROSI             Reviewed;         328 AA.
AC   P81893;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 1.
DT   25-MAY-2022, entry version 77.
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 simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=St. Lucia;
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).
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; AF121109; AAD25393.1; -; mRNA.
DR   AlphaFoldDB; P81893; -.
DR   SMR; P81893; -.
DR   GO; GO:0019239; F:deaminase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0036468; F:L-dopa decarboxylase activity; IEA:EnsemblMetazoa.
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:0042424; P:catecholamine catabolic process; IEA:EnsemblMetazoa.
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   2: Evidence at transcript level;
KW   Catecholamine metabolism; Cuticle; Decarboxylase; Lyase;
KW   Pyridoxal phosphate.
FT   CHAIN           <1..>328
FT                   /note="3,4-dihydroxyphenylacetaldehyde synthase 2"
FT                   /id="PRO_0000147011"
FT   MOD_RES         222
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         328
SQ   SEQUENCE   328 AA;  35978 MW;  DF027FC84442254A CRC64;
     TSTSYPSIVG EMLASGFGVI GFSWICSPAC TELEVVVMDW LAKFLKPPAH FQHASDGPGG
     GVIQGSASEA VLVAVLAARE QAVASYRESH PELSESEVRG RLVAYSSDQS NSCIEKAGVL
     AAMPIRLLPA GEDFVLRGDT LRGAIEEDVA AGRIPVICVA TLGTTGTCAY DDIESLSAVC
     EEFKVWLHVD AAYAGGAFAL EECSDLRKGL DRVDSLNFNL HKFMLVNFDC SAMWLRDANK
     VVDSFNVDRI YLKHKHEGQS QIPDFRHWQI PLGRRFRALK VWITFRTLGA EGLRNHVRKH
     IELAKQFEQL VLKDSRFELV APSALGLV