ID   M1LEZ1_9NEOP            Unreviewed;       152 AA.
AC   M1LEZ1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE            EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE   AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
DE   Flags: Fragment;
OS   Ypsolopha ustella.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Yponomeutoidea;
OC   Ypsolophidae; Ypsolopha.
OX   NCBI_TaxID=1101069 {ECO:0000313|EMBL:AGF41283.1};
RN   [1] {ECO:0000313|EMBL:AGF41283.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sohn J.-C., Regier J.C., Mitter C., Davis D., Landry J.-F., Zwick A.,
RA   Cummings M.P.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGF41283.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23383061; DOI=10.1371/journal.pone.0055066;
RA   Sohn J.C., Regier J.C., Mitter C., Davis D., Landry J.F., Zwick A.,
RA   Cummings M.P.;
RT   "A molecular phylogeny for yponomeutoidea (insecta, lepidoptera, ditrysia)
RT   and its implications for classification, biogeography and the evolution of
RT   host plant use.";
RL   PLoS ONE 8:E55066-E55066(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         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; KC243059; AGF41283.1; -; mRNA.
DR   AlphaFoldDB; M1LEZ1; -.
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   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
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   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 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.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGF41283.1"
FT   NON_TER         152
FT                   /evidence="ECO:0000313|EMBL:AGF41283.1"
SQ   SEQUENCE   152 AA;  18073 MW;  800EA84C25938376 CRC64;
     MLVNFDCSAM WLKQPRWIID AFNVDPLYLK HDQQGSAPDY RHWQIPLGRR FRALKLWFVL
     RLYGVENLQK HIRKHIALAH LFEKLCVADE RFEIFEEVTM GLVCFRLKGS NELNEDLLRR
     INGRGKIHLV PSKIDDVYFL RLAICSRFSE ES
//