ID   B3TE73_9NEOP            Unreviewed;       436 AA.
AC   B3TE73;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 45.
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   Mirina christophi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Endromidae; Mirina.
OX   NCBI_TaxID=475302 {ECO:0000313|EMBL:ABW39106.1};
RN   [1] {ECO:0000313|EMBL:ABW39106.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Regier J.C.;
RT   "PCR primers that amplify across Panarthropoda.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; EU032839; ABW39106.1; -; mRNA.
DR   AlphaFoldDB; B3TE73; -.
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   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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: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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
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         283
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABW39106.1"
FT   NON_TER         436
FT                   /evidence="ECO:0000313|EMBL:ABW39106.1"
SQ   SEQUENCE   436 AA;  49307 MW;  3A9BC82A84D6ABFF CRC64;
     LENIRDRQVV PSVKPGYLRP LVPERAPEQP EPWTSVMADI ERVVMSGVTH WHSPRFHAYF
     PTANSYPAIV ADMLSGAIAC IGFTWIASPA CTELEVVMLD WLGQMLGLPE QFLARSGGEG
     GGVIQGTASE ATLVALLGAK ARTMQRVKEQ HPEWSDNDVL AKLVGYCNKQ AHSSVERAGL
     LGGVKLRNLQ PDGKRRLRGD ILREAIEEDI RNGLIPFYVV ATLGTTSSCT FDALDEIGDV
     CASHNVWLHV DAAYAGSAFI CPEYRYLMKG IEKADSFNFN PHKWLLVNFD CSAMWLKEPR
     WIVDAFNVDP LYLKHDQQGS APDYRHWQIP LGRRFRALKL WFVLRLYGVE NLQKHIRKQI
     ALAHLFERLC VSDERFELFE EVTMGLVCFR LKGGNDINEE LLRRINGRGK IHLVPSKIDD
     VYFLRLAICS RFTEDS
//