ID   A0A183SJP5_SCHSO        Unreviewed;       695 AA.
AC   A0A183SJP5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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};
OS   Schistocephalus solidus (Tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX   NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000459101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SSLN_0000459101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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DR   AlphaFoldDB; A0A183SJP5; -.
DR   WBParaSite; SSLN_0000459101-mRNA-1; SSLN_0000459101-mRNA-1; SSLN_0000459101.
DR   Proteomes; UP000050788; Unplaced.
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; 2.
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   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 2.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50}.
FT   REGION          199..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         521
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   695 AA;  78518 MW;  2F1A6F57DCADF81A CRC64;
     LKIWMVLRSY GVEGVQKHIR RQVEMAHYLE RIILEDGRFE IISQVVLGIV CFRLKQSNRL
     TRLLHKKIEA DGRFLLVMGS TKHPKELFYI RVAICYQFPD NDEYADVPWK GFLGVGLFYL
     AISPSQSSLM PQSPVRAGHP TACGHLELVG LLTPEDLGFR LVLNYQYLNI DLGIQKGSGS
     DDWQEEMKQC AGDEYTINGT QDGRRENDFA ESSGQNQQEH EYYQDMRTYC KRAVDVTAAY
     LEGVAKHRVF PEVEPGYLRP LLPAEAPQNP ESWDAIFDDV NNVLMPGAVH WHHPHFHAYF
     MTANSYAALC ADIMSNAIGG LGITWATSPV NTELEVVMVD WLAKALNLPE FFLSHTQGGG
     VIHSSPGEST FICMLAARNA AIAKYQVEHP VASNFQVMEK LVAYYSDQAH ATVERAGRLS
     MLRVRALPSN KDFELDGETL RKAVEEDLTS GLIPFFCTAT LGTTGTCSYD RLTELGPVCQ
     QYDIWLHADA AYAGSALICP EFRSLMPGLE YLSSFTFNPH KWLHMNFDLS VLWLKDSQAF
     VTTFSVDATY LQHSKLGKMP DFRHVAIAHI LEGLLIEDGR FEIVGKVTLG LVCFRLEVTS
     KAKHCGSSYP FAFLYFNFQS SNELTRLLHE RIESDGRLHM VTSRIKRPVE KLYIRVSINY
     QFITEDLIRK TFDVICELAT EILAKYDLPD TAASV
//