ID A0A183TGN2_SCHSO Unreviewed; 319 AA.
AC A0A183TGN2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
GN ORFNames=SSLN_LOCUS15628 {ECO:0000313|EMBL:VDM02014.1};
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_0001622101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0001622101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM02014.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDM02014.1,
RC ECO:0000313|Proteomes:UP000275846};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYSU01040137; VDM02014.1; -; Genomic_DNA.
DR STRING; 70667.A0A183TGN2; -.
DR WBParaSite; SSLN_0001622101-mRNA-1; SSLN_0001622101-mRNA-1; SSLN_0001622101.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; Unassembled WGS sequence.
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; 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 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 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000275846}.
SQ SEQUENCE 319 AA; 35371 MW; F61CA501E68B42A0 CRC64;
MRTQCTKAIN LSVDYLQGIA KHRVFPQVEP GYLRPLLPEE APLEPEPWEQ IFSDVDKLLM
PGVTHWNHPH FHAYLAAANS YPALCADIIS TSIGGIGFTW ASSPVSTELE VVMLDWLAKL
LKLPEFFLSH TEGGGVIQGT SSESTFVSLL AARNVALEKY LRLHPKSSKF EILEKLVGYH
SDQAHASVER AGLLSLLRFR ALPCNQKFEL DGQTLRRAVE EDVANGLIPF YCAATLGTTA
TCSYDRLPEI GPICQEYDMW LHVDAAYAGS ALICPEFHRL MPGLEVRLHH LPQPQVCKKI
SLTCSGEGQR FTVLESSVA
//
