ID A0A0N5CMI2_THECL Unreviewed; 512 AA.
AC A0A0N5CMI2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=TCLT_LOCUS1365 {ECO:0000313|EMBL:VDM96763.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000136401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000136401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM96763.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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|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; UYYF01000167; VDM96763.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5CMI2; -.
DR WBParaSite; TCLT_0000136401-mRNA-1; TCLT_0000136401-mRNA-1; TCLT_0000136401.
DR OMA; LKHEHQA; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; 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; 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 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; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776}.
FT MOD_RES 340
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 512 AA; 58348 MW; F79EDC981E64D08A CRC64;
MNSDEFCKYG SQMIDIVAKY WKSLRTRTPV PDVQPGFMRQ LVPQDPPAAP ESWENIFQDI
DKVVINGNTH WQHPNFFAYF PTACSYQAIM ADILSGGLAS IGFSWKSSPS MTELEISMMD
WLAKALALPS EFLNSSTESG LGIIQNTASD ATYIALLAAR ARAVEYIKSN ENSTEQKQQV
VLNEEGSNLD LGELCEYPYH DATIISKLIA YCSDQAHSSV SKGAMLAAVR LRKLKSVKND
CNGNFSVTAK MLEAAIKVDR ANGLIPFIFI MTLGTTSTCG VDPIDELASI CRRENIWVHV
DSAYADRMLH LSGAFLLLPE YRYLTRGFEY IDSFNMNTHK ALQMNFDCSP MWFRNGKKYL
KYFEVDPVYL KHDQTSATDY RHLQIALGRR FRSLKIWFVL RNIGITGLQQ HLRKMIDLAQ
HFEFLIQNDP LLELFVPRAW GLVCFRMKNS TNEMNEELNS KINLDRRIHI VASSVHGVYF
LRFVACSTLT NHDDVRQAYQ IIHNYAEEIR KS
//
