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Database: UniProt
Entry: V5D508_TRYCR
LinkDB: V5D508_TRYCR
Original site: V5D508_TRYCR 
ID   V5D508_TRYCR            Unreviewed;       370 AA.
AC   V5D508;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TCDM_09801 {ECO:0000313|EMBL:ESS62526.1};
OS   Trypanosoma cruzi Dm28c.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS62526.1, ECO:0000313|Proteomes:UP000017861};
RN   [1] {ECO:0000313|EMBL:ESS62526.1, ECO:0000313|Proteomes:UP000017861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dm28c {ECO:0000313|EMBL:ESS62526.1,
RC   ECO:0000313|Proteomes:UP000017861};
RX   PubMed=24482508;
RA   Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA   Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT   "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL   Genome Announc. 2:e01114-13(2014).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESS62526.1}.
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DR   EMBL; AYLP01000178; ESS62526.1; -; Genomic_DNA.
DR   EnsemblProtists; ESS62526; ESS62526; TCDM_09801.
DR   VEuPathDB; TriTrypDB:TCDM_09801; -.
DR   Proteomes; UP000017861; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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   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:UP000017861}.
SQ   SEQUENCE   370 AA;  40176 MW;  AE6820892F69F205 CRC64;
     MLKKAARCIG IRHIRVLKTV YSPHVHNYPM QPDMLKASLA EDVANGLYPL LVCGVFGART
     TGAVDPLEEL AEICHRVKVW FHXXXXDASH SGLALAASAA YGFRDGAEQS GEFASVDEKD
     AAAERMWEQC TSTFHRAALL ADSIHFGVST SFLPTLSANI SASLLYVADV AKVKVTMQGM
     NAEDEAGGNT WCTPGMTDVA SLRLDAPEMR SNEIFRLALM LMPCIHASVG SAVRAHQATL
     RYLERRLRAD GRFDCSLHAS CFGMVLFRWL TLADEETAGL MQRWSDLLAS SSAMNEAGGH
     RYPHRVSLGL TQVQRRVYIC VALAAEGGDG DACVSRCDVD ALVDLLKTAA DEWRDISSSV
     TSAISSKSKT
//
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