ID   C5IXK9_ENTFC            Unreviewed;       361 AA.
AC   C5IXK9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Tyrosine decarboxylase {ECO:0000313|EMBL:ACS15338.1};
DE   Flags: Fragment;
OS   Enterococcus faecium (Streptococcus faecium).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1352 {ECO:0000313|EMBL:ACS15338.1};
RN   [1] {ECO:0000313|EMBL:ACS15338.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ef1 {ECO:0000313|EMBL:ACS15338.1};
RX   PubMed=21356448; DOI=10.1016/j.fm.2010.10.005;
RA   Capozzi V., Ladero V., Beneduce L., Fernandez M., Alvarez M.A., Benoit B.,
RA   Laurent B., Grieco F., Spano G.;
RT   "Isolation and characterization of tyramine-producing Enterococcus faecium
RT   strains from red wine.";
RL   Food Microbiol. 28:434-439(2011).
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|RuleBase:RU000382}.
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DR   EMBL; FJ972172; ACS15338.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5IXK9; -.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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}.
FT   MOD_RES         253
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACS15338.1"
FT   NON_TER         361
FT                   /evidence="ECO:0000313|EMBL:ACS15338.1"
SQ   SEQUENCE   361 AA;  40093 MW;  F5B7F55D275A616A CRC64;
     TKLQNNELKR GWGHIVADGS LANLEGLWYA RNIKSLPLAM KEVTPELVAG KSDWELMNLS
     TEEIMNLLDS VPEKIDEIKA HSARSGKHLE KLGKWLVPQT KHYSWLKAAD IIGIGLDQVI
     PVPVDHNYRM DINELEKIVR GLAAEKTPIL GVVGVVGSTE EGAIDGIDKI VALRRVLEKD
     GIYFYLHVDA AYGGYGRAIF LDEDNNFIPF EDLKDVHYKY NVFTENKDYI LEEVHSAYKA
     IEEAESVTID PHKMGYVPYS AGGIVIKDIR MRDVISYFAT YVFEKGADIP ALLGAYILEG
     SKAGATAASV WAAHHVLPLN VTGYGKLMGA SIEGAHRFYN FLKDLSFKVG TKNRSSSITT
     H
//