ID   U7PP52_SPOS1            Unreviewed;       373 AA.
AC   U7PP52;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1624_06715 {ECO:0000313|EMBL:ERS97383.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS97383.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(2014).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; KI440848; ERS97383.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7PP52; -.
DR   STRING; 1391915.U7PP52; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   HOGENOM; CLU_011856_6_0_1; -.
DR   OrthoDB; 51460at2759; -.
DR   Proteomes; UP000018087; 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:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 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|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT   MOD_RES         358
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   373 AA;  39508 MW;  297111FF142CE29B CRC64;
     MSSENITDIG FLSGGYERLR AAVDRLTKQD GADNAVPTLP SSARVQAALA AIPRPGQSDY
     LQPRGARVAH DHILDTIIPA LNGQNLSGRY YGFVTGSVLP IAEAADNIVT ALDQNLHAHL
     PAQTVSTAVE AAALQMLANV FGLDDGDWTG RIFTTGATAS NVLGLAMGRE AVINTRLRKR
     RRLSGKGVDS STASPVAVAE LGLLKACQEA GVSDIRILTS LGHSSLYKAA SIVGLGRAAI
     IDLPYSEAEP WRLNISAVEQ TLADAFQSPG GEGQTGSSVA YIISVSAGEI NTGRFATTGL
     EDMQRLRALA DKYGAWIHVD AAFGLFTRAL PSTLEFARIR QYTDGLELAD SITSDGHKLL
     NVVSKQQQKN HFA
//