ID A0A0D2E9W8_9EURO Unreviewed; 552 AA.
AC A0A0D2E9W8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_03222 {ECO:0000313|EMBL:KIW44774.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44774.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW44774.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44774.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847334; KIW44774.1; -; Genomic_DNA.
DR RefSeq; XP_016264990.1; XM_016403985.1.
DR AlphaFoldDB; A0A0D2E9W8; -.
DR STRING; 215243.A0A0D2E9W8; -.
DR GeneID; 27355296; -.
DR VEuPathDB; FungiDB:PV06_03222; -.
DR HOGENOM; CLU_011856_6_2_1; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000053342; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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; IPR015422; PyrdxlP-dep_Trfase_small.
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:UP000053342}.
FT MOD_RES 363
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 552 AA; 59371 MW; 2CB2424516DB44BC CRC64;
MDQSISITDV ITALQQIVSD PNLPTSQVQS RDASSATPGL ILPRDTPGLD QIQAQSNISK
PLAAFAKSNP GPGSLQSLAG HLTRTILPNL NLASLSPNYY GFVIGGATPA ALLGDFLASI
YDQNVHVHLP AETISTTVEA ATLNLLVQLF RLPREDWALA HPGRGNGGGI FTTGATASNT
LGLALGREYV VRKALMKSAG AGTIESADQS VGECGLAELL IKAGRTKIQV LSTLPHSSIA
KAASVVGIGR RNVVSVAVED DPLRIDMDRL RHEASRPEVL NILAISAGEV NTGRFATDSG
STMRELRDIC DEYGVWMHVD GAFGLFGRVL LQSARDDAET YNEIIRGVEG LELADSITGD
CHKLLNVPYD CGVFFTRHKR LSEDVFGNPG AAYLKAGSGD GVQSPLNIGL ENSRGFRALP
VYCTLLNYGR EGYVDMLKRQ IDLARRVVRW LANDSRFEVL GPRKPHGETE TSLTVDEMVA
KTFMIVLFRP RDDEVNKNFV KDVNATGKIY ISGTAWEGKP AARIAVSNWQ ADVQRDGDLI
EAVLDQVAGK VS
//
