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Database: UniProt
Entry: A0A1V6VA79_9EURO
LinkDB: A0A1V6VA79_9EURO
Original site: A0A1V6VA79_9EURO 
ID   A0A1V6VA79_9EURO        Unreviewed;       493 AA.
AC   A0A1V6VA79;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENCOP_c001G00992 {ECO:0000313|EMBL:OQE47518.1};
OS   Penicillium coprophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE47518.1, ECO:0000313|Proteomes:UP000191500};
RN   [1] {ECO:0000313|Proteomes:UP000191500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQE47518.1}.
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DR   EMBL; MDDG01000001; OQE47518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6VA79; -.
DR   STRING; 36646.A0A1V6VA79; -.
DR   OrthoDB; 51460at2759; -.
DR   Proteomes; UP000191500; 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:UP000191500}.
FT   MOD_RES         313
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   493 AA;  53448 MW;  FA632E15036A65E2 CRC64;
     MQTEFQQALW KAAQGPWESG VLPSTESLAR ARASLPVTLP DTGSSLESVQ QHIINDIVPA
     FNGGSLSANY YGFITGGTTP AALFADNVVS VYDQNVQVHL PNHSIVTDVE YNAIGLLLDL
     FRLERSIWHN GTFTTGATAS NILGLACGRE FVLQKAAERQ GSQLQSVGEE GLFQVLNALG
     LSGVQVLSTL PHSSLVKAAG VLGIGRANVH NICRADDPLR FDIDKLQKEL ARTDKVSIVA
     ISCGEVNTGR FATSGADLRE IRQLCDKYGA WIHADAAFGL FGRVLGESPE FATIKKGSEG
     IDLVDSITGD GHKLLNVPYD CGFFFTRHPN VASQVFQNAN AAYLTAGSSD GPSIPSPLNI
     GIENSRRFRA LPVYASLLSY GKFGYQEMLE RQIRLARKIY GWVFEHSAYT ALPQASSKSA
     LLDQTFMTVL LRANDESLNR KLGSKINESS QMFVSGTSWD GSPACRIAIS NWRVDVERDF
     ALVTDVLAKV ARN
//
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