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
//