ID A0A1Z5ST07_HORWE Unreviewed; 311 AA.
AC A0A1Z5ST07;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BTJ68_12463 {ECO:0000313|EMBL:OTA23940.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA23940.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA23940.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA23940.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={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:OTA23940.1}.
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DR EMBL; MUNK01000268; OTA23940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5ST07; -.
DR STRING; 1157616.A0A1Z5ST07; -.
DR VEuPathDB; FungiDB:BTJ68_12463; -.
DR InParanoid; A0A1Z5ST07; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000194280; 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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
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|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT REGION 205..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 35351 MW; A319A350296ABE21 CRC64;
MRRLLKIDLV SFEIPGITTE KSNDFALTGD QLRAKIEELH AKGLHPYYLT VTIGTTNTCA
IDDFESIAQV AKDYPDIWIH CDAAYAGAAL VLPEYHHLAQ HMSLKRRDLT DALSITPAYL
RNQFSDSGLV TDYRDWQIPL GRRFRSLKIW FVIRTWGVEG LHQHIRSHLR LGQIFTDLVR
SRSDLFTILV QPRFALTVLA VNPRRKQHHQ SGGDENIHGT GTDPRPYELQ HLPLGAEEPS
SQEIEQANEI TKEVYTAIDA RKDFFLTASV VGDTYAIRVV SANPLAAEKY VREVFGQLVE
EAEKAFQRRG M
//
