ID A0A0F4GD46_9PEZI Unreviewed; 484 AA.
AC A0A0F4GD46;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aromatic-l-amino-acid decarboxylase like protein {ECO:0000313|EMBL:KJX94110.1};
GN ORFNames=TI39_contig4216g00019 {ECO:0000313|EMBL:KJX94110.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX94110.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX94110.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX94110.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009533, 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:KJX94110.1}.
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DR EMBL; LAFY01004175; KJX94110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GD46; -.
DR STRING; 1047168.A0A0F4GD46; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
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 InterPro; IPR021115; Pyridoxal-P_BS.
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; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000033647}.
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 484 AA; 53585 MW; 405547D764CA867D CRC64;
MASGPVRSDV TPGFLLSKLP GEAPEKSEAW SAIESDLHHL IEPGLCHWMH PGFMAYFPAS
SSFEGILGEL YSAAFNDPAF DWICSPSITE LELAMGDWVG ELLGLPSSFR GPASSVIQST
TTECLITTMC AARDWMIDAM LAEGDDQTAK VRPNDVRNRL VVLSSSETHV STRKAAKVVG
VQHRPIPCDP SDGIALSGTQ LQTAVDECLA KGLIPFYFTA AFGTTNSCAV DDFPGIARVK
EKHPEIWIHV DAAYAGAALA CEEFRPLASG MDQFDSFSVN MGKWLLTNLD CTMLFARNRA
DIVCSMKNDC SILQNPVSAS QKTTDYRDLQ LSMGRRFRSL KVWFVLRSFG KQRIQQHIRR
HIEMASHFTE WVRQRSDFFA LTTEPRFALN VIRVSDAAAS RMGTDVSSTT AKLYDVVSQS
RQFWLSKTTI NRCVSIRIIA ANSNSDLDTL RHVFEVLSEE TQTLLDQSAI RSDGEDDGKR
CTPQ
//
