ID W7I216_9PEZI Unreviewed; 530 AA.
AC W7I216;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DRE_04484 {ECO:0000313|EMBL:EWC46313.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46313.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC46313.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC46313.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) 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}.
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DR EMBL; KI966419; EWC46313.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I216; -.
DR HOGENOM; CLU_011856_3_1_1; -.
DR Proteomes; UP000024837; 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:UP000024837}.
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 530 AA; 57672 MW; AA14C40F382AF0B8 CRC64;
MDSPQFRQAA HAAIDQSDNG QSSTTTTTSA PPGYLRELIP PGIPEDGESW ENIQRDIEAK
IMPGLTHWQS PNFLAFFPAN SSYPGILGDL YSGAFTCAAF NWQCSPAVTE LETIVLDNVA
RLINLPEEYH SAGEGGGVIQ GTASEAIVVA VVAARDRAIA QSKEIWATQN LTEDEIEDRV
CTLRGKLVAL GSDQAHSSTK KAAMIAGIRF QTISTVMGEY SLTGAQVTHK LEDLHARGLV
PFYLTTTLGT TPTCATDDFA SISTALLAYH TAHPTAPKIW THVDAAYAGA ALILPEYQHI
PLLFPSFADS FDFNMHKWLL TNFDCSCMYV RRRRDLTDAL SITPAYLRNE YSDSGLVTDY
RDWQVPLGRR FRSLKAWFVT RSYGVQGLRA HVRKALDGAA AFTQLVRADT VRFELVAEPA
FALNVVRVRP PPGVVGQLEG GEAGAGFARR CNEVTKKVAD RVNKEGKIFI TPTVLGHGEE
SITAIRVVGA APGVQVADLE NAFRIISETV DAVWAEETAV EEATVELQAV
//
