ID J5K5Q1_BEAB2 Unreviewed; 528 AA.
AC J5K5Q1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Dopa decarboxylase (Aromatic L-amino acid decarboxylase) {ECO:0000313|EMBL:EJP69401.1};
GN ORFNames=BBA_01366 {ECO:0000313|EMBL:EJP69401.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP69401.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP69401.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP69401.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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; JH725152; EJP69401.1; -; Genomic_DNA.
DR RefSeq; XP_008594685.1; XM_008596463.1.
DR AlphaFoldDB; J5K5Q1; -.
DR STRING; 655819.J5K5Q1; -.
DR GeneID; 19884378; -.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; J5K5Q1; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000002762; 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:UP000002762}.
FT MOD_RES 343
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 528 AA; 57312 MW; 0D52E6DF8E6C33FB CRC64;
MDINEYRKQA KKAVDEIADY YESIPSRPVL ADVSPGYLRP LLPDAAPFEG ESMDAITADL
QSKILPGITH WAHPGFMAFF ACTASHPANI AEMWSNAFNG AHFNWICSPA VTELETVVLD
WLAKALALPE CFLSGGPTHG GGVLHGSASE AIVTVMVAAR DRYLAQATAH LPEGEDKEEQ
TWRHRSRLVA LGSAGAHSST KKAAQVLGVR FDTVPVDEES GYAMTGEALA AKLAQLRGKG
LEPFYLTATF GSTDVCAVDD FVGIAATLAA DNNNNKSNSN GTTTTTSNGD TAAAAAAAAA
APRGEVWVHV DGAFAGSALL LPEYQHLTPP FASFHSFNFN PHKWLLTTFD CSAVWVRSRA
DLITALSIKP AYLRNEFSDS DLVTDYRDWQ IPLGRRFRSL KLWFVLRSYG IAGLRAHVAR
GIRLGQSLDD KLAARPDLFT LFTRARFALV SFRVVGADEQ ERNARTETLY ETLNASGKVY
LTSTVVNGKF AIRVSTSTAA VREEHVQATF DLIVKETEAL LAKVKNTQ
//
