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Database: UniProt
Entry: M5BY78_THACB
LinkDB: M5BY78_THACB
Original site: M5BY78_THACB 
ID   M5BY78_THACB            Unreviewed;       722 AA.
AC   M5BY78;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase Short=DABA decarboxylase {ECO:0000313|EMBL:CCO32116.1};
GN   Name=ddc {ECO:0000313|EMBL:CCO32116.1};
GN   ORFNames=BN14_06169 {ECO:0000313|EMBL:CCO32116.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO32116.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO32116.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:CCO32116.1}.
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DR   EMBL; CAOJ01009323; CCO32116.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5BY78; -.
DR   HOGENOM; CLU_005446_1_0_1; -.
DR   Proteomes; UP000012065; 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; 3.40.640.10; 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   PANTHER; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF4; TYROSINE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
SQ   SEQUENCE   722 AA;  81535 MW;  84D0A41B35EAE43F CRC64;
     MTYDTSMPAL LGYLATTLYN PNNVATEASP LTSVMEREVG LQLCEMLGYD VSITDNSRPW
     GHITCGGSIA NLESIWAARN LKFYPLSLAC ALEPGAPLES IRDIFNVELC DGETKLFSQL
     DTWELLNLKP ETVFAIPERL ENEFDISSSF LSAVMSKYLI QNLGKDVLEK KYNVTKPTRY
     FVGGTKHYSW PKGAAITGIG SDNIKDIPVD INARLDASKL DQLLQECLDE KRAVYAVVAI
     MGSTEHGAVD PLKDVWELRN KYQKLGLSFA IHADAAWGGY FASLLREEHK VGRGLPIDPD
     NKYVPELALS DHTRTQLDHL KYADSITIDP HKSGYIPYPG GGLCYRDGRM RFLVTWLNPD
     VYKDSDVNLE HLLWQPGFLT ESLVYTRMDM GPYSEKLCLA MYTNWVTMDM GDPNLIVIPM
     NPIPAERNGG SQEEIQKQRE YIRDHIVCRP NLELVRDDKA MALVREMGSD LSINAFACNF
     RLANGEINQD VVESNYLNTR IYERLSVTKI EDNIFDKPLF IMSTSMEQKV YDVCCNNLKR
     RLGVVGDQDL EILVNCVMSP FPTVSNFTKS VADDFKTIAH EEIERCLFRN TVTEDDFRFI
     LQGTDKPYLT LLPMFNMANY RHQLILSCEI PANVMDIYRA ERAKDPSATF FVGTTKDVKL
     DSILAGSFDA MLEKGLPVKN QPAPPRYASN FKVTNVKVLK DSPIDSKYLD RAFPDYISPP
     IK
//
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