ID K2RCN5_MACPH Unreviewed; 494 AA.
AC K2RCN5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Pyridoxal phosphate-dependent decarboxylase {ECO:0000313|EMBL:EKG10662.1};
GN ORFNames=MPH_12241 {ECO:0000313|EMBL:EKG10662.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG10662.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG10662.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG10662.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC 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:EKG10662.1}.
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DR EMBL; AHHD01000510; EKG10662.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RCN5; -.
DR STRING; 1126212.K2RCN5; -.
DR VEuPathDB; FungiDB:MPH_12241; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_6_2_1; -.
DR InParanoid; K2RCN5; -.
DR OrthoDB; 51460at2759; -.
DR Proteomes; UP000007129; 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:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
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|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 494 AA; 53158 MW; 7A1D9C81D1993869 CRC64;
MPNSDFSIDG RVSPGVPSPV TYSTSKEPHQ PVLPSREVLD RARTGLVAAL PRDGIGYERT
TKHILDHIAP ALNGSSNSPN YYGFVTGGVT PAAALADNIV TAYDQNVQVH LPNETVTTDV
EDQALKLLSS NVVGLACARE HVILSAAARN GHSISVAELG LAGAMRAAGV DDIQILTTVP
HSSLGKAASI VGLGRASLKA VGLPDAPHRF DPAKLEAALA LDRTGSIVAI SCSEVNTGRF
ATSAYADMAA IRELCDKYGS WIHVDAAFGL LGRALNKSEF PKITAATEGM ELADSITGDG
HKLLNVPYDC GFFLSRHLRI GQNTFQNANA AYLNANAGRG AASIPSPLNI GIENSRRFRA
LPVYATLVAY GKQGYRAMLE RQIRLARAIA RFIMDHEAYE LLPQSDLACD HILEEIYIIV
LFRAKNEKLN SELVSRINAT SRIYVSGTSW EGTPACRFAV SNWQVDFDRD LQIICEVLDV
VSRAPTEAWV RKVA
//