ID K2QKD9_MACPH Unreviewed; 245 AA.
AC K2QKD9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:EKG10321.1};
GN ORFNames=MPH_12602 {ECO:0000313|EMBL:EKG10321.1};
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:EKG10321.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG10321.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG10321.1,
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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:EKG10321.1}.
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DR EMBL; AHHD01000523; EKG10321.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QKD9; -.
DR STRING; 1126212.K2QKD9; -.
DR VEuPathDB; FungiDB:MPH_12602; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; K2QKD9; -.
DR OrthoDB; 1701404at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43008; BENZIL REDUCTASE; 1.
DR PANTHER; PTHR43008:SF10; CHAIN DEHYDROGENASE_OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15740)-RELATED; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
SQ SEQUENCE 245 AA; 26535 MW; 23F1905054835FC5 CRC64;
MATSAVDFYC LDRLEHPSDD FYAASLRIPP SFGGSLHYAC VDVRDARSLD RVVGAIADRH
QRLDGVIAAA GIQHLKAAID CSVEEVREIM DVNYSGVFMT CASAARAMFK WNPGKRDGAM
VIIASMSGSV ANKGLICPVY NSSKAALLQL TRNLAMEWSS VGRGHKGGLG GIRVNSLSPG
HIVTPMVRKN FEEVPGLCEK WERENMMGRL ARPEEFKGAG LFLLSRASSF MTGANLIIDG
GHTAW
//
