ID K2RML5_MACPH Unreviewed; 337 AA.
AC K2RML5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Beta-lactamase-like protein {ECO:0000313|EMBL:EKG11429.1};
GN ORFNames=MPH_11444 {ECO:0000313|EMBL:EKG11429.1};
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:EKG11429.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG11429.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG11429.1,
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 NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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:EKG11429.1}.
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DR EMBL; AHHD01000469; EKG11429.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RML5; -.
DR STRING; 1126212.K2RML5; -.
DR VEuPathDB; FungiDB:MPH_11444; -.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_2_1; -.
DR InParanoid; K2RML5; -.
DR OrthoDB; 1200131at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05227; AR_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10366:SF564; 3BETA_HSD DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 3..255
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 337 AA; 37053 MW; E32B87A21E600EF7 CRC64;
MHVLLTGGSG FIAAHVLDAL LERGHSVVTT VRSNDKASRI RDAHPEVSQD KLGFAIVPDI
AVMGAFDTAV QSNPPFDAVI HTASPLSLSV TDVQKEVLDP AIIGTVGLLS SVKQFAPTVK
RVVVLSSFAA MVDLAKGDWP SHTYTAADWN PITPEEALQD AVAAYRGSKT FAERAAWEFV
EREKPGFSLT TLNPPFVFGP VVHYLSGLDA LNNSNRRFVG FLNGMLLPTT FYAWLDVRDM
ALGHVRAMED PAAAGERIFF TSPEQFSNRD ILQIIDEEFP ELRHRLPPKE QWSSVGYPDG
GVYKVDHARA RELLGRDFIP LRKCVVDTVN LLKKYGV
//
