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Database: UniProt
Entry: K2S1F5_MACPH
LinkDB: K2S1F5_MACPH
Original site: K2S1F5_MACPH 
ID   K2S1F5_MACPH            Unreviewed;       334 AA.
AC   K2S1F5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:EKG16339.1};
GN   ORFNames=MPH_06466 {ECO:0000313|EMBL:EKG16339.1};
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:EKG16339.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG16339.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG16339.1,
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:EKG16339.1}.
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DR   EMBL; AHHD01000277; EKG16339.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2S1F5; -.
DR   STRING; 1126212.K2S1F5; -.
DR   VEuPathDB; FungiDB:MPH_06466; -.
DR   eggNOG; KOG1200; Eukaryota.
DR   HOGENOM; CLU_010194_13_2_1; -.
DR   InParanoid; K2S1F5; -.
DR   OrthoDB; 2654086at2759; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0044249; P:cellular 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; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   PANTHER; PTHR44229:SF4; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   PRINTS; PR00081; GDHRDH.
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   334 AA;  36269 MW;  7A575F0064FC6942 CRC64;
     MQVGDFPLSD KIVVVTGGGS GIGLQIVKEA VAAGSKVILA DLRLTQEVAA FVRSRDSKDL
     VFQKCDVSKR QEQEKLVEVA EQKWGDVPDV YISSAGLFEP LYISFPNTRG SVLFYSVLSA
     TSFTSPNEYG VLIDSQSSSN FWTDTEADDY ATVSVNVTAP IKLTRIAMRA LLRKNKKGVV
     LLVSSIAGYG GTYAVPLYCA TKHAVVGFVK SMRKAEQEEG VKVVALCPGV VRTPLWSPDR
     GTDLLQLFKY SQDAILEPED VARAAKQLVE EGRYGGGTVL EVTTVGTRVI PEWGVMPPPQ
     AEKNTGAPQE IVPPAQVEVK EYLKEERGAI RPKL
//
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