ID A0A423X3I2_9PEZI Unreviewed; 252 AA.
AC A0A423X3I2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Short-chain dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_01642 {ECO:0000313|EMBL:ROW10390.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW10390.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW10390.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW10390.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROW10390.1}.
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DR EMBL; LKEA01000003; ROW10390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X3I2; -.
DR STRING; 356882.A0A423X3I2; -.
DR Proteomes; UP000283895; 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 CDD; cd05367; SPR-like_SDR_c; 1.
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:SF8; BENZIL REDUCTASE ((S)-BENZOIN FORMING) IRC24; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00822; PKS_KR; 1.
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:UP000283895}.
SQ SEQUENCE 252 AA; 27279 MW; D7D1C2A5B874F861 CRC64;
MASKTIIVTG AGRGIGLAVS QYLLQKSHKV VLVARTESEL EALKKQYPSQ VEYLAADLTD
FENATKITDL AVKLGGKVDG IVINHGALEP LKPVGDSSLE EWKKLYDINL FSPLALVQAV
LPHLRETKGR IIFTSSGAAI KGYKAWGAYG SSKAALHSLA QHLAVEEKDI VSISLSPGRT
DTGMQKLLRE QGYGFMDDRD HASFVSAFEE GKLNPPEGPG NVIAKLALDA TLDLSGKFLQ
WNGPELTSYR ED
//
