ID A0A0A2JIL8_PENEN Unreviewed; 267 AA.
AC A0A0A2JIL8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:KGO54543.1};
GN ORFNames=PEX2_070760 {ECO:0000313|EMBL:KGO54543.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54543.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54543.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54543.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54543.1}.
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DR EMBL; JQFZ01000221; KGO54543.1; -; Genomic_DNA.
DR RefSeq; XP_016596914.1; XM_016744347.1.
DR AlphaFoldDB; A0A0A2JIL8; -.
DR STRING; 27334.A0A0A2JIL8; -.
DR GeneID; 27679767; -.
DR HOGENOM; CLU_010194_1_0_1; -.
DR OrthoDB; 2089071at2759; -.
DR PhylomeDB; A0A0A2JIL8; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite 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; PTHR42760:SF40; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE; 1.
DR PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 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 Reference proteome {ECO:0000313|Proteomes:UP000030143}.
SQ SEQUENCE 267 AA; 28291 MW; 9466989B5EDB2C9E CRC64;
MLSLNGKVAL ITGLGQTQSE GWGIGAAIAV LLARQGAKIF GGNRTLASTV STKEAIETEG
GICDVVETNV TSSTSTKALV EACMARHGRI DILINNVGRS EPGCPATMTE EVWDSQVDLN
LKSVFLMCQH VLPIMEQQGS GAVVSVASIA GLRYIGKPQV GYSATKAAII QLMKTTAVIY
APKGVRLNTV VPGLMDTPYT KCMVSRYADG QAERYMEMRH AQVPMGKMGN AWDVANATLF
LVSDEAQYIT GQELIVDGGI TSSTGRT
//
