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Database: UniProt
Entry: A0A1V6QHP5_9EURO
LinkDB: A0A1V6QHP5_9EURO
Original site: A0A1V6QHP5_9EURO 
ID   A0A1V6QHP5_9EURO        Unreviewed;       259 AA.
AC   A0A1V6QHP5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD88532.1};
GN   ORFNames=PENSOL_c071G01673 {ECO:0000313|EMBL:OQD88532.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD88532.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQD88532.1}.
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DR   EMBL; MDYO01000071; OQD88532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QHP5; -.
DR   STRING; 60172.A0A1V6QHP5; -.
DR   OrthoDB; 2046911at2759; -.
DR   Proteomes; UP000191612; 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   CDD; cd05233; 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; PTHR43618; 7-ALPHA-HYDROXYSTEROID DEHYDROGENASE; 1.
DR   PANTHER; PTHR43618:SF13; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17650)-RELATED; 1.
DR   Pfam; PF13561; adh_short_C2; 1.
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:UP000191612}.
SQ   SEQUENCE   259 AA;  27967 MW;  B26C536A319E39F3 CRC64;
     MGFPRVALVT GASRGVGAAV ARALAAQGNT RIVINYHNNA TAADQLIAEL SELRSQSNDG
     TIDNQCPWFT AIQADIASRA EMTRLVHQTV ERMGRLDVVV SNVGWTRMTD FMNLEDADCE
     ADWDRCFDVN VKSHFRLFRA CQPYLESSEG VFIATASVAG VKPSGSSLAY AVTKAALIHL
     VRSLAVIAGP KIRVNSVAPG VLMTDWGQGF PAEKIKAVEE KNVLKRLATP EDVAEHVKFL
     SMSRSITGMN AVIDAGFSL
//
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