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Database: UniProt
Entry: D4D0H1_TRIVH
LinkDB: D4D0H1_TRIVH
Original site: D4D0H1_TRIVH 
ID   D4D0H1_TRIVH            Unreviewed;       355 AA.
AC   D4D0H1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Aldehyde reductase II {ECO:0000313|EMBL:EFE44639.1};
GN   ORFNames=TRV_00566 {ECO:0000313|EMBL:EFE44639.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE44639.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE44639.1}.
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DR   EMBL; ACYE01000032; EFE44639.1; -; Genomic_DNA.
DR   RefSeq; XP_003025250.1; XM_003025204.1.
DR   AlphaFoldDB; D4D0H1; -.
DR   GeneID; 9580742; -.
DR   KEGG; tve:TRV_00566; -.
DR   HOGENOM; CLU_007383_9_2_1; -.
DR   OrthoDB; 1200131at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366:SF849; FATTY ACID HYDROXYLASE UHD1; 1.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          10..141
FT                   /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01073"
SQ   SEQUENCE   355 AA;  39473 MW;  8CC8C5834214B6CA CRC64;
     MPFANSDLIV VTGANGHVAQ HVVSQLLSFH APVRVRGTVR SSTVAQKLYA AFDSFVSSGR
     LEIAIVPDLT VDSAFDDAIQ GATYVAHIAS PLNMSPENVE NDLLMPAIKG NICILESIMK
     KSGIKAVVIT SSFVAAFDAR HGFREGYTYS SADWNPISYD EAADPRQDMS QYPEKWRPWI
     TYMASRKLAE KAAWDFYRKH QPTWALSTLL PSFIGGPFVL PLTKGAGSLT FSTSLIWRTA
     LGSEPLFHND FPHWVDVRDV AKAHIQALIT PAAWGRRIVR KHYPEMGPSR EKQQVTAVAE
     LRYKWSLTDL IQVHHYSIDS GSSLSILGMD SWISPEQMIV DLIKQLKRTT LSDAL
//
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