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Database: UniProt
Entry: A0A2H3IS19_9EURO
LinkDB: A0A2H3IS19_9EURO
Original site: A0A2H3IS19_9EURO 
ID   A0A2H3IS19_9EURO        Unreviewed;       387 AA.
AC   A0A2H3IS19;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=3-beta hydroxysteroid dehydrogenase/isomerase {ECO:0000313|EMBL:PCG96887.1};
GN   ORFNames=PENO1_066010 {ECO:0000313|EMBL:PCG96887.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG96887.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG96887.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG96887.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family.
CC       {ECO:0000256|ARBA:ARBA00009219}.
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:PCG96887.1}.
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DR   EMBL; NPFK01000200; PCG96887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IS19; -.
DR   STRING; 290292.A0A2H3IS19; -.
DR   OrthoDB; 1133at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR   PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:PCG96887.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   DOMAIN          20..300
FT                   /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01073"
SQ   SEQUENCE   387 AA;  42786 MW;  60A6D138D3C2C952 CRC64;
     MSEQIPQTNH PEKDEGLKVI ITGGAGCIGF ATIKSLLKHH PNASIHVLDL TIPSLEVYPF
     SNFQEKKNQL HFYKADITSP TSLSAVFDAV RPQAVIHTAS IIPSAARKRQ LNNEGLWKVN
     VEGTRNILDI AERTEEVKAL VYTSSCDAVK PDSWMDFVNA TESSTQHLRD TDIKGWDNGA
     KAAAETLVLS SDLRIKTCAI RTHGVVGTLD QNLFPLVATS PRKISLGSGK NLYDFTSADN
     VGLAHVLAMN NLLGLSSTNK DREEKESANR RAFFITDGNP KPFRELQEMI WRVVDDDDPE
     ASYAKYTVIP VWLFKGILKI AGLFTKATIS PVEVGDAVSM RYYDIGEARR VLGYRPEGNK
     GLEESMRDAS EWWKMSSMSI SAKGGKK
//
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