ID A0A0A2JJS7_PENEN Unreviewed; 480 AA.
AC A0A0A2JJS7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=3-beta hydroxysteroid dehydrogenase/isomerase {ECO:0000313|EMBL:KGO54943.1};
GN ORFNames=PEX2_090050 {ECO:0000313|EMBL:KGO54943.1};
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:KGO54943.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54943.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54943.1,
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 -!- 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:KGO54943.1}.
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DR EMBL; JQFZ01000210; KGO54943.1; -; Genomic_DNA.
DR RefSeq; XP_016597224.1; XM_016746275.1.
DR AlphaFoldDB; A0A0A2JJS7; -.
DR STRING; 27334.A0A0A2JJS7; -.
DR GeneID; 27681695; -.
DR HOGENOM; CLU_045580_1_0_1; -.
DR OrthoDB; 1649721at2759; -.
DR PhylomeDB; A0A0A2JJS7; -.
DR Proteomes; UP000030143; 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:KGO54943.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..480
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009752642"
FT DOMAIN 77..348
FT /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF01073"
SQ SEQUENCE 480 AA; 52852 MW; 57243B05DB72F4C0 CRC64;
MTSLITTGLA GLGALYMWHV NSAMKVVPEE AQKLSPHRWT VEEIKAAYKK SLETPIDVTK
SLPPKQSRRY VIVGGTVSHL LTRGEDPKAI RILDLMSPEQ DILNKGVRWT KTNITDKLAV
TTAFEEPWPA NVTSLALTVY HTAAIIRPQD RLKSFLPLSS KVNIDGTRNV LNAARAAGAT
AFIWTSSGSI ALHQPTFWIA PWATQPKRVV QVISDSTKLP ESHYEFFGNY AVTKSEAELL
VRAADNPAEN FRTGCIRPTN GVYGTGGQAN NVITGLYLRN GGSPTWARPM LQSFVHAENV
SIAHLLYEQR LIQQSEPGSQ LPNTGGQAFT VSDPNPAIAF DDLYTLLTTL SSTPLSFPEV
QPLPLLVVAY FVEMYTFLQY RYLSWFLPRL SGDIGQLQPS LFSIINVHVF ADDSRAKLAP
EMGGLGYNPP LNTLEGLCRR LVDWNTKAEG EGVEVRGKKI RLGPVKVAED GVDVAMPRVL
//
