ID   EBP1_CANAX              Reviewed;         407 AA.
AC   P43084;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Probable NADPH dehydrogenase;
DE            EC=1.6.99.1 {ECO:0000269|PubMed:8302868};
DE   AltName: Full=Estrogen-binding protein {ECO:0000303|PubMed:8302868};
DE            Short=EBP {ECO:0000303|PubMed:8302868};
GN   Name=EBP1 {ECO:0000303|PubMed:8302868};
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10 AND 265-279,
RP   FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=158 / STN 1;
RX   PubMed=8302868; DOI=10.1073/pnas.91.3.922;
RA   Madani N.D., Malloy P.J., Rodriguez-Pombo P., Krishnan A.V., Feldman D.;
RT   "Candida albicans estrogen-binding protein gene encodes an oxidoreductase
RT   that is inhibited by estradiol.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:922-926(1994).
CC   -!- FUNCTION: Oxidoreductase that binds mammalian estrogens with high
CC       affinity. {ECO:0000269|PubMed:8302868}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1;
CC         Evidence={ECO:0000269|PubMed:8302868};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:Q02899};
CC   -!- DEVELOPMENTAL STAGE: The expression is high during the lag and early
CC       logarithmic phases of growth, and low at or near stationary phase.
CC       {ECO:0000269|PubMed:8302868}.
CC   -!- SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase
CC       family. {ECO:0000305}.
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DR   EMBL; L25759; AAA18013.1; -; Unassigned_RNA.
DR   PIR; A36990; A36990.
DR   AlphaFoldDB; P43084; -.
DR   SMR; P43084; -.
DR   COMPLUYEAST-2DPAGE; P43084; -.
DR   VEuPathDB; FungiDB:C6_01180C_A; -.
DR   VEuPathDB; FungiDB:CAWG_05243; -.
DR   GO; GO:0099130; F:estrogen binding; IDA:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018548; F:pentaerythritol trinitrate reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   InterPro; IPR045247; Oye-like.
DR   PANTHER; PTHR22893; PTHR22893; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8302868"
FT   CHAIN           2..407
FT                   /note="Probable NADPH dehydrogenase"
FT                   /id="PRO_0000194479"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q02899"
FT   BINDING         49
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q02899"
FT   BINDING         124
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q02899"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:C5H429"
FT   BINDING         254
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q02899"
FT   BINDING         357
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:Q02899"
FT   SITE            225
FT                   /note="May interact with the steroid"
SQ   SEQUENCE   407 AA;  46074 MW;  DDDDB7BD0220639A CRC64;
     MTIESTNSFV VPSDTKLIDV TPLGSTKLFQ PIKVGNNVLP QRIAYVPTTR FRASKDHIPS
     DLQLNYYNAR SQYPGTLIIT EATFASERGG IDLHVPGIYN DAQAKSWKKI NEAIHGNGSF
     SSVQLWYLGR VANAKDLKDS GLPLIAPSAV YWDENSEKLA KEAGNELRAL TEEEIDHIVE
     VEYPNAAKHA LEAGFDYVEI HGAHGYLLDQ FLNLASNKRT DKYGCGSIEN RARLLLRVVD
     KLIEVVGANR LALRLSPWAS FQGMEIEGEE IHSYILQQLQ QRADNGQQLA YISLVEPRVT
     GIYDVSLKDQ QGRSNEFAYK IWKGNFIRAG NYTYDAPEFK TLINDLKNDR SIIGFSRFFT
     SNPDLVEKLK LGKPLNYYNR EEFYKYYNYG YNSYDESEKQ VIGKPLA