NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10 AND 265-279.
STRAIN=158 / STN 1;
PubMed=8302868 [NCBI, ExPASy, EBI, Israel, Japan]
Madani N.D., Malloy P.J., Rodriguez-Pombo P., Krishnan A.V., Feldman D.;
"Candida albicans estrogen-binding protein gene encodes an oxidoreductase that is inhibited by estradiol.";
Proc. Natl. Acad. Sci. U.S.A. 91:922-926(1994).

Comments

FUNCTION: Oxidoreductase that binds mammalian estrogens with high affinity.
CATALYTIC ACTIVITY: NADPH + acceptor = NADP⁺ + reduced acceptor.
COFACTOR: FMN (By similarity).
DEVELOPMENTAL STAGE: The expression is high during the lag and early logarithmic phases of growth, and low at or near stationary phase.
SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L25759; AAA18013.1; -; Unassigned_RNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36990; A36990.

3D structure databases

HSSP

Q02899; 1OYC. [HSSP ENTRY / PDB]

ModBase

P43084.

Ontologies

GO:0010181;	Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0003959;	Molecular function: NADPH dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

Pfam

PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.

ProtoNet

P43084.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Flavoprotein; FMN; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 407`	`406`	`Probable NADPH dehydrogenase.`	`PRO_0000194479`
`REGION`	`201 204`	`4`	`Substrate-binding (By similarity).`
`ACT_SITE`	`206 206`		`Proton donor (By similarity).`
`BINDING`	`124 124`		`FMN (By similarity).`
`BINDING`	`254 254`		`FMN (By similarity).`
`BINDING`	`357 357`		`FMN (By similarity).`
`SITE`	`225 225`	`1`	`May interact with the steroid.`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 46074 Da [This is the MW of the unprocessed precursor]

CRC64: DDDDB7BD0220639A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTIESTNSFV VPSDTKLIDV TPLGSTKLFQ PIKVGNNVLP QRIAYVPTTR FRASKDHIPS 

        70         80         90        100        110        120 
DLQLNYYNAR SQYPGTLIIT EATFASERGG IDLHVPGIYN DAQAKSWKKI NEAIHGNGSF 

       130        140        150        160        170        180 
SSVQLWYLGR VANAKDLKDS GLPLIAPSAV YWDENSEKLA KEAGNELRAL TEEEIDHIVE 

       190        200        210        220        230        240 
VEYPNAAKHA LEAGFDYVEI HGAHGYLLDQ FLNLASNKRT DKYGCGSIEN RARLLLRVVD 

       250        260        270        280        290        300 
KLIEVVGANR LALRLSPWAS FQGMEIEGEE IHSYILQQLQ QRADNGQQLA YISLVEPRVT 

       310        320        330        340        350        360 
GIYDVSLKDQ QGRSNEFAYK IWKGNFIRAG NYTYDAPEFK TLINDLKNDR SIIGFSRFFT 

       370        380        390        400 
SNPDLVEKLK LGKPLNYYNR EEFYKYYNYG YNSYDESEKQ VIGKPLA

P43084 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools