NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CAI-8;
PubMed=10783002 [NCBI, ExPASy, EBI, Israel, Japan]
Kennedy M.A., Johnson T.A., Lees N.D., Barbuch R., Eckstein J.A., Bard M.;
"Cloning and sequencing of the Candida albicans C-4 sterol methyl oxidase gene (ERG25) and expression of an ERG25 conditional lethal mutation in Saccharomyces cerevisiae.";
Lipids 35:257-262(2000).

Comments

FUNCTION: Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol (By similarity).
CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O₂ = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)⁺ + H₂O.
CATALYTIC ACTIVITY: 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O₂ = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)⁺ + 2 H₂O.
CATALYTIC ACTIVITY: 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O₂ = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)⁺ + H₂O.
COFACTOR: Iron (By similarity).
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6 .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein (Probable).
DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding.
SIMILARITY: Belongs to the sterol desaturase 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

AF051914; AAC06014.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O59933.

Organism-specific databases

CGD

CAL0001165; ERG25.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0000254;	Molecular function: C-4 methylsterol oxidase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016126;	Biological process: sterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006088; Sterol_desatur.
Graphical view of domain structure.

Pfam

PF01598; Sterol_desat; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

O59933.

UniRef

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

Keywords

Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 308`	`308`	`C-4 methylsterol oxidase.`	`PRO_0000117037`
`TRANSMEM`	`56 76`	`21`	`Potential.`
`MOTIF`	`160 164`	`5`	`Histidine box-1.`
`MOTIF`	`173 177`	`5`	`Histidine box-2.`
`MOTIF`	`257 263`	`7`	`Histidine box-3.`

Sequence information

Length: 308 AA [This is the length of the unprocessed precursor]

Molecular weight: 36561 Da [This is the MW of the unprocessed precursor]

CRC64: 45D7D7AE4081BC15 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSISNVYHD YSSFSNATTF SQVYQNFNQL DNLNVFEKLW GSYYYYMAND LFATGLLFFL 

        70         80         90        100        110        120 
THEIFYFGRC LPWAIIDRIP YFRKWKIQDE KIPSDKEQWE CLKSVLTSHF LVEAFPIWFF 

       130        140        150        160        170        180 
HPLCQKIGIS YQVPFPKITD MLIQWAVFFV LEDTWHYWFH RGLHYGVFYK YIHKQHHRYA 

       190        200        210        220        230        240 
APFGLAAEYA HPVEVALLGL GTVGIPIVWC LITGNLHLFT VSIWIILRLF QAVDAHSGYE 

       250        260        270        280        290        300 
FPWSLHNFLP FWAGADHHDE HHHYFIGGYS SSFRWWDFIL DTEAGPKAKK GREDKVKQNV 


EKLQKKNL

O59933 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