Reviewed, UniProtKB/Swiss-Prot O59933 (ERG25_CANAL)

Names and origin

Protein names

Recommended name:
    C-4 methylsterol oxidase
    EC=1.14.13.72
Alternative name(s):
    Methylsterol monooxygenase

Gene names

Name:	ERG25
ORF Names:	CaO19.3732, CaO19.11216

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	308 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. 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. 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.
Sequence similarities	Belongs to the sterol desaturase family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Iron NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	C-4 methylsterol oxidase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 308	308	C-4 methylsterol oxidase		PRO_0000117037
Regions
	Transmembrane	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

Sequences

	Sequence		Length	Mass (Da)
	O59933-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 45D7D7AE4081BC15	FASTA	308	36,561
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Kennedy M.A., Johnson T.A., Lees N.D., Barbuch R., Eckstein J.A., Bard M. Lipids 35:257-262(2000) [PubMed: 10783002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CAI-8.
[2]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF051914 Genomic DNA. Translation: AAC06014.1. AACQ01000127 Genomic DNA. Translation: EAK94304.1. AACQ01000126 Genomic DNA. Translation: EAK94341.1.
RefSeq	XP_713420.1. XP_713456.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3644906. 3644933.
Organism-specific databases
CGD	CAL0001165. ERG25.
Phylogenomic databases
OMA	O59933. EDTWHYW.
Enzyme and pathway databases
BRENDA	1.14.13.72. 1124.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ERG25_CANAL

Accession

Primary (citable) accession number: O59933
Secondary accession number(s): Q59V08

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)