ID   ERG25_CANAL             Reviewed;         308 AA.
AC   O59933; Q59V08;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=C-4 methylsterol oxidase;
DE            EC=1.14.13.72;
DE   AltName: Full=Methylsterol monooxygenase;
GN   Name=ERG25; ORFNames=CaO19.3732, CaO19.11216;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CAI-8;
RX   MEDLINE=20243096; PubMed=10783002; DOI=10.1007/s11745-000-0521-2;
RA   Kennedy M.A., Johnson T.A., Lees N.D., Barbuch R., Eckstein J.A.,
RA   Bard M.;
RT   "Cloning and sequencing of the Candida albicans C-4 sterol methyl
RT   oxidase gene (ERG25) and expression of an ERG25 conditional lethal
RT   mutation in Saccharomyces cerevisiae.";
RL   Lipids 35:257-262(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC   -!- FUNCTION: Catalyzes the first step in the removal of the two C-4
CC       methyl groups of 4,4-dimethylzymosterol (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol +
CC       NAD(P)H + O(2) = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-
CC       cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-
CC       cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-
CC       methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2
CC       H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-
CC       7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4-
CC       beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+)
CC       + H(2)O.
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol
CC       from lanosterol: step 3/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (Probable).
CC   -!- DOMAIN: The histidine box domains may contain the active site
CC       and/or be involved in metal ion binding.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family.
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DR   EMBL; AF051914; AAC06014.1; -; Genomic_DNA.
DR   EMBL; AACQ01000127; EAK94304.1; -; Genomic_DNA.
DR   EMBL; AACQ01000126; EAK94341.1; -; Genomic_DNA.
DR   RefSeq; XP_713420.1; -.
DR   RefSeq; XP_713456.1; -.
DR   GeneID; 3644906; -.
DR   GeneID; 3644933; -.
DR   CGD; CAL0001165; ERG25.
DR   OMA; O59933; EDTWHYW.
DR   BRENDA; 1.14.13.72; 1124.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000254; F:C-4 methylsterol oxidase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD;
KW   Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis;
KW   Transmembrane.
FT   CHAIN         1    308       C-4 methylsterol oxidase.
FT                                /FTId=PRO_0000117037.
FT   TRANSMEM     56     76       Potential.
FT   MOTIF       160    164       Histidine box-1.
FT   MOTIF       173    177       Histidine box-2.
FT   MOTIF       257    263       Histidine box-3.
SQ   SEQUENCE   308 AA;  36561 MW;  45D7D7AE4081BC15 CRC64;
     MSSISNVYHD YSSFSNATTF SQVYQNFNQL DNLNVFEKLW GSYYYYMAND LFATGLLFFL
     THEIFYFGRC LPWAIIDRIP YFRKWKIQDE KIPSDKEQWE CLKSVLTSHF LVEAFPIWFF
     HPLCQKIGIS YQVPFPKITD MLIQWAVFFV LEDTWHYWFH RGLHYGVFYK YIHKQHHRYA
     APFGLAAEYA HPVEVALLGL GTVGIPIVWC LITGNLHLFT VSIWIILRLF QAVDAHSGYE
     FPWSLHNFLP FWAGADHHDE HHHYFIGGYS SSFRWWDFIL DTEAGPKAKK GREDKVKQNV
     EKLQKKNL
//