Reviewed, UniProtKB/Swiss-Prot Q9UUH4 (ERG25_SCHPO)

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:	SPAC630.08c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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
Technical term	Complete proteome
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 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 300	300	C-4 methylsterol oxidase		PRO_0000117038
Regions
	Transmembrane	186 – 206	21	Potential
	Motif	154 – 158	5	Histidine box-1
	Motif	167 – 171	5	Histidine box-2
	Motif	251 – 257	7	Histidine box-3

Sequences

	Sequence		Length	Mass (Da)
	Q9UUH4-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AA8C2603D35DF331	FASTA	300	35,803
	10 20 30 40 50 60 MNTTSEVIVG TGFQAIRQQL AQMHPELNFV EQLWLAYYKW FDNDVVATGL MSFLLHELIY 70 80 90 100 110 120 FGRCIPWMII DAMPYFRRWK IQPKKVPTLA EQWECTRLVL LSHFTVELPQ IWLFDPMCAT 130 140 150 160 170 180 FGLSTSVPFP PVTKMIWQIT LFFFLEDTWH YWAHRLFHYG IFYRFIHKVH HRYSAPFGLS 190 200 210 220 230 240 AEYAHPLEII LLGAGTVFVP LMWCYFTHDL HLVTMYIWIT LRLFQAVDSH AGYDFPWSLN 250 260 270 280 290 300 KFLPIWAGAD HHDYHHMAFK DNFSSSFRWW DAVLKTDQNY HQFKARRLAA KYEAESKKAK

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB52730.1.
PIR	T38986.
RefSeq	NP_592903.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UUH4.
Genome annotation databases
GeneID	2543373.
GenomeReviews	Gene locus erg25 in contig CU329670_GR.
KEGG	spo:SPAC630.08c.
NMPDR	fig|4896.1.peg.2873.
Organism-specific databases
GeneDB_Spombe	SPAC630.08c.
Phylogenomic databases
OMA	EDTWHYW.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000634-MON.
BRENDA	1.14.13.72. 653.
Gene expression databases
ArrayExpress	Q9UUH4.
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_SCHPO

Accession

Primary (citable) accession number: Q9UUH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2003
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)