UniProtKB - Q9UUH4 (ERG25_SCHPO)
C-4 methylsterol oxidase erg25
erg25
Functioni
C-4 methylsterol oxidase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:8474436).
The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity).
Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids (PubMed:8474436).
Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7 (PubMed:8604986, PubMed:33223513).
The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (PubMed:27585850).
In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol (By similarity).
Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins (Probable). Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:18310029).
The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol (PubMed:18310029).
The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (PubMed:18310029).
The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (PubMed:18310029).
Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (PubMed:18310029).
In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (PubMed:8586261).
By similarity1 Publication6 PublicationsMiscellaneous
Catalytic activityi
- 4,4-dimethyl-5α-cholesta-8,24-dien-3β-ol + 6 Fe(II)-[cytochrome b5] + 5 H+ + 3 O2 = 4β-methylzymosterol-4α-carboxylate + 6 Fe(III)-[cytochrome b5] + 4 H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 4α-methylzymosterol + 6 Fe(II)-[cytochrome b5] + 5 H+ + 3 O2 = 4α-carboxyzymosterol + 6 Fe(III)-[cytochrome b5] + 4 H2OBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
: zymosterol biosynthesis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes zymosterol from lanosterol.By similarity This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.
Pathwayi: ergosterol biosynthesis
This protein is involved in the pathway ergosterol biosynthesis, which is part of Steroid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway ergosterol biosynthesis and in Steroid metabolism.
GO - Molecular functioni
- C-4 methylsterol oxidase activity Source: PomBase
- iron ion binding Source: PomBase
- oxidoreductase activity Source: GO_Central
GO - Biological processi
- ergosterol biosynthetic process Source: PomBase
- sterol biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism |
Ligand | Iron, NAD |
Enzyme and pathway databases
Reactomei | R-SPO-191273, Cholesterol biosynthesis R-SPO-192105, Synthesis of bile acids and bile salts |
UniPathwayi | UPA00768 UPA00770;UER00756 |
Names & Taxonomyi
Protein namesi | Recommended name: C-4 methylsterol oxidase erg251 Publication (EC:1.14.18.-By similarity)Alternative name(s): Ergosterol biosynthetic protein 25By similarity Sterol-C4-methyl oxidase erg25By similarity Short name: SMOBy similarity |
Gene namesi | Name:erg251 Publication ORF Names:SPAC630.08c |
Organismi | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
Taxonomic identifieri | 284812 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › |
Proteomesi |
|
Organism-specific databases
PomBasei | SPAC630.08c, erg25 |
VEuPathDBi | FungiDB:SPAC630.08c |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Single-pass membrane protein Sequence analysis
Endoplasmic reticulum
- endoplasmic reticulum Source: PomBase
- endoplasmic reticulum membrane Source: PomBase
Other locations
- integral component of membrane Source: UniProtKB-KW
- membrane Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 186 – 206 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000117038 | 1 – 300 | C-4 methylsterol oxidase erg25Add BLAST | 300 |
Proteomic databases
MaxQBi | Q9UUH4 |
PaxDbi | Q9UUH4 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Heterotetramer of erg25, erg26, erg27 and erg28 (By similarity). Erg28 acts as a scaffold to tether erg27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum (By similarity).
By similarityProtein-protein interaction databases
STRINGi | 4896.SPAC630.08c.1 |
Structurei
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 140 – 276 | Fatty acid hydroxylaseSequence analysisAdd BLAST | 137 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 154 – 158 | Histidine box-1 | 5 | |
Motifi | 167 – 171 | Histidine box-2 | 5 | |
Motifi | 251 – 257 | Histidine box-3 | 7 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0873, Eukaryota |
HOGENOMi | CLU_047036_5_0_1 |
InParanoidi | Q9UUH4 |
OMAi | PGFIFQF |
PhylomeDBi | Q9UUH4 |
Family and domain databases
InterProi | View protein in InterPro IPR006694, Fatty_acid_hydroxylase |
Pfami | View protein in Pfam PF04116, FA_hydroxylase, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MNTTSEVIVG TGFQAIRQQL AQMHPELNFV EQLWLAYYKW FDNDVVATGL
60 70 80 90 100
MSFLLHELIY FGRCIPWMII DAMPYFRRWK IQPKKVPTLA EQWECTRLVL
110 120 130 140 150
LSHFTVELPQ IWLFDPMCAT FGLSTSVPFP PVTKMIWQIT LFFFLEDTWH
160 170 180 190 200
YWAHRLFHYG IFYRFIHKVH HRYSAPFGLS AEYAHPLEII LLGAGTVFVP
210 220 230 240 250
LMWCYFTHDL HLVTMYIWIT LRLFQAVDSH AGYDFPWSLN KFLPIWAGAD
260 270 280 290 300
HHDYHHMAFK DNFSSSFRWW DAVLKTDQNY HQFKARRLAA KYEAESKKAK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CU329670 Genomic DNA Translation: CAB52730.1 |
PIRi | T38986 |
RefSeqi | NP_592903.1, NM_001018303.2 |
Genome annotation databases
EnsemblFungii | SPAC630.08c.1; SPAC630.08c.1:pep; SPAC630.08c |
GeneIDi | 2543373 |
KEGGi | spo:SPAC630.08c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CU329670 Genomic DNA Translation: CAB52730.1 |
PIRi | T38986 |
RefSeqi | NP_592903.1, NM_001018303.2 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 4896.SPAC630.08c.1 |
Proteomic databases
MaxQBi | Q9UUH4 |
PaxDbi | Q9UUH4 |
Genome annotation databases
EnsemblFungii | SPAC630.08c.1; SPAC630.08c.1:pep; SPAC630.08c |
GeneIDi | 2543373 |
KEGGi | spo:SPAC630.08c |
Organism-specific databases
PomBasei | SPAC630.08c, erg25 |
VEuPathDBi | FungiDB:SPAC630.08c |
Phylogenomic databases
eggNOGi | KOG0873, Eukaryota |
HOGENOMi | CLU_047036_5_0_1 |
InParanoidi | Q9UUH4 |
OMAi | PGFIFQF |
PhylomeDBi | Q9UUH4 |
Enzyme and pathway databases
UniPathwayi | UPA00768 UPA00770;UER00756 |
Reactomei | R-SPO-191273, Cholesterol biosynthesis R-SPO-192105, Synthesis of bile acids and bile salts |
Miscellaneous databases
PROi | PR:Q9UUH4 |
Family and domain databases
InterProi | View protein in InterPro IPR006694, Fatty_acid_hydroxylase |
Pfami | View protein in Pfam PF04116, FA_hydroxylase, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ERG25_SCHPO | |
Accessioni | Q9UUH4Primary (citable) accession number: Q9UUH4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 22, 2003 |
Last sequence update: | May 1, 2000 | |
Last modified: | February 23, 2022 | |
This is version 128 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Schizosaccharomyces pombe
Schizosaccharomyces pombe: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families