Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating

Gene

ERG26

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A 3-beta-hydroxysteroid-4-alpha-carboxylate + NAD(P)+ = a 3-oxosteroid + CO2 + NAD(P)H.

Pathway: zymosterol biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (ERG11)
  2. Delta(14)-sterol reductase (ERG24)
  3. Methylsterol monooxygenase (ERG25)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (ERG26)
  5. 3-keto-steroid reductase (ERG27)
  6. no protein annotated in this organism
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei151 – 1511Proton acceptorBy similarity
Binding sitei155 – 1551NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:YGL001C-MONOMER.
YEAST:YGL001C-MONOMER.
ReactomeiREACT_283157. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00757.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (EC:1.1.1.170)
Gene namesi
Name:ERG26
Ordered Locus Names:YGL001C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL001c.
EuPathDBiFungiDB:YGL001C.
SGDiS000002969. ERG26.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylatingPRO_0000087798Add
BLAST

Proteomic databases

MaxQBiP53199.
PaxDbiP53199.
PeptideAtlasiP53199.

Interactioni

Subunit structurei

Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERG28P400303EBI-6514,EBI-22518
MCM7P381322EBI-6514,EBI-4300

Protein-protein interaction databases

BioGridi33244. 123 interactions.
DIPiDIP-6786N.
IntActiP53199. 22 interactions.
MINTiMINT-666123.
STRINGi4932.YGL001C.

Structurei

3D structure databases

ProteinModelPortaliP53199.
SMRiP53199. Positions 2-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-beta-HSD family.Curated

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
InParanoidiP53199.
KOiK07748.
OMAiSEMNKTI.
OrthoDBiEOG72G1HV.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIDSVLII GGSGFLGLHL IQQFFDINPK PDIHIFDVRD LPEKLSKQFT
60 70 80 90 100
FNVDDIKFHK GDLTSPDDME NAINESKANV VVHCASPMHG QNPDIYDIVN
110 120 130 140 150
VKGTRNVIDM CKKCGVNILV YTSSAGVIFN GQDVHNADET WPIPEVPMDA
160 170 180 190 200
YNETKAIAED MVLKANDPSS DFYTVALRPA GIFGPGDRQL VPGLRQVAKL
210 220 230 240 250
GQSKFQIGDN NNLFDWTYAG NVADAHVLAA QKLLDPKTRT AVSGETFFIT
260 270 280 290 300
NDTPTYFWAL ARTVWKADGH IDKHVIVLKR PVAICAGYLS EWVSKMLGKE
310 320 330 340
PGLTPFRVKI VCAYRYHNIA KAKKLLGYTP RVGIEEGINK TLAWMDEGL
Length:349
Mass (Da):38,706
Last modified:October 1, 1996 - v1
Checksum:i87CA8FF8D64B0327
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72523 Genomic DNA. Translation: CAA96701.1.
AY693026 Genomic DNA. Translation: AAT93045.1.
BK006941 Genomic DNA. Translation: DAA08098.1.
PIRiS64003.
RefSeqiNP_011514.1. NM_001180866.1.

Genome annotation databases

EnsemblFungiiYGL001C; YGL001C; YGL001C.
GeneIDi852883.
KEGGisce:YGL001C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72523 Genomic DNA. Translation: CAA96701.1.
AY693026 Genomic DNA. Translation: AAT93045.1.
BK006941 Genomic DNA. Translation: DAA08098.1.
PIRiS64003.
RefSeqiNP_011514.1. NM_001180866.1.

3D structure databases

ProteinModelPortaliP53199.
SMRiP53199. Positions 2-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33244. 123 interactions.
DIPiDIP-6786N.
IntActiP53199. 22 interactions.
MINTiMINT-666123.
STRINGi4932.YGL001C.

Proteomic databases

MaxQBiP53199.
PaxDbiP53199.
PeptideAtlasiP53199.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL001C; YGL001C; YGL001C.
GeneIDi852883.
KEGGisce:YGL001C.

Organism-specific databases

CYGDiYGL001c.
EuPathDBiFungiDB:YGL001C.
SGDiS000002969. ERG26.

Phylogenomic databases

eggNOGiCOG0451.
GeneTreeiENSGT00550000074557.
HOGENOMiHOG000167989.
InParanoidiP53199.
KOiK07748.
OMAiSEMNKTI.
OrthoDBiEOG72G1HV.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00757.
BioCyciMetaCyc:YGL001C-MONOMER.
YEAST:YGL001C-MONOMER.
ReactomeiREACT_283157. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi972532.
PROiP53199.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Characterization of the Saccharomyces cerevisiae ERG26 gene encoding the C-3 sterol dehydrogenase (C-4 decarboxylase) involved in sterol biosynthesis."
    Gachotte D., Barbuch R., Gaylor J., Nickel E., Bard M.
    Proc. Natl. Acad. Sci. U.S.A. 95:13794-13799(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, FUNCTION.
  5. Erratum
    Gachotte D., Barbuch R., Gaylor J., Nickel E., Bard M.
    Proc. Natl. Acad. Sci. U.S.A. 96:1810-1810(1999)
  6. "Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis."
    Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M.
    Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
    Mo C., Bard M.
    J. Lipid Res. 46:1991-1998(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERG28.
  9. "The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy."
    Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S., Kohlwein S.D.
    Mol. Cell. Proteomics 4:662-672(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiERG26_YEAST
AccessioniPrimary (citable) accession number: P53199
Secondary accession number(s): D6VUD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2580 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.