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P53199 (ERG26_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating

EC=1.1.1.170
Gene names
Name:ERG26
Ordered Locus Names:YGL001C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 4/6.

Subunit structure

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. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein Ref.6 Ref.9.

Miscellaneous

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

Sequence similarities

Belongs to the 3-beta-HSD family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERG28P400303EBI-6514,EBI-22518
MCM7P381322EBI-6514,EBI-4300

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
PRO_0000087798

Sites

Active site1511Proton acceptor By similarity
Binding site1551NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P53199 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 87CA8FF8D64B0327

FASTA34938,706
        10         20         30         40         50         60 
MSKIDSVLII GGSGFLGLHL IQQFFDINPK PDIHIFDVRD LPEKLSKQFT FNVDDIKFHK 

        70         80         90        100        110        120 
GDLTSPDDME NAINESKANV VVHCASPMHG QNPDIYDIVN VKGTRNVIDM CKKCGVNILV 

       130        140        150        160        170        180 
YTSSAGVIFN GQDVHNADET WPIPEVPMDA YNETKAIAED MVLKANDPSS DFYTVALRPA 

       190        200        210        220        230        240 
GIFGPGDRQL VPGLRQVAKL GQSKFQIGDN NNLFDWTYAG NVADAHVLAA QKLLDPKTRT 

       250        260        270        280        290        300 
AVSGETFFIT NDTPTYFWAL ARTVWKADGH IDKHVIVLKR PVAICAGYLS EWVSKMLGKE 

       310        320        330        340 
PGLTPFRVKI VCAYRYHNIA KAKKLLGYTP RVGIEEGINK TLAWMDEGL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72523 Genomic DNA. Translation: CAA96701.1.
AY693026 Genomic DNA. Translation: AAT93045.1.
BK006941 Genomic DNA. Translation: DAA08098.1.
PIRS64003.
RefSeqNP_011514.1. NM_001180866.1.

3D structure databases

ProteinModelPortalP53199.
SMRP53199. Positions 2-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33244. 121 interactions.
DIPDIP-6786N.
IntActP53199. 22 interactions.
MINTMINT-666123.
STRING4932.YGL001C.

Proteomic databases

PaxDbP53199.
PeptideAtlasP53199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL001C; YGL001C; YGL001C.
GeneID852883.
KEGGsce:YGL001C.

Organism-specific databases

CYGDYGL001c.
SGDS000002969. ERG26.

Phylogenomic databases

eggNOGCOG0451.
GeneTreeENSGT00550000074557.
HOGENOMHOG000167989.
KOK07748.
OMAEPMRDQV.
OrthoDBEOG72G1HV.

Enzyme and pathway databases

BioCycMetaCyc:YGL001C-MONOMER.
YEAST:YGL001C-MONOMER.
UniPathwayUPA00770; UER00757.

Gene expression databases

GenevestigatorP53199.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002225. 3Beta_OHSteriod_DH/Estase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01073. 3Beta_HSD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972532.
PROP53199.

Entry information

Entry nameERG26_YEAST
AccessionPrimary (citable) accession number: P53199
Secondary accession number(s): D6VUD7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways