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Q6CE88 (ERG27_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-keto-steroid reductase

EC=1.1.1.270
Gene names
Name:ERG27
Ordered Locus Names:YALI0B17644g
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Responsible for the reduction of the keto group on the C-3 of sterols By similarity.

Catalytic activity

4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NADP+ = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + NADPH.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsteroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-keto sterol reductase activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3433433-keto-steroid reductase
PRO_0000054594

Sites

Active site2031Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6CE88 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: A6A0233F4A782283

FASTA34338,724
        10         20         30         40         50         60 
MIHNRKTQTV VITGASSNLG IAIGKRLIDE KKEDAHLTIV VTSRTLRNVR VAIKTLKAHA 

        70         80         90        100        110        120 
VAKEVGPEVD FDYLLFDLAD MTSINGALVE LKLRFSRIDT LIFNSNAANY IGINWPLAMW 

       130        140        150        160        170        180 
RFTTQFKSEI ENPSCMIQAV GVKSDDGMGS AYQSNVFGPW YMVLELTEQL KNGGKVIWIS 

       190        200        210        220        230        240 
SITSSEKYVD LEDIELIHNK EPYKGSKRLI DVAHNYYSPK LEEEHGIYSY LTDPGIFTSS 

       250        260        270        280        290        300 
SASEYLNIFS AFGMYLMFYF ARLIGLTTMN IDPYKGANVP VWVTLSEDPS ALKREYRLGS 

       310        320        330        340 
RTGRWGTEMM DATKLQYEGS EEVGAYIDKG VGEWREKLKD QIN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382128 Genomic DNA. Translation: CAG83277.1.
RefSeqXP_501024.1. XM_501024.1.

3D structure databases

ProteinModelPortalQ6CE88.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6CE88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2907211.
GenomeReviewsGene locus YALI0B17644g in contig CR382128_GR.
KEGGyli:YALI0B17644g.

Phylogenomic databases

eggNOGfuNOG05767.
HOGENOMHBG398311.
OMAVIWISSI.
OrthoDBEOG4FBN2N.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK09827.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
ProtoNetSearch...

Entry information

Entry nameERG27_YARLI
AccessionPrimary (citable) accession number: Q6CE88
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: August 16, 2004
Last modified: December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families