Reviewed, UniProtKB/Swiss-Prot O74732 (ERG27_SCHPO)

Names and origin

Protein names

Recommended name:
    3-keto-steroid reductase
    EC=1.1.1.270

Gene names

Name:	erg27
ORF Names:	SPBC1709.07

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

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 process	Lipid synthesis Steroid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-keto-steroid reductase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	3-keto-steroid reductase		PRO_0000371806
Sites
	Active site	203	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	103 – 105	3	AGA → SGS in BAA13878. Ref.1
	Sequence conflict	251	1	A → P in BAA13878. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O74732-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E056C3A0E284A60C	FASTA	338	38,725
	10 20 30 40 50 60 MSFRKYALIT GSNSGLGFGI ATRLLQFYQP RLQDEPEVFT VILTCRSREK AEDACRRLKE 70 80 90 100 110 120 FFPDRKIRLE YVLLDLSNMA SVEAAVQDIA TRFPKLDFVY LNAGAWDLEG IQWLKAIFST 130 140 150 160 170 180 LINPIQALTH PTFYKETAGR VSNDSLGYIF ESNVFGHFYL KNRLAELKVL RSSTKVVLTS 190 200 210 220 230 240 SLVAEKKSLD FEDLQCFHGE QPYQSSKRLL DVLHYAELEK GLPFEQYLVH PGLCTTNMYE 250 260 270 280 290 300 TFLGPILVMC AKLGFYICRL LGSPWHTISP YVAAFAFLWT ALHATKEDQS IKWGAAVTRF 310 320 330 GHERVLSTPV ELILPSEQEK ALEYMTKLYQ EWKKKLVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: PR745.
[2]	"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	D89217 mRNA. Translation: BAA13878.1. Different initiation. CU329671 Genomic DNA. Translation: CAA21246.1.
PIR	T39635. T43038.
RefSeq	NP_595440.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O74732.
Genome annotation databases
GeneID	2540195.
GenomeReviews	Gene locus erg27 in contig CU329671_GR.
KEGG	spo:SPBC1709.07.
NMPDR	fig|4896.1.peg.1306.
Organism-specific databases
GeneDB_Spombe	SPBC1709.07.
Phylogenomic databases
OMA	EQYLVHP.
Gene expression databases
ArrayExpress	O74732.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
PRINTS	PR00081. GDHRDH.
ProtoNet	Search...

Entry information

Entry name

ERG27_SCHPO

Accession

Primary (citable) accession number: O74732
Secondary accession number(s): P78867, Q1L846

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)