ERG27_SCHPO
ID ERG27_SCHPO Reviewed; 338 AA.
AC O74732; P78867; Q1L846;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=3-keto-steroid reductase erg27 {ECO:0000250|UniProtKB:Q12452};
DE EC=1.1.1.270 {ECO:0000250|UniProtKB:Q12452};
DE AltName: Full=Ergosterol biosynthetic protein 27 {ECO:0000250|UniProtKB:Q12452};
GN Name=erg27 {ECO:0000250|UniProtKB:Q12452}; ORFNames=SPBC1709.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=8586261; DOI=10.1111/j.1574-6968.1995.tb07929.x;
RA Harmouch N., Coulon J., Bonaly R.;
RT "Identification of 24-methylene-24,25-dihydrolanosterol as a precursor of
RT ergosterol in the yeasts Schizosaccharomyces pombe and Schizosaccharomyces
RT octosporus.";
RL FEMS Microbiol. Lett. 134:147-152(1995).
RN [4]
RP FUNCTION.
RX PubMed=18310029; DOI=10.1099/mic.0.2007/011155-0;
RA Iwaki T., Iefuji H., Hiraga Y., Hosomi A., Morita T., Giga-Hama Y.,
RA Takegawa K.;
RT "Multiple functions of ergosterol in the fission yeast Schizosaccharomyces
RT pombe.";
RL Microbiology 154:830-841(2008).
CC -!- FUNCTION: 3-keto-steroid reductase; part of the third module of
CC ergosterol biosynthesis pathway that includes by the late steps of the
CC pathway (By similarity). Erg27 is a catalytic component of the C-4
CC demethylation complex that catalyze the reduction of the keto group on
CC the C-3 (By similarity). The third module or late pathway involves the
CC ergosterol synthesis itself through consecutive reactions that mainly
CC occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene
CC synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate
CC moieties to form squalene, which is the precursor of all steroids.
CC Secondly, squalene is converted into lanosterol by the consecutive
CC action of the squalene epoxidase erg1 and the lanosterol synthase erg7.
CC The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-
CC demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-
CC triene-3-beta-ol. In the next steps, a complex process involving
CC various demethylation, reduction and desaturation reactions catalyzed
CC by the C-14 reductase erg24 and the C-4 demethylation complex erg25-
CC erg26-erg27 leads to the production of zymosterol. Erg28 likely
CC functions in the C-4 demethylation complex reaction by tethering erg26
CC and Erg27 to the endoplasmic reticulum or to facilitate interaction
CC between these proteins. Then, the sterol 24-C-methyltransferase erg6
CC catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of
CC zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes
CC the reaction which results in unsaturation at C-7 in the B ring of
CC sterols and thus converts fecosterol to episterol. The sterol-C5-
CC desaturases erg31 and erg32 then catalyze the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol. The C-22
CC sterol desaturase erg5 further converts 5-dehydroepisterol into
CC ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double
CC bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-
CC 3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce
CC ergosterol (PubMed:18310029) (Probable). In the genus
CC Schizosaccharomyces, a second route exists between lanosterol and
CC fecosterol, via the methylation of lanosterol to eburicol by erg6,
CC followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the
CC demethylation complex erg25-erg26-erg27 (PubMed:8586261) (Probable).
CC {ECO:0000250|UniProtKB:Q12452, ECO:0000305|PubMed:18310029,
CC ECO:0000305|PubMed:8586261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-4alpha-methylzymosterol + H(+) + NADPH = 4alpha-
CC methylzymosterol + NADP(+); Xref=Rhea:RHEA:36379, ChEBI:CHEBI:1949,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:136486; EC=1.1.1.270;
CC Evidence={ECO:0000250|UniProtKB:Q12452};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36380;
CC Evidence={ECO:0000250|UniProtKB:Q12452};
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 5/6. {ECO:0000250|UniProtKB:Q12452}.
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC {ECO:0000250|UniProtKB:Q12452}.
CC -!- SUBUNIT: Heterotetramer of erg25, erg26, erg27 and erg28 (By
CC similarity). Erg28 acts as a scaffold to tether erg27 and other 4,4-
CC demethylation-related enzymes, forming a demethylation enzyme complex,
CC in the endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:Q12452}.
CC -!- MISCELLANEOUS: In Aspergillus, the biosynthesis pathway of the sterol
CC precursors leading to the prevalent sterol ergosterol differs from
CC yeast. The ringsystem of lanosterol in S.cerevisiae is firstly
CC demethylised in three enzymatic steps leading to the intermediate
CC zymosterol and secondly a methyl group is added to zymosterol by the
CC sterol 24-C-methyltransferase to form fecosterol. In Aspergillus,
CC lanosterol is firstly transmethylated by the sterol 24-C-
CC methyltransferase leading to the intermediate eburicol and secondly
CC demethylated in three steps to form fecosterol. In the genus
CC Schizosaccharomyces, 2 routes exist from lanosterol to erposterol: the
CC classical one via zymosterol and the second one via the formation of
CC eburicol followed by demethylation. {ECO:0000269|PubMed:8586261}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. ERG27 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13878.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89217; BAA13878.1; ALT_INIT; mRNA.
DR EMBL; CU329671; CAA21246.1; -; Genomic_DNA.
DR PIR; T39635; T39635.
DR PIR; T43038; T43038.
DR RefSeq; NP_595440.1; NM_001021348.2.
DR AlphaFoldDB; O74732; -.
DR SMR; O74732; -.
DR BioGRID; 276728; 1.
DR STRING; 4896.SPBC1709.07.1; -.
DR iPTMnet; O74732; -.
DR MaxQB; O74732; -.
DR PaxDb; O74732; -.
DR PRIDE; O74732; -.
DR EnsemblFungi; SPBC1709.07.1; SPBC1709.07.1:pep; SPBC1709.07.
DR GeneID; 2540195; -.
DR KEGG; spo:SPBC1709.07; -.
DR PomBase; SPBC1709.07; erg27.
DR VEuPathDB; FungiDB:SPBC1709.07; -.
DR eggNOG; KOG1478; Eukaryota.
DR HOGENOM; CLU_029944_1_0_1; -.
DR InParanoid; O74732; -.
DR OMA; ASYEGSK; -.
DR PhylomeDB; O74732; -.
DR UniPathway; UPA00768; -.
DR UniPathway; UPA00770; UER00758.
DR PRO; PR:O74732; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:PomBase.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0000253; F:3-keto sterol reductase activity; ISS:PomBase.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISS:PomBase.
DR CDD; cd08941; 3KS_SDR_c; 1.
DR InterPro; IPR042829; HSD17B7/Erg27.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis.
FT CHAIN 1..338
FT /note="3-keto-steroid reductase erg27"
FT /id="PRO_0000371806"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 103..105
FT /note="AGA -> SGS (in Ref. 1; BAA13878)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> P (in Ref. 1; BAA13878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38725 MW; E056C3A0E284A60C CRC64;
MSFRKYALIT GSNSGLGFGI ATRLLQFYQP RLQDEPEVFT VILTCRSREK AEDACRRLKE
FFPDRKIRLE YVLLDLSNMA SVEAAVQDIA TRFPKLDFVY LNAGAWDLEG IQWLKAIFST
LINPIQALTH PTFYKETAGR VSNDSLGYIF ESNVFGHFYL KNRLAELKVL RSSTKVVLTS
SLVAEKKSLD FEDLQCFHGE QPYQSSKRLL DVLHYAELEK GLPFEQYLVH PGLCTTNMYE
TFLGPILVMC AKLGFYICRL LGSPWHTISP YVAAFAFLWT ALHATKEDQS IKWGAAVTRF
GHERVLSTPV ELILPSEQEK ALEYMTKLYQ EWKKKLVS
