ERG3A_SCHPO
ID ERG3A_SCHPO Reviewed; 300 AA.
AC O94457; Q9UU10;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Delta(7)-sterol 5(6)-desaturase erg31 {ECO:0000303|PubMed:18310029};
DE EC=1.14.19.20 {ECO:0000305|PubMed:18310029};
DE AltName: Full=C-5 sterol desaturase erg31 {ECO:0000303|PubMed:18310029};
DE AltName: Full=Ergosterol Delta(5,6) desaturase erg31 {ECO:0000305};
DE AltName: Full=Ergosterol biosynthetic protein 31 {ECO:0000303|PubMed:18310029};
DE AltName: Full=Sterol-C5-desaturase erg31 {ECO:0000303|PubMed:18310029};
GN Name=erg31 {ECO:0000303|PubMed:18310029}; Synonyms=erg3;
GN ORFNames=SPAC1687.16c;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 147-261, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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 INDUCTION.
RX PubMed=16537923; DOI=10.1128/mcb.26.7.2817-2831.2006;
RA Todd B.L., Stewart E.V., Burg J.S., Hughes A.L., Espenshade P.J.;
RT "Sterol regulatory element binding protein is a principal regulator of
RT anaerobic gene expression in fission yeast.";
RL Mol. Cell. Biol. 26:2817-2831(2006).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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: C-5 sterol desaturase; part of the third module of ergosterol
CC biosynthesis pathway that includes by the late steps of the pathway
CC (PubMed:18310029). Erg31 and erg32 catalyze the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol (By
CC similarity). The third module or late pathway involves the ergosterol
CC synthesis itself through consecutive reactions that mainly occur in the
CC endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase
CC erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to
CC form squalene, which is the precursor of all steroids. Secondly,
CC squalene is converted into lanosterol by the consecutive action of the
CC squalene epoxidase erg1 and the lanosterol synthase erg7. The
CC lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation
CC of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-
CC ol. In the next steps, a complex process involving various
CC demethylation, reduction and desaturation reactions catalyzed by the C-
CC 14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27
CC leads to the production of zymosterol. Erg28 likely functions in the C-
CC 4 demethylation complex reaction by tethering erg26 and Erg27 to the
CC endoplasmic reticulum or to facilitate interaction between these
CC proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the
CC methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to
CC form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction
CC which results in unsaturation at C-7 in the B ring of sterols and thus
CC converts fecosterol to episterol. The sterol-C5-desaturases erg31 and
CC erg32 then catalyze the introduction of a C-5 double bond in the B ring
CC to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further
CC converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol
CC by forming the C-22(23) double bond in the sterol side chain. Finally,
CC ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28)
CC sterol reductase erg4 to produce ergosterol (PubMed:18310029)
CC (Probable). In the genus Schizosaccharomyces, a second route exists
CC between lanosterol and fecosterol, via the methylation of lanosterol to
CC eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-
CC demethylation by the demethylation complex erg25-erg26-erg27
CC (PubMed:8586261) (Probable). {ECO:0000250|UniProtKB:P32353,
CC ECO:0000269|PubMed:18310029, ECO:0000305|PubMed:18310029,
CC ECO:0000305|PubMed:8586261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-
CC dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:52972; EC=1.14.19.20;
CC Evidence={ECO:0000305|PubMed:18310029};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561;
CC Evidence={ECO:0000305|PubMed:18310029};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P53045};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis.
CC {ECO:0000269|PubMed:18310029}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is anaerobically up-regulated via the sterol
CC regulatory element binding protein sre1. {ECO:0000269|PubMed:16537923}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000250|UniProtKB:P53045}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of ergosterol when erg32
CC is also deleted (PubMed:18310029). The double disruptant also leads to
CC susceptibility to cycloheximide and to staurosporine, but does not
CC affect tolerance to nystatin and to amphotericin B (PubMed:18310029).
CC {ECO:0000269|PubMed:18310029}.
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 sterol desaturase family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22610.1; -; Genomic_DNA.
DR EMBL; AB027881; BAA87185.1; -; Genomic_DNA.
DR PIR; T37759; T37759.
DR RefSeq; NP_593135.1; NM_001018531.2.
DR AlphaFoldDB; O94457; -.
DR BioGRID; 278585; 33.
DR STRING; 4896.SPAC1687.16c.1; -.
DR PaxDb; O94457; -.
DR EnsemblFungi; SPAC1687.16c.1; SPAC1687.16c.1:pep; SPAC1687.16c.
DR GeneID; 2542109; -.
DR KEGG; spo:SPAC1687.16c; -.
DR PomBase; SPAC1687.16c; erg31.
DR VEuPathDB; FungiDB:SPAC1687.16c; -.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_3_0_1; -.
DR InParanoid; O94457; -.
DR OMA; IFPLQKM; -.
DR PhylomeDB; O94457; -.
DR Reactome; R-SPO-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-SPO-6807062; Cholesterol biosynthesis via lathosterol.
DR UniPathway; UPA00768; -.
DR PRO; PR:O94457; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; ISO:PomBase.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; ISM:PomBase.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IGI:PomBase.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..300
FT /note="Delta(7)-sterol 5(6)-desaturase erg31"
FT /id="PRO_0000117025"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 123..248
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 137..141
FT /note="Histidine box-1"
FT MOTIF 150..154
FT /note="Histidine box-2"
FT MOTIF 225..229
FT /note="Histidine box-3"
SQ SEQUENCE 300 AA; 35626 MW; 8F0E08972CE29EF9 CRC64;
MDYLLNYADQ YALDSIYNAV YPLARDNIVR QSISLFFLTW FGGMFLYLTF ASLSYQFVFD
KSLMDHPKFL KNQVFMEVLT ALQNLPGMAL LTVPWFLAEL HGYSYLYDNI SDYGLKYFLC
SLPLFVMFSD FGIYWAHRFL HHRYVYPRLH KLHHKWIICT PYASHAFKSA DGFLQSLPYH
LFPFFFPLHK LTYLALFTFV NFWSIMIHDG KYISNNPIIN GAAHHNGHHI YFNYNYGQFT
TLFDRLGNSF RAPDEAWFDK DLRQNEDVLR VELMEYEAIR NEVEGDDDRE YIANSAKKNH
