ERG3B_SCHPO
ID ERG3B_SCHPO Reviewed; 329 AA.
AC O13666;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Delta(7)-sterol 5(6)-desaturase erg32 {ECO:0000303|PubMed:18310029};
DE EC=1.14.19.20 {ECO:0000305|PubMed:18310029};
DE AltName: Full=C-5 sterol desaturase erg32 {ECO:0000303|PubMed:18310029};
DE AltName: Full=Ergosterol Delta(5,6) desaturase erg32 {ECO:0000305};
DE AltName: Full=Ergosterol biosynthetic protein 32 {ECO:0000303|PubMed:18310029};
DE AltName: Full=Sterol-C5-desaturase erg32 {ECO:0000303|PubMed:18310029};
GN Name=erg32 {ECO:0000303|PubMed:18310029}; ORFNames=pi075, SPBC27B12.03c;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
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 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 [5]
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:0000250|UniProtKB:P32353};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561;
CC Evidence={ECO:0000250|UniProtKB:P32353};
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
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372};
CC Multi-pass membrane protein {ECO:0000255}.
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 erg31
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; AB004539; BAA21457.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16898.1; -; Genomic_DNA.
DR PIR; T40027; T40027.
DR RefSeq; NP_001018791.2; NM_001021446.3.
DR AlphaFoldDB; O13666; -.
DR BioGRID; 280342; 1.
DR STRING; 4896.SPBC27B12.03c.1; -.
DR MaxQB; O13666; -.
DR PaxDb; O13666; -.
DR EnsemblFungi; SPBC27B12.03c.1; SPBC27B12.03c.1:pep; SPBC27B12.03c.
DR GeneID; 3361266; -.
DR KEGG; spo:SPBC27B12.03c; -.
DR PomBase; SPBC27B12.03c; erg32.
DR VEuPathDB; FungiDB:SPBC27B12.03c; -.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_3_1_1; -.
DR InParanoid; O13666; -.
DR OMA; HHMYFNY; -.
DR PhylomeDB; O13666; -.
DR BRENDA; 1.14.19.20; 1577.
DR Reactome; R-SPO-6807047; Cholesterol biosynthesis via desmosterol.
DR Reactome; R-SPO-6807062; Cholesterol biosynthesis via lathosterol.
DR UniPathway; UPA00768; -.
DR PRO; PR:O13666; -.
DR Proteomes; UP000002485; Chromosome II.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC: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; IMP: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 3: Inferred from homology;
KW Endoplasmic reticulum; Golgi apparatus; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..329
FT /note="Delta(7)-sterol 5(6)-desaturase erg32"
FT /id="PRO_0000117026"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 156..281
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 170..175
FT /note="Histidine box-1"
FT MOTIF 183..187
FT /note="Histidine box-2"
FT MOTIF 257..262
FT /note="Histidine box-3"
SQ SEQUENCE 329 AA; 39063 MW; C9DEF93732BC4BFA CRC64;
MDVVLQYADK YVFDTFYGKI AESFDSSSSF ANTAVNSTTL GLAEKVNFAI TSGLLDRNNV
WRQFTSLFLI TWIMGTLSYF LSASFAYYVY FDREEARRHP KFLKNQEHLE LMVALKNLPG
MAILTAPWFL AEIRGYGYVY DKLDEYGYFY LFFSIALFLL FSDFLIYWIH RALHHRWLYA
PLHKLHHKWI VPTPYSSHAF HYLDGYSQSL PYHMFPFFFP LNKYVYLLLF GSVNYWTVLI
HDGKYFSNNA VVNGAAHHAA HHMYFNYNYG QFFTLFDRLC SSYRQPDQEL FDAELRNEKL
QEQRIRFMET VQYTVEGKDD RTYASKKDN
