ERG3_NEUCR
ID ERG3_NEUCR Reviewed; 344 AA.
AC Q7SBB6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Probable Delta(7)-sterol 5(6)-desaturase;
DE EC=1.14.19.20;
DE AltName: Full=C-5 sterol desaturase;
DE AltName: Full=Ergosterol Delta(5,6) desaturase;
DE AltName: Full=Sterol-C5-desaturase;
GN ORFNames=NCU06207;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Catalyzes the introduction of a C-5 double bond in the B ring
CC of ergosterol. May contribute to the regulation of ergosterol
CC biosynthesis. {ECO:0000250|UniProtKB:P32353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a Delta(7)-sterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC Delta(5),Delta(7)-sterol + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:54320, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:138130,
CC ChEBI:CHEBI:138131; EC=1.14.19.20;
CC Evidence={ECO:0000250|UniProtKB:P32353};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from
CC zymosterol: step 3/5.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002238; EAA33687.1; -; Genomic_DNA.
DR RefSeq; XP_962923.1; XM_957830.2.
DR AlphaFoldDB; Q7SBB6; -.
DR SMR; Q7SBB6; -.
DR STRING; 5141.EFNCRP00000006022; -.
DR EnsemblFungi; EAA33687; EAA33687; NCU06207.
DR GeneID; 3879071; -.
DR KEGG; ncr:NCU06207; -.
DR VEuPathDB; FungiDB:NCU06207; -.
DR HOGENOM; CLU_047036_3_0_1; -.
DR InParanoid; Q7SBB6; -.
DR OMA; IFPLQKM; -.
DR UniPathway; UPA00768; UER00762.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000248; F:C-5 sterol desaturase activity; IBA:GO_Central.
DR GO; GO:0050046; F:delta7-sterol 5(6)-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
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; 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..344
FT /note="Probable Delta(7)-sterol 5(6)-desaturase"
FT /id="PRO_0000117024"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 167..292
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 181..185
FT /note="Histidine box-1"
FT MOTIF 194..198
FT /note="Histidine box-2"
FT MOTIF 269..273
FT /note="Histidine box-3"
SQ SEQUENCE 344 AA; 40663 MW; 392432B46C40E448 CRC64;
MDVVLEVTDQ FMFDYMYAWL LPARPALYDF PDKTNGTAQA FSSWVYEPAT KFFSLEPSQA
AYQSIWTRDN IYRQALSLFL ILWLFGLVTY YVFASLSYIF VFDKKTMEHP KFLKNQVWLE
IKQTNAALPV MAFFTFPFLV AEVRGYSLLY DTTAEGPGRW YDFFQFPLFI MFTDFGIYWI
HRGLHHPLVY KHLHKPHHKW IMPTPYASHA FHPIDGFAQS IPYHIFPFIF PLQKMAYVGL
FVFINFWTIM IHDGEYYANN PVINGAACHS VHHFAFNYNY GQFTTLWDRL GGSYREPDGD
MFAKEKKMST TTWKKQVNEM EKIVKEVEGE DDRLYEPTET KKSK
