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ERG3_ASHGO
ID   ERG3_ASHGO              Reviewed;         351 AA.
AC   Q754B9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=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   Name=ERG3; OrderedLocusNames=AFR151C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 178.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR   EMBL; AE016819; AAS53522.2; -; Genomic_DNA.
DR   RefSeq; NP_985698.2; NM_211052.2.
DR   AlphaFoldDB; Q754B9; -.
DR   SMR; Q754B9; -.
DR   STRING; 33169.AAS53522; -.
DR   EnsemblFungi; AAS53522; AAS53522; AGOS_AFR151C.
DR   GeneID; 4621950; -.
DR   KEGG; ago:AGOS_AFR151C; -.
DR   eggNOG; KOG0872; Eukaryota.
DR   HOGENOM; CLU_047036_3_0_1; -.
DR   InParanoid; Q754B9; -.
DR   OMA; HHMYFNY; -.
DR   UniPathway; UPA00768; UER00762.
DR   Proteomes; UP000000591; Chromosome VI.
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..351
FT                   /note="Delta(7)-sterol 5(6)-desaturase"
FT                   /id="PRO_0000117019"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          180..305
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           194..198
FT                   /note="Histidine box-1"
FT   MOTIF           207..211
FT                   /note="Histidine box-2"
FT   MOTIF           282..286
FT                   /note="Histidine box-3"
SQ   SEQUENCE   351 AA;  41169 MW;  5334940168035EC7 CRC64;
     MDLVLEFCDS YFFDYVYATL LPASLSPKMG GTWQQAMIKE QMVNATRVFG RSLERPLEVY
     GYAPFMFEVS PHAFGSVLPR YSLLRQSLSL FLVTTVFGWL LYLIVASFSY VFVFDKSVFN
     HPRYLKNQMS MEIKQGLGAI PYMAVMTVPW FLLELHGYSH LYMGLELNVR GYVRLALEAL
     FFILFTDFGI YLLHRWLHWP AVYKVLHKKH HKWLVCTPFA SHAFHPIDGY LQSLPYHLFP
     MLFPLHKVSY LVLFTFVNVW TVMIHDGEYL SNDPVINGAA CHTVHHLYFN YNYGQFTTLW
     DRLGGSYREP DHELFDSNLK KDKAVWEQQI KEVDEMIKNV EGPADDRVYE R
 
 
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