SC5D1_ARATH
ID SC5D1_ARATH Reviewed; 281 AA.
AC Q39208; Q8L9C0; Q9SWU4; Q9SYS2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Delta(7)-sterol-C5(6)-desaturase 1;
DE EC=1.14.19.20 {ECO:0000269|PubMed:10651635, ECO:0000269|PubMed:8919915, ECO:0000269|PubMed:9927639};
DE AltName: Full=Delta(7)-sterol-C5-desaturase 1;
DE AltName: Full=Delta-7-C-5 sterol desaturase 1;
DE AltName: Full=Protein DWARF 7;
DE AltName: Full=Protein STEROL 1;
GN Name=STE1 {ECO:0000303|PubMed:8919915};
GN Synonyms=DWF7 {ECO:0000303|PubMed:9927639}; OrderedLocusNames=At3g02580;
GN ORFNames=F16B3.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8919915; DOI=10.1046/j.1365-313x.1996.09030391.x;
RA Gachotte D., Husselstein T., Bard M., Lacroute F., Benveniste P.;
RT "Isolation and characterization of an Arabidopsis thaliana cDNA encoding a
RT Delta7-sterol-C5-desaturase by functional complementation of a defective
RT yeast mutant.";
RL Plant J. 9:391-398(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT DWF7-1, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=9927639; DOI=10.2307/3870851;
RA Choe S., Noguchi T., Fujioka S., Takatsuto S., Tissier C.P., Gregory B.D.,
RA Ross A.S., Tanaka A., Yoshida S., Tax F.E., Feldmann K.A.;
RT "The Arabidopsis dwf7/ste1 mutant is defective in the Delta7 sterol C-5
RT desaturation step leading to brassinosteroid biosynthesis.";
RL Plant Cell 11:207-221(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT STE1-1.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10344195; DOI=10.1023/a:1006113919172;
RA Husselstein T., Schaller H., Gachotte D., Benveniste P.;
RT "Delta7-sterol-C5-desaturase: molecular characterization and functional
RT expression of wild-type and mutant alleles.";
RL Plant Mol. Biol. 39:891-906(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CATALYTIC ACTIVITY, ENZYME KINETICS, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF THR-114; LYS-115; HIS-147; HIS-151; HIS-161; HIS-164;
RP HIS-165; PRO-175; PRO-201; HIS-203; HIS-222; GLY-234; HIS-238 AND HIS-242.
RX PubMed=10651635; DOI=10.1021/bi991467t;
RA Taton M., Husselstein T., Benveniste P., Rahier A.;
RT "Role of highly conserved residues in the reaction catalyzed by recombinant
RT Delta7-sterol-C5(6)-desaturase studied by site-directed mutagenesis.";
RL Biochemistry 39:701-711(2000).
RN [8]
RP PROPOSED CATALYTIC MECHANISM.
RX PubMed=11141078; DOI=10.1021/bi001696b;
RA Taton M., Husselstein T., Benveniste P., Rahier A.;
RT "Deuterated Delta7-cholestenol analogues as mechanistic probes for wild-
RT type and mutated Delta7-sterol-C5(6)-desaturase.";
RL Biochemistry 40:256-267(2001).
CC -!- FUNCTION: Involved in the biosynthesis of sitosterol and campesterol, a
CC precursor of growth-promoting brassinosteroids.
CC {ECO:0000269|PubMed:8919915, ECO:0000269|PubMed:9927639}.
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:0000269|PubMed:10651635, ECO:0000269|PubMed:8919915,
CC ECO:0000269|PubMed:9927639};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for Delta(7)-cholesterol {ECO:0000269|PubMed:10651635};
CC Vmax=2.6 nmol/h/mg enzyme with Delta(7)-cholesterol as substrate
CC {ECO:0000269|PubMed:10651635};
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; X90454; CAA62079.1; -; mRNA.
DR EMBL; AF105034; AAD38120.1; -; Genomic_DNA.
DR EMBL; AF069468; AAD12944.1; -; Genomic_DNA.
DR EMBL; AC021640; AAF32465.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73832.1; -; Genomic_DNA.
DR EMBL; AY088527; AAM66060.1; -; mRNA.
DR PIR; S71251; S71251.
DR RefSeq; NP_186907.1; NM_111126.4.
DR AlphaFoldDB; Q39208; -.
DR STRING; 3702.AT3G02580.1; -.
DR PaxDb; Q39208; -.
DR PRIDE; Q39208; -.
DR ProteomicsDB; 232765; -.
DR EnsemblPlants; AT3G02580.1; AT3G02580.1; AT3G02580.
DR GeneID; 820679; -.
DR Gramene; AT3G02580.1; AT3G02580.1; AT3G02580.
DR KEGG; ath:AT3G02580; -.
DR Araport; AT3G02580; -.
DR TAIR; locus:2076884; AT3G02580.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_2_1_1; -.
DR InParanoid; Q39208; -.
DR OMA; HTLHHMY; -.
DR OrthoDB; 1249774at2759; -.
DR PhylomeDB; Q39208; -.
DR BioCyc; ARA:AT3G02580-MON; -.
DR BRENDA; 1.14.19.20; 399.
DR SABIO-RK; Q39208; -.
DR PRO; PR:Q39208; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39208; baseline and differential.
DR Genevisible; Q39208; AT.
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:0016132; P:brassinosteroid biosynthetic process; IMP:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 1: Evidence at protein 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..281
FT /note="Delta(7)-sterol-C5(6)-desaturase 1"
FT /id="PRO_0000117030"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 133..262
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 147..151
FT /note="Histidine box-1"
FT MOTIF 161..165
FT /note="Histidine box-2"
FT MOTIF 238..242
FT /note="Histidine box-3"
FT MUTAGEN 114
FT /note="T->I: In ste1-1; 85% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 114
FT /note="T->S: Increased maximal velocity and KM value of the
FT enzyme."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 115
FT /note="K->L: No effect."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 147
FT /note="H->L,E: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 151
FT /note="H->L,E: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 161
FT /note="H->L,E: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 164
FT /note="H->L: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 165
FT /note="H->L: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 175
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 175
FT /note="P->V: Increased catalytic efficiency and maximal
FT velocity of the enzyme."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 201
FT /note="P->A: 80% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 203
FT /note="H->L: 85% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 222
FT /note="H->E: 93% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 222
FT /note="H->L: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 230..281
FT /note="Missing: In dwf7-1; loss of function resulting in a
FT dwarf phenotype."
FT MUTAGEN 234
FT /note="G->A: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 234
FT /note="G->D: 98% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 238
FT /note="H->L,E: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT MUTAGEN 241
FT /note="H->L: 100% activity loss."
FT MUTAGEN 242
FT /note="H->L: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:10651635"
FT CONFLICT 54
FT /note="F -> I (in Ref. 1; CAA62079)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="L -> R (in Ref. 1; CAA62079)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="G -> D (in Ref. 2; AAD38120)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> A (in Ref. 1; CAA62079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 33143 MW; D32BB1BCDC4467D7 CRC64;
MAADNAYLMQ FVDETSFYNR IVLSHLLPAN LWEPLPHFLQ TWLRNYLAGT LLYFISGFLW
CFYIYYLKIN VYLPKDAIPT IKAMRLQMFV AMKAMPWYTL LPTVSESMIE RGWTKCFASI
GEFGWILYFV YIAIYLVFVE FGIYWMHREL HDIKPLYKYL HATHHIYNKQ NTLSPFAGLA
FHPVDGILQA VPHVIALFIV PIHFTTHIGL LFMEAIWTAN IHDCIHGNIW PVMGAGYHTI
HHTTYKHNYG HYTIWMDWMF GSLRDPLLEE DDNKDSFKKA E
