SC5D2_ARATH
ID SC5D2_ARATH Reviewed; 279 AA.
AC Q9M883;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative Delta(7)-sterol-C5(6)-desaturase 2;
DE EC=1.14.19.20;
DE AltName: Full=Delta(7)-sterol-C5-desaturase 2;
DE AltName: Full=Delta-7-C-5 sterol desaturase 2;
DE AltName: Full=Homolog of DWF7 protein;
GN Name=HDF7; OrderedLocusNames=At3g02590; ORFNames=F16B3.22;
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 [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 [2]
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).
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:Q39208};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
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; AC021640; AAF32466.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73833.1; -; Genomic_DNA.
DR RefSeq; NP_186908.1; NM_111127.2.
DR AlphaFoldDB; Q9M883; -.
DR STRING; 3702.AT3G02590.1; -.
DR PaxDb; Q9M883; -.
DR PRIDE; Q9M883; -.
DR EnsemblPlants; AT3G02590.1; AT3G02590.1; AT3G02590.
DR GeneID; 820687; -.
DR Gramene; AT3G02590.1; AT3G02590.1; AT3G02590.
DR KEGG; ath:AT3G02590; -.
DR Araport; AT3G02590; -.
DR TAIR; locus:2076899; AT3G02590.
DR eggNOG; KOG0872; Eukaryota.
DR HOGENOM; CLU_047036_2_1_1; -.
DR InParanoid; Q9M883; -.
DR OMA; YWLHRMF; -.
DR OrthoDB; 1249774at2759; -.
DR PhylomeDB; Q9M883; -.
DR BioCyc; ARA:AT3G02590-MON; -.
DR PRO; PR:Q9M883; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M883; baseline and differential.
DR Genevisible; Q9M883; 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: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..279
FT /note="Putative Delta(7)-sterol-C5(6)-desaturase 2"
FT /id="PRO_0000117031"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 134..263
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
FT MOTIF 148..152
FT /note="Histidine box-1"
FT MOTIF 162..166
FT /note="Histidine box-2"
FT MOTIF 239..243
FT /note="Histidine box-3"
SQ SEQUENCE 279 AA; 33111 MW; DCAB107445FA2795 CRC64;
MAATMADYND QIVNETSFYN RMVLSHLLPV NLWEPLPHFL QTWLRNYLAG NILYFISGFL
WCFYIYYLKL NVYVPKESIP TRKAMLLQIY VAMKAMPWYT LLPAVSEYMI EHGWTKCYST
LDHFNWFLCF LYIALYLVLV EFMIYWVHKE LHDIKFLYKH LHATHHMYNK QNTLSPFAGL
AFHPLDGILQ AIPHVIALFI VPIHLITHLS LLFLEGIWTA SIHDCIHGNI WPIMGAGYHT
IHHTTYKHNY GHYTIWMDWM FGSLMVPLAE KDSFKEKEK
