FAD3D_ARATH
ID FAD3D_ARATH Reviewed; 435 AA.
AC P48622;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Temperature-sensitive sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic {ECO:0000303|PubMed:12232435};
DE EC=1.14.19.35 {ECO:0000303|PubMed:12232435};
DE AltName: Full=Temperature-sensitive omega-3 fatty acid desaturase 8, chloroplastic {ECO:0000303|PubMed:7846164};
DE Flags: Precursor;
GN Name=FAD8 {ECO:0000303|PubMed:7846164};
GN OrderedLocusNames=At5g05580 {ECO:0000312|Araport:AT5G05580};
GN ORFNames=MOP10.12 {ECO:0000312|EMBL:AED90892.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION BY COLD.
RC STRAIN=cv. Columbia; TISSUE=Aerial part;
RX PubMed=7846164; DOI=10.1104/pp.106.4.1615;
RA Gibson S., Arondel V., Iba K., Somerville C.R.;
RT "Cloning of a temperature-regulated gene encoding a chloroplast omega-3
RT desaturase from Arabidopsis thaliana.";
RL Plant Physiol. 106:1615-1621(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RX PubMed=7972507; DOI=10.1104/pp.105.4.1451;
RA Watahiki M.C., Yamamoto K.T.;
RT "A new isozyme of plastid omega-3 fatty acid desaturase in Arabidopsis
RT thaliana.";
RL Plant Physiol. 105:1451-1452(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=12232435; DOI=10.1104/pp.106.4.1609;
RA McConn M., Hugly S., Browse J., Somerville C.;
RT "A Mutation at the fad8 Locus of Arabidopsis Identifies a Second
RT Chloroplast [omega]-3 Desaturase.";
RL Plant Physiol. 106:1609-1614(1994).
CC -!- FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the
CC third double bond in the biosynthesis of 16:3 and 18:3 fatty acids,
CC important constituents of plant membranes. It is thought to use
CC ferredoxin as an electron donor and to act on fatty acids esterified to
CC galactolipids, sulfolipids and phosphatidylglycerol.
CC {ECO:0000269|PubMed:7846164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (7Z,10Z)-hexadecadienoyl-containing glycerolipid + 2 H(+) +
CC O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (7Z,10Z,13Z)-
CC hexadecatrienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:46412, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:88268, ChEBI:CHEBI:88269; EC=1.14.19.35;
CC Evidence={ECO:0000269|PubMed:12232435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H(+) +
CC O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z,12Z,15Z)-octadecatrienoyl-
CC containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46408, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:88351,
CC ChEBI:CHEBI:90078; EC=1.14.19.35;
CC Evidence={ECO:0000269|PubMed:12232435};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:7846164}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=P48622-1; Sequence=Displayed;
CC -!- INDUCTION: By low temperature. {ECO:0000269|PubMed:7846164}.
CC -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC involved in metal ion binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; L27158; AAA65621.1; -; mRNA.
DR EMBL; U08216; AAB60302.1; -; Genomic_DNA.
DR EMBL; D17578; BAA04504.1; -; mRNA.
DR EMBL; AB005241; BAB11547.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90892.1; -; Genomic_DNA.
DR EMBL; AF361837; AAK32849.1; -; mRNA.
DR EMBL; AY078043; AAL77744.1; -; mRNA.
DR RefSeq; NP_196177.1; NM_120640.4. [P48622-1]
DR AlphaFoldDB; P48622; -.
DR BioGRID; 15720; 2.
DR STRING; 3702.AT5G05580.1; -.
DR PaxDb; P48622; -.
DR PRIDE; P48622; -.
DR ProteomicsDB; 222315; -. [P48622-1]
DR EnsemblPlants; AT5G05580.1; AT5G05580.1; AT5G05580. [P48622-1]
DR GeneID; 830441; -.
DR Gramene; AT5G05580.1; AT5G05580.1; AT5G05580. [P48622-1]
DR KEGG; ath:AT5G05580; -.
DR Araport; AT5G05580; -.
DR TAIR; locus:2169677; AT5G05580.
DR eggNOG; ENOG502QQQ2; Eukaryota.
DR InParanoid; P48622; -.
DR OMA; NSVMGHI; -.
DR OrthoDB; 577374at2759; -.
DR PhylomeDB; P48622; -.
DR BioCyc; ARA:AT5G05580-MON; -.
DR BioCyc; MetaCyc:AT5G05580-MON; -.
DR BRENDA; 1.14.19.35; 399.
DR BRENDA; 1.14.19.36; 399.
DR UniPathway; UPA00658; -.
DR PRO; PR:P48622; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P48622; baseline and differential.
DR Genevisible; P48622; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0102874; F:1-16:0-2-18:2-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102842; F:1-18:1-2-16:2-monogalactosyldiacylglycerol desaturase activity (SN2-16:3 forming); IEA:UniProtKB-EC.
DR GO; GO:0102835; F:1-18:2-2-16:0-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102837; F:1-18:2-2-16:1-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102839; F:1-18:2-2-16:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102840; F:1-18:2-2-16:3-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102848; F:1-18:2-2-18:2-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102875; F:1-18:2-2-18:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102849; F:1-18:2-2-18:3-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102993; F:linolenate delta15 desaturase activity; IEA:RHEA.
DR GO; GO:0042389; F:omega-3 fatty acid desaturase activity; IMP:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR021863; FAS_N.
DR Pfam; PF11960; DUF3474; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..435
FT /note="Temperature-sensitive sn-2 acyl-lipid omega-3
FT desaturase (ferredoxin), chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007122"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 156..160
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 192..196
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 359..363
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 50136 MW; 3D77A8035A6214E1 CRC64;
MASSVLSECG FRPLPRFYPK HTTSFASNPK PTFKFNPPLK PPSSLLNSRY GFYSKTRNWA
LNVATPLTTL QSPSEEDTER FDPGAPPPFN LADIRAAIPK HCWVKNPWMS MSYVVRDVAI
VFGLAAVAAY FNNWLLWPLY WFAQGTMFWA LFVLGHDCGH GSFSNDPRLN SVAGHLLHSS
ILVPYHGWRI SHRTHHQNHG HVENDESWHP LPESIYKNLE KTTQMFRFTL PFPMLAYPFY
LWNRSPGKQG SHYHPDSDLF LPKEKKDVLT STACWTAMAA LLVCLNFVMG PIQMLKLYGI
PYWIFVMWLD FVTYLHHHGH EDKLPWYRGK EWSYLRGGLT TLDRDYGWIN NIHHDIGTHV
IHHLFPQIPH YHLVEATEAA KPVLGKYYRE PKNSGPLPLH LLGSLIKSMK QDHFVSDTGD
VVYYEADPKL NGQRT
