ADS3_ARATH
ID ADS3_ARATH Reviewed; 371 AA.
AC Q949X0; Q8LCQ8; Q9LVZ4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Palmitoyl-monogalactosyldiacylglycerol delta-7 desaturase, chloroplastic {ECO:0000303|PubMed:15579662};
DE EC=1.14.19.42 {ECO:0000269|PubMed:15579662};
DE AltName: Full=Acyl-lipid desaturase 3 {ECO:0000303|PubMed:15240892};
DE AltName: Full=Fatty acid desaturase 5 {ECO:0000303|PubMed:15579662};
DE Short=FAD5 {ECO:0000303|PubMed:15579662};
DE AltName: Full=Fatty acid desaturase B {ECO:0000303|PubMed:16666902};
DE Short=FADB {ECO:0000303|PubMed:16666902};
DE AltName: Full=Monogalactosyldiacylglycerol-specific palmitic acid desaturase {ECO:0000303|PubMed:15579662};
DE Flags: Precursor;
GN Name=ADS3 {ECO:0000303|PubMed:15240892};
GN Synonyms=FAD5 {ECO:0000303|PubMed:15579662},
GN FADB {ECO:0000303|PubMed:16666902};
GN OrderedLocusNames=At3g15850 {ECO:0000312|Araport:AT3G15850};
GN ORFNames=MSJ11.25 {ECO:0000312|EMBL:BAB02316.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PATHWAY.
RX PubMed=15579662; DOI=10.1104/pp.104.052951;
RA Heilmann I., Mekhedov S., King B., Browse J., Shanklin J.;
RT "Identification of the Arabidopsis palmitoyl-monogalactosyldiacylglycerol
RT Delta7-desaturase gene FAD5, and effects of plastidial retargeting of
RT Arabidopsis desaturases on the fad5 mutant phenotype.";
RL Plant Physiol. 136:4237-4245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Hamada T.;
RT "FAD5 gene encoding Arabidopsis monogalactosyldiacylglycerol-specific
RT palmitic acid desaturase.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 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 FUNCTION.
RX PubMed=16666902; DOI=10.1104/pp.90.3.943;
RA Kunst L., Browse J., Somerville C.;
RT "A mutant of Arabidopsis deficient in desaturation of palmitic Acid in leaf
RT lipids.";
RL Plant Physiol. 90:943-947(1989).
RN [8]
RP FUNCTION.
RX PubMed=16668849; DOI=10.1104/pp.99.1.197;
RA Hugly S., Somerville C.;
RT "A role for membrane lipid polyunsaturation in chloroplast biogenesis at
RT low temperature.";
RL Plant Physiol. 99:197-202(1992).
RN [9]
RP FUNCTION, AND SPECIFICITY.
RX PubMed=15240892; DOI=10.1073/pnas.0402200101;
RA Heilmann I., Pidkowich M.S., Girke T., Shanklin J.;
RT "Switching desaturase enzyme specificity by alternate subcellular
RT targeting.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10266-10271(2004).
CC -!- FUNCTION: Fatty acid desaturase involved in the first desaturation step
CC leading to the formation of hexadeca 7,10,13-trienoic acid
CC (16:3(7Z,10Z,13Z)), the major functional components of thylakoid
CC membranes (PubMed:15579662, PubMed:16666902, PubMed:15240892). Required
CC for chloroplast biogenesis at low temperature (PubMed:16668849). Also
CC indirectly involved in the production of the oxylipin dinor-oxo-phyto-
CC dienoic acid implicated in wound signaling (PubMed:15579662).
CC {ECO:0000269|PubMed:15240892, ECO:0000269|PubMed:15579662,
CC ECO:0000269|PubMed:16666902, ECO:0000269|PubMed:16668849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced
CC [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(7Z)-hexadecenoyl]-glycerolipid +
CC 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:46756,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:86999, ChEBI:CHEBI:87000;
CC EC=1.14.19.42; Evidence={ECO:0000269|PubMed:15579662};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:15579662}.
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:15579662}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:15240892}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in young leaves. Low expression in
CC roots. {ECO:0000269|PubMed:15579662}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- MISCELLANEOUS: Substrate specificity shifts from delta-7 to delta-9
CC desaturation when the protein is retargeted to the cytoplasm.
CC {ECO:0000269|PubMed:15240892}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AY734684; AAW51920.1; -; Genomic_DNA.
DR EMBL; AB113831; BAD23903.1; -; mRNA.
DR EMBL; AB017071; BAB02316.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75737.1; -; Genomic_DNA.
DR EMBL; AY050838; AAK92773.1; -; mRNA.
DR EMBL; BT000957; AAN41357.1; -; mRNA.
DR EMBL; AY086456; AAM63459.1; -; mRNA.
DR RefSeq; NP_566529.1; NM_112455.4.
DR AlphaFoldDB; Q949X0; -.
DR SMR; Q949X0; -.
DR STRING; 3702.AT3G15850.1; -.
DR PaxDb; Q949X0; -.
DR PRIDE; Q949X0; -.
DR ProteomicsDB; 244653; -.
DR EnsemblPlants; AT3G15850.1; AT3G15850.1; AT3G15850.
DR GeneID; 820828; -.
DR Gramene; AT3G15850.1; AT3G15850.1; AT3G15850.
DR KEGG; ath:AT3G15850; -.
DR Araport; AT3G15850; -.
DR TAIR; locus:2093302; AT3G15850.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_1_0_1; -.
DR InParanoid; Q949X0; -.
DR OMA; SCGESWH; -.
DR OrthoDB; 971318at2759; -.
DR PhylomeDB; Q949X0; -.
DR BioCyc; ARA:AT3G15850-MON; -.
DR BioCyc; MetaCyc:AT3G15850-MON; -.
DR BRENDA; 1.14.19.42; 399.
DR UniPathway; UPA00382; -.
DR UniPathway; UPA00658; -.
DR PRO; PR:Q949X0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q949X0; baseline and differential.
DR Genevisible; Q949X0; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0009579; C:thylakoid; TAS:TAIR.
DR GO; GO:0102657; F:1-18:1-2-16:0-monogalactosyldiacylglycerol palmitoyl-lipid 7-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102843; F:1-18:2-2-16:0-monogalactosyldiacylglycerol desaturase activity (SN2-16:1 forming); IEA:UniProtKB-EC.
DR GO; GO:0009979; F:16:0 monogalactosyldiacylglycerol desaturase activity; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010205; P:photoinhibition; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:TAIR.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 1: Evidence at protein level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Oxylipin biosynthesis; Plastid; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 68..371
FT /note="Palmitoyl-monogalactosyldiacylglycerol delta-7
FT desaturase, chloroplastic"
FT /id="PRO_0000007144"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 148..153
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 185..189
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 317..321
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> G (in Ref. 5; AAK92773)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="D -> V (in Ref. 6; AAM63459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 371 AA; 42580 MW; F1D62B9F44795FCC CRC64;
MASLLTKPKP VFLCSPSLSP RTLNTATPSL NFTRISFTHH QKLAPFKPPS LVVAFSEKGL
KRDVTTAAAA TEGDYRRIML SDVLVKKKEK VVWWEREWKA MDFGAVAVVL SMHLLSLLAP
FQFNWRAVSV AFGLYIVTGL LGITLSFHRN LSHKAFKLPK WLEYLFAYCG AQALQGNPID
WVSTHRYHHQ FCDSDRDPHS PLDGFWFSHM NWMFDTNTIT QRCGEPNNVG DLEKQPFYRF
LRTTYILHPL ALAVALYAMG GFPFIVWGMG VRIVWVYHIT WLVNSACHVW GKQAWNTGDL
SKNNWWVAAL AFGEGWHNNH HAFEFSARHG LEWWQLDMTW YVVKFLQAIG LATDVKLPSE
AQKQRMAFTS D
