FAD3C_HELAN
ID FAD3C_HELAN Reviewed; 443 AA.
AC Q56VS4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=sn-2 acyl-lipid omega-3 desaturase (ferredoxin), chloroplastic {ECO:0000303|PubMed:17064923};
DE EC=1.14.19.35 {ECO:0000269|PubMed:17064923};
DE AltName: Full=Omega-3 fatty acid desaturase 7, chloroplastic {ECO:0000303|PubMed:17064923};
DE Short=HaFAD7 {ECO:0000303|PubMed:17064923};
DE Flags: Precursor;
GN Name=FAD7 {ECO:0000303|PubMed:17064923};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000312|EMBL:AAP78965.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=17064923; DOI=10.1016/j.plaphy.2006.09.005;
RA Venegas-Caleron M., Muro-Pastor A.M., Garces R., Martinez-Force E.;
RT "Functional characterization of a plastidial omega-3 desaturase from
RT sunflower (Helianthus annuus) in cyanobacteria.";
RL Plant Physiol. Biochem. 44:517-525(2006).
CC -!- FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the
CC third double bond in the biosynthesis of 18:3, and probably also 16:3
CC fatty acids, important constituents of plant membranes. It is thought
CC to use ferredoxin as an electron donor and to act on fatty acids
CC esterified to galactolipids, sulfolipids and phosphatidylglycerol.
CC {ECO:0000269|PubMed:17064923}.
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:0000305};
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:17064923};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:17064923}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and cotyledons, while no
CC or little expression detected in mature seeds, roots and stems.
CC {ECO:0000269|PubMed:17064923}.
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; AY254858; AAP78965.1; -; mRNA.
DR AlphaFoldDB; Q56VS4; -.
DR BRENDA; 1.14.19.35; 2597.
DR UniPathway; UPA00658; -.
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: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:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IDA:UniProtKB.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IDA:UniProtKB.
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 Chloroplast; Membrane; Oxidoreductase; Plastid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..443
FT /note="sn-2 acyl-lipid omega-3 desaturase (ferredoxin),
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435457"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 165..169
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 201..205
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 368..372
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 50808 MW; 0E928F06F32EDC94 CRC64;
MAGLVLSGCA IKPFSQSLPI PTKRFITNPS NINLLHPKDP IFSPNFHGFS RWAVKVSAPL
RIPSIDQQDL DLDLERERIS SLDVQEEEIF DAGAPPPFKL ADIRAAIPKR CWVKDPWRSM
SYVVRDVAIV LGLAAAAAHL NNWLVWPLYW AAQGTMFWAL FVLGHDCGHG SFSNNAKLNS
VVGHLLHSSI LVPYHGWRIS HRTHHQNHGH VENDESWHPL TEKTFKSLDW ITRTLRFTLP
FPMLAYPFYL WNRSPGKSGS HFDPSSDLFV PAEQKDVITS TICWTTMLAL LFGLNFVVGP
VQMLKLYGIP YLINVMWLDF VTYLHHHGHE DKLPWYRGKE WSYLRGGLTT IDRDYGWINN
IHHDIGTHVI HHLFPQIPHY HLIEATEAAK PVLGKYYREP KKSSPIPFHL LGELVRSLKK
DHYVSDTGDV LYYQTDDKLS KEK
