ID   FAD6C_SPIOL             Reviewed;         447 AA.
AC   P48629;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=Omega-6 fatty acid desaturase, chloroplastic {ECO:0000303|PubMed:7948918};
DE            EC=1.14.19.23 {ECO:0000269|PubMed:7948918};
DE   Flags: Precursor;
GN   Name=FAD6 {ECO:0000303|PubMed:7948918};
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 66-78, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Subito; TISSUE=Leaf;
RX   PubMed=7948918; DOI=10.1007/bf00013749;
RA   Schmidt H., Dresselhaus T., Buck F., Heinz E.;
RT   "Purification and PCR-based cDNA cloning of a plastidial n-6 desaturase.";
RL   Plant Mol. Biol. 26:631-642(1994).
CC   -!- FUNCTION: Chloroplast omega-6 fatty acid desaturase introduces the
CC       second 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:7948918}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (9Z)-octadecenoyl-containing glycerolipid + 2 reduced [2Fe-
CC         2S]-[ferredoxin] + O2 + 2 H(+) = a (9Z,12Z)-octadecadienoyl-
CC         containing glycerolipid + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 H2O;
CC         Xref=Rhea:RHEA:46376, 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:88240,
CC         ChEBI:CHEBI:88351; EC=1.14.19.23;
CC         Evidence={ECO:0000269|PubMed:7948918};
CC   -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:7948918}; Peripheral membrane protein
CC       {ECO:0000305}.
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; X78311; CAA55121.1; -; mRNA.
DR   PIR; S53309; S53309.
DR   AlphaFoldDB; P48629; -.
DR   SMR; P48629; -.
DR   BioCyc; MetaCyc:MONOMER-14124; -.
DR   BRENDA; 1.14.19.23; 5812.
DR   UniPathway; UPA00658; -.
DR   Proteomes; UP000813463; Unplaced.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102850; F:acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) activity; EXP:UniProtKB.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03507; Delta12-FADS-like; 1.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR32100; OMEGA-6 FATTY ACID DESATURASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chloroplast; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:7948918"
FT   CHAIN           66..447
FT                   /note="Omega-6 fatty acid desaturase, chloroplastic"
FT                   /id="PRO_0000007126"
FT   MOTIF           171..175
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           207..211
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           367..371
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         66
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P46312"
SQ   SEQUENCE   447 AA;  51306 MW;  2BA7C87FFF95350E CRC64;
     MESAITISNH VNLAFSLSRN PSLSTKNSAG ISCIKWQRPC LRNLGHVRLN QQRKGTRRKS
     TLVQAVAVPV AQPSAFPPTD NTEHLKQLAE RYGFQQIGEP LPDDVTMRDI ITSLPKQVFE
     INDTKAWGTV LISVTSYALG IFMIAKAPWY LLPLAWAWTG TAITGFFVIG HDCAHKSFSK
     NKLVEDIVGT LAFMPLIYPY EPWRFKHDQH HTKTNMLRED TAWLPIMKED IESSPGLRKA
     LIYAYGPLRT WMSIAHWLKV HFNLKDFRQS EVKRATISLA AVFAFMVIGW PLIIYKTGIV
     GWIKFWLMPW LGYHFWMSTF TIVHHTAPHI PFKSSKEWNA AQAQLSGTVH CDYPRWIEIL
     CHDISVHIPH HISPKIPSYN LRAANQSLNE NWGEYLNKPK SNWRLMRTIM TTCHIYDKDG
     NYVSFEKAVP EESQPISIPK RVMPDYA
//