FAD6C_SPIOL
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 03-AUG-2022, entry version 85.
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; Chenopodiaceae; 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 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = a (9Z,12Z)-octadecadienoyl-containing
CC glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
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 PRIDE; P48629; -.
DR BioCyc; MetaCyc:MON-14124; -.
DR BRENDA; 1.14.19.23; 5812.
DR UniPathway; UPA00658; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102873; F:1-18:1-2-16:0-digalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102834; F:1-18:1-2-16:0-monogalactosyldiacylglycerol acyl-lipid omega-6 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102850; F:1-18:1-2-16:0-phosphatidylglycerol omega-6 desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102836; F:1-18:1-2-16:1-monogalactosyldiacylglyceroldesaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102838; F:1-18:1-2-16:2-monogalactosyldiacylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102841; F:1-18:1-2-16:2-monogalactosyldiacylglycerol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102655; F:1-18:1-2-trans-16:1-phosphatidylglycerol desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0102844; F:1-18:2-2-16:1-monogalactosyldiacylglycerol desaturase activity (SN2-16:2 forming); IEA:UniProtKB-EC.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005804; FA_desaturase_dom.
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; 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