FADX_VERFO
ID FADX_VERFO Reviewed; 386 AA.
AC Q8GZC2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Bifunctional desaturase/conjugase FADX {ECO:0000303|PubMed:12481086};
DE AltName: Full=Acyl-lipid (9+3)-(E)-desaturase {ECO:0000305};
DE EC=1.14.19.34 {ECO:0000269|PubMed:12481086};
DE AltName: Full=Delta(12) acyl-lipid conjugase (11E,13E-forming) {ECO:0000305};
DE EC=1.14.19.33 {ECO:0000269|PubMed:12481086};
OS Vernicia fordii (Tung) (Aleurites fordii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Aleuritideae;
OC Vernicia.
OX NCBI_TaxID=73154 {ECO:0000312|EMBL:AAN87574.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12481086; DOI=10.1104/pp.102.010835;
RA Dyer J.M., Chapital D.C., Kuan J.C., Mullen R.T., Turner C., McKeon T.A.,
RA Pepperman A.B.;
RT "Molecular analysis of a bifunctional fatty acid conjugase/desaturase from
RT tung. Implications for the evolution of plant fatty acid diversity.";
RL Plant Physiol. 130:2027-2038(2002).
CC -!- FUNCTION: Converts linoleic acid to alpha-eleostearic acid
CC (18:3(9Z,11E,13E)) and alpha-linolenic acid to alpha-parinaric acid
CC (18:4(9Z,11E,13E,15Z)). Converts a single cis double bond at carbon 12
CC to two conjugated trans bonds at positions 11 and 13. Can also act as a
CC 12(E) desaturase when acting on the monounsaturated fatty acids oleate
CC and palmitoleate, stereoselectively introducing a trans double bond.
CC {ECO:0000269|PubMed:12481086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13E)-octadecatrienoyl-
CC containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46368, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88254,
CC ChEBI:CHEBI:88351; EC=1.14.19.33;
CC Evidence={ECO:0000269|PubMed:12481086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-containing glycerolipid + 2
CC Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13E,15Z)-
CC octadecatetraenoyl-containing glycerolipid + 2 Fe(III)-[cytochrome
CC b5] + 2 H2O; Xref=Rhea:RHEA:46372, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88251,
CC ChEBI:CHEBI:90078; EC=1.14.19.33;
CC Evidence={ECO:0000269|PubMed:12481086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z)-octadecenoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,12E)-octadecadienoyl-containing
CC glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:38047, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88240,
CC ChEBI:CHEBI:88241; EC=1.14.19.34;
CC Evidence={ECO:0000269|PubMed:12481086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z)-hexadecenoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,12E)-hexadecadienoyl-containing
CC glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46240, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:88261,
CC ChEBI:CHEBI:88262; EC=1.14.19.34;
CC Evidence={ECO:0000269|PubMed:12481086};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12481086}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in developing seeds.
CC {ECO:0000269|PubMed:12481086}.
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; AF525535; AAN87574.1; -; mRNA.
DR AlphaFoldDB; Q8GZC2; -.
DR KEGG; ag:AAN87574; -.
DR BRENDA; 1.14.19.14; 9082.
DR BRENDA; 1.14.19.33; 9082.
DR UniPathway; UPA00658; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="Bifunctional desaturase/conjugase FADX"
FT /id="PRO_0000434405"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..112
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 144..148
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 318..322
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 44375 MW; 7CAAAD4BEC83D35A CRC64;
MGAGGRMSVA PNNSKCEKKE SRSVKRVPHT KPPFTLGQLK QAIPSHCFKR SLLRSFSYVV
YDLSLSFIFY SIATTYFHLL PSPITYIAWP VYWAFQGCIL TSVWVLGHEC GHHAFSEYNW
LDDTIGLILH SSLLVPYFSF KISHRRHHSN IASLERDEVF VPRLKSAIPW YSKYLNNPPG
RALTLVATLF IGWPLYLAFN VSGRYYDRFA CHYDPYSPIY SDRERLQIYI SDAMIFVAAY
VLYKIAMAKG LAWLVCIYGV PLLIVNALVV TITSLQHTHV ALPHYDSSEW DWLRGGLATV
DRDYGVFNKI FHNATDTHVI HHLFSSMPHY HGVEATRAIK PILGDYYLFD DTPIHVALWR
EAKECLFVEP DEGDNNNGVF WYSNKF
