FAD21_DIMSI
ID FAD21_DIMSI Reviewed; 380 AA.
AC Q6RS95;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Acyl-lipid (9+3)-(E)-desaturase {ECO:0000305};
DE EC=1.14.19.34 {ECO:0000269|PubMed:14718523};
DE AltName: Full=Fatty acid desaturase 2-1 {ECO:0000303|PubMed:14718523};
DE Short=DsFAD2-1 {ECO:0000303|PubMed:14718523};
DE AltName: Full=Trans-delta(12) oleic acid desaturase {ECO:0000303|PubMed:14718523};
OS Dimorphotheca sinuata (African daisy).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Calenduleae;
OC Dimorphotheca.
OX NCBI_TaxID=112408;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14718523; DOI=10.1074/jbc.m314329200;
RA Cahoon E.B., Kinney A.J.;
RT "Dimorphecolic acid is synthesized by the coordinate activities of two
RT divergent Delta12-oleic acid desaturases.";
RL J. Biol. Chem. 279:12495-12502(2004).
CC -!- FUNCTION: Involved in the biosynthesis of dimorphecolic acid (9-OH-
CC 18:2(10E,12E)). Converts oleic acid (18:1(9Z)) into 18:2(9Z,12E) and
CC probably palmitoleic acid (16:1(9Z)) into 16:2(9Z,12E). Very limited
CC ability to catalyze (Z)-delta(12) desaturation.
CC {ECO:0000269|PubMed:14718523}.
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:14718523};
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:14718523};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AY494986; AAS72902.1; -; mRNA.
DR AlphaFoldDB; Q6RS95; -.
DR KEGG; ag:AAS72902; -.
DR BioCyc; MetaCyc:MON-12589; -.
DR BRENDA; 1.14.19.34; 14177.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005804; FA_desaturase_dom.
DR Pfam; PF00487; FA_desaturase; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="Acyl-lipid (9+3)-(E)-desaturase"
FT /id="PRO_0000434888"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..107
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 139..143
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 313..317
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43570 MW; D889920A8566AF51 CRC64;
MGAGGCISVS ETKPNQKNSL ERAPYDKPPF TISDLKKAIP PHLFKRSLIR SLSYVASDLT
VAFLLYHATT YFHHLPQPFT ALAWLAYWVA QGCVLTGVWV IGHECGHHGL SEYRGVDDTV
GYILHSSLLV PYFSWKYSHR RHHSNTGSLD RDEVFVPKPR SKISWYSKYF NNPVGRIGVL
FITLTLGWPL YLTFNVSGRP YDRFACHYSP NSPIYNNRER FQIYLSDIGI VITSLVLLRA
AMVKGLVWLI CVYGVPLMIT NGFLVLVTYL QHTHPSLPHY DNSEWEWLKG ALVTVDRDFG
VLNTVFHHAT DGHIVHHLFP TIPHYNAMEA TKAVKPLMGE YYQYDATPFY VAMWREAKEC
LFVDRDEGEK GGVFWYKNKM
