ID   FAD22_DIMSI             Reviewed;         375 AA.
AC   Q6RS96;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Delta(9) fatty acid conjugase-like enzyme {ECO:0000305};
DE   AltName: Full=Fatty acid desaturase 2-2 {ECO:0000303|PubMed:14718523};
DE            Short=DsFAD2-2 {ECO:0000303|PubMed:14718523};
DE            EC=1.14.19.- {ECO:0000305};
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], AND FUNCTION.
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)). Catalyzes the formation of the C-9 hydroxyl group and
CC       the (E)-delta(10) double bond from the trans-linoleic acid
CC       (16:2(9Z,12E)) produced by FAD2-1. Very limited activity with cis-
CC       linoleic acid (16:2(9Z,12Z)). {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; AY494985; AAS72901.1; -; mRNA.
DR   AlphaFoldDB; Q6RS96; -.
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   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="Delta(9) fatty acid conjugase-like enzyme"
FT                   /id="PRO_0000434889"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           94..98
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           130..134
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           307..311
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  43887 MW;  63A4F8295AC07DDB CRC64;
     MGASEEMKVL ERVPVSKPPF EYNDLKKAVP PHCFTRSLSL SFYYLFYDLI KVCILFYVAS
     KYIPMLPYSL SCIVWPLYWF FQGAFLGRLW MIGHECGHHS FSNYRWLDDT VGFLVHTATL
     TPYFSFKYSH RNHHAHTNSL EYDEVHVPKI RKFKSEHLYS EFLTNNPFGL VVNMVFELTF
     GYPSYLIFNY SGRKLTQAGF ASHLYPQSPI FNDSERNHVF FSDVGICIVL YALYRIAIAK
     GAMLVLYVYG LPWVVMSAFI FSLTYLQHTH PSIPHYDSTE WNWLRGALSS IDRELAGAFN
     IKKTHYHVVH HLFPFIPEYH AHDATEALKP ILGPYYKYDG TPFYKALWRE MKDCLYVESD
     DGPNKTGVYW FKTKT