FADX_TRIKI
ID FADX_TRIKI Reviewed; 387 AA.
AC Q84UC0;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Bifunctional fatty acid conjugase/Delta(12)-oleate desaturase {ECO:0000303|PubMed:12464604};
DE Short=TkFAC {ECO:0000303|PubMed:12464604};
DE AltName: Full=Delta(12)-oleate desaturase {ECO:0000303|PubMed:12464604};
DE EC=1.14.19.- {ECO:0000305};
DE AltName: Full=Linoleoyl-lipid Delta(12) conjugase (11E,13Z-forming) {ECO:0000305|PubMed:12464604};
DE EC=1.14.19.16 {ECO:0000269|PubMed:12464604};
GN Name=FAC {ECO:0000303|PubMed:12464604};
OS Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Trichosanthes.
OX NCBI_TaxID=3677 {ECO:0000312|EMBL:AAO37751.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=12464604; DOI=10.1074/jbc.m210748200;
RA Iwabuchi M., Kohno-Murase J., Imamura J.;
RT "Delta 12-oleate desaturase-related enzymes associated with formation of
RT conjugated trans-delta 11, cis-delta 13 double bonds.";
RL J. Biol. Chem. 278:4603-4610(2003).
CC -!- FUNCTION: Converts a single cis double bond at position 12 of linoleate
CC incorporated into phosphatidylcholine into conjugated 11-trans and 13-
CC cis double bonds (PubMed:12464604). 16:2(9Z,12Z), 18:3(9Z,12Z,15Z) and
CC 18:2(9Z,12Z) are substrates for the conjugase to form trans-Delta(11)
CC and cis-Delta(13) double bonds (PubMed:12464604). No activity on the
CC cis-Delta(9) double bonds of oleic and palmitoleic acids
CC (PubMed:12464604). {ECO:0000269|PubMed:12464604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 Fe(II)-
CC [cytochrome b5] + 2 H(+) + O2 = a (9Z,11E,13Z)-octadeca-9,11,13-
CC trienoyl-containing glycerolipid + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46532, 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:88259,
CC ChEBI:CHEBI:88351; EC=1.14.19.16;
CC Evidence={ECO:0000269|PubMed:12464604};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
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; AY178444; AAO37751.1; -; mRNA.
DR AlphaFoldDB; Q84UC0; -.
DR KEGG; ag:AAO37751; -.
DR BRENDA; 1.14.19.16; 6463.
DR UniPathway; UPA00658; -.
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 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..387
FT /note="Bifunctional fatty acid conjugase/Delta(12)-oleate
FT desaturase"
FT /id="PRO_0000434636"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 105..109
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 141..145
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 315..319
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44918 MW; 13385E2D0775124C CRC64;
MGGGEGIEVR SGSSSTKLAF GERITHAKPP FSISQIKKAI PPHCFQRSLY RSFSYVIFDF
IFASTFYHIA ATNFHRLPHP LHYLAWPLYW FCQGSVFTGL WVIAHECGHR AFSDYQLVDD
VVGFLLHTSF LIPYFSFKIS HRRHHSNTAS LERDEVFVPK PKAKMPWYFK HLTNPPARVL
IIFITLTLGW PMYLAFNISG RFYERFTSHF DPNSPIFSEN EWLQVHISNA GIVAVWYLLY
KLAAAKGIAW VIRMYVVPVT IMNAFVVLIT SLQHTHPSFP YYDSTEWNWL RGNLVTLDRD
YGILNKVFHN ITDTHVVHHL FPSMPHYNAM EATRAVKQVL GEYYHFDGTP IFKAAWREFR
ECIYVEPDND EGASSSSKGV FWFRNKL
