FADX_MOMCH
ID FADX_MOMCH Reviewed; 399 AA.
AC Q9SP61;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Delta(12) acyl-lipid conjugase (11E,13E-forming) {ECO:0000305};
DE Short=MomoFadX {ECO:0000303|PubMed:10536026};
DE EC=1.14.19.33 {ECO:0000269|PubMed:10536026};
GN Name=FADX {ECO:0000303|PubMed:10536026};
OS Momordica charantia (Bitter gourd) (Balsam pear).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX NCBI_TaxID=3673 {ECO:0000312|EMBL:AAF05916.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10536026; DOI=10.1073/pnas.96.22.12935;
RA Cahoon E.B., Carlson T.J., Ripp K.G., Schweiger B.J., Cook G.A., Hall S.E.,
RA Kinney A.J.;
RT "Biosynthetic origin of conjugated double bonds: production of fatty acid
RT components of high-value drying oils in transgenic soybean embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12935-12940(1999).
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
CC 12 to two conjugated trans bonds at positions 11 and 13.
CC {ECO:0000269|PubMed:10536026}.
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:10536026};
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:10536026};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing seeds, but not in leaves.
CC {ECO:0000269|PubMed:10536026}.
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; AF182521; AAF05916.1; -; mRNA.
DR AlphaFoldDB; Q9SP61; -.
DR BioCyc; MetaCyc:MON-12619; -.
DR BRENDA; 1.14.19.33; 3398.
DR UniPathway; UPA00658; -.
DR Proteomes; UP000504603; Unplaced.
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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..399
FT /note="Delta(12) acyl-lipid conjugase (11E,13E-forming)"
FT /id="PRO_0000434406"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 11..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..118
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 150..154
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 325..329
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 45570 MW; 3664552A93B06FDC CRC64;
MGGRGAIGVL RNGGGPKKKM GPGQGLGPGE RITHARPPFS ISQIKKAIPP HCFQRSLRRS
FSYLLSDIAL VSAFYYVADT YFHRLPHPLL HYLAWPVYWF CQGAVLTGMW GIAHDCGHHA
FSDYQLVDDV VGFLIHSLVF VPYFSFKISH RRHHSNTSSV DRDEVFVPKP KAKMPWYFKY
LTNPPARVFI IFITLTLGWP MYLTFNISGR YYGRFTSHFD PNSPIFSPKE RVLVHISNAG
LVATGYLLYR IAMAKGVGWL IRLYGVPLIV LNACVVLITA LQHTHPSFPY YDSTEWDWLR
GNLVTVDRDY GPIMNRVFHH ITDTHVVHHL FPSMPHYNGK EATVAAKRIL GEYYQFDGTP
IWKAAWREFR ECVYVEPDED DGATSGSSSK GVFWYHNKL
