FADX_IMPBA
ID FADX_IMPBA Reviewed; 383 AA.
AC Q9SP62;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Delta(12) acyl-lipid conjugase (11E,13E-forming) {ECO:0000305};
DE Short=ImpFadX {ECO:0000303|PubMed:10536026};
DE EC=1.14.19.33 {ECO:0000269|PubMed:10536026};
GN Name=FADX {ECO:0000303|PubMed:10536026};
OS Impatiens balsamina (Balsam).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Balsaminaceae; Impatiens; Impatiens subgen. Impatiens;
OC Impatiens sect. Uniflorae.
OX NCBI_TaxID=63779 {ECO:0000312|EMBL:AAF05915.1};
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; AF182520; AAF05915.1; -; mRNA.
DR AlphaFoldDB; Q9SP62; -.
DR BRENDA; 1.14.19.33; 14021.
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 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..383
FT /note="Delta(12) acyl-lipid conjugase (11E,13E-forming)"
FT /id="PRO_0000434407"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 44743 MW; BCB027C1F6EB345A CRC64;
MGEVGPTNRT KTKLDKQQES ENRVPHEPPP FTLSDLKKAI PPHCFERSLV KSFYHVIHDI
IILSFFYYVA ANYIPMLPQN LRYVAWPIYW AIQGCVQLGI LVLGHECGHH AFSDYQWVDD
MVGFVLHSSQ LIPYFSWKHS HRRHHSNTAS IERDEVYPPA YKNDLPWFAK YLRNPVGRFL
MIFGALLFGW PSYLLFNANG RLYDRFASHY DPQSPIFNNR ERLQVIASDV GLVFAYFVLY
KIALAKGFVW LICVYGVPYV ILNGLIVLIT FLQHTHPNLP RYDLSEWDWL RGALSTVDRD
YGMLNKVFHN VTDTHLVHHL FTTMPHYRAK EATEVIKPIL GDYYKFDDTP FLKALWKDMG
KCIYVESDVP GKNKGVYWYN NDI
