ICO5D_LIMDO
ID ICO5D_LIMDO Reviewed; 356 AA.
AC Q9FV68;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Icosanoyl-CoA 5-desaturase {ECO:0000305};
DE EC=1.14.19.10;
DE AltName: Full=Delta(5) acyl-CoA desaturase {ECO:0000303|PubMed:10982439};
DE Flags: Fragment;
OS Limnanthes douglasii (Douglas' meadowfoam).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Limnanthaceae; Limnanthes.
OX NCBI_TaxID=28973;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=10982439; DOI=10.1104/pp.124.1.243;
RA Cahoon E.B., Marillia E.F., Stecca K.L., Hall S.E., Taylor D.C.,
RA Kinney A.J.;
RT "Production of fatty acid components of meadowfoam oil in somatic soybean
RT embryos.";
RL Plant Physiol. 124:243-251(2000).
CC -!- FUNCTION: Desaturase involved in the biosynthesis of (5Z)-icos-5-
CC enoate, an unusual monounsaturated fatty acid that makes up to 60% of
CC the total fatty acids in Limnanthes sp. seed oil. Only acts on
CC saturated fatty acids. {ECO:0000269|PubMed:10982439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 =
CC (5Z)-eicosenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:45464, 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:57380,
CC ChEBI:CHEBI:85268; EC=1.14.19.10;
CC Evidence={ECO:0000269|PubMed:10982439};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC -!- PATHWAY: Lipid metabolism; monounsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:10982439}.
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:0000255|RuleBase:RU000581}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AF247133; AAG28599.1; -; mRNA.
DR AlphaFoldDB; Q9FV68; -.
DR SMR; Q9FV68; -.
DR PRIDE; Q9FV68; -.
DR KEGG; ag:AAG28599; -.
DR BioCyc; MetaCyc:MON-12558; -.
DR UniPathway; UPA01038; -.
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; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR PRINTS; PR00075; FACDDSATRASE.
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..356
FT /note="Icosanoyl-CoA 5-desaturase"
FT /id="PRO_0000433902"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..137
FT /note="Histidine box-1"
FT /evidence="ECO:0000255"
FT MOTIF 169..173
FT /note="Histidine box-2"
FT /evidence="ECO:0000255"
FT MOTIF 302..306
FT /note="Histidine box-3"
FT /evidence="ECO:0000255"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 41039 MW; E0CD4BCB8F7B534C CRC64;
LRLSLYFPIS ISLSLSLEAM ASFIATTTPA MPAFASVLDP KIPTKPEPKT ETPKPKDDLE
RFRTSEVVLE RKAKGFWRRK WNPRDIQNAV TLLVLHALAA MAPFYFSWDA FWISFILLGF
ASGVLGITLC FHRCLTHGGF KLPKLVEYFF AYCGSLALQG DPMEWVSNHR YHHQFVDTER
DVHSPTQGFW FCHIGWVLDK DLFVEKRGGR RNNVNDLKKQ AFYRFLQKTY MYHQLALIAL
LYYVGGFPYI VWGMGFRLVF MFHSTFAINS VCHKWGGRPW NTGDLSTNNM FVALCAFGEG
WHNNHHAFEQ SARHGLEWWE IDVTWYVIRT LQAIGLATNV KLPTEAQKQK LKAKSA