AL10_ANELE
ID AL10_ANELE Reviewed; 312 AA.
AC P0DOW2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Acyl-CoA C20 Delta5-desaturase {ECO:0000303|PubMed:17384161};
DE EC=1.14.19.37 {ECO:0000269|PubMed:17384161};
DE AltName: Full=Acyl-CoA 5-desaturase (non-methylene-interrupted) {ECO:0000303|PubMed:17384161};
DE AltName: Full=Acyl-CoA 5-desaturase AL10 {ECO:0000305};
GN Name=AL10 {ECO:0000303|PubMed:17384161};
OS Anemone leveillei (Windflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC Anemoneae; Anemone.
OX NCBI_TaxID=212809;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=17384161; DOI=10.1104/pp.107.098202;
RA Sayanova O., Haslam R., Venegas Caleron M., Napier J.A.;
RT "Cloning and characterization of unusual fatty acid desaturases from
RT Anemone leveillei: identification of an acyl-coenzyme A C20 Delta5-
RT desaturase responsible for the synthesis of sciadonic acid.";
RL Plant Physiol. 144:455-467(2007).
CC -!- FUNCTION: Catalyzes the desaturation of 20:2Delta(11,14) and
CC 20:3Delta(11,14,17) to generate sciadonic acid (20:3Delta(5,11,14)) and
CC juniperonic acid (20:4Delta(5,11,14,17)).
CC {ECO:0000269|PubMed:17384161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z)-eicosadienoyl-CoA + AH2 + O2 = (5Z,11Z,14Z)-
CC eicosatrienoyl-CoA + A + 2 H2O; Xref=Rhea:RHEA:42160,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:76410, ChEBI:CHEBI:78663;
CC EC=1.14.19.37; Evidence={ECO:0000269|PubMed:17384161};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + AH2 + O2 =
CC (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + A + 2 H2O;
CC Xref=Rhea:RHEA:42164, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:74328,
CC ChEBI:CHEBI:78664; EC=1.14.19.37;
CC Evidence={ECO:0000269|PubMed:17384161};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O00767};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O00767};
CC -!- PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
CC {ECO:0000269|PubMed:17384161}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0DOW2; -.
DR SMR; P0DOW2; -.
DR UniPathway; UPA00658; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; PTHR11351; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..312
FT /note="Acyl-CoA C20 Delta5-desaturase"
FT /id="PRO_0000438498"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 90..95
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 127..131
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 259..263
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 90
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 259
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
SQ SEQUENCE 312 AA; 36952 MW; DABA4F1E819AB117 CRC64;
MDLTSMAMQE TTAAAEEDRL PCSEVPVKEK TKKITWVRKW NSTDVFHILF IGGLHVLCLF
APSTFSWKSF WVCFALYAIC GVFGTTLSFH RNLTHRSFKL PKYLEYFFAY VGLHALQGDP
VWWVSTHRYH HKYTDTYLDP HSPIEGFWFC HIFWLFDSKY IIEKCGRYEN AGDLMKQSYY
RFLERTFVYH VYLQAALLYL FGGFPFIVWG MAVRTILGFH LSWLVNSVCH RWGNRPWNTG
DLSTNNWFIA MLTSGEGWHN NHHAFEYSAR HGIEWWQIDT TWYIIKLLEY LGLATDIKVP
SEIHKRKMSF KN
