AL21_ANELE
ID AL21_ANELE Reviewed; 321 AA.
AC P0DOW3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Acyl-CoA 5-desaturase AL21 {ECO:0000305};
DE EC=1.14.19.37 {ECO:0000269|PubMed:17384161};
DE AltName: Full=Acyl-CoA 5-desaturase (non-methylene-interrupted) {ECO:0000303|PubMed:17384161};
GN Name=AL21 {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)). The enzyme can also use 16:0
CC and 18:0 as substrates. {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; P0DOW3; -.
DR SMR; P0DOW3; -.
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..321
FT /note="Acyl-CoA 5-desaturase AL21"
FT /id="PRO_0000438499"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 87..92
FT /note="Histidine box-1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 124..128
FT /note="Histidine box-2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT MOTIF 256..260
FT /note="Histidine box-3"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 92
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 124
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="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 256
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="1"
FT /evidence="ECO:0000250|UniProtKB:O00767"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O00767"
SQ SEQUENCE 321 AA; 37831 MW; 8164212F1BA31DEA CRC64;
MELPAMALQS ELKQDKFPSS DVPVKDKTKK ITWVRVWNST DIFHIILVGG LHVLCLSAPF
TFSWSAFWLS LTLYAVCGVF GTTLSYHRNL THRSFKLPKY LEYFFAYVGL HALQGDPVWW
VSTHRYHHKF TDTYLDPHSP IEGFWFSHIF WLFDSKYILE ECGRYENAGD LLKQSYYRFL
ERTFVFHVYL QAALLYMFGG FPFIVWGMAV RTVWGFHASW LVNSVCHRYG HQAWDTGDLS
TNNWFIAMLT SGEGWHNNHH AFEYSARHGI EWWQIDTTWY VIKLLEYLGL ATDVKVPSEV
HKRKMSFKNC VQDKQFCVND K
