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Information on EC 1.2.1.84 - alcohol-forming fatty acyl-CoA reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q39152

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EC Tree
IUBMB Comments
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
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Arabidopsis thaliana
UNIPROT: Q39152
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
far11, fatty acyl-coenzyme a reductase, maqu_2220, psfar i, psfar ii, alcohol-forming fatty acyl-coa reductase, far10, alcohol-forming far, peroxisomal fatty acyl-coa reductase 1, far14, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
FAR
-
-
-
-
fatty acyl-CoA reductase 3
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain acyl-CoA:NADPH reductase
The enzyme has been characterized from the plant Simmondsia chinensis (jojoba). The alcohol is formed by a four-electron reduction of fatty acyl-CoA. Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released. The recombinant enzyme was shown to accept saturated and mono-unsaturated fatty acyl-CoAs of 16 to 22 carbons.
CAS REGISTRY NUMBER
COMMENTARY hide
37350-23-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
root endodermal cell
Manually annotated by BRENDA team
of stem and leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
after heterologous expression in yeast
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
in a T-DNA-insertion mutant, suberin composition of root and seed coat is reduced in C22:0 primary alcohol, and wounding does not induce an increase in C22:0 primary alcohol. Heterologous expression in yeast confirms that FAR1 is an active alcohol-forming fatty acyl-coenzyme A reductase
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FACR1_ARATH
491
0
55481
Swiss-Prot
other Location (Reliability: 4)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by wounding and salt stress, wounding results in increase in basal levles of C18:0-C22:0 primary alcohols
expression is induced by wounding and salt stress, wounding results in increase in basal levels of C18:0-C22:0 primary alcohols
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rowland, O.; Zheng, H.; Hepworth, S.; Lam, P.; Jetter, R.; Kunst, L.
CER4 encodes an alcohol-forming fatty acyl-coenzyme A reductase involved in cuticular wax production in Arabidopsis
Plant Physiol.
142
866-877
2006
Arabidopsis thaliana (Q93ZB9)
Manually annotated by BRENDA team
Domergue, F.; Vishwanath, S.; Joubes, J.; Ono, J.; Lee, J.; Bourdon, M.; Alhattab, R.; Lowe, C.; Pascal, S.; Lessire, R.; Rowland, O.
Three Arabidopsis fatty acyl-coenzyme a reductases, FAR1, FAR4, and FAR5, generate primary fatty alcohols associated with suberin deposition
Plant Physiol.
153
1539-1554
2010
Arabidopsis thaliana (Q0WRB0), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q9LXN3)
Manually annotated by BRENDA team