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Information on EC 1.2.1.50 - long-chain acyl-protein thioester reductase and Organism(s) Arabidopsis thaliana and UniProt Accession Q39152

for references in articles please use BRENDA:EC1.2.1.50
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EC Tree
IUBMB Comments
Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
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This record set is specific for:
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: Bacteria, Eukaryota, Archaea
Synonyms
acyl-coa reductase, fatty acyl-coa reductase 1, amfar1, acyl coenzyme a reductase, fatty acyl-coa reductase 2, fatty acyl-coa reductase 6, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
fatty acyl-CoA reductase 1
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acyl coenzyme A reductase
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-
-
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acyl-CoA reductase
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-
-
-
fatty acyl-CoA reductase 2
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fatty acyl-CoA reductase 3
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fatty acyl-CoA reductase 6
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fatty acyl-CoA reductase 8
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long-chain-fatty-acyl-CoA reductase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
long-chain-aldehyde:NADP+ oxidoreductase (protein thioesther-forming)
Together with a hydrolase component (EC 3.1.2.2 and EC 3.1.2.14) and a synthetase component (EC 6.2.1.19), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme is acylated by receiving an acyl group from EC 6.2.1.19, and catalyses the reduction of the acyl group, releasing the aldehyde product. The enzyme is also able to accept the acyl group from a long-chain acyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
50936-56-6
-
75718-33-1
complex of three enzymes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55500
theoretical value, verified by SDS-PAGE
51000
theoretical value, verified by SDS-PAGE
56000
theoretical value, verified by SDS-PAGE
61600
theoretical value, verified by SDS-PAGE
68400
theoretical value, verified by SDS-PAGE, heavily degraded
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pET15b for expression in Escherichia coli Rosetta cells
into the vector pET15b for expression in Escherichia coli Rosetta cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doan, T.T.; Carlsson, A.S.; Hamberg, M.; Buelow, L.; Stymne, S.; Olsson, P.
Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli
J. Plant Physiol.
166
787-796
2009
Arabidopsis thaliana (B9TSP7), Arabidopsis thaliana (Q08891), Arabidopsis thaliana (Q1PEI6), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q93ZB9)
Manually annotated by BRENDA team