Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.16.1.7 - ferric-chelate reductase (NADH) and Organism(s) Arabidopsis thaliana and UniProt Accession Q3KTM0

for references in articles please use BRENDA:EC1.16.1.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.1 With NAD+ or NADP+ as acceptor
                1.16.1.7 ferric-chelate reductase (NADH)
IUBMB Comments
Contains FAD. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The plant enzyme is involved in the transport of iron across plant plasma membranes. The enzyme from the bacterium Paracoccus denitrificans can also reduce chromate. cf. EC 1.16.1.9, ferric-chelate reductase (NADPH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q3KTM0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
2
Fe(II)-siderophore
+
+
=
2
Fe(III)-siderophore
+
Synonyms
ferric-chelate reductase, fe(iii) reductase, fe(iii)-chelate reductase, fe(iii) chelate reductase, ahfro1, ferric reductase oxidase, iron chelate reductase, root fe(iii) reductase, fe3+-chelate reductase, ferric-chelate reductase (nadh), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe(III) chelate reductase
-
-
Fe(III)-ethylenediaminetetraacetic complex reductase
-
-
-
-
Fe3+-chelate reductase
-
-
-
-
ferric chelate reductase
ferric reductase oxidase
-
-
iron chelate reductase
-
-
-
-
NADH-linked FeEDTA reductase
-
-
-
-
NADH-linked ferric chelate (turbo) reductase
-
-
-
-
NADH:Fe3+ oxidoreductase
-
-
-
-
reductase, iron chelate
-
-
-
-
[Fe(III)-EDTA] reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
Fe(II)-siderophore:NAD+ oxidoreductase
Contains FAD. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The plant enzyme is involved in the transport of iron across plant plasma membranes. The enzyme from the bacterium Paracoccus denitrificans can also reduce chromate. cf. EC 1.16.1.9, ferric-chelate reductase (NADPH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
CAS REGISTRY NUMBER
COMMENTARY hide
122097-10-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 Fe(II) + NAD+
2 Fe(III) + NADH + H+
show the reaction diagram
-
chloroplats with 300 micromolar ferrozine and 100 micromolar Fe-EDTA in Hepes-sorbitol buffer, pH 7.3
-
-
?
additional information
?
-
-
reduction of ferric iron to ferous iron is the rate-limiting step in iron uptake
-
-
?
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
?
-
-
reduction of ferric iron to ferous iron is the rate-limiting step in iron uptake
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
ferric reductase oxidase 7 is a chloroplast Fe(III) chelate reductase required for survival under ironlimiting conditions, for efficient photosynthesis, and for proper chloroplast iron acquisition in young seedlings
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform AtFRO7
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoforms AtFRO5, AtFRO6
Manually annotated by BRENDA team
isoform AtFRO7
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
structure contains 8 transmembrane helices, 4 of which build up the highly conserved core of the protein. The large water soluble domain contains NADPH, FAD and oxidoreductase sequence motifs and is situated on the inside of the membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
in response to iron deficiency, dicots employ a reduction-based mechanism by inducing FCR at the root plasma membrane to enhance iron uptake
additional information
-
ferric reductase activity in leaves of transgenic plants grown under iron-sufficient or iron-deficient conditions is 2.13 and 1.26fold higher than in control plants, respectively. The enhanced ferric reductase activity leads to increased concentrations of ferrous iron and chlorophyll, and reduces the iron deficiency chlorosis in the transgenic plants, compared to the control plants. In roots, the concentration of ferrous iron and ferric reductase activity are not significantly different in the transgenic plants compared to the control plants, phenotype, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FRO7_ARATH
747
10
84126
Swiss-Prot
other Location (Reliability: 5)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme is subject to posttranscriptional regulation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
frd4 mutations reside in cpFtsY, which encodes a component of one of the pathways responsible for the insertion of proteins into the thylakoid membranes of the chloroplast. In frd4 mutants, ferric-chelate reductase FRO2 mRNA is expressed normally in the root, but plants do not induce the enzyme under iron deficiency
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression the gene AtFRO6 under the control of a 35S promoter in transgenic Nicotiana tabacum cv. Xanthi plants using the Agrobacterium tumefaciens strain EHA105 for transfection. Ferric reductase activity in leaves of transgenic plants grown under iron-sufficient or iron-deficient conditions is 2.13 and 1.26fold higher than in control plants, respectively. Light-responsive elements within the FRO6 promoter regionmediate gene activation on exposure to light
-
transient expression of yeast ferric reductase oxidase FRO6-GFP or FRO7-GFP in Arabidopsis protoplasts, generation of transgenic plants expressing glucuronidase reporter gene fused to the FRO7 promoter, generation of Fro7 mutants missing the Fe(III) chelate reductase
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
nitric oxide acts downstream of auxin to trigger root ferric-chelate reductase activity in response to iron deficiency in Arabidopsis thaliana, signal pathway leading to FCR induction, overview. The induction is suppressed by either polar auxin transport inhibition with 1-naphthylphthalamic acid or NO scavenging with 2-(4-carboxyphenyl)-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide, tungstate, or Nomega-nitro-L-arginine methyl ester hydrochloride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Connolly, E.L.; Campbell, N.H.; Grotz, N.; Prichard, C.L.; Guerinot, M.L.
Overexpression of the FRO2 ferric chelate reductase confers tolerance to growth on low iron and uncovers posttranscriptional control
Plant Physiol.
133
1102-1110
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Wu, H.; Li, L.; Du, J.; Yuan, Y.; Cheng, X.; Ling, H.Q.
Molecular and biochemical characterization of the Fe(III) chelate reductase gene family in Arabidopsis thaliana
Plant Cell Physiol.
46
1505-1514
2005
Arabidopsis thaliana, Arabidopsis thaliana (Q3KTM0)
Manually annotated by BRENDA team
Durrett, T.P.; Connolly, E.L.; Rogers, E.E.
Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an inability to increase iron deficiency-inducible root Fe(III) chelate reductase activity
Plant J.
47
467-479
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Schagerloef, U.; Wilson, G.; Hebert, H.; Al-Karadaghi, S.; Haegerhaell, C.
Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana
Plant Mol. Biol.
62
215-221
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Feng, H.; An, F.; Zhang, S.; Ji, Z.; Ling, H.Q.; Zuo, J.
Light-regulated, tissue-specific, and cell differentiation-specific expression of the Arabidopsis Fe(III)-chelate reductase gene AtFRO6
Plant Physiol.
140
1345-1354
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Mukherjee, I.; Campbell, N.H.; Ash, J.S.; Connolly, E.L.
Expression profiling of the Arabidopsis ferric chelate reductase (FRO) gene family reveals differential regulation by iron and copper
Planta
223
1178-1190
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Vasconcelos, M.; Eckert, H.; Arahana, V.; Graef, G.; Grusak, M.A.; Clemente, T.
Molecular and phenotypic characterization of transgenic soybean expressing the Arabidopsis ferric chelate reductase gene, FRO2
Planta
224
1116-1128
2006
Arabidopsis thaliana
Manually annotated by BRENDA team
Jeong, J.; Cohu, C.; Kerkeb, L.; Pilon, M.; Connolly, E.L.; Guerinot, M.L.
Chloroplast Fe(III) chelate reductase activity is essential for seedling viability under iron limiting conditions
Proc. Natl. Acad. Sci. USA
105
10619-10624
2008
Arabidopsis thaliana, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Li, L.Y.; Cai, Q.Y.; Yu, D.S.; Guo, C.H.
Overexpression of AtFRO6 in transgenic tobacco enhances ferric chelate reductase activity in leaves and increases tolerance to iron-deficiency chlorosis
Mol. Biol. Rep.
38
3605-3616
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Chen, W.W.; Yang, J.L.; Qin, C.; Jin, C.W.; Mo, J.H.; Ye, T.; Zheng, S.J.
Nitric oxide acts downstream of auxin to trigger root ferric-chelate reductase activity in response to iron deficiency in Arabidopsis
Plant Physiol.
154
810-819
2010
Arabidopsis thaliana
Manually annotated by BRENDA team