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Information on EC 1.16.1.10 - ferric-chelate reductase [NAD(P)H] and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29428

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EC Tree
     1 Oxidoreductases
         1.16 Oxidizing metal ions
             1.16.1 With NAD+ or NADP+ as acceptor
                1.16.1.10 ferric-chelate reductase [NAD(P)H]
IUBMB Comments
A flavoprotein. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III). cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.9, ferric-chelate reductase (NADPH).
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Archaeoglobus fulgidus
UNIPROT: O29428
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Word Map
  • 1.16.1.10
  • epileptic
  • encephalopathy
  • hyperkinetic
  • choreoathetosis
  • excitatory
  • biallelic
  • neurodevelopmental
  • ampa-receptors
  • ampars
  • sleep
  • neurotransmission
  • glutamatergic
  • electrograph
  • synapses
  • dyskinesia
  • monogenic
  • electroencephalogram
  • co-assembled
  • pore-forming
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
2
Fe(II)-siderophore
+
+
=
2
Fe(III)-siderophore
+
Synonyms
frrs1l, af0830, fro protein, chloroplast ferric chelate oxidoreductase, ferric chelate reductase 1 like protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferric reductase
-
ferric-chelate reductase (NAD(P)H)
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Fe(II)-siderophore:NAD(P)+ oxidoreductase
A flavoprotein. The enzyme catalyses the reduction of bound ferric iron in a variety of iron chelators (siderophores), resulting in the release of ferrous iron. The enzyme from the hyperthermophilic archaeon Archaeoglobus fulgidus is not active with uncomplexed Fe(III). cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.9, ferric-chelate reductase (NADPH).
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(III)-EDTA + NADH
2 Fe(II)-EDTA + NAD+ + H+
show the reaction diagram
no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
-
-
?
2 Fe(III)-EDTA + NADPH
2 Fe(II)-EDTA + NADP+ + H+
show the reaction diagram
no activity is obtained with uncomplexed Fe3+, i.e. FeCl3 and Fe(OH)3, with the menaquinone analog dimethylnaphthoquinone or with Fe2+-EDTA. The enzyme does not reduce EDTA-chelated Ag+ and Cu2+. With Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
flavoprotein, enzyme bound flavin is involved in catalysis, contains 1.4 FMN per monomer, non-covalently bound to the enzyme
NADH
with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
NADPH
with Fe3+-EDTA as the electron acceptor, the purified enzyme exhibits a slightly higher affinity and Vmax for NADH than for NADPH as the electron donor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
Fe(III)-EDTA
pH 7.0, 85°C, cosubstrate: NADPH
0.061
NADH
pH 7.0, 85°C
0.08
NADPH
pH 7.0, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3503
pH 7.0, 85°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
pH 6.0: about 40% of maximal activity, pH 8.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 100
50°C: about 50% of maximal activity, 100°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.84
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
2 * 18000, SDS-PAGE
18659
2 * 18659, calculated from sequence
40000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the homodimeric enzyme are grown at 4°C by the hanging drop vapor diffusion technique, with protein solution at a concentration of 25 mg/ml in 0.1 M Tris-HCl (pH 7.5) and a reservoir consisting of 21%–22% w/v PEG4000, 0.1 M sodium acetate, and 0.1 M Tris-HCl (pH 8.4). The crystallization drops are microseeded after 20–24 hr. Crystal structure of recombinant enzyme containing a bound FMN solved at 1.5 A resolution. The NADP+-bound enzyme complex is determined at 1.65 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vadas, A.; Monbouquette, H.G.; Johnson, E.; Schroeder, I.
Identification and characterization of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus
J. Biol. Chem.
274
36715-36721
1999
Archaeoglobus fulgidus (O29428), Archaeoglobus fulgidus
Manually annotated by BRENDA team
Chiu, H.J.; Johnson, E.; Schroeder, I.; Rees, D.C.
Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+
Structure
9
311-319
2001
Archaeoglobus fulgidus (O29428)
Manually annotated by BRENDA team