Information on EC 1.16.1.10 - ferric-chelate reductase [NAD(P)H]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.16.1.10
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RECOMMENDED NAME
GeneOntology No.
ferric-chelate reductase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 Fe(II)-siderophore + NAD(P)+ + H+ = 2 Fe(III)-siderophore + NAD(P)H
show the reaction diagram
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
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-
?
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
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?
2 Fe(III)-ferrozine + NADPH
2 Fe(II)-ferrozine + NADP+ + H+
show the reaction diagram
2 Fe3+ + 3 ferrozine + NADH
2 Fe(II)-ferrozine + NAD+ + H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMN
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flavoprotein, enzyme bound flavin is involved in catalysis, contains 1.4 FMN per monomer, non-covalently bound to the enzyme
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme does not require Mg2+ for optimal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
Fe(III)-EDTA
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pH 7.0, 85°C, cosubstrate: NADPH
0.061
NADH
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pH 7.0, 85°C
0.08
NADPH
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pH 7.0, 85°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3503
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pH 7.0, 85°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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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
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50°C: about 50% of maximal activity, 100°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.84
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calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
high cellular abundance, 0.75% of the total soluble protein
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
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2 * 18000, SDS-PAGE
18659
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2 * 18659, calculated from sequence
40000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 18000, SDS-PAGE; 2 * 18659, calculated from sequence
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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE