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EC 1.16.1.9 Details
EC number
1.16.1.9
Accepted name
ferric-chelate reductase (NADPH)
Reaction
2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH
Other name(s)
ferric chelate reductase (ambiguous), iron chelate reductase (ambiguous), NADPH:Fe3+-EDTA reductase, NADPH-dependent ferric reductase, yqjH (gene name), Fe(II):NADP+ oxidoreductase
Systematic name
Fe(II)-siderophore:NADP+ oxidoreductase
CAS registry number
120720-17-4
Comment
Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [3]. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H].
History
created 1992 as EC 1.6.99.13, transferred 2002 to EC 1.16.1.7, transferred 2011 to EC 1.16.1.9, modified 2012, modified 2014
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EC Tree
1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.2 Acting on the aldehyde or oxo group of donors
1.3 Acting on the CH-CH group of donors
1.4 Acting on the CH-NH2 group of donors
1.5 Acting on the CH-NH group of donors
1.6 Acting on NADH or NADPH
1.7 Acting on other nitrogenous compounds as donors
1.8 Acting on a sulfur group of donors
1.9 Acting on a heme group of donors
1.10 Acting on diphenols and related substances as donors
1.11 Acting on a peroxide as acceptor
1.12 Acting on hydrogen as donor
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.15 Acting on superoxide as acceptor
1.16 Oxidizing metal ions
1.17 Acting on CH or CH2 groups
1.18 Acting on iron-sulfur proteins as donors
1.19 Acting on reduced flavodoxin as donor
1.20 Acting on phosphorus or arsenic in donors
1.21 Catalysing the reaction X-H + Y-H = X-Y
1.21.1 With NAD+ or NADP+ as acceptor
1.21.3 With oxygen as acceptor
1.21.4 With a disulfide as acceptor
1.21.98 With other, known, physiological acceptors
1.21.99 With unknown physiological acceptors
1.22 Acting on halogen in donors
1.23 Reducing C-O-C group as acceptor
1.97 Other oxidoreductases
1.98 Enzymes using H2 as reductant (deleted subclass)
1.99 Other enzymes using O2 as oxidant (deleted subclass)
2 Transferases
3 Hydrolases
3.1 Acting on ester bonds
3.1.1 Carboxylic-ester hydrolases
3.1.1.1 carboxylesterase
3.1.1.2 arylesterase
3.1.1.3 triacylglycerol lipase
3.1.1.4 phospholipase A2
3.1.1.5 lysophospholipase
3.1.1.6 acetylesterase
3.1.1.7 acetylcholinesterase
3.1.1.8 cholinesterase
3.1.1.9 created 1961, deleted 1972
3.1.1.10 tropinesterase
3.1.1.11 pectinesterase
3.1.1.12 created 1961, deleted 1972
3.1.1.13 sterol esterase
3.1.1.14 chlorophyllase
3.1.1.15 L-arabinonolactonase
3.1.1.16 created 1961, deleted 1972
3.1.1.17 gluconolactonase
3.1.1.18 created 1961, deleted 1982
3.1.1.19 uronolactonase
3.1.1.20 tannase
3.1.1.21 retinyl-palmitate esterase
3.1.1.22 hydroxybutyrate-dimer hydrolase
3.1.1.23 acylglycerol lipase
3.1.1.24 3-oxoadipate enol-lactonase
3.1.1.25 1,4-lactonase
3.1.1.26 galactolipase
3.1.1.27 4-pyridoxolactonase
3.1.1.28 acylcarnitine hydrolase
3.1.1.29 aminoacyl-tRNA hydrolase
3.1.1.30 D-arabinonolactonase
3.1.1.31 6-phosphogluconolactonase
3.1.1.32 phospholipase A1
3.1.1.33 6-acetylglucose deacetylase
3.1.1.34 lipoprotein lipase
3.1.1.35 dihydrocoumarin hydrolase
3.1.1.36 limonin-D-ring-lactonase
3.1.1.37 steroid-lactonase
3.1.1.38 triacetate-lactonase
3.1.1.39 actinomycin lactonase
3.1.1.40 orsellinate-depside hydrolase
3.1.1.41 cephalosporin-C deacetylase
3.1.1.42 chlorogenate hydrolase
3.1.1.43 α-amino-acid esterase
3.1.1.44 4-methyloxaloacetate esterase
3.1.1.45 carboxymethylenebutenolidase
3.1.1.46 deoxylimonate A-ring-lactonase
3.1.1.47 1-alkyl-2-acetylglycerophosphocholine esterase
3.1.1.48 fusarinine-C ornithinesterase
3.1.1.49 sinapine esterase
3.1.1.50 wax-ester hydrolase
3.1.1.51 phorbol-diester hydrolase
3.1.1.52 phosphatidylinositol deacylase
3.1.1.53 sialate O-acetylesterase
3.1.1.54 acetoxybutynylbithiophene deacetylase
3.1.1.55 acetylsalicylate deacetylase
3.1.1.56 methylumbelliferyl-acetate deacetylase
3.1.1.57 2-pyrone-4,6-dicarboxylate lactonase
3.1.1.58 N-acetylgalactosaminoglycan deacetylase
3.1.1.59 juvenile-hormone esterase
3.1.1.60 bis(2-ethylhexyl)phthalate esterase
3.1.1.61 protein-glutamate methylesterase
3.1.1.62 created 1989, deleted 1992
3.1.1.63 11-cis-retinyl-palmitate hydrolase
3.1.1.64 retinoid isomerohydrolase
3.1.1.65 L-rhamnono-1,4-lactonase
3.1.1.66 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene deacetylase
3.1.1.67 fatty-acyl-ethyl-ester synthase
3.1.1.68 xylono-1,4-lactonase
3.1.1.69 created 1992, deleted 2002
3.1.1.70 cetraxate benzylesterase
3.1.1.71 acetylalkylglycerol acetylhydrolase
3.1.1.72 acetylxylan esterase
3.1.1.73 feruloyl esterase
3.1.1.74 cutinase
3.1.1.75 poly(3-hydroxybutyrate) depolymerase
3.1.1.76 poly(3-hydroxyoctanoate) depolymerase
3.1.1.77 acyloxyacyl hydrolase
3.1.1.78 polyneuridine-aldehyde esterase
3.1.1.79 hormone-sensitive lipase
3.1.1.80 acetylajmaline esterase
3.1.1.81 quorum-quenching N-acyl-homoserine lactonase
3.1.1.82 pheophorbidase
3.1.1.83 monoterpene ε-lactone hydrolase
3.1.1.84 cocaine esterase
3.1.1.85 pimelyl-[acyl-carrier protein] methyl ester esterase
3.1.1.86 rhamnogalacturonan acetylesterase
3.1.1.87 fumonisin B1 esterase
3.1.1.88 pyrethroid hydrolase
3.1.1.89 protein phosphatase methylesterase-1
3.1.1.90 all-trans-retinyl ester 13-cis isomerohydrolase
3.1.1.91 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase
3.1.1.92 4-sulfomuconolactone hydrolase
3.1.1.93 mycophenolic acid acyl-glucuronide esterase
3.1.1.94 versiconal hemiacetal acetate esterase
3.1.1.95 aclacinomycin methylesterase
3.1.1.96 D-aminoacyl-tRNA deacylase
3.1.1.97 methylated diphthine methylhydrolase
3.1.1.98 [Wnt protein] O-palmitoleoyl-L-serine hydrolase
3.1.1.99 6-deoxy-6-sulfogluconolactonase
3.1.1.100 chlorophyllide a hydrolase
3.1.1.101 poly(ethylene terephthalate) hydrolase
3.1.1.102 mono(ethylene terephthalate) hydrolase
3.1.1.103 teichoic acid D-alanine hydrolase
3.1.1.104 5-phospho-D-xylono-1,4-lactonase
3.1.1.105 3-O-acetylpapaveroxine carboxylesterase
3.1.1.106 O-acetyl-ADP-ribose deacetylase
3.1.1.107 apo-salmochelin esterase
3.1.1.108 iron(III)-enterobactin esterase
3.1.1.109 iron(III)-salmochelin esterase
3.1.1.110 xylono-1,5-lactonase
3.1.1.111 phosphatidylserine sn-1 acylhydrolase
3.1.1.112 isoamyl acetate esterase
3.1.1.113 ethyl acetate hydrolase
3.1.1.114 methyl acetate hydrolase
3.1.1.115 D-apionolactonase
3.1.1.116 sn-1-specific diacylglycerol lipase
3.1.1.117 (4-O-methyl)-D-glucuronate—lignin esterase
3.1.1.118 phospholipid sn-1 acylhydrolase
3.1.1.119 exo-acting protein-α-N-acetylgalactosaminidase
3.1.2 Thioester hydrolases
3.1.3 Phosphoric-monoester hydrolases
3.1.4 Phosphoric-diester hydrolases
3.1.5 Triphosphoric-monoester hydrolases
3.1.6 Sulfuric-ester hydrolases
3.1.7 Diphosphoric-monoester hydrolases
3.1.8 Phosphoric-triester hydrolases
3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters
3.1.11.1 exodeoxyribonuclease I
3.1.11.2 exodeoxyribonuclease III
3.1.11.3 exodeoxyribonuclease (lambda-induced)
3.1.11.4 exodeoxyribonuclease (phage SP3-induced)
3.1.11.5 exodeoxyribonuclease V
3.1.11.6 exodeoxyribonuclease VII
3.1.11.7 adenosine-5′-diphospho-5′-[DNA] diphosphatase
3.1.11.8 guanosine-5′-diphospho-5′-[DNA] diphosphatase
3.1.12 Exodeoxyribonucleases producing 3′-phosphomonoesters
3.1.13 Exoribonucleases producing 5′-phosphomonoesters
3.1.14 Exoribonucleases producing 3'-phosphomonoesters
3.1.15 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters
3.1.16 Exonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters
3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
3.1.22 Endodeoxyribonucleases producing 3'-phosphomonoesters
3.1.23 Site-specific endodeoxyribonucleases: cleavage is sequence specific (deleted sub-subclass)
3.1.24 Site specific endodeoxyribonucleases: cleavage is not sequence specific (deleted sub-subclass)
3.1.25 Site-specific endodeoxyribonucleases that are specific for altered bases
3.1.26 Endoribonucleases producing 5'-phosphomonoesters
3.1.27 Endoribonucleases producing 3'-phosphomonoesters
3.1.30 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 5'-phosphomonoesters
3.1.31 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters
3.2 Glycosylases
3.3 Acting on ether bonds
3.4 Acting on peptide bonds (peptidases)
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
3.6 Acting on acid anhydrides
3.7 Acting on carbon-carbon bonds
3.8 Acting on halide bonds
3.9 Acting on phosphorus-nitrogen bonds
3.10 Acting on sulfur-nitrogen bonds
3.10.1 Acting on sulfur-nitrogen bonds (only sub-subclass identified to date)
3.11 Acting on carbon-phosphorus bonds
3.12 Acting on sulfur-sulfur bonds
3.13 Acting on carbon-sulfur bonds
4 Lyases
5 Isomerases
6 Ligases
7 Translocases