Information on EC 1.5.1.38 - FMN reductase (NADPH):
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EC NUMBERCOMMENTARY
1.5.1.38-

RECOMMENDED NAMEGeneOntology No.
FMN reductase (NADPH)GO:0052873

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
FMNH2 + NADP+ = FMN + NADPH + H+
show the reaction diagram		the enzyme exhibits double displacement or ping-pong kineticsVibrio harveyi-392180
FMNH2 + NADP+ = FMN + NADPH + H+
show the reaction diagram		ping-pong kinetic patternVibrio harveyi-392200
FMNH2 + NADP+ = FMN + NADPH + H+
show the reaction diagram		the first step in catalysis, which is hydride transfer from C4 of NADPH to cofactor FMN, involves addition to the re face of the FMN, probably at the N5 position. The limited accessibility of the FMN binding pocket and the extensive FMN-protein hydrogen bond network are consistent with the observed ping-pong bisubstrate-biproduct reaction kineticsVibrio harveyiQ56691392299
FMNH2 + NADP+ = FMN + NADPH + H+
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
two-component alkanesulfonate monooxygenase-ALKANEMONOX-PWY

SYSTEMATIC NAMEIUBMB Comments
FMNH2:NADP+ oxidoreductaseThe enzymes from bioluminescent bacteria contain FMN [4], while the enzyme from Escherichia coli does not [8]. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
flavin reductase P----
flavin reductase PVibrio harveyi--392297, 392299
FRP----
FRPVibrio harveyi--392200, 392297
NADPH specific FMN reductaseVibrio harveyi--392180
NADPH-flavin oxidoreductaseVibrio harveyi--392297
NADPH-FMN oxidoreductaseVibrio harveyi--392200
NADPH:FMN oxidoreductaseVibrio harveyi--392180, 392299, 392300
SsuE----
SsuEEscherichia coli--438770, 672426, 674310, 713622

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Escherichia coli-438770P80644SwissProtManually annotated by BRENDA team
Escherichia coli-672426, 674310, 713622--Manually annotated by BRENDA team
Vibrio harveyi-392179, 392180, 392200, 392297, 392300--Manually annotated by BRENDA team
Vibrio harveyi-392299Q56691SwissProtManually annotated by BRENDA team
Vibrio harveyi No. 392-392180--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionVibrio harveyiQ56691NADPH:FMN oxidoreductase is involved in bioluminescence by providing reduced FMN to luciferase392299
physiological functionEscherichia coliP80644SsuD is a monooxygenase that catalyzes the desulfonation of alkanesulfonates and requires reduced FMN, which is provided by the NAD(P)H:flavin oxidoreductase SsuE438770
physiological functionEscherichia coli-FMN reductase (SsuE) catalyzes the reduction of FMN by NADPH, and the reduced flavin is transferred to the monooxygenase (SsuD)672426

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2-thioFMN + NADPH + H+2-thioFMNH2 + NADP+
show the reaction diagram		Vibrio harveyi-the holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate392300--?
FAD + NADPH + H+FADH2 + NADP+
show the reaction diagram		Vibrio harveyi--392180--?
FAD + NADPH + H+FADH2 + NADP+
show the reaction diagram		Escherichia coliP80644FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not438770--?
FAD + NADPH + H+FADH2 + NADP+
show the reaction diagram		Vibrio harveyi-Vmax/KM for riboflavin is 6fold lower compared to Vmax/Km for FMN392300--?
FMN + NADH + H+FMNH2 + NAD+
show the reaction diagram		Escherichia coliP80644when NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity438770--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Escherichia coli--672426--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Vibrio harveyi--392179, 392180, 392200, 392297, 392300--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Escherichia coliP80644FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not. When NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration leads to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity438770--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Escherichia coli-results from single-wavelength analyses at 450 and 550 nm show that reduction of FMN occurs in three distinct phases. Following a possible rapid equilibrium binding of FMN and NADPH to SsuE (MC-1) that occurs before the first detectable step, an initial fast phase (241 s-1) corresponds to the interaction of NADPH with FMN (CT-1). The second phase is a slow conversion (11 s-1) to form a charge-transfer complex of reduced FMNH2 with NADP+ (CT-2), and represents electron transfer from the pyridine nucleotide to the flavin. The third step (19 s-1) is the decay of the charge-transfer complex to SsuE with bound products (MC-2) or product release from the CT-2 complex. Results from isotope studies with [(4R)-2H]NADPH demonstrates a rate-limiting step in electron transfer from NADPH to FMN672426--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Vibrio harveyi-the affinity of the NADPH-specific reductase for NADPH is 1000 times greater than for NADH392179--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Vibrio harveyi-the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate392300--?
riboflavin + NADPH + H+reduced riboflavin + NADP+
show the reaction diagram		Escherichia coliP80644FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not438770--?
riboflavin + NADPH + H+reduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi-Vmax/KM for riboflavin is 13fold lower compared to Vmax/Km for FMN392300--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Vibrio harveyi-the NADPH specific FMN reductase does not utilize NADH392180--?
additional information?-Vibrio harveyi-the enzyme also exhibits appreciable activity with some artificial acceptors: menadione, 2,6-dichlorophenolindophenol, KFeCN6 or 5,5'-dithiobis(2-nitrobenzoic acid). Low activity with methylene blue as acceptor392180---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Escherichia coli--672426--
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Vibrio harveyi--392179, 392180, 392200, 392297, 392300--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
2-thio-FMNVibrio harveyi-binds to the cofactor site of the apoenzyme with an affinity similar to that for FMN binding. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate392300 2D-image
FMNVibrio harveyi-contains a tightly bound FMN cofactor392297 2D-image
FMNVibrio harveyiQ56691the enzyme is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity392299 2D-image
NADHEscherichia coliP80644kcat/KM for NADPH is 335fold higher compared to kcat/KM for NADH438770 2D-image
NADPHVibrio harveyi-the affinity of the NADPH-specific reductase for NADPH is 1000 times greater than for NADH392179 2D-image
NADPHVibrio harveyi-the NADPH specific FMN reductase does not utilize NADH392180 2D-image
NADPHEscherichia coliP80644kcat/KM for NADPH is 335fold higher compared kcat/KM for NADH438770 2D-image
FMNVibrio harveyi-the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme392300 2D-image
additional informationEscherichia coliP80644the enzyme does not contain any bound flavin cofactor438770-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
No entries in this field

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolineVibrio harveyi-0.005 M, 14% inhibition392180 2D-image
AMPVibrio harveyi-0.01 M, 28% inhibition392180 2D-image
DicoumarolVibrio harveyi-0.000325 M, 15% inhibition392180 2D-image
FMNEscherichia coliP80644when NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration led to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity438770 2D-image
N-ethylmaleimideVibrio harveyi-0.001 M, 26% inhibition392180 2D-image
p-hydroxymercuribenzoateVibrio harveyi-0.001 M, 80% inhibition392180 2D-image
rotenoneVibrio harveyi-0.0004 M, 30% inhibition392180 2D-image
KCNVibrio harveyi-0.01 M, 10% inhibition392180 2D-image
additional informationVibrio harveyi-FMN at concentrations over 0.002 mM significantly inhibits the coupled reaction in both light intensity and quantum yield, and shows apparent noncompetitive and competitive inhibition patterns against NADPH and luciferase, respectively. No inhibition of the NADPH oxidation is detected under identical conditions392200-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.007-2-thioFMNVibrio harveyi-pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN392300 2D-image
0.0027-FADEscherichia coliP80644pH 7.9, 30°C438770 2D-image
0.019-FADVibrio harveyi-pH 7.0, 23°C, native enzyme392300 2D-image
5.4e-05-FMNEscherichia coliP80644pH 7.9, 30°C438770 2D-image
0.0005-FMNVibrio harveyi-pH 6.8, 23°C392179 2D-image
0.005-FMNVibrio harveyi-pH 7.0, 23°C, native enzyme392300 2D-image
0.008-FMNVibrio harveyi-pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation392200 2D-image
0.014-FMNVibrio harveyi-pH 7.0, 23°C, spectrometric assay392180 2D-image
0.5555-NADHEscherichia coliP80644pH 7.9, 30°C, 0.0005 mM FMN438770 2D-image
0.003-NADPHVibrio harveyi-pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN392300 2D-image
0.011-NADPHVibrio harveyi-pH 7.0, 23°C, native enzyme392300 2D-image
0.02-NADPHVibrio harveyi-pH 5.6, 23°C, spectrometric assay392180 2D-image
0.02-NADPHVibrio harveyi-pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation392200 2D-image
0.04-NADPHVibrio harveyi-pH 7.0, 23°C; pH 7.0, 23°C, spectrometric assay392180 2D-image
0.046-NADPHEscherichia coliP80644pH 7.9, 30°C, 0.003 mM FMN438770 2D-image
0.025-riboflavinVibrio harveyi-pH 7.0, 23°C, native enzyme392300 2D-image
0.018-FMNVibrio harveyi-pH 5.6, 23°C, spectrometric assay392180 2D-image
additional information-additional informationVibrio harveyi-the kinetic mechanism of FRP is changed to a sequential pattern with a Km(FMN) of 0.003 mM and a Km(NADPH) of 0.02 mM in a luciferase-coupled assay measuring light emission392200-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
34-NADPHVibrio harveyi-pH 7.0, 23°C392180 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.28-FADEscherichia coliP80644pH 7.9, 30°C43877010459
0.0079-FMNEscherichia coliP80644pH 7.9, 30°C43877010560
0.00167-NADHEscherichia coliP80644pH 7.9, 30°C, 0.0005 mM FMN43877014331
0.56-NADPHEscherichia coliP80644pH 7.9, 30°C, 0.003 mM FMN43877027498

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
1.85-Vibrio harveyi-pH 6.8, 23°C392179
51-Vibrio harveyi-pH 7.0, 23°C392180
88.4-Vibrio harveyi-23°C, pH not specified in the publication392297

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5.5-Vibrio harveyi--392180
6.8-Vibrio harveyi-assay at392179
7-Vibrio harveyi-assay at392180, 392300
7.9-Escherichia coliP80644assay at438770

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
510Vibrio harveyi-the enzyme exhibits a maximum activity at pH 5.5 which drops to a broad shoulder from pH 6.5 to pH 8.5 with an activity 75% that of maximum at pH 7.0. About 60% of maximal activity at pH 5.0, about 50% of maximal activity at pH 10.0392180

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
23-Vibrio harveyi-assay at392179, 392180, 392297, 392300
30-Escherichia coliP80644assay at438770

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
40000-Vibrio harveyi-gel filtration392179, 392180
58400-Escherichia coliP80644gel filtration438770
63000-Vibrio harveyi-sucrose density gradient centrifugation392179
additional information-Escherichia coli-formation of a stable complex between the flavin mononucleotide (FMN) reductase (SsuE) and monooxygenase (SsuD) of the alkanesulfonate monooxygenase system. The stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD. Interactions between the two proteins do not lead to overall conformational changes in protein structure674310

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
homodimerEscherichia coliP806442 * 23700, calculated from sequence; 2 * 25400, SDS-PAGE438770
monomerVibrio harveyi-1 * 26312, calculated from sequence; 1 * 28000, SDS-PAGE392297

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
vapor-diffusion technique yields single crystals that grow as hexagonal rods and diffract to 2.9 A resolution using synchrotron X-ray radiation. The protein crystallizes in the primitive hexagonal space group P622. Substitution of two leucine residues (Leu114 and Leu165) to methionine is performed to obtain selenomethionine-containing SsuE for MAD phasing. The selenomethionine derivative of SsuE has been expressed and purified and crystals of the protein have been obtained with and without bound FMNEscherichia coli-713622
the 1.8 A crystal structure of flavin reductase P from Vibrio harVeyi is solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A(2) of surface area buried in the dimer interface. Each subunit comprises two domainsVibrio harveyiQ56691392299

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
55-Vibrio harveyi-5 min, complete loss of activity392179

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°C, considerable loss of activity of reductase preparationsVibrio harveyi-392179
4°C, considerable loss of activity of reductase preparationsVibrio harveyi-392179

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
SsuE is purified to homogeneity as an N-terminal histidine-tagged fusion proteinEscherichia coliP80644438770
-Vibrio harveyi-392179, 392180, 392297, 392300

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Escherichia coliP80644438770
overexpression in Escherichia coliVibrio harveyi-392297

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
392179Gerlo, E.; Charlier, J.Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyiEur. J. Biochem.57461-4671975Vibrio harveyi PubMed
392180Jablonski, E.; DeLuca, M.Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyiBiochemistry162932-29361977Vibrio harveyi PubMed
392200Lei, B.; Tu, S.C.Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferaseBiochemistry3714623-146291998Vibrio harveyi PubMed
392297Lei, B.; Liu, M.; Huang, S.; Tu, S.C.Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzymeJ. Bacteriol.1763552-35581994Vibrio harveyi PubMed
392299Tanner, J.J.; Lei, B.; Tu, S.C.; Krause, K.L.Flavin reductase P: structure of a dimeric enzyme that reduces flavinBiochemistry3513531-135391996Vibrio harveyi PubMed
392300Liu, M.; Lei, B.; Ding, Q.; Lee, J.C.; Tu, S.C.Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibriumArch. Biochem. Biophys.33789-951997Vibrio harveyi PubMed
438770Eichhorn, E.; van der Ploeg, J.R.; Leisinger, T.Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coliJ. Biol. Chem.27426639-266461999Escherichia coli PubMed
672426Gao, B.; Ellis, H.R.Mechanism of flavin reduction in the alkanesulfonate monooxygenase systemBiochim. Biophys. Acta1774359-3672007Escherichia coli PubMed
674310Abdurachim, K.; Ellis, H.R.Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coliJ. Bacteriol.1888153-81592006Escherichia coli PubMed
713622Gao, B.; Bertrand, A.; Boles, W.H.; Ellis, H.R.; Mallett, T.C.Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coliActa Crystallogr. Sect. F61837-8402005Escherichia coli PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.38)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)