NFRA2_BACSU
ID NFRA2_BACSU Reviewed; 249 AA.
AC P94424; Q548A6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=FMN reductase [NAD(P)H];
DE EC=1.5.1.39 {ECO:0000269|PubMed:16229462};
DE AltName: Full=NAD(P)H-dependent FMN reductase;
DE AltName: Full=NAD(P)H-dependent nitro/flavin reductase;
DE AltName: Full=NAD(P)H-dependent nitroreductase;
DE AltName: Full=NAD(P)H-dependent oxidoreductase;
GN Name=nfrA2; Synonyms=ycnD; OrderedLocusNames=BSU03860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Park C.H., Gonzalez C.F., Ackerley D., Keyhan M., Matin A.;
RT "Molecular engineering of soluble bacterial proteins with chromate
RT reductase activity.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=17407181; DOI=10.1002/pmic.200700008;
RA Nguyen V.D., Wolf C., Maeder U., Lalk M., Langer P., Lindequist U.,
RA Hecker M., Antelmann H.;
RT "Transcriptome and proteome analyses in response to 2-methylhydroquinone
RT and 6-brom-2-vinyl-chroman-4-on reveal different degradation systems
RT involved in the catabolism of aromatic compounds in Bacillus subtilis.";
RL Proteomics 7:1391-1408(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH FMN, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP NOMENCLATURE, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16229462; DOI=10.1021/bi0510835;
RA Morokutti A., Lyskowski A., Sollner S., Pointner E., Fitzpatrick T.B.,
RA Kratky C., Gruber K., Macheroux P.;
RT "Structure and function of YcnD from Bacillus subtilis, a flavin-containing
RT oxidoreductase.";
RL Biochemistry 44:13724-13733(2005).
CC -!- FUNCTION: Reduces FMNH(2) to FMN, with NADH or NADPH as reductant. It
CC also reduces nitroaromatic compounds, quinones, chromates and azo dyes.
CC It could supply the reduced form of FMN to luciferase-like protein and
CC contribute to the degradation of aromatic compounds.
CC {ECO:0000269|PubMed:16229462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NADP(+) = FMN + 2 H(+) + NADPH; Xref=Rhea:RHEA:21624,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.5.1.39;
CC Evidence={ECO:0000269|PubMed:16229462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMNH2 + NAD(+) = FMN + 2 H(+) + NADH; Xref=Rhea:RHEA:21620,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58210; EC=1.5.1.39;
CC Evidence={ECO:0000269|PubMed:16229462};
CC -!- ACTIVITY REGULATION: FMN is a competitive inhibitor of NADH, and
CC therefore leads to the preferential utilization of NADPH.
CC {ECO:0000269|PubMed:16229462}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for 4-nitrophenol (NP)(at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC KM=0.7 uM for 5-nitro-2-furaldehyde semicarbazone (NF)(at pH 8 and 25
CC degrees Celisus) {ECO:0000269|PubMed:16229462};
CC KM=4.2 uM for FMN (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC KM=4.4 uM for NADPH (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC KM=5.0 uM for chromate (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC KM=6.4 uM for NADH (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC KM=96 uM for methyl-4-nitrobenzenesulfonate (NBS)(at pH 8 and 25
CC degrees Celisus) {ECO:0000269|PubMed:16229462};
CC Vmax=0.9 umol/min/mg enzyme with chromate as substrate (at pH 8 and
CC 25 degrees Celisus) {ECO:0000269|PubMed:16229462};
CC Vmax=4.0 umol/min/mg enzyme with 5-nitro-2-furaldehyde semicarbazone
CC (nitrofurazone, NF) as substrate (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC Vmax=7.0 umol/min/mg enzyme with 4-nitrophenol (NP) as substrate (at
CC pH 8 and 25 degrees Celisus) {ECO:0000269|PubMed:16229462};
CC Vmax=73.6 umol/min/mg enzyme with methyl-4-nitrobenzenesulfonate
CC (NBS) as substrate (at pH 8 and 25 degrees Celisus)
CC {ECO:0000269|PubMed:16229462};
CC Vmax=200 umol/min/mg enzyme with FMN as substrate
CC {ECO:0000269|PubMed:16229462};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16229462}.
CC -!- INDUCTION: Strongly induced by stress due to exposure to 6-brom-2-
CC vinyl-chroman-4-on (chromanon) and less strongly induced after exposure
CC to 2-methylhydroquinone (2-MHQ) or catechol stress.
CC {ECO:0000269|PubMed:17407181}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism. The reduction of nitro-organic compounds and
CC inorganic chromate occur in the absence of external FMN and are
CC therefore believed to require binding of these substrates in the active
CC site. In contrast to these reduction processes, azo dyes are reduced
CC only in the presence of external FMN, indicating that azo dye reduction
CC occurs outside the active site of the enzyme.
CC -!- SIMILARITY: Belongs to the flavin oxidoreductase frp family.
CC {ECO:0000305}.
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DR EMBL; D50453; BAA09018.1; -; Genomic_DNA.
DR EMBL; AF417208; AAL09698.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12194.1; -; Genomic_DNA.
DR PIR; H69763; H69763.
DR RefSeq; NP_388268.1; NC_000964.3.
DR RefSeq; WP_003234479.1; NZ_JNCM01000031.1.
DR PDB; 1ZCH; X-ray; 1.85 A; A=1-249.
DR PDBsum; 1ZCH; -.
DR AlphaFoldDB; P94424; -.
DR SMR; P94424; -.
DR STRING; 224308.BSU03860; -.
DR PaxDb; P94424; -.
DR PRIDE; P94424; -.
DR EnsemblBacteria; CAB12194; CAB12194; BSU_03860.
DR GeneID; 938267; -.
DR KEGG; bsu:BSU03860; -.
DR PATRIC; fig|224308.179.peg.409; -.
DR eggNOG; COG0778; Bacteria.
DR InParanoid; P94424; -.
DR OMA; FRHDETY; -.
DR PhylomeDB; P94424; -.
DR BioCyc; BSUB:BSU03860-MON; -.
DR SABIO-RK; P94424; -.
DR EvolutionaryTrace; P94424; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0052874; F:FMN reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR CDD; cd02146; NfsA-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR016446; Flavin_OxRdtase_Frp.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR PANTHER; PTHR43425; PTHR43425; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR PIRSF; PIRSF005426; Frp; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Detoxification;
KW Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..249
FT /note="FMN reductase [NAD(P)H]"
FT /id="PRO_0000205513"
FT BINDING 11..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 67
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16229462"
FT BINDING 134..136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT BINDING 173..175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1ZCH"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1ZCH"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 104..127
FT /evidence="ECO:0007829|PDB:1ZCH"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1ZCH"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1ZCH"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 190..212
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:1ZCH"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:1ZCH"
SQ SEQUENCE 249 AA; 27868 MW; 691BEAE44234FA59 CRC64;
MNEVIKSLTD HRSIRSYTDE PVAQEQLDQI IEAVQSAPSS INGQQVTVIT VQDKERKKKI
SELAGGQPWI DQAPVFLLFC ADFNRAKIAL EDLHDFKMEI TNGLESVLVG AVDAGIALGT
ATAAAESLGL GTVPIGAVRG NPQELIELLE LPKYVFPLSG LVIGHPADRS AKKPRLPQEA
VNHQETYLNQ DELTSHIQAY DEQMSEYMNK RTNGKETRNW SQSIASYYER LYYPHIREML
EKQGFKVEK
