(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 116.
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}.
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   SMR; P94424; -.
DR   STRING; 224308.BSU03860; -.
DR   PaxDb; P94424; -.
DR   PRIDE; P94424; -.
DR   EnsemblBacteria; CAB12194; CAB12194; BSU03860.
DR   GeneID; 938267; -.
DR   KEGG; bsu:BSU03860; -.
DR   PATRIC; fig|224308.179.peg.409; -.
DR   eggNOG; ENOG4108DBC; Bacteria.
DR   eggNOG; COG0778; LUCA.
DR   HOGENOM; HOG000272869; -.
DR   InParanoid; P94424; -.
DR   KO; K19286; -.
DR   OMA; FRHDETY; -.
DR   PhylomeDB; P94424; -.
DR   BioCyc; BSUB:BSU03860-MONOMER; -.
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: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_FRP; 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;
DR   PRODOM; P94424.
DR   SWISS-2DPAGE; P94424.
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   REGION          11..15
FT                   /note="FMN-binding"
FT   REGION          134..136
FT                   /note="FMN-binding"
FT   REGION          173..175
FT                   /note="FMN-binding"
FT   BINDING         67
FT                   /note="FMN"
FT                   /evidence="ECO:0000269|PubMed:16229462"
FT   HELIX           3..9
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           24..36
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           40..42
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   STRAND          46..51
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           54..63
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           68..72
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   STRAND          73..82
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           84..94
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           100..102
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           104..127
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   STRAND          131..135
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           136..139
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           142..148
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   STRAND          155..164
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           178..181
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   STRAND          184..186
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           190..212
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           220..228
FT                   /evidence="ECO:0000244|PDB:1ZCH"
FT   HELIX           236..242
FT                   /evidence="ECO:0000244|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
//

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