NFRA1_BACSU
ID NFRA1_BACSU Reviewed; 249 AA.
AC P39605;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=FMN reductase (NADPH);
DE EC=1.5.1.38 {ECO:0000269|PubMed:9836433};
DE AltName: Full=NADPH-dependent FMN reductase;
DE AltName: Full=NADPH-dependent nitro/flavin reductase;
DE AltName: Full=NADPH-dependent nitroreductase;
DE AltName: Full=NADPH-dependent oxidoreductase;
GN Name=nfrA1; Synonyms=nfrA, ywcG; OrderedLocusNames=BSU38110;
GN ORFNames=ipa-43d;
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=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP REACTION MECHANISM, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=9836433; DOI=10.1271/bbb.62.1978;
RA Zenno S., Kobori T., Tanokura M., Saigo K.;
RT "Purification and characterization of NfrA1, a Bacillus subtilis
RT nitro/flavin reductase capable of interacting with the bacterial
RT luciferase.";
RL Biosci. Biotechnol. Biochem. 62:1978-1987(1998).
CC -!- FUNCTION: Reduces FMNH(2) to FMN, with NADPH as reductant. It also
CC reduces nitroaromatic compounds, quinones and azo dyes.
CC {ECO:0000269|PubMed:9836433}.
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=1.5.1.38;
CC Evidence={ECO:0000269|PubMed:9836433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.85 uM for NADPH (with nitrofurazone at pH 7 and at 23 degrees
CC Celsius) {ECO:0000269|PubMed:9836433};
CC KM=3.9 uM for NADPH (with FMN at pH 7 and at 23 degrees Celsius)
CC {ECO:0000269|PubMed:9836433};
CC KM=4.7 uM for FMN (with NADPH at pH 7 and at 23 degrees Celsius)
CC {ECO:0000269|PubMed:9836433};
CC KM=16.3 uM for nitrofurazone (with NADPH at pH 7 and at 23 degrees
CC Celsius) {ECO:0000269|PubMed:9836433};
CC Vmax=9 umol/min/mg enzyme with FMN as substrate (with NADPH at pH 7
CC and at 23 degrees Celsius) {ECO:0000269|PubMed:9836433};
CC Vmax=97 umol/min/mg enzyme with nitrofurazone as substrate (with
CC NADPH at pH 7 and at 23 degrees Celsius)
CC {ECO:0000269|PubMed:9836433};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:9836433}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism. NADPH is more effective as an electron donor than
CC NADH.
CC -!- SIMILARITY: Belongs to the flavin oxidoreductase frp family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51599.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15837.1; -; Genomic_DNA.
DR PIR; S39698; S39698.
DR RefSeq; NP_391690.1; NC_000964.3.
DR RefSeq; WP_003244098.1; NZ_JNCM01000034.1.
DR PDB; 3N2S; X-ray; 1.95 A; A/B/C/D=1-249.
DR PDBsum; 3N2S; -.
DR AlphaFoldDB; P39605; -.
DR SMR; P39605; -.
DR MINT; P39605; -.
DR STRING; 224308.BSU38110; -.
DR jPOST; P39605; -.
DR PaxDb; P39605; -.
DR PRIDE; P39605; -.
DR EnsemblBacteria; CAB15837; CAB15837; BSU_38110.
DR GeneID; 937279; -.
DR KEGG; bsu:BSU38110; -.
DR PATRIC; fig|224308.179.peg.4125; -.
DR eggNOG; COG0778; Bacteria.
DR InParanoid; P39605; -.
DR OMA; GMCLGYP; -.
DR PhylomeDB; P39605; -.
DR BioCyc; BSUB:BSU38110-MON; -.
DR SABIO-RK; P39605; -.
DR EvolutionaryTrace; P39605; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0052873; F:FMN reductase (NADPH) activity; IEA:UniProtKB-EC.
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; Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..249
FT /note="FMN reductase (NADPH)"
FT /id="PRO_0000205512"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 104..127
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 191..213
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:3N2S"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3N2S"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:3N2S"
SQ SEQUENCE 249 AA; 28320 MW; A36FDAECEC3692CF CRC64;
MNNTIETILN HRSIRSFTDQ LLTAEEIDTL VKSAQAASTS SYVQAYSIIG VSDPEKKREL
SVLAGNQPYV EKNGHFFVFC ADLYRHQQLA EEKGEHISEL LENTEMFMVS LIDAALAAQN
MSIAAESMGL GICYIGGIRN ELDKVTEVLQ TPDHVLPLFG LAVGHPANLS GKKPRLPKQA
VYHENTYNVN TDDFRHTMNT YDKTISDYYR ERTNGKREET WSDQILNFMK QKPRTYLNDY
VKEKGFNKN
