MHQN_BACSU
ID MHQN_BACSU Reviewed; 206 AA.
AC P96692;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative NAD(P)H nitroreductase MhqN;
DE EC=1.-.-.-;
GN Name=mhqN; Synonyms=ydfN; OrderedLocusNames=BSU05480;
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;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=17725564; DOI=10.1111/j.1365-2958.2007.05891.x;
RA Toewe S., Leelakriangsak M., Kobayashi K., Van Duy N., Hecker M., Zuber P.,
RA Antelmann H.;
RT "The MarR-type repressor MhqR (YkvE) regulates multiple
RT dioxygenases/glyoxalases and an azoreductase which confer resistance to 2-
RT methylhydroquinone and catechol in Bacillus subtilis.";
RL Mol. Microbiol. 66:40-54(2007).
RN [4]
RP INDUCTION, IDENTIFICATION OF THE YDFNOP OPERON, SUBCELLULAR LOCATION, AND
RP NOMENCLATURE.
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 (1.65 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of putative nitroreductase ydfN (2632848) from Bacillus
RT subtilis at 1.65 A resolution.";
RL Submitted (DEC-2007) to the PDB data bank.
CC -!- FUNCTION: Putative nitroreductase that may contribute to the
CC degradation of aromatic compounds. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17407181,
CC ECO:0000269|PubMed:17725564}.
CC -!- INDUCTION: Repressed by MhqR. Strongly induced by stress due to
CC exposure to 2-methylhydroquinone (2-MHQ) and less strongly induced
CC after diamide or catechol stress. Not induced by oxidative stress due
CC to hydrogen peroxide or methylglyoxal. {ECO:0000269|PubMed:17407181,
CC ECO:0000269|PubMed:17725564}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB001488; BAA19382.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12355.1; -; Genomic_DNA.
DR PIR; D69781; D69781.
DR RefSeq; NP_388429.1; NC_000964.3.
DR RefSeq; WP_003244392.1; NZ_JNCM01000031.1.
DR PDB; 3BEM; X-ray; 1.65 A; A/B=1-206.
DR PDBsum; 3BEM; -.
DR AlphaFoldDB; P96692; -.
DR SMR; P96692; -.
DR STRING; 224308.BSU05480; -.
DR PaxDb; P96692; -.
DR PRIDE; P96692; -.
DR EnsemblBacteria; CAB12355; CAB12355; BSU_05480.
DR GeneID; 939899; -.
DR KEGG; bsu:BSU05480; -.
DR PATRIC; fig|224308.179.peg.588; -.
DR eggNOG; COG0778; Bacteria.
DR InParanoid; P96692; -.
DR OMA; AFNLQHT; -.
DR PhylomeDB; P96692; -.
DR BioCyc; BSUB:BSU05480-MON; -.
DR EvolutionaryTrace; P96692; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..206
FT /note="Putative NAD(P)H nitroreductase MhqN"
FT /id="PRO_0000072717"
FT BINDING 11..13
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 68..70
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 157..158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 193
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 196
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.5"
FT HELIX 1..10
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3BEM"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:3BEM"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3BEM"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 105..122
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 124..148
FT /evidence="ECO:0007829|PDB:3BEM"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3BEM"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3BEM"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3BEM"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3BEM"
SQ SEQUENCE 206 AA; 23559 MW; 99BFE7FDBD9075FC CRC64;
MAEFTHLVNE RRSASNFLSG HPITKEDLNE MFELVALAPS AFNLQHTKYV TVLDQDVKEK
LKQAANGQYK VVSSSAVLLV LGDKQAYQQA ADIYEGLKVL GILNKQEYDH MVQDTVSFYE
NRGEQFKRDE AIRNASLSAM MFMLSAKEKG WDTCPMIGFD AEAVKRILNI DDQFEVVMMI
TIGKEKTESR RPRGYRKPVN EFVEYM
