YODC_BACSU
ID YODC_BACSU Reviewed; 202 AA.
AC P81102; Q9R9J6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative NAD(P)H nitroreductase YodC;
DE EC=1.-.-.-;
GN Name=yodC; Synonyms=yolG; OrderedLocusNames=BSU19550;
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 Ghim S.-Y., Jeong Y.-M., Choi S.-K., Park S.-H.;
RT "Sequence analysis of the 30 kb region (182') of the Bacillus subtilis
RT chromosome containing the cge cluster.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 PROTEIN SEQUENCE OF 2-24.
RC STRAIN=168 / JH642;
RA Graumann P.L., Schmid R., Marahiel M.A.;
RL Submitted (OCT-1997) to UniProtKB.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17407181}.
CC -!- INDUCTION: Repressed by YodB. Strongly induced by stress due to
CC exposure to catechol and less strongly induced after diamide or 2-
CC methylhydroquinone (2-MHQ) stress. Not induced by oxidative stress due
CC to hydrogen peroxide or methylglyoxal. {ECO:0000269|PubMed:17407181}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; AF006665; AAB81173.1; -; Genomic_DNA.
DR EMBL; AF015775; AAB72053.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13846.1; -; Genomic_DNA.
DR PIR; H69902; H69902.
DR RefSeq; NP_389836.1; NC_000964.3.
DR RefSeq; WP_003231196.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P81102; -.
DR SMR; P81102; -.
DR STRING; 224308.BSU19550; -.
DR jPOST; P81102; -.
DR PaxDb; P81102; -.
DR PRIDE; P81102; -.
DR EnsemblBacteria; CAB13846; CAB13846; BSU_19550.
DR GeneID; 939506; -.
DR KEGG; bsu:BSU19550; -.
DR PATRIC; fig|224308.179.peg.2137; -.
DR eggNOG; COG0778; Bacteria.
DR InParanoid; P81102; -.
DR OMA; HLQNWRF; -.
DR PhylomeDB; P81102; -.
DR BioCyc; BSUB:BSU19550-MON; -.
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 Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification;
KW Direct protein sequencing; Flavoprotein; FMN; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..202
FT /note="Putative NAD(P)H nitroreductase YodC"
FT /id="PRO_0000072716"
FT BINDING 11..13
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 68..70
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT CONFLICT 139..140
FT /note="QL -> HV (in Ref. 1; AAB81173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22340 MW; A148E201BA118445 CRC64;
MTNTLDVLKA RASVKEYDTN APISKEELTE LLDLATKAPS AWNLQHWHFT VFHSDESKAE
LLPVAYNQKQ IVESSAVVAI LGDLKANENG EEVYAELASQ GYITDEIKQT LLGQINGAYQ
SEQFARDSAF LNASLAAMQL MIAAKAKGYD TCAIGGFNKE QFQKQFDISE RYVPVMLISI
GKAVKPAHQS NRLPLSKVST WL
