CHRR_SHIFL
ID CHRR_SHIFL Reviewed; 188 AA.
AC P0AGE8; P31465;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Quinone reductase {ECO:0000250|UniProtKB:P0AGE6};
DE EC=1.6.5.2 {ECO:0000250|UniProtKB:P0AGE6};
DE AltName: Full=Chromate reductase {ECO:0000250|UniProtKB:P0AGE6};
DE Short=CHRR {ECO:0000250|UniProtKB:P0AGE6};
DE EC=1.6.-.- {ECO:0000250|UniProtKB:P0AGE6};
DE AltName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000250|UniProtKB:P0AGE6};
GN Name=chrR; Synonyms=yieF; OrderedLocusNames=SF3747, S4025;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the reduction of quinones. Acts by simultaneous
CC two-electron transfer, avoiding formation of highly reactive
CC semiquinone intermediates and producing quinols that promote tolerance
CC of H(2)O(2). Quinone reduction is probably the primary biological role
CC of ChrR. Can also reduce toxic chromate to insoluble and less toxic
CC Cr(3+). Catalyzes the transfer of three electrons to Cr(6+) producing
CC Cr(3+) and one electron to molecular oxygen without producing the toxic
CC Cr(5+) species and only producing a minimal amount of reactive oxygen
CC species (ROS). Chromate reduction protects the cell against chromate
CC toxicity, but is likely a secondary activity.
CC {ECO:0000250|UniProtKB:P0AGE6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cr(6+) + 2 NADH + O2 = Cr(3+) + 2 H(+) + 2 NAD(+) +
CC superoxide; Xref=Rhea:RHEA:44372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18421, ChEBI:CHEBI:33007,
CC ChEBI:CHEBI:49544, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cr(6+) + 2 NADPH + O2 = Cr(3+) + 2 H(+) + 2 NADP(+) +
CC superoxide; Xref=Rhea:RHEA:44368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18421, ChEBI:CHEBI:33007,
CC ChEBI:CHEBI:49544, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P0AGE6};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P0AGE6};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. The tetrameric configuration
CC has a central role in chromate reductase activity.
CC {ECO:0000250|UniProtKB:P0AGE6}.
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
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DR EMBL; AE005674; AAN45191.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19006.1; -; Genomic_DNA.
DR RefSeq; NP_709484.1; NC_004337.2.
DR RefSeq; WP_001291268.1; NZ_WPGW01000226.1.
DR AlphaFoldDB; P0AGE8; -.
DR SMR; P0AGE8; -.
DR STRING; 198214.SF3747; -.
DR EnsemblBacteria; AAN45191; AAN45191; SF3747.
DR EnsemblBacteria; AAP19006; AAP19006; S4025.
DR GeneID; 1026147; -.
DR GeneID; 58391852; -.
DR KEGG; sfl:SF3747; -.
DR KEGG; sfx:S4025; -.
DR PATRIC; fig|198214.7.peg.4423; -.
DR HOGENOM; CLU_055322_4_2_6; -.
DR OMA; YGGVWAQ; -.
DR OrthoDB; 1818437at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..188
FT /note="Quinone reductase"
FT /id="PRO_0000160598"
FT BINDING 13..20
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT BINDING 82..85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AGE6"
SQ SEQUENCE 188 AA; 20376 MW; 78E163CC4826905D CRC64;
MSEKLQVVTL LGSLRKGSFN GMVARTLPKI APASMEVNAL PSIADIPLYD ADVQQEEGFP
ATVEALAEQI RQADGVVIVT PEYNYSVPGG LKNAIDWLSR LPDQPLAGKP VLIQTSSMGV
IGGARCQYHL RQILVFLDAM VMNKPEFMGG VIQNKVDPQT GEVIDQGTLD HLTGQLTAFG
EFIQRVKI
