ID   NORW_ECOLI              Reviewed;         377 AA.
AC   P37596; Q2MAB8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Nitric oxide reductase FlRd-NAD(+) reductase;
DE            EC=1.18.1.-;
DE   AltName: Full=Flavorubredoxin reductase;
DE            Short=FlRd-reductase;
DE            Short=FlavoRb reductase;
GN   Name=norW; Synonyms=flrR, ygbD; OrderedLocusNames=b2711, JW2681;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Yano K., Ikebukuro K., Takada Y., Tomiyama M., Karube I.;
RT   "Sequencing and characterization of the downstream region of hydA in
RT   Escherichia coli.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 143-377.
RC   STRAIN=K12;
RA   Ikebukuro K., Nishio M., Yano K., Tomiyama M., Tamiya E., Karube I.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
RN   [6]
RP   PROTEIN SEQUENCE OF N-TERMINUS, AND CHARACTERIZATION.
RX   PubMed=11123953; DOI=10.1021/bi001844y;
RA   Gomes C.M., Vicente J.B., Wasserfallen A., Teixeira M.;
RT   "Spectroscopic studies and characterization of a novel electron-transfer
RT   chain from Escherichia coli involving a flavorubredoxin and its
RT   flavoprotein reductase partner.";
RL   Biochemistry 39:16230-16237(2000).
RN   [7]
RP   IDENTIFICATION OF FUNCTION.
RC   STRAIN=K12 / AB1157;
RX   PubMed=11751865; DOI=10.1074/jbc.m110471200;
RA   Gardner A.M., Helmick R.A., Gardner P.R.;
RT   "Flavorubredoxin, an inducible catalyst for nitric oxide reduction and
RT   detoxification in Escherichia coli.";
RL   J. Biol. Chem. 277:8172-8177(2002).
RN   [8]
RP   IDENTIFICATION OF FUNCTION.
RX   PubMed=12101220; DOI=10.1074/jbc.m203886200;
RA   Gomes C.M., Giuffre A., Forte E., Vicente J.B., Saraiva L.M., Brunori M.,
RA   Teixeira M.;
RT   "A novel type of nitric-oxide reductase. Escherichia coli
RT   flavorubredoxin.";
RL   J. Biol. Chem. 277:25273-25276(2002).
RN   [9]
RP   REGULATION OF EXPRESSION; ANAEROBIC AND NO INDUCED EXPRESSION, AND
RP   REQUIREMENT FOR SIGMA 54.
RC   STRAIN=K12 / AB1157;
RX   PubMed=12529359; DOI=10.1074/jbc.m212462200;
RA   Gardner A.M., Gessner C.R., Gardner P.R.;
RT   "Regulation of the nitric oxide reduction operon (norRVW) in Escherichia
RT   coli: role of NorR and sigma 54 in the nitric oxide stress response.";
RL   J. Biol. Chem. 278:10081-10086(2003).
CC   -!- FUNCTION: One of at least two accessory proteins for anaerobic nitric
CC       oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [nitric oxide reductase rubredoxin
CC         domain] = NADH + 2 oxidized [nitric oxide reductase rubredoxin
CC         domain]; Xref=Rhea:RHEA:42960, Rhea:RHEA-COMP:10304, Rhea:RHEA-
CC         COMP:10305, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Submicromolar concentrations of NO induce anaerobic
CC       expression. Repressed by oxygen in the presence of NO.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D28595; BAA05934.1; -; Genomic_DNA.
DR   EMBL; U29579; AAA69221.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75753.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76788.1; -; Genomic_DNA.
DR   EMBL; D14422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C65051; C65051.
DR   RefSeq; NP_417191.1; NC_000913.3.
DR   RefSeq; WP_000064752.1; NZ_STEB01000027.1.
DR   AlphaFoldDB; P37596; -.
DR   SMR; P37596; -.
DR   BioGRID; 4259424; 14.
DR   STRING; 511145.b2711; -.
DR   PaxDb; P37596; -.
DR   PRIDE; P37596; -.
DR   EnsemblBacteria; AAC75753; AAC75753; b2711.
DR   EnsemblBacteria; BAE76788; BAE76788; BAE76788.
DR   GeneID; 947088; -.
DR   KEGG; ecj:JW2681; -.
DR   KEGG; eco:b2711; -.
DR   PATRIC; fig|1411691.4.peg.4031; -.
DR   EchoBASE; EB2344; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   InParanoid; P37596; -.
DR   OMA; IHHFWTF; -.
DR   PhylomeDB; P37596; -.
DR   BioCyc; EcoCyc:EG12450-MON; -.
DR   BioCyc; MetaCyc:EG12450-MON; -.
DR   UniPathway; UPA00638; -.
DR   PRO; PR:P37596; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc.
DR   GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR   GO; GO:0015044; F:rubredoxin-NAD+ reductase activity; IDA:EcoCyc.
DR   GO; GO:0071732; P:cellular response to nitric oxide; IEP:EcoCyc.
DR   GO; GO:0046210; P:nitric oxide catabolic process; IMP:EcoCyc.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01313; NorW; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR023961; NO_rdtase_NorW.
DR   InterPro; IPR041364; Rbx-bd.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18113; Rbx_binding; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..377
FT                   /note="Nitric oxide reductase FlRd-NAD(+) reductase"
FT                   /id="PRO_0000167662"
FT   CONFLICT        264
FT                   /note="S -> N (in Ref. 1 and 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  41404 MW;  DDE49A55B99E268B CRC64;
     MSNGIVIIGS GFAARQLVKN IRKQDATIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
     RQTAGEFAEQ FNLHLFPQTW VTDIDAEARV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
     LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
     MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGIQATL DRQRNIEVDA VIAATGLRPE
     TALARRAGLT INRGVCVDSY LQTSNTDIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
     GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DADQLRAFVV
     SEDRMKEAFG LLKTLPM