ID   NORW_ECODH              Reviewed;         377 AA.
AC   B1XCN8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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; OrderedLocusNames=ECDH10B_2879;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
RN   [2]
RP   FUNCTION.
RX   PubMed=12142437; DOI=10.1128/jb.184.16.4640-4643.2002;
RA   Hutchings M.I., Mandhana N., Spiro S.;
RT   "The NorR protein of Escherichia coli activates expression of the
RT   flavorubredoxin gene norV in response to reactive nitrogen species.";
RL   J. Bacteriol. 184:4640-4643(2002).
CC   -!- FUNCTION: One of at least two accessory proteins for anaerobic nitric
CC       oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:12142437}.
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:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000948; ACB03829.1; -; Genomic_DNA.
DR   RefSeq; WP_000064752.1; NC_010473.1.
DR   AlphaFoldDB; B1XCN8; -.
DR   SMR; B1XCN8; -.
DR   KEGG; ecd:ECDH10B_2879; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   BioCyc; ECOL316385:ECDH10B_RS14620-MON; -.
DR   UniPathway; UPA00638; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016731; F:oxidoreductase activity, acting on iron-sulfur proteins as donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..377
FT                   /note="Nitric oxide reductase FlRd-NAD(+) reductase"
FT                   /id="PRO_0000341314"
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