ID   NORW_ECO7I              Reviewed;         377 AA.
AC   B7NSJ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Nitric oxide reductase FlRd-NAD(+) reductase {ECO:0000255|HAMAP-Rule:MF_01313};
DE            EC=1.18.1.- {ECO:0000255|HAMAP-Rule:MF_01313};
DE   AltName: Full=Flavorubredoxin reductase {ECO:0000255|HAMAP-Rule:MF_01313};
DE            Short=FlRd-reductase {ECO:0000255|HAMAP-Rule:MF_01313};
DE            Short=FlavoRb reductase {ECO:0000255|HAMAP-Rule:MF_01313};
GN   Name=norW {ECO:0000255|HAMAP-Rule:MF_01313};
GN   Synonyms=flrR {ECO:0000255|HAMAP-Rule:MF_01313};
GN   OrderedLocusNames=ECIAI39_2897;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: One of at least two accessory proteins for anaerobic nitric
CC       oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
CC       {ECO:0000255|HAMAP-Rule:MF_01313}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01313};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01313};
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC       {ECO:0000255|HAMAP-Rule:MF_01313}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01313}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01313}.
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DR   EMBL; CU928164; CAR19018.1; -; Genomic_DNA.
DR   RefSeq; WP_000071561.1; NC_011750.1.
DR   RefSeq; YP_002408830.1; NC_011750.1.
DR   AlphaFoldDB; B7NSJ1; -.
DR   SMR; B7NSJ1; -.
DR   STRING; 585057.ECIAI39_2897; -.
DR   EnsemblBacteria; CAR19018; CAR19018; ECIAI39_2897.
DR   KEGG; ect:ECIAI39_2897; -.
DR   PATRIC; fig|585057.6.peg.3005; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000749; Chromosome.
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_1000141169"
SQ   SEQUENCE   377 AA;  41385 MW;  573E94AE2E2FD67E CRC64;
     MSNSIVIIGS GFAARQLVKN IRKQDASIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
     RQTAGEFAEQ FNLRLFPHTW VTDIDAEAHV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
     LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGIELAMDF CRAGKAVTLI DNAASILASL
     MLPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGILATL DRQRSIEVDA VIAATGLRPE
     TALARRAGLT INRGVCVDSY LQTSNADIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
     GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DGDQLRAFVV
     SEDRMKEAFG LLKTLPM