ID   NORW_ECO27              Reviewed;         377 AA.
AC   B7UHC3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=E2348C_2968;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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; FM180568; CAS10516.1; -; Genomic_DNA.
DR   RefSeq; WP_000064719.1; NC_011601.1.
DR   AlphaFoldDB; B7UHC3; -.
DR   SMR; B7UHC3; -.
DR   EnsemblBacteria; CAS10516; CAS10516; E2348C_2968.
DR   KEGG; ecg:E2348C_2968; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000008205; 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_1000165583"
SQ   SEQUENCE   377 AA;  41406 MW;  90AA456987C71265 CRC64;
     MSNGIVIIGS GFAARQLVKN IRKQDASIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
     RQTAGEFAEQ FNLRLFPHTW VTDIDAEAHV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
     LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKMVTLI DNAASILASL
     MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTNSGILATL DRQRSIEVDT VIAATGLRPE
     TALARRAGLT INRGVCVDSY LQTSNADIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
     GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DADQLRAFVV
     SEDRMKEAFG LLKTLSM