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NORW_ECOSE
ID   NORW_ECOSE              Reviewed;         377 AA.
AC   B6I697;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=ECSE_2959;
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11;
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA   Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL   DNA Res. 15:375-386(2008).
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; AP009240; BAG78483.1; -; Genomic_DNA.
DR   RefSeq; WP_000064758.1; NC_011415.1.
DR   AlphaFoldDB; B6I697; -.
DR   SMR; B6I697; -.
DR   PRIDE; B6I697; -.
DR   EnsemblBacteria; BAG78483; BAG78483; ECSE_2959.
DR   KEGG; ecy:ECSE_2959; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000008199; 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_1000141172"
SQ   SEQUENCE   377 AA;  41319 MW;  E206768E04E36682 CRC64;
     MSNGIVIIGS GFAARQLVKN IRKQDATIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
     RQTAGEFAEQ FNLRLFPHTW VTDIDAEARV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
     LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
     MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGILATL DRQRSIEVDA VIAATGLRPE
     TALARRAGLT INRGVCVDSY LQTRNADIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
     GNNTPLKLPA MLVKIKTPEL PLHLAGETQR RDLRWQICTE SQGMVARGVD GADQLRAFVV
     SEDRMKEAFG LLKTLPM
 
 
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