ID   NORW_SHIBS              Reviewed;         377 AA.
AC   Q31X75;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   25-MAY-2022, entry version 86.
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=SBO_2807;
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB67333.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000036; ABB67333.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q31X75; -.
DR   SMR; Q31X75; -.
DR   EnsemblBacteria; ABB67333; ABB67333; SBO_2807.
DR   KEGG; sbo:SBO_2807; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000007067; 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_0000305610"
SQ   SEQUENCE   377 AA;  41473 MW;  9DE791659DB56EC8 CRC64;
     MSNGIVIIGS GFAARQLVKN IRKQDATIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
     RQTAGEFAEQ FNLHLFPQTW VTDIDAEARV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
     LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
     MPPEVSSRLQ HRLTEMGVYL LLKSQLQGLE KTDSGILATL DHQRSIEVDA VIAATGLRPE
     TALARRAGLT INRGVCVDSY LQTSNDDIYA LGDYAEINGQ VLPFLQPIQL SAMVLAKNLL
     GNNTPLKLPT MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DADQLRAFVV
     SEDRMKEAFG LLKTLPM