ID   NORW_SALPK              Reviewed;         377 AA.
AC   B5BEP9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=SSPA2513;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR60749.1; -; Genomic_DNA.
DR   RefSeq; WP_000086345.1; NC_011147.1.
DR   AlphaFoldDB; B5BEP9; -.
DR   SMR; B5BEP9; -.
DR   KEGG; sek:SSPA2513; -.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000001869; 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_1000141183"
SQ   SEQUENCE   377 AA;  41148 MW;  8AEFA0D50FED869F CRC64;
     MSRGIIIIGS GFAARQLVKN IRKQDAHVPL TLIAADSMDE YNKPDLSHVI SQSQRADDLT
     RQLAGEFAEQ FNLRLFPHTW VTDIDADAHV VKSQDKQWQY DKLVLATGAA AFVPPIAGRE
     LMLTLNNQQE YRACETPLRD AQRVLIVGGG LIGSELAMDF CRAGKTVTLM DNAASLLASL
     MPPEVSSRLQ HHLTDMGVHL LLKSQLQKLE KIEAGIRATL ASQRSIEVDA VIAATGLRPE
     TALARRAGVV VNRGVCVDSY LQTSHPDIYA IGDCAEINGQ VLPFLQPIQL SAMYLAKNLL
     GGNAPLKLPA MLVKVKTPEL PLHLAGETQR RDLSWQITAE SDGMIAKGMS GEGQLRAFVV
     SEDRMKEAFA LLKTLSV