ID   NORW_SERP5              Reviewed;         379 AA.
AC   A8GG95;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Spro_3034;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV42135.1; -; Genomic_DNA.
DR   RefSeq; WP_012145756.1; NC_009832.1.
DR   AlphaFoldDB; A8GG95; -.
DR   SMR; A8GG95; -.
DR   STRING; 399741.Spro_3034; -.
DR   EnsemblBacteria; ABV42135; ABV42135; Spro_3034.
DR   KEGG; spe:Spro_3034; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OMA; IHHFWTF; -.
DR   OrthoDB; 1149616at2; -.
DR   UniPathway; UPA00638; -.
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..379
FT                   /note="Nitric oxide reductase FlRd-NAD(+) reductase"
FT                   /id="PRO_0000341316"
SQ   SEQUENCE   379 AA;  41401 MW;  A7EE0544EB63BC60 CRC64;
     MNPGILIVGS GFAARQLVKN LRRQDGEVPI RLIAADSCDE YNKPELSHVF SLNQTADALT
     RQSFGDFAEQ FQLTVHPHTR ITAIDTQQKM VRSGEQVWHY DKLVLAIGAA AMVPQVPGHE
     LMLTLNSQQE FRDSQLTLLQ AQRVLILGGG LIGCELAMDM CRAGKQVTLV DRSGSLLSGL
     MPVEASCRLQ HALQQMGVEL LLNQQLGALT QHDEGIQATL SNGRQLWVDA AIASVGLRPN
     VGLARQAGLQ INRGIQVNNR LQTSQVDVYA LGDCAEIEGQ LLPFLQPIQF SAMTLAKNLL
     GAAEAVKLPA MLVKVKTPSL PLQLAGETRR QDLSWTIVAE PQGMIAKGFD QHQQLRAFIV
     SEDHMKLAFG LLKELNALT