NORW_SHIB3
ID NORW_SHIB3 Reviewed; 377 AA.
AC B2U036;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-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=SbBS512_E3166;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) 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; CP001063; ACD08329.1; -; Genomic_DNA.
DR RefSeq; WP_000064747.1; NC_010658.1.
DR AlphaFoldDB; B2U036; -.
DR SMR; B2U036; -.
DR STRING; 344609.SbBS512_E3166; -.
DR EnsemblBacteria; ACD08329; ACD08329; SbBS512_E3166.
DR KEGG; sbc:SbBS512_E3166; -.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; IHHFWTF; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000001030; 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_1000141185"
SQ SEQUENCE 377 AA; 41447 MW; CDF69DCEFCA46263 CRC64;
MSNGIVIIGS GFAARQLVKN IRKQDATIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
RQTAGEFAEQ FNLHLFPQTW VTDIDAEARV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGILATL DHQRSIEVDA VIAATGLRPE
TALARRAGLT INRGVCVDSY LQTSNDDIYA LGDYAEINGQ VLPFLQPIQL SAMVLAKNLL
GNNTPLKLPT MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DADQLRAFVV
SEDRMKEAFG LLKTLPM
