NORW_ECOLU
ID NORW_ECOLU Reviewed; 377 AA.
AC B7N6U1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=ECUMN_3032;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928163; CAR14202.1; -; Genomic_DNA.
DR RefSeq; WP_000064692.1; NC_011751.1.
DR RefSeq; YP_002413724.1; NC_011751.1.
DR AlphaFoldDB; B7N6U1; -.
DR SMR; B7N6U1; -.
DR STRING; 585056.ECUMN_3032; -.
DR EnsemblBacteria; CAR14202; CAR14202; ECUMN_3032.
DR KEGG; eum:ECUMN_3032; -.
DR PATRIC; fig|585056.7.peg.3209; -.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; IHHFWTF; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000007097; 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_1000141171"
SQ SEQUENCE 377 AA; 41465 MW; 43F8941837757B18 CRC64;
MSNGIVIIGS GFAARQLVKN IRKQDACIPL TLIAADSMDE YNKPDLSHVI SQRQRADDLT
RQTAGEFAEQ FNLHLFPHTW IMDIDAEAHV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
LMLTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGILATL DRQRSIEVDA VIAATGLRPE
TALARRAGLT INRGVCVDSY LQTSNADIYA LGDCTEINGQ VLPFLQPIQL SAMVLAKNLL
GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWQINTE RQGMVARGVD DADQLRAFVV
SEDRMKEAFG LLKTLPV