NORW_ECOL5
ID NORW_ECOL5 Reviewed; 377 AA.
AC Q0TEG9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=ECP_2671;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG70660.1; -; Genomic_DNA.
DR RefSeq; WP_000064709.1; NC_008253.1.
DR AlphaFoldDB; Q0TEG9; -.
DR SMR; Q0TEG9; -.
DR STRING; 362663.ECP_2671; -.
DR EnsemblBacteria; ABG70660; ABG70660; ECP_2671.
DR KEGG; ecp:ECP_2671; -.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; IHHFWTF; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000009182; 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_0000305608"
SQ SEQUENCE 377 AA; 41373 MW; 6A2BC2F0E9B274EE CRC64;
MSNGIVIIGS GFAARQLVKN IRKQDASIPL TLIAADSMDE YNKPDLSHVI SQGQRADDLT
RQTAGEFAEQ FNLRLFPHTW VTDIDAEAHV VKSQNNQWQY DKLVLATGAS AFVPPVPGRE
LILTLNSQQE YRACETQLRD ARRVLIVGGG LIGSELAMDF CRAGKAVTLI DNAASILASL
MPPEVSSRLQ HRLTEMGVHL LLKSQLQGLE KTDSGILATL DRQRCIEVDA VIAATGLRPE
TALARRAGLT INRGVCVDSY LQTSNADIYA LGDCAEINGQ VLPFLQPIQL SAMVLAKNLL
GNNTPLKLPA MLVKIKTPEL PLHLAGETQR QDLRWHIYTE RQGMVARGVD DADQLRAFVV
SEDRMKEAFG LLKTLSM