ID G5NH42_SALET Unreviewed; 377 AA.
AC G5NH42;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Nitric oxide reductase FlRd-NAD(+) reductase {ECO:0000256|HAMAP-Rule:MF_01313};
DE EC=1.18.1.- {ECO:0000256|HAMAP-Rule:MF_01313};
DE AltName: Full=Flavorubredoxin reductase {ECO:0000256|HAMAP-Rule:MF_01313};
DE Short=FlRd-reductase {ECO:0000256|HAMAP-Rule:MF_01313};
DE Short=FlavoRb reductase {ECO:0000256|HAMAP-Rule:MF_01313};
GN Name=norW {ECO:0000256|HAMAP-Rule:MF_01313};
GN Synonyms=flrR {ECO:0000256|HAMAP-Rule:MF_01313};
GN ORFNames=LTSEINV_4237 {ECO:0000313|EMBL:EHC53409.1};
OS Salmonella enterica subsp. enterica serovar Inverness str. R8-3668.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913075 {ECO:0000313|EMBL:EHC53409.1, ECO:0000313|Proteomes:UP000003532};
RN [1] {ECO:0000313|EMBL:EHC53409.1, ECO:0000313|Proteomes:UP000003532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-3668 {ECO:0000313|EMBL:EHC53409.1,
RC ECO:0000313|Proteomes:UP000003532};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01313};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01313};
CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC {ECO:0000256|HAMAP-Rule:MF_01313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01313}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442, ECO:0000256|HAMAP-Rule:MF_01313}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC53409.1}.
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DR EMBL; AFCO01001398; EHC53409.1; -; Genomic_DNA.
DR AlphaFoldDB; G5NH42; -.
DR SMR; G5NH42; -.
DR PATRIC; fig|913075.3.peg.3288; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000003532; Unassembled WGS sequence.
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; 3.30.390.120; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18113; Rbx_binding; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01313};
KW FAD {ECO:0000256|HAMAP-Rule:MF_01313};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01313};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01313};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01313}.
FT DOMAIN 5..275
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 306..375
FT /note="Rubredoxin binding"
FT /evidence="ECO:0000259|Pfam:PF18113"
SQ SEQUENCE 377 AA; 41158 MW; 743F29BAE86BAE29 CRC64;
MSRGIIIIGS GFAARQLVKN IRKQDAHVPL TLIAADSMDE YNKPDLSHVI SQSQRADDLT
RQLAGEFAEQ FNLRLFPHTW VADIDADAHV VKSQDKQWQY DKLVLATGAT AFVPPIAGRE
LMLTLNSQQE YRACETQLRD AQRVLIVGGG LIGSELAMDF CRAGKTVTLM DNAASLLASL
MPPEVSSRLQ HHLTDMGVHL LLKSQLQKLE KTEAGIRATL VSQHSIEVDA VIAATGLRPE
TALARRAGVV VNRGVCVDSY LQTSHPDIYA IGDCAEINGQ VLPFLQPIQL SAMYLAKNLL
GGNAPLKLPA MLVKVKTPEL PLHLAGETQR RDLSWHITAE SDGMIAKGMS GEGQLRAFVV
SEDRMKEAFA LLKTLSV
//
