NORW_SALPB
ID NORW_SALPB Reviewed; 377 AA.
AC A9N0E0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SPAB_03533;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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; CP000886; ABX68874.1; -; Genomic_DNA.
DR RefSeq; WP_000086341.1; NC_010102.1.
DR AlphaFoldDB; A9N0E0; -.
DR SMR; A9N0E0; -.
DR KEGG; spq:SPAB_03533; -.
DR PATRIC; fig|1016998.12.peg.3325; -.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; IHHFWTF; -.
DR BioCyc; SENT1016998:SPAB_RS14390-MON; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000008556; 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_1000086222"
SQ SEQUENCE 377 AA; 41174 MW; 9C5400DF795C6F00 CRC64;
MSRGIIIIGS GFAARQLVKN IRKQDAHVPL TLIAADSMDE YNKPDLSHVI SQSQRADDLT
RQLAGEFAEQ FNLRLFPHTW VADIDADAHV VKSQDKQWQY DKLVLATGAT AFVPPITGRE
LMLTLNSQQE YRACETQLRD AQRVLIIGGG LIGSELAMDF CRAGKTVTLM DNAASLLASL
MPPEVSSRLQ HHLTDMGVHL LLKSQLQKLE KTEAGIRATL VSQHSIEVDA VIAATGLRPE
TALARRAGVA VNRGVCVDSY LQTSHPDIYA IGDCAEINGQ VLPFLQPIQL SAMYLAKNLL
GGNAPLKLPA MLVKVKTPEL PLHLAGETQR RDLSWHITAE SDGMIAKGMS GEGQLRAFVV
SEDRMKEAFA LLKTLSV