NORW_AERS4
ID NORW_AERS4 Reviewed; 388 AA.
AC A4STH3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=ASA_4271;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO92195.1; -; Genomic_DNA.
DR RefSeq; WP_005320623.1; NC_009348.1.
DR AlphaFoldDB; A4STH3; -.
DR SMR; A4STH3; -.
DR STRING; 382245.ASA_4271; -.
DR EnsemblBacteria; ABO92195; ABO92195; ASA_4271.
DR KEGG; asa:ASA_4271; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OMA; IHHFWTF; -.
DR OrthoDB; 1149616at2; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000000225; 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..388
FT /note="Nitric oxide reductase FlRd-NAD(+) reductase"
FT /id="PRO_0000305604"
SQ SEQUENCE 388 AA; 41077 MW; 3B94D4EAB5FD1013 CRC64;
MKAATLSEAG VSREILVIGS GFAAQQLVKS LRKLDAEQPI RLITADSGDE YNKPDLSHVV
SRGCTAAAMT RLSGSDFAEQ QRIALVPHCP VLGIDPARRI VMTVQGEFAY GQLVLATGAS
AARPDLPGSE QLVTLNSQQE YAAAEGPIQQ ARRILVLGAG LIGCELAMDM ASDGREVTLV
DLADSPLSAL LPAVLSQPLQ QALRSQGVSL QFGLGIARID AQPGDGWRVT LTDGRTSEQD
LVIAAIGLKP NLVLAQAAGL AVERGILVDD SLQTSAPHIF ALGDCAQWRG QLLPFLQPIV
LGANALARTL LGTPTPLTLP PMLVKVKTPR YPLQLAGRTK GEDLAWQCRW NSHGLVAEAR
AEDGELCGFV VGGDQMSAAF PLLRQLPR