(data stored in ACNUC7421 zone)

SWISSPROT: NORW_AERHH

ID   NORW_AERHH              Reviewed;         388 AA.
AC   A0KEJ2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=AHA_0120;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: One of at least two accessory proteins for anaerobic
CC       nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO
CC       reductase. {ECO:0000255|HAMAP-Rule:MF_01313}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [nitric oxide reductase
CC         rubredoxin domain] = NADH + 2 oxidized [nitric oxide reductase
CC         rubredoxin domain]; Xref=Rhea:RHEA:42960, Rhea:RHEA-COMP:10304,
CC         Rhea:RHEA-COMP:10305, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; CP000462; ABK37047.1; -; Genomic_DNA.
DR   RefSeq; WP_011704148.1; NC_008570.1.
DR   RefSeq; YP_854651.1; NC_008570.1.
DR   SMR; A0KEJ2; -.
DR   STRING; 380703.AHA_0120; -.
DR   EnsemblBacteria; ABK37047; ABK37047; AHA_0120.
DR   GeneID; 4487500; -.
DR   KEGG; aha:AHA_0120; -.
DR   PATRIC; fig|380703.7.peg.113; -.
DR   eggNOG; ENOG4108EQM; Bacteria.
DR   eggNOG; COG0446; LUCA.
DR   HOGENOM; HOG000009393; -.
DR   KO; K12265; -.
DR   OMA; ALMYVYM; -.
DR   BioCyc; AHYD380703:G1G7B-120-MONOMER; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000756; 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;
DR   PRODOM; A0KEJ2.
DR   SWISS-2DPAGE; A0KEJ2.
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    388       Nitric oxide reductase FlRd-NAD(+)
FT                                reductase.
FT                                /FTId=PRO_0000305603.
SQ   SEQUENCE   388 AA;  41275 MW;  B1B517A163DFC56F CRC64;
     MSTTTQSDAG ISREIVVIGS GFAAQQLVKS LRKLDAEQPI RLITADSGDE YNKPDLSHVV
     SRGCAAAAMT RQSGSDFAEQ QRIALLPHCP VLGIDPVRRL VLTEQGEFPY GQLVLATGAS
     AVRPELPGSE HLVTLNSQQE YAAVEGAIQQ ARRILVLGAG LIGCELAMDM ASDGREVTLL
     DLADSPLSAL LPATLTQPLQ QALRSQGVSL QFGTGLARID GQPGDGWRVT LTDGRTSEQD
     LVIAAIGLRP NLALARGAGL AVERGILVGD RLQTSDPHIF ALGDCVQWQG QLLPFLQPIV
     LGANALARTL LGTPTPLALP PMLVKVKTPR YPLQLAGRTQ GEDLAWQCRW NSHGMVAEAR
     DQAGELCGFV VGGDQMSAAF PLLRQLPR
//

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