(data stored in SCRATCH zone)

SWISSPROT: B2UI50_RALPJ

ID   B2UI50_RALPJ            Unreviewed;       208 AA.
AC   B2UI50;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.7.-.- {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN   OrderedLocusNames=Rpic_4152 {ECO:0000313|EMBL:ACD29251.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29251.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic
CC       azo compounds to the corresponding amines. Requires NADH, but not
CC       NADPH, as an electron donor for its activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01216, ECO:0000256|SAAS:SAAS00016147}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01216};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01216};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01216,
CC       ECO:0000256|SAAS:SAAS00016163}.
CC   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00540904}.
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DR   EMBL; CP001069; ACD29251.1; -; Genomic_DNA.
DR   RefSeq; WP_004627558.1; NC_010678.1.
DR   STRING; 402626.Rpic_4152; -.
DR   EnsemblBacteria; ACD29251; ACD29251; Rpic_4152.
DR   GeneID; 6285565; -.
DR   KEGG; rpi:Rpic_4152; -.
DR   PATRIC; fig|402626.5.peg.397; -.
DR   eggNOG; ENOG4108V3G; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; GAPFYNF; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_01216; Azoreductase_type1; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR023048; NADH-azoreductase_FMN-depdnt.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UI50.
DR   SWISS-2DPAGE; B2UI50.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01216,
KW   ECO:0000256|SAAS:SAAS00016150};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00016179};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00016149};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216,
KW   ECO:0000256|SAAS:SAAS00016167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN        1    200       Flavodoxin_2. {ECO:0000259|Pfam:PF02525}.
SQ   SEQUENCE   208 AA;  21961 MW;  C4599AC76A954662 CRC64;
     MQVLHIDSSI LGDASASRLL SAAIVDELRR ENPSATVVHR DLSVEAIPHL DGAIAAGFRA
     TGADDFDDAT RAEHARSETL VNELLASDVI VVGAPMYNFS VPSQLKAWID RVAQAGRTFK
     YTETGPVGLA GGKKVIVAST RGGMYSAGPA AAMDFQEAYL KTVFGFFGIT DVQFVRAERL
     AMGPDARAQA LEAAHAAMRD VVSQAVAA
//

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