(data stored in ACNUC7421 zone)

SWISSPROT: B2UHL2_RALPJ

ID   B2UHL2_RALPJ            Unreviewed;       208 AA.
AC   B2UHL2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
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_3958 {ECO:0000313|EMBL:ACD29063.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29063.1, 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; ACD29063.1; -; Genomic_DNA.
DR   RefSeq; WP_012430088.1; NC_010678.1.
DR   STRING; 402626.Rpic_3958; -.
DR   EnsemblBacteria; ACD29063; ACD29063; Rpic_3958.
DR   GeneID; 6285195; -.
DR   KEGG; rpi:Rpic_3958; -.
DR   PATRIC; fig|402626.5.peg.197; -.
DR   eggNOG; ENOG4105FYA; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; IGTPMNN; -.
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; B2UHL2.
DR   SWISS-2DPAGE; B2UHL2.
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        3    199       Flavodoxin_2. {ECO:0000259|Pfam:PF02525}.
SQ   SEQUENCE   208 AA;  22457 MW;  8AF9712059975BAC CRC64;
     MTTLLHVTVS PRDDRSHSRR GAKWVVAQLA EAVGGLRVIE RDLAATPLPH PDAGFVEASL
     TPDADRTAAH RAALALSETL IGELGAADAV LISTPVHNYT VPSALKAWID LVVRPERTFR
     RTPTGKVGML TDRSVLVVSA SGGHFDGAHA QTDFLMPYLR YVFATVGIHQ VEGIRLQNTA
     RGADSAMQAF ESFRQELAAR MLLMPLVA
//

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