(data stored in ACNUC7421 zone)

SWISSPROT: AZOR_RUEPO

ID   AZOR_RUEPO              Reviewed;         204 AA.
AC   Q5LXG9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216};
GN   OrderedLocusNames=SPO0383;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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:0000255|HAMAP-
CC       Rule:MF_01216}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2
CC         NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2
CC         NADH; Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15783, ChEBI:CHEBI:16567, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:71579; EC=1.7.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01216};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01216};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01216};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01216}.
CC   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01216}.
DR   EMBL; CP000031; AAV93701.1; -; Genomic_DNA.
DR   RefSeq; WP_011046144.1; NC_003911.12.
DR   SMR; Q5LXG9; -.
DR   STRING; 246200.SPO0383; -.
DR   EnsemblBacteria; AAV93701; AAV93701; SPO0383.
DR   KEGG; sil:SPO0383; -.
DR   eggNOG; ENOG4105TVB; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; PAPLKEY; -.
DR   OrthoDB; 1402654at2; -.
DR   BioCyc; RPOM246200:G1G48-390-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0008770; F:[acyl-carrier-protein] phosphodiesterase activity; ISS:TIGR.
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   GO; GO:0006631; P:fatty acid metabolic process; ISS:TIGR.
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; Q5LXG9.
DR   SWISS-2DPAGE; Q5LXG9.
KW   Complete proteome; Flavoprotein; FMN; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    204       FMN-dependent NADH-azoreductase.
FT                                /FTId=PRO_0000245973.
SQ   SEQUENCE   204 AA;  22385 MW;  161CE232F2665BFB CRC64;
     MTKLLQIIAS PRGGDSKSNA LADAFVAAQR AKDSTLQVDH LDLWAEDLPA FDGDPAAAKM
     TFFGVGQMDP SKEQAWSAVA RITERFMSAD HVVMGVPMWN GGIPYRLKHY IDIITQPGML
     FGFDPDNGYS GLLRNRKATV VTTSGVWSEG ADARFGSDFH STYLKWWFET IGITDVTFVR
     YQPSLLTDDP QAGYDRALAA LTAA
//

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