(data stored in ACNUC7421 zone)

SWISSPROT: AZOR_ALCBS

ID   AZOR_ALCBS              Reviewed;         198 AA.
AC   Q0VTN3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 81.
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}; OrderedLocusNames=ABO_0027;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic azo
CC       compounds to the corresponding amines. Requires NADH, but not NADPH, as
CC       an electron donor for its activity. {ECO:0000255|HAMAP-Rule:MF_01216}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NAD(+) =
CC         2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADH;
CC         Xref=Rhea:RHEA:55872, ChEBI:CHEBI:15378, ChEBI:CHEBI:15783,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:71579; EC=1.7.1.17; Evidence={ECO:0000255|HAMAP-
CC         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; AM286690; CAL15475.1; -; Genomic_DNA.
DR   RefSeq; WP_011587325.1; NC_008260.1.
DR   SMR; Q0VTN3; -.
DR   STRING; 393595.ABO_0027; -.
DR   PRIDE; Q0VTN3; -.
DR   EnsemblBacteria; CAL15475; CAL15475; ABO_0027.
DR   KEGG; abo:ABO_0027; -.
DR   eggNOG; ENOG4108V3G; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; AFIGIHD; -.
DR   OrthoDB; 1402654at2; -.
DR   BioCyc; ABOR393595:ABO_RS00140-MONOMER; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; 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; Q0VTN3.
DR   SWISS-2DPAGE; Q0VTN3.
KW   Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..198
FT                   /note="FMN-dependent NADH-azoreductase"
FT                   /id="PRO_1000066491"
SQ   SEQUENCE   198 AA;  21367 MW;  F3E718832FBE8DFB CRC64;
     MNILVIKSSV FGDNGNSSAL VNAQVDALKA KHPQATVRVR DLSTDPIPHL DGNRVSAFFT
     SATQRTDEQQ AIDAFSLALI DEIKAADHIV LGLPMYNFGI PSQLKSWIDH VARAGITFRY
     TEKGPQGLLE NKPVTVLAAR GGIYAGTSND TVTPYIKLFF GFIGITDVEF VFAEGLNMGD
     DVKEKALAVA RSELLAST
//

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