(data stored in ACNUC7421 zone)

SWISSPROT: AZOR_SHESH

ID   AZOR_SHESH              Reviewed;         197 AA.
AC   A8FPZ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE            EC=1.7.-.- {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=Ssed_0307;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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: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; CP000821; ABV34920.1; -; Genomic_DNA.
DR   RefSeq; WP_012004446.1; NC_009831.1.
DR   ProteinModelPortal; A8FPZ7; -.
DR   SMR; A8FPZ7; -.
DR   STRING; 425104.Ssed_0307; -.
DR   EnsemblBacteria; ABV34920; ABV34920; Ssed_0307.
DR   KEGG; sse:Ssed_0307; -.
DR   eggNOG; ENOG4108V3G; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; AGITFKY; -.
DR   OrthoDB; POG091H0DQS; -.
DR   Proteomes; UP000002015; Chromosome.
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_dom.
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; A8FPZ7.
DR   SWISS-2DPAGE; A8FPZ7.
KW   Complete proteome; Flavoprotein; FMN; NAD; Oxidoreductase.
FT   CHAIN         1    197       FMN-dependent NADH-azoreductase.
FT                                /FTId=PRO_1000085588.
SQ   SEQUENCE   197 AA;  21206 MW;  4E1AE03699280E8A CRC64;
     MSKVLILKSS ILGDYSQSGQ LVEHLKQHWE QQGAEISVRD LAAEPLPMLD GEIASGLRGG
     DQLSARQEQA LLLSDSLIQE LKAHDTIVIA APMYNFSIPT QLKNWIDLVA RAGVSFTYTE
     TGPKGLITGK RAVLITTRGG VHKGGASDHV VPYLKTVLGF IGIEEVETVY SEALNMGPEA
     SKQGIESAQQ ALEKIVA
//

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