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Protein

FMN-dependent NADH-azoreductase

Gene

azoR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Kineticsi

  1. KM=17.9 µM for methyl red
  2. KM=31.6 µM for NADH

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101FMN1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 183FMN1 Publication
    Nucleotide bindingi96 – 994FMN1 Publication
    Nucleotide bindingi140 – 1456FMN1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • response to oxidative stress Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN, NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:G6731-MONOMER.
    ECOL316407:JW1409-MONOMER.
    MetaCyc:G6731-MONOMER.
    BRENDAi1.7.1.6. 2026.
    SABIO-RKP41407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FMN-dependent NADH-azoreductase (EC:1.7.-.-)
    Alternative name(s):
    Azo-dye reductase
    FMN-dependent NADH-azo compound oxidoreductase
    Gene namesi
    Name:azoR
    Synonyms:acpD
    Ordered Locus Names:b1412, JW1409
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG12695. azoR.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Chemistry

    DrugBankiDB02325. Isopropyl Alcohol.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 201200FMN-dependent NADH-azoreductasePRO_0000166310Add
    BLAST

    Proteomic databases

    PaxDbiP41407.
    PRIDEiP41407.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi4261518. 6 interactions.
    STRINGi511145.b1412.

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Helixi13 – 153Combined sources
    Helixi17 – 3216Combined sources
    Beta strandi36 – 427Combined sources
    Turni43 – 475Combined sources
    Helixi53 – 586Combined sources
    Helixi68 – 8619Combined sources
    Beta strandi88 – 936Combined sources
    Helixi103 – 11210Combined sources
    Turni115 – 1173Combined sources
    Beta strandi118 – 1225Combined sources
    Beta strandi125 – 1284Combined sources
    Beta strandi134 – 1407Combined sources
    Helixi153 – 16311Combined sources
    Beta strandi169 – 1746Combined sources
    Helixi177 – 1793Combined sources
    Helixi181 – 19919Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TIKX-ray2.30A2-201[»]
    1V4BX-ray1.80A2-201[»]
    2D5IX-ray2.20A2-201[»]
    2Z98X-ray1.40A2-201[»]
    2Z9BX-ray1.70A2-201[»]
    2Z9CX-ray2.30A2-201[»]
    2Z9DX-ray2.10A/B2-201[»]
    ProteinModelPortaliP41407.
    SMRiP41407. Positions 2-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41407.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the azoreductase type 1 family.Curated

    Phylogenomic databases

    eggNOGiENOG4108V3G. Bacteria.
    COG1182. LUCA.
    HOGENOMiHOG000247892.
    InParanoidiP41407.
    KOiK01118.
    OMAiWMKPEEQ.
    PhylomeDBiP41407.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    HAMAPiMF_01216. Azoreductase_type1. 1 hit.
    InterProiIPR003680. Flavodoxin_fold.
    IPR029039. Flavoprotein-like_dom.
    IPR023048. NADH-azoreductase_FMN-depdnt.
    [Graphical view]
    PfamiPF02525. Flavodoxin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P41407-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKVLVLKSS ILAGYSQSNQ LSDYFVEQWR EKHSADEITV RDLAANPIPV
    60 70 80 90 100
    LDGELVGALR PSDAPLTPRQ QEALALSDEL IAELKAHDVI VIAAPMYNFN
    110 120 130 140 150
    ISTQLKNYFD LVARAGVTFR YTENGPEGLV TGKKAIVITS RGGIHKDGPT
    160 170 180 190 200
    DLVTPYLSTF LGFIGITDVK FVFAEGIAYG PEMAAKAQSD AKAAIDSIVS

    A
    Length:201
    Mass (Da):21,658
    Last modified:January 23, 2007 - v3
    Checksum:iE28D30DC4DA42297
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 3513DYFVE…EKHSA → IILLNNGAKSTPR in BAA25408 (Ref. 1) CuratedAdd
    BLAST
    Sequence conflicti23 – 3513DYFVE…EKHSA → IILLNNGAKSTPR in BAA07684 (PubMed:7899078).CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85081 Genomic DNA. Translation: BAA25408.1.
    U00096 Genomic DNA. Translation: AAC74494.1.
    AP009048 Genomic DNA. Translation: BAA15024.1.
    D42105 Genomic DNA. Translation: BAA07684.1.
    PIRiG64892.
    RefSeqiNP_415930.1. NC_000913.3.
    WP_000048950.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74494; AAC74494; b1412.
    BAA15024; BAA15024; BAA15024.
    GeneIDi947569.
    KEGGiecj:JW1409.
    eco:b1412.
    PATRICi32118110. VBIEscCol129921_1475.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D85081 Genomic DNA. Translation: BAA25408.1.
    U00096 Genomic DNA. Translation: AAC74494.1.
    AP009048 Genomic DNA. Translation: BAA15024.1.
    D42105 Genomic DNA. Translation: BAA07684.1.
    PIRiG64892.
    RefSeqiNP_415930.1. NC_000913.3.
    WP_000048950.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TIKX-ray2.30A2-201[»]
    1V4BX-ray1.80A2-201[»]
    2D5IX-ray2.20A2-201[»]
    2Z98X-ray1.40A2-201[»]
    2Z9BX-ray1.70A2-201[»]
    2Z9CX-ray2.30A2-201[»]
    2Z9DX-ray2.10A/B2-201[»]
    ProteinModelPortaliP41407.
    SMRiP41407. Positions 2-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261518. 6 interactions.
    STRINGi511145.b1412.

    Chemistry

    DrugBankiDB02325. Isopropyl Alcohol.

    Proteomic databases

    PaxDbiP41407.
    PRIDEiP41407.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74494; AAC74494; b1412.
    BAA15024; BAA15024; BAA15024.
    GeneIDi947569.
    KEGGiecj:JW1409.
    eco:b1412.
    PATRICi32118110. VBIEscCol129921_1475.

    Organism-specific databases

    EchoBASEiEB2558.
    EcoGeneiEG12695. azoR.

    Phylogenomic databases

    eggNOGiENOG4108V3G. Bacteria.
    COG1182. LUCA.
    HOGENOMiHOG000247892.
    InParanoidiP41407.
    KOiK01118.
    OMAiWMKPEEQ.
    PhylomeDBiP41407.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6731-MONOMER.
    ECOL316407:JW1409-MONOMER.
    MetaCyc:G6731-MONOMER.
    BRENDAi1.7.1.6. 2026.
    SABIO-RKP41407.

    Miscellaneous databases

    EvolutionaryTraceiP41407.
    PROiP41407.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    HAMAPiMF_01216. Azoreductase_type1. 1 hit.
    InterProiIPR003680. Flavodoxin_fold.
    IPR029039. Flavoprotein-like_dom.
    IPR023048. NADH-azoreductase_FMN-depdnt.
    [Graphical view]
    PfamiPF02525. Flavodoxin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAZOR_ECOLI
    AccessioniPrimary (citable) accession number: P41407
    Secondary accession number(s): P77143, Q93V21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The stoichiometry implies that 2 cycles of the ping-pong mechanism are required for the cleavage.

    Caution

    Was originally thought to be an ACP phosphodiesterase.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.