ID   A0A926M5B2_9PROT        Unreviewed;       195 AA.
AC   A0A926M5B2;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   24-JUL-2024, entry version 6.
DE   RecName: Full=FMN dependent NADH:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.6.5.- {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};
DE   AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.7.1.17 {ECO:0000256|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN   ORFNames=IDH22_01440 {ECO:0000313|EMBL:MBD1142629.1};
OS   Pelagibacterales bacterium SAG-MED35.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales.
OX   NCBI_TaxID=2760037 {ECO:0000313|EMBL:MBD1142629.1, ECO:0000313|Proteomes:UP000611396};
RN   [1] {ECO:0000313|EMBL:MBD1142629.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAG-MED35 {ECO:0000313|EMBL:MBD1142629.1};
RX   PubMed=31840364;
RA   Haro-Moreno J.M., Rodriguez-Valera F., Rosselli R., Martinez-Hernandez F.,
RA   Roda-Garcia J.J., Gomez M.L., Fornas O., Martinez-Garcia M.,
RA   Lopez-Perez M.;
RT   "Ecogenomics of the SAR11 clade.";
RL   Environ. Microbiol. 22:1748-1763(2020).
CC   -!- FUNCTION: Also exhibits azoreductase activity. Catalyzes the reductive
CC       cleavage of the azo bond in aromatic azo compounds to the corresponding
CC       amines. {ECO:0000256|HAMAP-Rule:MF_01216}.
CC   -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC       stress caused by electrophilic quinones. {ECO:0000256|HAMAP-
CC       Rule:MF_01216}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+);
CC         Xref=Rhea:RHEA:65952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:132124, ChEBI:CHEBI:134225;
CC         Evidence={ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00023925};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55874;
CC         Evidence={ECO:0000256|ARBA:ARBA00023925};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|HAMAP-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   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01216}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01216}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBD1142629.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JACWEF010000005; MBD1142629.1; -; Genomic_DNA.
DR   Proteomes; UP000611396; Unassembled WGS sequence.
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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; 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; IPR050104; FMN-dep_NADH:Q_OxRdtase_AzoR1.
DR   InterPro; IPR023048; NADH:quinone_OxRdtase_FMN_depd.
DR   PANTHER; PTHR43741; FMN-DEPENDENT NADH-AZOREDUCTASE 1; 1.
DR   PANTHER; PTHR43741:SF2; FMN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_01216};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01216};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01216};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01216}; Reference proteome {ECO:0000313|Proteomes:UP000611396}.
FT   DOMAIN          1..190
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
FT   BINDING         9
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         15..17
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
FT   BINDING         137..140
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01216"
SQ   SEQUENCE   195 AA;  22144 MW;  A7B77B77E51FBFE6 CRC64;
     MKIYQIDSSA RKKGSTSRAL AKKLLDKIKK PGDEVLYRDL DEEMLFVSGL TESGMKIDEK
     DQTEHHKKMF ELSDQLVKEL KESDIIIISA PIYNYGPPAT LKAWTDLAAR IGETFKFKPN
     GRREGLLKNK QAYLVITSGG TKLNSSEDFL TPWLKFILNF FGIEKVDVIS ADQMALDYDK
     SIKDAEAQIE SLFKK
//