ID AZOR_SALTY Reviewed; 201 AA.
AC P63462; Q8XFP4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=FMN-dependent NADH:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.6.5.- {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};
DE AltName: Full=FMN-dependent NADH-azoreductase {ECO:0000255|HAMAP-Rule:MF_01216};
DE EC=1.7.1.17 {ECO:0000255|HAMAP-Rule:MF_01216};
GN Name=azoR {ECO:0000255|HAMAP-Rule:MF_01216}; Synonyms=acpD;
GN OrderedLocusNames=STM1642;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2] {ECO:0007744|PDB:1T5B}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH FMN.
RA Zhang R., Wu R., Collart F., Joachimiak A.;
RT "1.4 A crystal structure of a protein from Salmonella typhimurium similar
RT to E. coli acyl carrier protein phosphodiesterase.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Quinone reductase that provides resistance to thiol-specific
CC stress caused by electrophilic quinones. {ECO:0000255|HAMAP-
CC Rule:MF_01216}.
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:0000255|HAMAP-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: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}.
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DR EMBL; AE006468; AAL20560.1; -; Genomic_DNA.
DR RefSeq; NP_460601.1; NC_003197.2.
DR RefSeq; WP_000048924.1; NC_003197.2.
DR PDB; 1T5B; X-ray; 1.40 A; A/B=1-201.
DR PDBsum; 1T5B; -.
DR AlphaFoldDB; P63462; -.
DR SMR; P63462; -.
DR STRING; 99287.STM1642; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; 99287-STM1642; -.
DR DNASU; 1253160; -.
DR GeneID; 1253160; -.
DR KEGG; stm:STM1642; -.
DR PATRIC; fig|99287.12.peg.1734; -.
DR HOGENOM; CLU_088964_0_0_6; -.
DR OMA; FIARPRV; -.
DR PhylomeDB; P63462; -.
DR BioCyc; SENT99287:STM1642-MONOMER; -.
DR EvolutionaryTrace; P63462; -.
DR Proteomes; UP000001014; 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: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; 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 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..201
FT /note="FMN-dependent NADH:quinone oxidoreductase"
FT /id="PRO_0000166316"
FT BINDING 10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1T5B"
FT BINDING 16..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1T5B"
FT BINDING 96..99
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01216,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:1T5B"
FT BINDING 140..145
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T5B"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1T5B"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1T5B"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1T5B"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1T5B"
FT HELIX 181..200
FT /evidence="ECO:0007829|PDB:1T5B"
SQ SEQUENCE 201 AA; 21628 MW; 8E266557BCEF093D CRC64;
MSKVLVLKSS ILAGYSQSGQ LTDYFIEQWR EKHVADEITV RDLAANPVPV LDGELVGAMR
PGDAPLTPRQ QDALALSDEL IAELKAHDVI VIAAPMYNFN IPTQLKNYFD LIARAGITFR
YTEKGPEGLV TGKRAVVLSS RGGIHKDTPT DLIAPYLKVF LGFIGITDVN FVFAEGIAYG
PEVAAKAQAD AKAAIDSVVA A
//
