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FMN-dependent NADH-azoreductase (EC 1.7.-.-) (Azo-dye reductase) (FMN-dependent NADH-azo compound oxidoreductase)

 AZOR_ECOLI              Reviewed;         201 AA.
P41407; P77143; Q93V21;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 139.
RecName: Full=FMN-dependent NADH-azoreductase;
EC=1.7.-.-;
AltName: Full=Azo-dye reductase;
AltName: Full=FMN-dependent NADH-azo compound oxidoreductase;
Name=azoR; Synonyms=acpD; OrderedLocusNames=b1412, JW1409;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
Kitakawa M., Kasai H., Baba T., Honjo A., Isono K.;
"Nucleotide sequence of the replication terminus region of Escherichia
coli.";
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144.
STRAIN=K12;
PubMed=7899078; DOI=10.1093/nar/23.4.595;
Moriya H., Kasai H., Isono K.;
"Cloning and characterization of the hrpA gene in the terC region of
Escherichia coli that is highly similar to the DEAH family RNA
helicase genes of Saccharomyces cerevisiae.";
Nucleic Acids Res. 23:595-598(1995).
[6]
PROTEIN SEQUENCE OF 2-16, AND PRELIMINARY FUNCTION.
PubMed=2168383; DOI=10.1128/jb.172.9.5445-5449.1990;
Fischl A.S., Kennedy E.P.;
"Isolation and properties of acyl carrier protein phosphodiesterase of
Escherichia coli.";
J. Bacteriol. 172:5445-5449(1990).
[7]
PROTEIN SEQUENCE OF 2-8, COFACTOR, SUBUNIT, AND CHARACTERIZATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=11583992; DOI=10.1074/jbc.M104483200;
Nakanishi M., Yatome C., Ishida N., Kitade Y.;
"Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase.";
J. Biol. Chem. 276:46394-46399(2001).
[8]
CRYSTALLIZATION.
PubMed=16511052; DOI=10.1107/S1744309105007918;
Ito K., Nakanishi M., Lee W.-C., Sasaki H., Zenno S., Saigo K.,
Kitade Y., Tanokura M.;
"Crystallization and preliminary X-ray analysis of azoR (azoreductase)
from Escherichia coli.";
Acta Crystallogr. F 61:399-402(2005).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
New York structural genomics research consortium (NYSGRC);
"Crystal structure of acyl carrier protein phosphodiesterase.";
Submitted (JUN-2004) to the PDB data bank.
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FMN.
Ito K., Tanokura M.;
"The crystal structure of AzoR (Azo Reductase) from Escherichia coli:
oxidized form.";
Submitted (JAN-2005) to the PDB data bank.
-!- FUNCTION: 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.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:11583992};
Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:11583992};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17.9 uM for methyl red;
KM=31.6 uM for NADH;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11583992,
ECO:0000269|Ref.10}.
-!- MISCELLANEOUS: The stoichiometry implies that 2 cycles of the
ping-pong mechanism are required for the cleavage.
-!- SIMILARITY: Belongs to the azoreductase type 1 family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be an ACP phosphodiesterase.
{ECO:0000305|PubMed:2168383}.
-----------------------------------------------------------------------
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EMBL; D85081; BAA25408.1; -; Genomic_DNA.
EMBL; U00096; AAC74494.1; -; Genomic_DNA.
EMBL; AP009048; BAA15024.1; -; Genomic_DNA.
EMBL; D42105; BAA07684.1; -; Genomic_DNA.
PIR; G64892; G64892.
RefSeq; NP_415930.1; NC_000913.3.
RefSeq; WP_000048950.1; NZ_LN832404.1.
PDB; 1TIK; X-ray; 2.30 A; A=2-201.
PDB; 1V4B; X-ray; 1.80 A; A=2-201.
PDB; 2D5I; X-ray; 2.20 A; A=2-201.
PDB; 2Z98; X-ray; 1.40 A; A=2-201.
PDB; 2Z9B; X-ray; 1.70 A; A=2-201.
PDB; 2Z9C; X-ray; 2.30 A; A=2-201.
PDB; 2Z9D; X-ray; 2.10 A; A/B=2-201.
PDBsum; 1TIK; -.
PDBsum; 1V4B; -.
PDBsum; 2D5I; -.
PDBsum; 2Z98; -.
PDBsum; 2Z9B; -.
PDBsum; 2Z9C; -.
PDBsum; 2Z9D; -.
ProteinModelPortal; P41407; -.
SMR; P41407; -.
BioGrid; 4261518; 20.
STRING; 316385.ECDH10B_1538; -.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB03247; Riboflavin Monophosphate.
PaxDb; P41407; -.
PRIDE; P41407; -.
EnsemblBacteria; AAC74494; AAC74494; b1412.
EnsemblBacteria; BAA15024; BAA15024; BAA15024.
GeneID; 947569; -.
KEGG; ecj:JW1409; -.
KEGG; eco:b1412; -.
PATRIC; fig|1411691.4.peg.859; -.
EchoBASE; EB2558; -.
EcoGene; EG12695; azoR.
eggNOG; ENOG4108V3G; Bacteria.
eggNOG; COG1182; LUCA.
HOGENOM; HOG000247892; -.
InParanoid; P41407; -.
KO; K01118; -.
OMA; AGITFKY; -.
PhylomeDB; P41407; -.
BioCyc; EcoCyc:G6731-MONOMER; -.
BioCyc; MetaCyc:G6731-MONOMER; -.
BRENDA; 1.7.1.6; 2026.
SABIO-RK; P41407; -.
EvolutionaryTrace; P41407; -.
PRO; PR:P41407; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0050446; F:azobenzene reductase activity; IDA:EcoCyc.
GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
Gene3D; 3.40.50.360; -; 1.
HAMAP; MF_01216; Azoreductase_type1; 1.
InterPro; IPR003680; Flavodoxin_fold.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR023048; NADH-azoreductase_FMN-depdnt.
Pfam; PF02525; Flavodoxin_2; 1.
SUPFAM; SSF52218; SSF52218; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11583992,
ECO:0000269|PubMed:2168383}.
CHAIN 2 201 FMN-dependent NADH-azoreductase.
/FTId=PRO_0000166310.
NP_BIND 16 18 FMN. {ECO:0000269|Ref.10}.
NP_BIND 96 99 FMN. {ECO:0000269|Ref.10}.
NP_BIND 140 145 FMN. {ECO:0000269|Ref.10}.
BINDING 10 10 FMN. {ECO:0000269|Ref.10}.
CONFLICT 23 35 DYFVEQWREKHSA -> IILLNNGAKSTPR (in Ref.
1; BAA25408 and 5; BAA07684).
{ECO:0000305}.
STRAND 3 8 {ECO:0000244|PDB:2Z98}.
HELIX 13 15 {ECO:0000244|PDB:2Z98}.
HELIX 17 32 {ECO:0000244|PDB:2Z98}.
STRAND 36 42 {ECO:0000244|PDB:2Z98}.
TURN 43 47 {ECO:0000244|PDB:2Z98}.
HELIX 53 58 {ECO:0000244|PDB:2Z98}.
HELIX 68 86 {ECO:0000244|PDB:2Z98}.
STRAND 88 93 {ECO:0000244|PDB:2Z98}.
HELIX 103 112 {ECO:0000244|PDB:2Z98}.
TURN 115 117 {ECO:0000244|PDB:2Z98}.
STRAND 118 122 {ECO:0000244|PDB:2Z98}.
STRAND 125 128 {ECO:0000244|PDB:2Z98}.
STRAND 134 140 {ECO:0000244|PDB:2Z98}.
HELIX 153 163 {ECO:0000244|PDB:2Z98}.
STRAND 169 174 {ECO:0000244|PDB:2Z98}.
HELIX 177 179 {ECO:0000244|PDB:2Z9D}.
HELIX 181 199 {ECO:0000244|PDB:2Z98}.
SEQUENCE 201 AA; 21658 MW; E28D30DC4DA42297 CRC64;
MSKVLVLKSS ILAGYSQSNQ LSDYFVEQWR EKHSADEITV RDLAANPIPV LDGELVGALR
PSDAPLTPRQ QEALALSDEL IAELKAHDVI VIAAPMYNFN ISTQLKNYFD LVARAGVTFR
YTENGPEGLV TGKKAIVITS RGGIHKDGPT DLVTPYLSTF LGFIGITDVK FVFAEGIAYG
PEMAAKAQSD AKAAIDSIVS A


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