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EDTA monooxygenase

 Q9F9T3_9PROT            Unreviewed;       430 AA.
Q9F9T3;
01-MAR-2001, integrated into UniProtKB/TrEMBL.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 60.
SubName: Full=EDTA monooxygenase {ECO:0000313|EMBL:AAG09252.1};
Name=emoA {ECO:0000313|EMBL:AAG09252.1};
EDTA-degrading bacterium BNC1.
Bacteria; Proteobacteria; Alphaproteobacteria.
NCBI_TaxID=85561 {ECO:0000313|EMBL:AAG09252.1};
[1] {ECO:0000313|EMBL:AAG09252.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BNC1 {ECO:0000313|EMBL:AAG09252.1};
PubMed=11157232; DOI=10.1128/AEM.67.2.688-695.2001;
Bohuslavek J., Payne J.W., Liu Y., Bolton H.Jr., Xun L.;
"Cloning, sequencing, and characterization of a gene cluster involved
in EDTA degradation from the bacterium BNC1.";
Appl. Environ. Microbiol. 67:688-695(2001).
[2] {ECO:0000313|EMBL:AAG09252.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BNC1 {ECO:0000313|EMBL:AAG09252.1};
PubMed=11157233; DOI=10.1128/AEM.67.2.696-701.2001;
Liu Y., Louie T.M., Payne J., Bohuslavek J., Bolton H.Jr., Xun L.;
"Identification, purification, and characterization of iminodiacetate
oxidase from the EDTA-degrading bacterium BNC1.";
Appl. Environ. Microbiol. 67:696-701(2001).
[3] {ECO:0000213|PDB:5DQP}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
PubMed=26928990; DOI=10.1111/mmi.13363;
Jun S.Y., Lewis K.M., Youn B., Xun L., Kang C.;
"Structural and biochemical characterization of EDTA monooxygenase and
its physical interaction with a partner flavin reductase.";
Mol. Microbiol. 100:989-1003(2016).
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|PIRSR:PIRSR000337-1};
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EMBL; AF176664; AAG09252.1; -; Genomic_DNA.
PDB; 5DQP; X-ray; 2.15 A; A/B=1-430.
PDBsum; 5DQP; -.
ProteinModelPortal; Q9F9T3; -.
SMR; Q9F9T3; -.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
Gene3D; 3.20.20.30; -; 1.
InterPro; IPR011251; Luciferase-like_dom.
InterPro; IPR036661; Luciferase-like_sf.
InterPro; IPR016215; NTA_MOA.
Pfam; PF00296; Bac_luciferase; 1.
PIRSF; PIRSF000337; NTA_MOA; 1.
SUPFAM; SSF51679; SSF51679; 1.
TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:5DQP};
Flavoprotein {ECO:0000256|PIRSR:PIRSR000337-1};
FMN {ECO:0000256|PIRSR:PIRSR000337-1};
Monooxygenase {ECO:0000313|EMBL:AAG09252.1};
Oxidoreductase {ECO:0000313|EMBL:AAG09252.1}.
DOMAIN 28 376 Bac_luciferase.
{ECO:0000259|Pfam:PF00296}.
NP_BIND 143 147 FMN binding.
{ECO:0000256|PIRSR:PIRSR000337-1}.
NP_BIND 213 216 FMN binding.
{ECO:0000256|PIRSR:PIRSR000337-1}.
BINDING 57 57 FMN; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR000337-
1}.
BINDING 94 94 FMN. {ECO:0000256|PIRSR:PIRSR000337-1}.
SEQUENCE 430 AA; 47335 MW; 57FB3C0BC90E970B CRC64;
MRKRRMYLVS WLNSSGVLPN SWNEGRGNRA RIFDLENYIR SAEIARRGRI DAFFLADQPQ
LTPNPKVRPE YPFDPIVLAA AITGRVPDIG GIVTASTSFS LPYTLARQIA SVNLLSGGRI
GWNAVTTANP AVAANYGAAI ATHDNRYERA EEFLEVVHGL WNSWKFPWDE AIGPNPNPFG
EVMPINHEGK YFKVAGPLNV PLPPYGPPVV VQAGGSDQGK RLASRFGEII YAFLGSKPAG
RRFVAEARAA ARAQGRPEGS TLVLPSFVPL IGSTEAEVKR LVAEYEAGLD PAEQRIEALS
KQLGIDLERI NVDQVLQEKD FNLPKESATP IGILKSMVDV ALDEKLSLRQ LALRMRLIAG
TPDQVADRLI DWWQDEAADG FVINAPLLPD ALEIFVDQVV PILQSRGVFP RSYTESTLRE
RLGLPRNPLG


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