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Toluene o-xylene monooxygenase component

 Q6IV66_9PSED            Unreviewed;       498 AA.
Q6IV66;
05-JUL-2004, integrated into UniProtKB/TrEMBL.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 72.
SubName: Full=Toluene o-xylene monooxygenase component {ECO:0000313|EMBL:AAT40431.1};
Name=touA {ECO:0000313|EMBL:AAT40431.1};
Pseudomonas sp. OX1.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=320855 {ECO:0000313|EMBL:AAT40431.1};
[1] {ECO:0000313|EMBL:AAT40431.1}
NUCLEOTIDE SEQUENCE.
STRAIN=OX1 {ECO:0000313|EMBL:AAT40431.1};
PubMed=15184119; DOI=10.1128/AEM.70.6.3253-3262.2004;
Vardar G., Wood T.K.;
"Protein engineering of toluene-o-xylene monooxygenase from
Pseudomonas stutzeri OX1 for synthesizing 4-methylresorcinol,
methylhydroquinone, and pyrogallol.";
Appl. Environ. Microbiol. 70:3253-3262(2004).
[2] {ECO:0000213|PDB:3N1X, ECO:0000213|PDB:3N1Y, ECO:0000213|PDB:3N1Z}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON.
PubMed=20839885; DOI=10.1021/ja1063795;
Song W.J., McCormick M.S., Behan R.K., Sazinsky M.H., Jiang W.,
Lin J., Krebs C., Lippard S.J.;
"Active site threonine facilitates proton transfer during dioxygen
activation at the diiron center of toluene/o-xylene monooxygenase
hydroxylase.";
J. Am. Chem. Soc. 132:13582-13585(2010).
[3] {ECO:0000213|PDB:3RN9, ECO:0000213|PDB:3RNA, ECO:0000213|PDB:3RNB}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON.
PubMed=21859951; DOI=10.1073/pnas.1106514108;
Song W.J., Gucinski G., Sazinsky M.H., Lippard S.J.;
"Tracking a defined route for O migration in a dioxygen-activating
diiron enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 108:14795-14800(2011).
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EMBL; AY621080; AAT40431.1; -; Genomic_DNA.
PDB; 3N1X; X-ray; 2.40 A; A=1-498.
PDB; 3N1Y; X-ray; 2.10 A; A=1-498.
PDB; 3N1Z; X-ray; 2.90 A; A=1-498.
PDB; 3N20; X-ray; 1.90 A; A=1-498.
PDB; 3RN9; X-ray; 2.80 A; A=1-498.
PDB; 3RNA; X-ray; 3.00 A; A=1-498.
PDB; 3RNB; X-ray; 2.64 A; A=1-498.
PDB; 3RNC; X-ray; 2.74 A; A=1-498.
PDB; 3RNE; X-ray; 2.50 A; A=1-498.
PDB; 3RNF; X-ray; 2.20 A; A=1-498.
PDB; 3RNG; X-ray; 2.81 A; A=1-498.
PDBsum; 3N1X; -.
PDBsum; 3N1Y; -.
PDBsum; 3N1Z; -.
PDBsum; 3N20; -.
PDBsum; 3RN9; -.
PDBsum; 3RNA; -.
PDBsum; 3RNB; -.
PDBsum; 3RNC; -.
PDBsum; 3RNE; -.
PDBsum; 3RNF; -.
PDBsum; 3RNG; -.
ProteinModelPortal; Q6IV66; -.
SMR; Q6IV66; -.
DIP; DIP-59705N; -.
IntAct; Q6IV66; 1.
EvolutionaryTrace; Q6IV66; -.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR003430; Phenol_Hydrox.
InterPro; IPR007029; YHS_dom.
Pfam; PF02332; Phenol_Hydrox; 1.
Pfam; PF04945; YHS; 1.
SUPFAM; SSF47240; SSF47240; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:3N1X, ECO:0000213|PDB:3N1Y,
ECO:0000213|PDB:3N1Z, ECO:0000213|PDB:3N20};
Iron {ECO:0000213|PDB:3N1X, ECO:0000213|PDB:3N1Y,
ECO:0000213|PDB:3N1Z, ECO:0000213|PDB:3N20};
Metal-binding {ECO:0000213|PDB:3N1X, ECO:0000213|PDB:3N1Y,
ECO:0000213|PDB:3N1Z, ECO:0000213|PDB:3N20};
Monooxygenase {ECO:0000313|EMBL:AAT40431.1};
Oxidoreductase {ECO:0000313|EMBL:AAT40431.1}.
DOMAIN 408 447 YHS. {ECO:0000259|Pfam:PF04945}.
METAL 104 104 Iron 1. {ECO:0000213|PDB:3N1X,
ECO:0000213|PDB:3RN9,
ECO:0000213|PDB:3RNB}.
METAL 134 134 Iron 1. {ECO:0000213|PDB:3N1X,
ECO:0000213|PDB:3RN9,
ECO:0000213|PDB:3RNB}.
METAL 134 134 Iron 2. {ECO:0000213|PDB:3RNF}.
METAL 137 137 Iron 1; via pros nitrogen.
{ECO:0000213|PDB:3N1X,
ECO:0000213|PDB:3RN9,
ECO:0000213|PDB:3RNB}.
METAL 197 197 Iron 2. {ECO:0000213|PDB:3RNF}.
METAL 234 234 Iron 2; via tele nitrogen.
{ECO:0000213|PDB:3RNF}.
SEQUENCE 498 AA; 57726 MW; EA950C06D5B1E3D8 CRC64;
MSMLKREDWY DLTRTTNWTP KYVTENELFP EEMSGARGIS MEAWEKYDEP YKITYPEYVS
IQREKDSGAY SIKAALERDG FVDRADPGWV STMQLHFGAI ALEEYAASTA EARMARFAKA
PGNRNMATFG MMDENRHGQI QLYFPYANVK RSRKWDWAHK AIHTNEWAAI AARSFFDDMM
MTRDSVAVSI MLTFAFETGF TNMQFLGLAA DAAEAGDHTF ASLISSIQTD ESRHAQQGGP
SLKILVENGK KDEAQQMVDV AIWRSWKLFS VLTGPIMDYY TPLESRNQSF KEFMLEWIVA
QFERQLLDLG LDKPWYWDQF MQDLDETHHG MHLGVWYWRP TVWWDPAAGV SPEEREWLEE
KYPGWNDTWG QCWDVITDNL VNGKPELTVP ETLPTICNMC NLPIAHTPGN KWNVKDYQLE
YEGRLYHFGS EADRWCFQID PERYENHTNL VDRFLKGEIQ PADLAGALMY MSLEPGVMGD
DAHDYEWVKA YQKKTNAA


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