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Toluene o-xylene monooxygenase oxygenase subunit TouA (Toluene, o-xylene monooxygenase oxygenase subunit)

 O87798_PSEST            Unreviewed;       498 AA.
O87798;
01-NOV-1998, integrated into UniProtKB/TrEMBL.
01-NOV-1998, sequence version 1.
30-AUG-2017, entry version 88.
SubName: Full=Toluene o-xylene monooxygenase oxygenase subunit TouA {ECO:0000313|EMBL:ALP69204.1};
SubName: Full=Toluene, o-xylene monooxygenase oxygenase subunit {ECO:0000313|EMBL:CAA06654.1};
Name=touA {ECO:0000313|EMBL:CAA06654.1};
Pseudomonas stutzeri (Pseudomonas perfectomarina).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=316 {ECO:0000313|EMBL:CAA06654.1};
[1] {ECO:0000313|EMBL:CAA06654.1}
NUCLEOTIDE SEQUENCE.
STRAIN=OX1 {ECO:0000313|EMBL:CAA06654.1};
PubMed=9758777;
Bertoni G., Martino M., Galli E., Barbieri P.;
"Analysis of the gene cluster encoding toluene/o-xylene monooxygenase
from Pseudomonas stutzeri OX1.";
Appl. Environ. Microbiol. 64:3626-3632(1998).
[2] {ECO:0000313|EMBL:CAA06654.1}
NUCLEOTIDE SEQUENCE.
STRAIN=OX1 {ECO:0000313|EMBL:CAA06654.1};
PubMed=10473416;
Arenghi F.L.G., Pinti M., Galli E., Barbieri P.;
"Identification of the Pseudomonas stutzeri OX1 toluene-o-xylene
monooxygenase regulatory gene (touR) and of its cognate promoter.";
Appl. Environ. Microbiol. 65:4057-4063(1999).
[3] {ECO:0000313|EMBL:CAA06654.1}
NUCLEOTIDE SEQUENCE.
STRAIN=OX1 {ECO:0000313|EMBL:CAA06654.1};
Park S.Y., Min B.W.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PDB:1T0Q, ECO:0000213|PDB:1T0R, ECO:0000213|PDB:1T0S}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON.
PubMed=15096510; DOI=10.1074/jbc.M400710200;
Sazinsky M.H., Bard J., Di Donato A., Lippard S.J.;
"Crystal structure of the toluene/o-xylene monooxygenase hydroxylase
from Pseudomonas stutzeri OX1. Insight into the substrate specificity,
substrate channeling, and active site tuning of multicomponent
monooxygenases.";
J. Biol. Chem. 279:30600-30610(2004).
[5] {ECO:0000213|PDB:2INC, ECO:0000213|PDB:2IND}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-492 IN COMPLEX WITH IRON
AND MANGANESE.
PubMed=17117860; DOI=10.1021/ja064837r;
McCormick M.S., Sazinsky M.H., Condon K.L., Lippard S.J.;
"X-ray crystal structures of manganese(II)-reconstituted and native
toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in
conserved residues and an enhanced view of the protein interior.";
J. Am. Chem. Soc. 128:15108-15110(2006).
[6] {ECO:0000213|PDB:2RDB}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IRON.
PubMed=18044971; DOI=10.1021/bi7017128;
Murray L.J., Garcia-Serres R., McCormick M.S., Davydov R., Naik S.G.,
Kim S.H., Hoffman B.M., Huynh B.H., Lippard S.J.;
"Dioxygen activation at non-heme diiron centers: oxidation of a
proximal residue in the I100W variant of toluene/o-xylene
monooxygenase hydroxylase.";
Biochemistry 46:14795-14809(2007).
[7] {ECO:0000313|EMBL:ALP69204.1}
NUCLEOTIDE SEQUENCE.
STRAIN=2A20 {ECO:0000313|EMBL:ALP69204.1};
PubMed=27185632; DOI=10.1016/j.gene.2016.05.022;
Heinaru E., Naanuri E., Grunbach M., Joesaar M., Heinaru A.;
"Functional redundancy in phenol and toluene degradation in
Pseudomonas stutzeri strains isolated from the Baltic Sea.";
Gene 589:90-98(2016).
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EMBL; KT935509; ALP69204.1; -; Genomic_DNA.
EMBL; AJ005663; CAA06654.1; -; Genomic_DNA.
PDB; 1T0Q; X-ray; 2.15 A; A=1-498.
PDB; 1T0R; X-ray; 2.30 A; A=1-498.
PDB; 1T0S; X-ray; 2.20 A; A=1-498.
PDB; 2INC; X-ray; 1.85 A; A=2-492.
PDB; 2IND; X-ray; 2.20 A; A=2-492.
PDB; 2RDB; X-ray; 2.10 A; A=1-498.
PDBsum; 1T0Q; -.
PDBsum; 1T0R; -.
PDBsum; 1T0S; -.
PDBsum; 2INC; -.
PDBsum; 2IND; -.
PDBsum; 2RDB; -.
SMR; O87798; -.
DIP; DIP-37865N; -.
IntAct; O87798; 2.
EvolutionaryTrace; O87798; -.
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:1T0Q, ECO:0000213|PDB:1T0R,
ECO:0000213|PDB:1T0S, ECO:0000213|PDB:2INC};
Iron {ECO:0000213|PDB:1T0Q, ECO:0000213|PDB:1T0R,
ECO:0000213|PDB:1T0S, ECO:0000213|PDB:2INC};
Metal-binding {ECO:0000213|PDB:1T0Q, ECO:0000213|PDB:1T0R,
ECO:0000213|PDB:1T0S, ECO:0000213|PDB:2INC};
Monooxygenase {ECO:0000313|EMBL:CAA06654.1};
Oxidoreductase {ECO:0000313|EMBL:CAA06654.1}.
DOMAIN 408 447 YHS. {ECO:0000259|Pfam:PF04945}.
METAL 104 104 Iron 1. {ECO:0000213|PDB:1T0Q,
ECO:0000213|PDB:2RDB}.
METAL 134 134 Iron 1. {ECO:0000213|PDB:1T0Q,
ECO:0000213|PDB:2RDB}.
METAL 134 134 Iron 2. {ECO:0000213|PDB:2INC,
ECO:0000213|PDB:2RDB}.
METAL 137 137 Iron 1; via pros nitrogen.
{ECO:0000213|PDB:1T0Q,
ECO:0000213|PDB:2RDB}.
METAL 197 197 Iron 2. {ECO:0000213|PDB:2INC,
ECO:0000213|PDB:2RDB}.
METAL 231 231 Iron 2. {ECO:0000213|PDB:2RDB}.
METAL 234 234 Iron 2; via tele nitrogen.
{ECO:0000213|PDB:2INC,
ECO:0000213|PDB:2RDB}.
SEQUENCE 498 AA; 57725 MW; E49B0C06D5BB43D8 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 PERYKNHTNL VDRFLKGEIQ PADLAGALMY MSLEPGVMGD
DAHDYEWVKA YQKKTNAA


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