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Protein
Submitted name:

Toluene o-xylene monooxygenase oxygenase subunit TouA

Gene

touA

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi104 – 1041Iron 1Combined sources
Metal bindingi104 – 1041Manganese 1Combined sources
Metal bindingi134 – 1341Iron 1Combined sources
Metal bindingi134 – 1341Iron 2Combined sources
Metal bindingi134 – 1341Manganese 1Combined sources
Metal bindingi134 – 1341Manganese 2Combined sources
Metal bindingi137 – 1371Iron 1; via pros nitrogenCombined sources
Metal bindingi137 – 1371Manganese 1; via pros nitrogenCombined sources
Metal bindingi197 – 1971Iron 2Combined sources
Metal bindingi197 – 1971Manganese 2Combined sources
Metal bindingi231 – 2311Iron 2Combined sources
Metal bindingi231 – 2311Manganese 1Combined sources
Metal bindingi231 – 2311Manganese 2Combined sources
Metal bindingi234 – 2341Iron 2; via tele nitrogenCombined sources
Metal bindingi234 – 2341Manganese 2; via tele nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

MonooxygenaseImported, Oxidoreductase

Keywords - Ligandi

IronCombined sources, ManganeseCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Toluene o-xylene monooxygenase oxygenase subunit TouAImported
Submitted name:
Toluene, o-xylene monooxygenase oxygenase subunitImported
Gene namesi
Name:touAImported
OrganismiPseudomonas stutzeri (Pseudomonas perfectomarina)Imported
Taxonomic identifieri316 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Interactioni

Protein-protein interaction databases

DIPiDIP-37865N.
IntActiO87798. 2 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0QX-ray2.15A1-498[»]
1T0RX-ray2.30A1-498[»]
1T0SX-ray2.20A1-498[»]
2INCX-ray1.85A2-492[»]
2INDX-ray2.20A2-492[»]
2RDBX-ray2.10A1-498[»]
ProteinModelPortaliO87798.
SMRiO87798. Positions 2-492.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO87798.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini408 – 44740YHSInterPro annotationAdd
BLAST

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
IPR007029. YHS_dom.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
PF04945. YHS. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.

Sequencei

Sequence statusi: Complete.

O87798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLKREDWY DLTRTTNWTP KYVTENELFP EEMSGARGIS MEAWEKYDEP
60 70 80 90 100
YKITYPEYVS IQREKDSGAY SIKAALERDG FVDRADPGWV STMQLHFGAI
110 120 130 140 150
ALEEYAASTA EARMARFAKA PGNRNMATFG MMDENRHGQI QLYFPYANVK
160 170 180 190 200
RSRKWDWAHK AIHTNEWAAI AARSFFDDMM MTRDSVAVSI MLTFAFETGF
210 220 230 240 250
TNMQFLGLAA DAAEAGDHTF ASLISSIQTD ESRHAQQGGP SLKILVENGK
260 270 280 290 300
KDEAQQMVDV AIWRSWKLFS VLTGPIMDYY TPLESRNQSF KEFMLEWIVA
310 320 330 340 350
QFERQLLDLG LDKPWYWDQF MQDLDETHHG MHLGVWYWRP TVWWDPAAGV
360 370 380 390 400
SPEEREWLEE KYPGWNDTWG QCWDVITDNL VNGKPELTVP ETLPTICNMC
410 420 430 440 450
NLPIAHTPGN KWNVKDYQLE YEGRLYHFGS EADRWCFQID PERYKNHTNL
460 470 480 490
VDRFLKGEIQ PADLAGALMY MSLEPGVMGD DAHDYEWVKA YQKKTNAA
Length:498
Mass (Da):57,725
Last modified:November 1, 1998 - v1
Checksum:iE49B0C06D5BB43D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KT935509 Genomic DNA. Translation: ALP69204.1.
AJ005663 Genomic DNA. Translation: CAA06654.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KT935509 Genomic DNA. Translation: ALP69204.1.
AJ005663 Genomic DNA. Translation: CAA06654.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T0QX-ray2.15A1-498[»]
1T0RX-ray2.30A1-498[»]
1T0SX-ray2.20A1-498[»]
2INCX-ray1.85A2-492[»]
2INDX-ray2.20A2-492[»]
2RDBX-ray2.10A1-498[»]
ProteinModelPortaliO87798.
SMRiO87798. Positions 2-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37865N.
IntActiO87798. 2 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO87798.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
IPR007029. YHS_dom.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
PF04945. YHS. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the gene cluster encoding toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1."
    Bertoni G., Martino M., Galli E., Barbieri P.
    Appl. Environ. Microbiol. 64:3626-3632(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: OX1Imported.
  2. "Identification of the Pseudomonas stutzeri OX1 toluene-o-xylene monooxygenase regulatory gene (touR) and of its cognate promoter."
    Arenghi F.L.G., Pinti M., Galli E., Barbieri P.
    Appl. Environ. Microbiol. 65:4057-4063(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: OX1Imported.
  3. Park S.Y., Min B.W.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: OX1Imported.
  4. "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."
    Sazinsky M.H., Bard J., Di Donato A., Lippard S.J.
    J. Biol. Chem. 279:30600-30610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON.
  5. "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."
    McCormick M.S., Sazinsky M.H., Condon K.L., Lippard S.J.
    J. Am. Chem. Soc. 128:15108-15110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-492 IN COMPLEX WITH IRON AND MANGANESE.
  6. "Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase."
    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.
    Biochemistry 46:14795-14809(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IRON.
  7. "Functional redundancy of multicomponent monooxygenase genes is achieved by unified genetic regulation and expression of different catabolic operons in indigenous phenol- and toluene-degrading bacteria."
    Heinaru E., Naanuri E., Joesaar M., Grunbach M., Heinaru A.
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 2A20Imported.

Entry informationi

Entry nameiO87798_PSEST
AccessioniPrimary (citable) accession number: O87798
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.