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Q01468 (4OT1_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified September 18, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-hydroxymuconate tautomerase

EC=5.3.2.6
Alternative name(s):
4-oxalocrotonate tautomerase
Short name=4-OT
Gene names
Name:xylH
Encoded onPlasmid TOL pWW0
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length63 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate. Ref.1

Catalytic activity

(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate. Ref.1

Pathway

Xenobiotic degradation; toluene degradation.

Xenobiotic degradation; xylene degradation.

Subunit structure

Homohexamer. Ref.4

Sequence similarities

Belongs to the 4-oxalocrotonate tautomerase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological_processtoluene catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

xylene catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 63622-hydroxymuconate tautomerase
PRO_0000209514

Sites

Active site21Proton acceptor; via imino nitrogen Ref.6

Secondary structure

............. 63
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01468 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23804AB94A126802

FASTA636,942
        10         20         30         40         50         60 
MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH FGIGGELASK 


VRR 

« Hide

References

[1]"4-oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer."
Chen L.H., Kenyon G.L., Curtin F., Harayama S., Bembenek M.E., Hajipour G., Whitman C.P.
J. Biol. Chem. 267:17716-17721(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-34, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2.
[2]"Comparison of the nucleotide sequences of the meta-cleavage pathway genes of TOL plasmid pWW0 from Pseudomonas putida with other meta-cleavage genes suggests that both single and multiple nucleotide substitutions contribute to enzyme evolution."
Harayama S., Rekik M.
Mol. Gen. Genet. 239:81-89(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2.
[3]"Complete sequence of the IncP-9 TOL plasmid pWW0 from Pseudomonas putida."
Greated A., Lambertsen L., Williams P.A., Thomas C.M.
Environ. Microbiol. 4:856-871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases."
Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J., Wilson K.S., Wigley D.B.
Biochemistry 35:792-802(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, REACTION MECHANISM.
[5]"Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4-A resolution: analysis and implications for the mechanism of inactivation and catalysis."
Taylor A.B., Czerwinski R.M., Johnson W.H. Jr., Whitman C.P., Hackert M.L.
Biochemistry 37:14692-14700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Strain: ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2.
[6]"Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies."
Stivers J.T., Abeygunawardana C., Mildvan A.S., Hajipour G., Whitman C.P., Chen L.H.
Biochemistry 35:803-813(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95650 Genomic DNA. Translation: AAA26046.1.
M94186 Genomic DNA. Translation: AAA25694.1.
AJ344068 Genomic DNA. Translation: CAC86799.1.
PIRA43397.
RefSeqNP_542859.1. NC_003350.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJPX-ray2.40A/B/C/D/E2-63[»]
2FM7X-ray2.80A/B/C/D/E/F2-62[»]
4OTAX-ray2.75A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R2-62[»]
4OTBX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L2-62[»]
4OTCX-ray2.28A/B/C/D/E/F/G/H/I2-62[»]
ProteinModelPortalQ01468.
SMRQ01468. Positions 2-63.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218749.

Phylogenomic databases

ProtClustDBCLSK899099.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12750.
UniPathwayUPA00228.
UPA00273.

Family and domain databases

InterProIPR004370. 4-oxalocrotonate_tautomerase.
IPR014347. Tautomerase/MIF_sf.
IPR018191. Tautomerase_Pseudo-typ.
[Graphical view]
PfamPF01361. Tautomerase. 1 hit.
[Graphical view]
SUPFAMSSF55331. SSF55331. 1 hit.
TIGRFAMsTIGR00013. taut. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ01468.

Entry information

Entry name4OT1_PSEPU
AccessionPrimary (citable) accession number: Q01468
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: September 18, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways