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Protein

2-hydroxymuconate tautomerase

Gene

xylH

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Proton acceptor; via imino nitrogen1 Publication

GO - Molecular functioni

  1. isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. toluene catabolic process Source: UniProtKB-UniPathway
  2. xylene catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12750.
RETL1328306-WGS:GSTH-5985-MONOMER.
UniPathwayiUPA00228.
UPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
2-hydroxymuconate tautomerase (EC:5.3.2.6)
Alternative name(s):
4-oxalocrotonate tautomerase
Short name:
4-OT
Gene namesi
Name:xylH
Encoded oniPlasmid TOL pWW00 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 63622-hydroxymuconate tautomerasePRO_0000209514Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Structurei

Secondary structure

1
63
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi14 – 3219Combined sources
Helixi36 – 383Combined sources
Beta strandi40 – 467Combined sources
Helixi48 – 503Combined sources
Helixi58 – 603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/R2-63[»]
4OTBX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L2-63[»]
4OTCX-ray2.28A/B/C/D/E/F/G/H/I2-63[»]
ProteinModelPortaliQ01468.
SMRiQ01468. Positions 2-63.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01468.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR004370. 4-oxalocrotonate_tautomerase.
IPR014347. Tautomerase/MIF_sf.
IPR018191. Tautomerase_Pseudo-typ.
[Graphical view]
PfamiPF01361. Tautomerase. 1 hit.
[Graphical view]
SUPFAMiSSF55331. SSF55331. 1 hit.
TIGRFAMsiTIGR00013. taut. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH
60
FGIGGELASK VRR
Length:63
Mass (Da):6,942
Last modified:January 23, 2007 - v2
Checksum:i23804AB94A126802
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95650 Genomic DNA. Translation: AAA26046.1.
M94186 Genomic DNA. Translation: AAA25694.1.
AJ344068 Genomic DNA. Translation: CAC86799.1.
PIRiA43397.
RefSeqiNP_542859.1. NC_003350.1.
WP_011005902.1. NC_003350.1.

Genome annotation databases

GeneIDi1218749.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95650 Genomic DNA. Translation: AAA26046.1.
M94186 Genomic DNA. Translation: AAA25694.1.
AJ344068 Genomic DNA. Translation: CAC86799.1.
PIRiA43397.
RefSeqiNP_542859.1. NC_003350.1.
WP_011005902.1. NC_003350.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/R2-63[»]
4OTBX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L2-63[»]
4OTCX-ray2.28A/B/C/D/E/F/G/H/I2-63[»]
ProteinModelPortaliQ01468.
SMRiQ01468. Positions 2-63.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1218749.

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00273.
BioCyciMetaCyc:MONOMER-12750.
RETL1328306-WGS:GSTH-5985-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ01468.

Family and domain databases

InterProiIPR004370. 4-oxalocrotonate_tautomerase.
IPR014347. Tautomerase/MIF_sf.
IPR018191. Tautomerase_Pseudo-typ.
[Graphical view]
PfamiPF01361. Tautomerase. 1 hit.
[Graphical view]
SUPFAMiSSF55331. SSF55331. 1 hit.
TIGRFAMsiTIGR00013. taut. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry namei4OT1_PSEPU
AccessioniPrimary (citable) accession number: Q01468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.