Summary: Tautomerase enzyme
This is the Wikipedia entry entitled "4-Oxalocrotonate tautomerase". More...
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4-Oxalocrotonate tautomerase Edit Wikipedia article
4-Oxalocrotonate tautomerase (EC 5.3.2.-4-OT) is an enzyme that converts 2-hydroxymuconate to the αβ-unsaturated ketone, 2-oxo-3-hexenedioate. This enzyme forms part of a bacterial metabolic pathway that oxidatively catabolizes toluene, o-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene into intermediates of the citric acid cycle. With a monomer size of just 62 amino acid residues, the 4-Oxalocrotonate tautomerase is one of the smallest enzyme subunits known. However, in solution, the enzyme forms a hexamer of six identical subunits, so the active site may be formed by amino acid residues from several subunits. This enzyme is also unusual in that it uses a proline residue at the amino terminus as an active site residue.
- Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP (1992). "4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer". J. Biol. Chem. 267 (25): 17716–21. PMID 1339435.
- Whitman CP (2002). "The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a beta-alpha-beta structural motif". Arch. Biochem. Biophys. 402 (1): 1–13. doi:10.1016/S0003-9861(02)00052-8. PMID 12051677.
- Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. (1996) Biochemistry. 35(3):792-802. PMID 8547259
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This clan groups 5-(carboxymethyl)-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate tautomerase (4-OT) with macrophage inhibitory factor (MIF). Interestingly they all share an amino-terminal proline. Members of this clan for homotrimers .
The clan contains the following 6 members:CHMI DUF1904 MIF Tautomerase Tautomerase_2 Tautomerase_3
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This family is new in this Pfam release.
|Seed source:||CATH:3c6vA00, Pfam-B_819 (release 26.0)|
|Number in seed:||157|
|Number in full:||646|
|Average length of the domain:||79.40 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||61.58 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Tautomerase_2 domain has been found. There are 17 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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