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2-hydroxymuconate tautomerase (EC 5.3.2.6) (4-oxalocrotonate tautomerase) (4-OT)

 4OT1_PSEPU              Reviewed;          63 AA.
Q01468;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
15-MAR-2017, entry version 103.
RecName: Full=2-hydroxymuconate tautomerase;
EC=5.3.2.6;
AltName: Full=4-oxalocrotonate tautomerase;
Short=4-OT;
Name=xylH;
Pseudomonas putida (Arthrobacter siderocapsulatus).
Plasmid TOL pWW0.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-34, FUNCTION,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
PubMed=1339435;
Chen L.H., Kenyon G.L., Curtin F., Harayama S., Bembenek M.E.,
Hajipour G., Whitman C.P.;
"4-oxalocrotonate tautomerase, an enzyme composed of 62 amino acid
residues per monomer.";
J. Biol. Chem. 267:17716-17721(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
PubMed=8510667;
Harayama S., Rekik M.;
"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.";
Mol. Gen. Genet. 239:81-89(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12534468; DOI=10.1046/j.1462-2920.2002.00305.x;
Greated A., Lambertsen L., Williams P.A., Thomas C.M.;
"Complete sequence of the IncP-9 TOL plasmid pWW0 from Pseudomonas
putida.";
Environ. Microbiol. 4:856-871(2002).
[4]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND REACTION
MECHANISM.
PubMed=8547259; DOI=10.1021/bi951732k;
Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J.,
Wilson K.S., Wigley D.B.;
"Enzymatic ketonization of 2-hydroxymuconate: specificity and
mechanism investigated by the crystal structures of two isomerases.";
Biochemistry 35:792-802(1996).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
PubMed=9778344; DOI=10.1021/bi981607j;
Taylor A.B., Czerwinski R.M., Johnson W.H. Jr., Whitman C.P.,
Hackert M.L.;
"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.";
Biochemistry 37:14692-14700(1998).
[6]
STRUCTURE BY NMR, AND ACTIVE SITE.
PubMed=8547260; DOI=10.1021/bi951077g;
Stivers J.T., Abeygunawardana C., Mildvan A.S., Hajipour G.,
Whitman C.P., Chen L.H.;
"Catalytic role of the amino-terminal proline in 4-oxalocrotonate
tautomerase: affinity labeling and heteronuclear NMR studies.";
Biochemistry 35:803-813(1996).
-!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate
stereoselectively to yield 2-oxo-3-hexenedioate.
{ECO:0000269|PubMed:1339435}.
-!- CATALYTIC ACTIVITY: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-
2-oxohex-3-enedioate. {ECO:0000269|PubMed:1339435}.
-!- PATHWAY: Xenobiotic degradation; toluene degradation.
-!- PATHWAY: Xenobiotic degradation; xylene degradation.
-!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:8547259}.
-!- SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family.
{ECO:0000305}.
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EMBL; M95650; AAA26046.1; -; Genomic_DNA.
EMBL; M94186; AAA25694.1; -; Genomic_DNA.
EMBL; AJ344068; CAC86799.1; -; Genomic_DNA.
PIR; A43397; A43397.
RefSeq; NP_542859.1; NC_003350.1.
RefSeq; WP_011005902.1; NC_003350.1.
PDB; 1BJP; X-ray; 2.40 A; A/B/C/D/E=2-63.
PDB; 2FM7; X-ray; 2.80 A; A/B/C/D/E/F=2-62.
PDB; 4OTA; X-ray; 2.75 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-63.
PDB; 4OTB; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-63.
PDB; 4OTC; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I=2-63.
PDB; 4X19; X-ray; 1.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=2-63.
PDB; 4X1C; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-63.
PDB; 5CLN; X-ray; 2.71 A; A/B/C/D/E/F/G/H/I/J/K/L=2-58.
PDB; 5CLO; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-60.
PDBsum; 1BJP; -.
PDBsum; 2FM7; -.
PDBsum; 4OTA; -.
PDBsum; 4OTB; -.
PDBsum; 4OTC; -.
PDBsum; 4X19; -.
PDBsum; 4X1C; -.
PDBsum; 5CLN; -.
PDBsum; 5CLO; -.
ProteinModelPortal; Q01468; -.
SMR; Q01468; -.
DrugBank; DB02005; 2-Oxo-3-Pentenoic Acid.
GeneID; 1218749; -.
KEGG; ag:AAA26046; -.
KO; K01821; -.
BioCyc; MetaCyc:MONOMER-12750; -.
UniPathway; UPA00228; -.
UniPathway; UPA00273; -.
EvolutionaryTrace; Q01468; -.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0042184; P:xylene catabolic process; IEA:UniProtKB-UniPathway.
InterPro; IPR004370; 4-oxalocrotonate_tautomerase.
InterPro; IPR014347; Tautomerase/MIF_sf.
InterPro; IPR018191; Tautomerase_Pseudo-typ.
Pfam; PF01361; Tautomerase; 1.
SUPFAM; SSF55331; SSF55331; 1.
TIGRFAMs; TIGR00013; taut; 1.
1: Evidence at protein level;
3D-structure; Aromatic hydrocarbons catabolism;
Direct protein sequencing; Isomerase; Plasmid.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1339435}.
CHAIN 2 63 2-hydroxymuconate tautomerase.
/FTId=PRO_0000209514.
ACT_SITE 2 2 Proton acceptor; via imino nitrogen.
{ECO:0000269|PubMed:8547260}.
STRAND 4 9 {ECO:0000244|PDB:4X1C}.
HELIX 14 32 {ECO:0000244|PDB:4X1C}.
HELIX 36 38 {ECO:0000244|PDB:4X1C}.
STRAND 40 46 {ECO:0000244|PDB:4X1C}.
HELIX 48 50 {ECO:0000244|PDB:4X1C}.
STRAND 51 53 {ECO:0000244|PDB:4X1C}.
HELIX 58 60 {ECO:0000244|PDB:4OTC}.
SEQUENCE 63 AA; 6942 MW; 23804AB94A126802 CRC64;
MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH FGIGGELASK
VRR


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