ID   4OT1_PSEPU              Reviewed;          63 AA.
AC   Q01468;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=2-hydroxymuconate tautomerase;
DE            EC=5.3.2.6;
DE   AltName: Full=4-oxalocrotonate tautomerase;
DE            Short=4-OT;
GN   Name=xylH;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid TOL pWW0.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-34, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=1339435; DOI=10.1016/s0021-9258(19)37101-7;
RA   Chen L.H., Kenyon G.L., Curtin F., Harayama S., Bembenek M.E., Hajipour G.,
RA   Whitman C.P.;
RT   "4-oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues
RT   per monomer.";
RL   J. Biol. Chem. 267:17716-17721(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=8510667; DOI=10.1007/bf00281605;
RA   Harayama S., Rekik M.;
RT   "Comparison of the nucleotide sequences of the meta-cleavage pathway genes
RT   of TOL plasmid pWW0 from Pseudomonas putida with other meta-cleavage genes
RT   suggests that both single and multiple nucleotide substitutions contribute
RT   to enzyme evolution.";
RL   Mol. Gen. Genet. 239:81-89(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12534468; DOI=10.1046/j.1462-2920.2002.00305.x;
RA   Greated A., Lambertsen L., Williams P.A., Thomas C.M.;
RT   "Complete sequence of the IncP-9 TOL plasmid pWW0 from Pseudomonas
RT   putida.";
RL   Environ. Microbiol. 4:856-871(2002).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=8547259; DOI=10.1021/bi951732k;
RA   Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J.,
RA   Wilson K.S., Wigley D.B.;
RT   "Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism
RT   investigated by the crystal structures of two isomerases.";
RL   Biochemistry 35:792-802(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=9778344; DOI=10.1021/bi981607j;
RA   Taylor A.B., Czerwinski R.M., Johnson W.H. Jr., Whitman C.P., Hackert M.L.;
RT   "Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-
RT   pentynoate at 2.4-A resolution: analysis and implications for the mechanism
RT   of inactivation and catalysis.";
RL   Biochemistry 37:14692-14700(1998).
RN   [6]
RP   STRUCTURE BY NMR, AND ACTIVE SITE.
RX   PubMed=8547260; DOI=10.1021/bi951077g;
RA   Stivers J.T., Abeygunawardana C., Mildvan A.S., Hajipour G., Whitman C.P.,
RA   Chen L.H.;
RT   "Catalytic role of the amino-terminal proline in 4-oxalocrotonate
RT   tautomerase: affinity labeling and heteronuclear NMR studies.";
RL   Biochemistry 35:803-813(1996).
CC   -!- FUNCTION: Catalyzes the ketonization of 2-hydroxymuconate
CC       stereoselectively to yield 2-oxo-3-hexenedioate.
CC       {ECO:0000269|PubMed:1339435}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-
CC         enedioate; Xref=Rhea:RHEA:33431, ChEBI:CHEBI:28080,
CC         ChEBI:CHEBI:64908; EC=5.3.2.6; Evidence={ECO:0000269|PubMed:1339435};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC   -!- PATHWAY: Xenobiotic degradation; xylene degradation.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:8547259}.
CC   -!- SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family.
CC       {ECO:0000305}.
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DR   EMBL; M95650; AAA26046.1; -; Genomic_DNA.
DR   EMBL; M94186; AAA25694.1; -; Genomic_DNA.
DR   EMBL; AJ344068; CAC86799.1; -; Genomic_DNA.
DR   PIR; A43397; A43397.
DR   RefSeq; NP_542859.1; NC_003350.1.
DR   RefSeq; WP_011005902.1; NZ_LT852425.1.
DR   PDB; 1BJP; X-ray; 2.40 A; A/B/C/D/E=2-63.
DR   PDB; 2FM7; X-ray; 2.80 A; A/B/C/D/E/F=2-62.
DR   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.
DR   PDB; 4OTB; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-63.
DR   PDB; 4OTC; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I=2-63.
DR   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.
DR   PDB; 4X1C; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-63.
DR   PDB; 5CLN; X-ray; 2.71 A; A/B/C/D/E/F/G/H/I/J/K/L=2-58.
DR   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.
DR   PDB; 5TIG; X-ray; 2.70 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.
DR   PDB; 6BGN; X-ray; 1.51 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=2-61.
DR   PDB; 6FPS; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-63.
DR   PDB; 6GHW; X-ray; 2.30 A; A/B/C=2-63.
DR   PDB; 7PUO; X-ray; 2.35 A; A/B/C/D/E/F=2-63.
DR   PDBsum; 1BJP; -.
DR   PDBsum; 2FM7; -.
DR   PDBsum; 4OTA; -.
DR   PDBsum; 4OTB; -.
DR   PDBsum; 4OTC; -.
DR   PDBsum; 4X19; -.
DR   PDBsum; 4X1C; -.
DR   PDBsum; 5CLN; -.
DR   PDBsum; 5CLO; -.
DR   PDBsum; 5TIG; -.
DR   PDBsum; 6BGN; -.
DR   PDBsum; 6FPS; -.
DR   PDBsum; 6GHW; -.
DR   PDBsum; 7PUO; -.
DR   AlphaFoldDB; Q01468; -.
DR   SMR; Q01468; -.
DR   DrugBank; DB02005; 2-Oxo-3-Pentenoic Acid.
DR   KEGG; ag:AAA26046; -.
DR   BioCyc; MetaCyc:MONOMER-12750; -.
DR   BRENDA; 5.3.2.6; 5092.
DR   SABIO-RK; Q01468; -.
DR   UniPathway; UPA00228; -.
DR   UniPathway; UPA00273; -.
DR   EvolutionaryTrace; Q01468; -.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042184; P:xylene catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00491; 4Oxalocrotonate_Tautomerase; 1.
DR   Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR   InterPro; IPR018191; 4-OT.
DR   InterPro; IPR004370; 4-OT-like_dom.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   NCBIfam; TIGR00013; taut; 1.
DR   PANTHER; PTHR35530:SF1; TAUTOMERASE BSL7456-RELATED; 1.
DR   PANTHER; PTHR35530; TAUTOMERASE-RELATED; 1.
DR   Pfam; PF01361; Tautomerase; 1.
DR   SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   Isomerase; Plasmid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1339435"
FT   CHAIN           2..63
FT                   /note="2-hydroxymuconate tautomerase"
FT                   /id="PRO_0000209514"
FT   ACT_SITE        2
FT                   /note="Proton acceptor; via imino nitrogen"
FT                   /evidence="ECO:0000269|PubMed:8547260"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:6BGN"
FT   HELIX           14..32
FT                   /evidence="ECO:0007829|PDB:6BGN"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:6BGN"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:6BGN"
FT   HELIX           48..50
FT                   /evidence="ECO:0007829|PDB:6BGN"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:4X1C"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:4OTC"
SQ   SEQUENCE   63 AA;  6942 MW;  23804AB94A126802 CRC64;
     MPIAQIHILE GRSDEQKETL IREVSEAISR SLDAPLTSVR VIITEMAKGH FGIGGELASK
     VRR
//