4OT1_PSEPU
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 03-AUG-2022, entry version 119.
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; Proteobacteria; 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_QWEF01000005.1.
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 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 AlphaFoldDB; Q01468; -.
DR SMR; Q01468; -.
DR DrugBank; DB02005; 2-Oxo-3-Pentenoic Acid.
DR KEGG; ag:AAA26046; -.
DR BioCyc; MetaCyc:MON-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; -; 1.
DR InterPro; IPR004370; 4-oxalocrotonate_tautomerase.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR InterPro; IPR018191; Tautomerase_Pseudo-typ.
DR Pfam; PF01361; Tautomerase; 1.
DR SUPFAM; SSF55331; SSF55331; 1.
DR TIGRFAMs; TIGR00013; taut; 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
