ID   XYLI_PSEPU              Reviewed;         264 AA.
AC   P49155;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   10-JUN-2026, entry version 90.
DE   RecName: Full=2-oxo-3-hexenedioate decarboxylase {ECO:0000305};
DE            EC=4.1.1.77 {ECO:0000269|PubMed:2681159};
DE   AltName: Full=4-oxalocrotonate decarboxylase {ECO:0000303|PubMed:2681159};
DE            Short=4-OD {ECO:0000303|PubMed:10651637};
GN   Name=xylI {ECO:0000303|PubMed:2681159};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid TOL pWW0 {ECO:0000303|PubMed:8510667}.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1] {ECO:0000312|EMBL:AAA25693.1}
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   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=2681159; DOI=10.1128/jb.171.11.6251-6258.1989;
RA   Harayama S., Rekik M., Ngai K.L., Ornston L.N.;
RT   "Physically associated enzymes produce and metabolize 2-hydroxy-2,4-
RT   dienoate, a chemically unstable intermediate formed in catechol metabolism
RT   via meta cleavage in Pseudomonas putida.";
RL   J. Bacteriol. 171:6251-6258(1989).
RN   [3]
RP   FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 33015 / DSM 3931 / JCM 6156 / NCIMB 12182 / mt-2;
RX   PubMed=10651637; DOI=10.1021/bi9918902;
RA   Stanley T.M., Johnson W.H. Jr., Burks E.A., Whitman C.P., Hwang C.C.,
RA   Cook P.F.;
RT   "Expression and stereochemical and isotope effect studies of active 4-
RT   oxalocrotonate decarboxylase.";
RL   Biochemistry 39:718-726(2000).
RN   [4]
RP   ERRATUM OF PUBMED:10651637.
RX   PubMed=10727248; DOI=10.1021/bi005106l;
RA   Stanley T.M., Johnson W.H. Jr., Burks E.A., Whitman C.P., Hwang C.C.,
RA   Cook P.F.;
RL   Biochemistry 39:3514-3514(2000).
CC   -!- FUNCTION: Decarboxylase involved in catechol metabolism
CC       (PubMed:10651637, PubMed:2681159). Part of a complex that catalyzes the
CC       conversion of 2-oxohex-3-enedioate to 4-hydroxy-2-oxopentanoate, via
CC       the intermediate 2-hydroxypenta-2,4-dienoate (PubMed:10651637,
CC       PubMed:2681159). This subunit catalyzes the first step, the conversion
CC       of 2-oxohex-3-enedioate to 2-hydroxypenta-2,4-dienoate, which is
CC       unstable and can spontaneously form 2-oxopent-4-enoate
CC       (PubMed:10651637, PubMed:2681159). The enol form of the substrate
CC       cannot be used by the enzyme (PubMed:2681159).
CC       {ECO:0000269|PubMed:10651637, ECO:0000269|PubMed:2681159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3E)-2-oxohex-3-enedioate + H(+) = 2-oxopent-4-enoate + CO2;
CC         Xref=Rhea:RHEA:24260, ChEBI:CHEBI:11641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:64908; EC=4.1.1.77;
CC         Evidence={ECO:0000269|PubMed:2681159};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24261;
CC         Evidence={ECO:0000269|PubMed:2681159};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10651637, ECO:0000269|PubMed:2681159};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:10651637};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for 2-oxohex-3-enedioate {ECO:0000269|PubMed:2681159};
CC         KM=6.6 uM for 2-oxohex-3-enedioate {ECO:0000269|PubMed:10651637};
CC         Vmax=51 umol/min/mg enzyme {ECO:0000269|PubMed:2681159};
CC         Note=kcat is 68 sec(-1). {ECO:0000269|PubMed:10651637};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:2681159};
CC   -!- PATHWAY: Aromatic compound metabolism; catechol degradation.
CC       {ECO:0000305|PubMed:10651637, ECO:0000305|PubMed:2681159}.
CC   -!- SUBUNIT: Part of a complex composed of a decarboxylase (XylI) and an
CC       hydratase (XylJ) (PubMed:10651637, PubMed:2681159). Formation of a
CC       complex between the decarboxylase and the hydratase may assure
CC       efficient transformation of the unstable intermediate in vivo
CC       (PubMed:2681159). {ECO:0000269|PubMed:10651637,
CC       ECO:0000269|PubMed:2681159}.
CC   -!- SIMILARITY: Belongs to the hydratase/decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; M94186; AAA25693.1; -; Genomic_DNA.
DR   PIR; S35224; S35224.
DR   RefSeq; WP_011005903.1; NC_003350.1.
DR   AlphaFoldDB; P49155; -.
DR   SMR; P49155; -.
DR   BioCyc; MetaCyc:MONOMER-12752; -.
DR   UniPathway; UPA00750; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008684; F:2-oxopent-4-enoate hydratase activity; IEA:TreeGrafter.
DR   GO; GO:0047437; F:4-oxalocrotonate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR017630; 4-oxalocrotonate_decarboxylase.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR050772; Hydratase-Decarb/MhpD_sf.
DR   NCBIfam; TIGR03218; catechol_dmpH; 1.
DR   PANTHER; PTHR30143:SF0; 2-KETO-4-PENTENOATE HYDRATASE; 1.
DR   PANTHER; PTHR30143; ACID HYDRATASE; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Lyase; Magnesium; Manganese; Plasmid.
FT   CHAIN           1..264
FT                   /note="2-oxo-3-hexenedioate decarboxylase"
FT                   /id="PRO_0000066054"
SQ   SEQUENCE   264 AA;  28510 MW;  DDF93ACC910722F9 CRC64;
     MNRTLNREQV LALAEHIENA ELQAHDIHKV TNDYPEMTFA DAYTIQWEIR RRKEERGNKI
     VGLKMGLTSW AKMAQMGVET PIYGFLADYF SVPDGGVVDC SKLIHPKIEA EIAVVTKAPL
     VGPGCHIGDV IAAVDYVIPT VEVIDSRYEN FKFDLISVVA DNASSTRYIT GGRMANLEDV
     DLRTLGVVME KNGEVVELGA GAAVLGHPLS SVAMLANLLA ERGEHIPAGT FIMTGGITAA
     VAVAPGDNIT VRYQGLGSVS ARFV
//