ID   MHPC_COMTE              Reviewed;         286 AA.
AC   Q8KZP5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase;
DE            EC=3.7.1.14;
DE   AltName: Full=2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase;
DE   AltName: Full=2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase;
DE   AltName: Full=2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase;
GN   Name=mhpC; Synonyms=bphD;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TK102;
RX   PubMed=12324361; DOI=10.1128/aem.68.10.5104-5112.2002;
RA   Hiraoka Y., Yamada T., Tone K., Futaesaku Y., Kimbara K.;
RT   "Flow cytometry analysis of changes in the DNA content of the
RT   polychlorinated biphenyl degrader Comamonas testosteroni TK102: effect of
RT   metabolites on cell-cell separation.";
RL   Appl. Environ. Microbiol. 68:5104-5112(2002).
RN   [2]
RP   FUNCTION IN CATABOLISM OF 2-HYDROXY-6-OXONONADIENEDIOATE, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=TA441;
RX   PubMed=10537203; DOI=10.1099/00221287-145-10-2813;
RA   Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.;
RT   "Genetic organization and characteristics of the 3-(3-
RT   hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni
RT   TA441.";
RL   Microbiology 145:2813-2820(1999).
CC   -!- FUNCTION: Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-
CC       oxononadienedioate, and probably also 2-hydroxy-6-oxononatrienedioate,
CC       a dienol ring fission product of the bacterial meta-cleavage pathway
CC       for degradation of phenylpropionic acid. {ECO:0000269|PubMed:10537203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H2O = (2Z)-2-
CC         hydroxypenta-2,4-dienoate + H(+) + succinate; Xref=Rhea:RHEA:34187,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:66887, ChEBI:CHEBI:67152; EC=3.7.1.14;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H2O =
CC         (2Z)-2-hydroxypenta-2,4-dienoate + fumarate + H(+);
CC         Xref=Rhea:RHEA:34191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29806, ChEBI:CHEBI:66888, ChEBI:CHEBI:67152; EC=3.7.1.14;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=5.8 umol/min/mg enzyme with 3-(2,3-dihydroxyphenyl)propanoate
CC         (at pH 7.5) {ECO:0000269|PubMed:10537203};
CC         Vmax=0.4 umol/min/mg enzyme withd 3-methylcatechol (at pH 7.5)
CC         {ECO:0000269|PubMed:10537203};
CC         Vmax=0.1 umol/min/mg enzyme withd 2,3-dihydroxybiphenyl (at pH 7.5)
CC         {ECO:0000269|PubMed:10537203};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. BphD family.
CC       {ECO:0000305}.
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DR   EMBL; AB086835; BAC01057.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KZP5; -.
DR   SMR; Q8KZP5; -.
DR   ESTHER; comte-mhpC; Carbon-carbon_bond_hydrolase.
DR   MEROPS; S33.016; -.
DR   UniPathway; UPA00714; -.
DR   GO; GO:0052823; F:2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018771; F:2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01688; Biphenyl_BphD; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR017727; HOPD_hydrolase_BphD.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03343; biphenyl_bphD; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Hydrolase.
FT   CHAIN           1..286
FT                   /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT                   oxononatrienedioate hydrolase"
FT                   /id="PRO_0000337777"
FT   DOMAIN          36..271
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   SITE            112
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            190
FT                   /note="Catalytic role in ketonization of the dienol
FT                   substrate (substrate destabilization)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31570 MW;  48C004831FAA9800 CRC64;
     MSELNESTTS KFVTINEKGL SNFRIHLNDA GEGEAVIMLH GGGPGAGGWS NYYRNIGPFV
     KAGYRVILQD APGFNKSDTV VMDEQRGLVN ARSVKGMMDV LGIEKAHLVG NSMGGAGALN
     FALEYPERTG KLILMGPGGL GNSLFTAMPM EGIKLLFKLY AEPSLDTLKQ MLNVFLFDQS
     LITDELVQGR WANIQRNPEH LKNFLLSSQK LPLSSWNVSP RMGEIKAKTL VTWGRDDRFV
     PLDHGLKLVA NMPDAQLHVF PRCGHWAQWE HADAFNRLTL DFLANG