MHPC_PSESP
ID MHPC_PSESP Reviewed; 283 AA.
AC Q52532;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase {ECO:0000255|HAMAP-Rule:MF_01654};
DE EC=3.7.1.14 {ECO:0000255|HAMAP-Rule:MF_01654};
DE AltName: Full=2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase {ECO:0000255|HAMAP-Rule:MF_01654};
DE AltName: Full=2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase {ECO:0000255|HAMAP-Rule:MF_01654};
DE AltName: Full=2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase {ECO:0000255|HAMAP-Rule:MF_01654};
GN Name=mhpC {ECO:0000255|HAMAP-Rule:MF_01654}; Synonyms=pcbD;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8572703; DOI=10.1128/aem.62.1.262-265.1996;
RA Kim E., Kim Y., Kim C.K.;
RT "Genetic structures of the genes encoding 2,3-dihydroxybiphenyl 1,2-
RT dioxygenase and 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase
RT from biphenyl- and 4-chlorobiphenyl-degrading Pseudomonas sp. strain DJ-
RT 12.";
RL Appl. Environ. Microbiol. 62:262-265(1996).
CC -!- FUNCTION: Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-
CC oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring
CC fission product of the bacterial meta-cleavage pathway for degradation
CC of phenylpropionic acid. {ECO:0000255|HAMAP-Rule:MF_01654}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01654};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01654};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01654}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01654}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MhpC family.
CC {ECO:0000255|HAMAP-Rule:MF_01654}.
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DR EMBL; D44550; BAA07955.1; -; Genomic_DNA.
DR AlphaFoldDB; Q52532; -.
DR SMR; Q52532; -.
DR ESTHER; psesp-pcbD; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.016; -.
DR UniPathway; UPA00714; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01654; MhpC; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR023791; MhpC_alpha/beta_hydrolase.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase.
FT CHAIN 1..283
FT /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT oxononatrienedioate hydrolase"
FT /id="PRO_0000337786"
FT DOMAIN 35..269
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 111
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 189
FT /note="Catalytic role in ketonization of the dienol
FT substrate (substrate destabilization)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
SQ SEQUENCE 283 AA; 31032 MW; 6C493751B1E8C4CA CRC64;
MSAITEAGSS KFIDVTEGEI NGSIHVNDAG NGDEVVVMFH GSGPGASGWS NFHRNVDAFV
DAGYRVLLID SPGFNKSYPI VTKSRDGAYA QAAKGVMDKL GIKRAHMIGN SMGGATAMRM
AVDYPEMVGK LVMMGGGSVG GSTTTPMPTE GLKLLQGLYR NPSMENLRKM LDIFVYAPST
LTEELINGRF ENMMRRPEHL TNFVESLKAS GGRANYAHLL PTLTMPTMII WGRDDRFVPL
DLGLRMLWGM PDAELHVFSK CGHWAQWEHA DKFNQLVLNF LAR
