MHPC2_PSEPU
ID MHPC2_PSEPU Reviewed; 286 AA.
AC Q400K3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01654};
DE AltName: Full=2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01654};
DE AltName: Full=2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01654};
GN Name=mhpC2 {ECO:0000255|HAMAP-Rule:MF_01654}; Synonyms=orcC;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ORC;
RA Straganz G.D., Glieder A., Steiner W.;
RT "Cloning of genes involved in meta-cleavage pathways of Pseudomonas putida
RT orc: nucleotide sequences of genes, characterization of two dioxygenases
RT and identification of the orcinol pathway.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF534914; AAQ10535.1; -; Genomic_DNA.
DR AlphaFoldDB; Q400K3; -.
DR SMR; Q400K3; -.
DR ESTHER; psepu-mhpc2; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.995; -.
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; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR023791; MhpC_alpha/beta_hydrolase.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase.
FT CHAIN 1..286
FT /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT oxononatrienedioate hydrolase 2"
FT /id="PRO_0000337785"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 113
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 191
FT /note="Catalytic role in ketonization of the dienol
FT substrate (substrate destabilization)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
SQ SEQUENCE 286 AA; 31493 MW; D31D5455D5C3381E CRC64;
MTIDISEASS SRFARIREGE LDLQLHYNDL GEGAETVVML HGSGPGASGW ANFSRNLEPL
LAAGYRVVLM DCPGWSKSDP IVCRSSRSDL NATALKGLLD MLGLERVHIL GNSMGAHSAV
AFALANPRRV GKLVLMGGGT GGASPFVPMP TEGIKLLNGL YREPTIDNLK KMMNVFVYDA
SDLTEELFQT RLDNMLSRHE HLDNFVESLA ANPRQFPDFG SRLAEIQAPT LIVWGRNDRF
VPMDAGLRLL AGIPNSSLHV FNNCGHWAQW EHAEPFNRLV LDFLQH