MHPC_CUPPJ
ID MHPC_CUPPJ Reviewed; 289 AA.
AC Q476M7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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}; OrderedLocusNames=Reut_A0274;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ59656.1; -; Genomic_DNA.
DR RefSeq; WP_011296464.1; NC_007347.1.
DR AlphaFoldDB; Q476M7; -.
DR SMR; Q476M7; -.
DR STRING; 264198.Reut_A0274; -.
DR ESTHER; cuppj-mhpc; Carbon-carbon_bond_hydrolase.
DR PRIDE; Q476M7; -.
DR EnsemblBacteria; AAZ59656; AAZ59656; Reut_A0274.
DR KEGG; reu:Reut_A0274; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_13_2_4; -.
DR OMA; HFRCLVL; -.
DR OrthoDB; 1119700at2; -.
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..289
FT /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT oxononatrienedioate hydrolase"
FT /id="PRO_0000337787"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 116
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 194
FT /note="Catalytic role in ketonization of the dienol
FT substrate (substrate destabilization)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
SQ SEQUENCE 289 AA; 31460 MW; FBC1A4941AB5F9B0 CRC64;
MQANVQAITE AGTSRFVTVK DGDTEFRIHC NDTGAGAETV VMLHGSGPGA TGWANFNRNV
EPLVAAGYRV LLVDCPGWGK SDPVVNAGSR SELNGRVLKG VLDELDIERV HILGNSMGGH
SAVAFALANP QRVGKLVLMG GGTGGPSLYA PMPTEGIKLL NGLYREPSIE NLKRMMNVFV
YDASSLTDDL MQARLDNMLA RRDHLENFVK SLAANPKQFT DYGSRLGEIT APTLVIWGRD
DRFVPMDVGL RLIAGIPNAQ MHIFNRCGHW AQWEHAKAFN RMVVDFLGN
