MHPC_PARXL
ID MHPC_PARXL Reviewed; 289 AA.
AC Q13QH4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=Bxeno_B0697;
GN ORFNames=Bxe_B2323;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE33665.1; -; Genomic_DNA.
DR RefSeq; WP_011491025.1; NZ_CP008762.1.
DR AlphaFoldDB; Q13QH4; -.
DR SMR; Q13QH4; -.
DR STRING; 266265.Bxe_B2323; -.
DR ESTHER; burxl-mhpc; Carbon-carbon_bond_hydrolase.
DR EnsemblBacteria; ABE33665; ABE33665; Bxe_B2323.
DR KEGG; bxb:DR64_4655; -.
DR KEGG; bxe:Bxe_B2323; -.
DR PATRIC; fig|266265.5.peg.5389; -.
DR eggNOG; COG1073; Bacteria.
DR OMA; HFRCLVL; -.
DR OrthoDB; 1119700at2; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000001817; Chromosome 2.
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; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase; Reference proteome.
FT CHAIN 1..289
FT /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT oxononatrienedioate hydrolase"
FT /id="PRO_0000337776"
FT DOMAIN 39..275
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
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; 31587 MW; 5EB5DE4809B1A090 CRC64;
MTSNVSAITE ASTSKFVRIK EGDGEVQLHY NDAGQGAETV VMLHGSGPGA SGWANFNRNV
EPLVAAGYRV ILLDCLGWSK SDPVVCDGSR SELNARSLKG LLDALDIERV HIIGNSMGGH
SAVAFALANP QRVGKLVLMG GGTGGPSQFV PMPTEGIKLL QGLYREPTID NLKRMMNVFV
FDASALTDDL MQARLDNMLA RRDHLENFVK SLAANPKQFN DFGPRLGEIA APTLVIWGRD
DRFVPMDVGL RLVAGMQNAE MHIFSRCGHW AQWEHAEKFN RMVVDFLAH
