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MHPC_PARP8
ID   MHPC_PARP8              Reviewed;         288 AA.
AC   B2JQW2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Bphy_4541;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001044; ACC73653.1; -; Genomic_DNA.
DR   RefSeq; WP_012403825.1; NZ_CADFGH010000009.1.
DR   AlphaFoldDB; B2JQW2; -.
DR   SMR; B2JQW2; -.
DR   STRING; 391038.Bphy_4541; -.
DR   ESTHER; burp8-mhpc; Carbon-carbon_bond_hydrolase.
DR   MEROPS; S33.995; -.
DR   EnsemblBacteria; ACC73653; ACC73653; Bphy_4541.
DR   KEGG; bph:Bphy_4541; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020336_13_2_4; -.
DR   OMA; HFRCLVL; -.
DR   OrthoDB; 1119700at2; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000001192; 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..288
FT                   /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT                   oxononatrienedioate hydrolase"
FT                   /id="PRO_1000187011"
FT   DOMAIN          39..274
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT   SITE            115
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT   SITE            193
FT                   /note="Catalytic role in ketonization of the dienol
FT                   substrate (substrate destabilization)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
SQ   SEQUENCE   288 AA;  31760 MW;  16CE8B59FA1D917C CRC64;
     MTDTVTHTEA ATSKYVNVLE GGTELRVHYN DTGAGKETLV LLHGSGPGAS GWANFYRNVD
     AFANAGYRVI LVDCPGWGKS DSIVCTGSRS DLNARVLKGV LDTLGIERAH LVGNSMGGHS
     AVAFALSYPE RVGKLVLMGG GTGGPSQFVP MPTEGIKLLQ GLYRDPTLEN LKKMLNVFVY
     DASTMTEELM QTRLDNMLAR RDHLENFVKS LTANPKQFPD YGHRLNEIKA PALVIWGRDD
     RFVPLDVGLR LVWGLPNAEF HVFGRCGHWA QWEHAERFNQ MLLDFLGQ
 
 
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