MHPC_ECODH
ID MHPC_ECODH Reviewed; 288 AA.
AC B1XBJ6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=ECDH10B_1361;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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 -!- SEQUENCE CAUTION:
CC Sequence=ACB02466.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000948; ACB02466.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000121907.1; NC_010473.1.
DR AlphaFoldDB; B1XBJ6; -.
DR SMR; B1XBJ6; -.
DR ESTHER; ecoli-mhpc; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.995; -.
DR KEGG; ecd:ECDH10B_1361; -.
DR HOGENOM; CLU_020336_13_2_6; -.
DR BioCyc; ECOL316385:ECDH10B_RS06995-MON; -.
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..288
FT /note="2-hydroxy-6-oxononadienedioate/2-hydroxy-6-
FT oxononatrienedioate hydrolase"
FT /id="PRO_1000187016"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 114
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01654"
FT SITE 192
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; 31937 MW; 8F7E5ADE584A45BA CRC64;
MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG WANFSRNIDP
LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV DQLDIAKIHL LGNSMGGHSS
VAFTLKWPER VGKLVLMGGG TGGMSLFTPM PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD
TSDLTDALFE ARLNNMLSRR DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR
FVPMDAGLRL LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP
