BPHD_COMTE
ID BPHD_COMTE Reviewed; 286 AA.
AC Q59324;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
DE Short=HOPDA hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
DE EC=3.7.1.8 {ECO:0000255|HAMAP-Rule:MF_01688};
DE AltName: Full=2,6-dioxo-6-phenylhexa-3-enoate hydrolase {ECO:0000255|HAMAP-Rule:MF_01688};
GN Name=bphD {ECO:0000255|HAMAP-Rule:MF_01688};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B-356;
RA Ahmad D.;
RT "Sequence of BPHDD.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-
CC 6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-
CC hydroxy-2,4-pentadienoic acid (HPD). {ECO:0000255|HAMAP-Rule:MF_01688}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6-dioxo-6-phenylhexa-3-enoate + H2O = 2-oxopent-4-enoate +
CC benzoate + H(+); Xref=Rhea:RHEA:17161, ChEBI:CHEBI:11641,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150,
CC ChEBI:CHEBI:64675; EC=3.7.1.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01688};
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 4/4. {ECO:0000255|HAMAP-
CC Rule:MF_01688}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01688}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. BphD family.
CC {ECO:0000255|HAMAP-Rule:MF_01688}.
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DR EMBL; L34338; AAA56853.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59324; -.
DR SMR; Q59324; -.
DR ESTHER; comte-bphD; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.016; -.
DR BRENDA; 3.7.1.8; 1590.
DR UniPathway; UPA00155; UER00253.
DR GO; GO:0018774; F:2,6-dioxo-6-phenylhexa-3-enoate 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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01688; Biphenyl_BphD; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR017727; HOPD_hydrolase_BphD.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03343; biphenyl_bphD; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase.
FT CHAIN 1..286
FT /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT /id="PRO_0000373811"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
FT SITE 112
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01688"
SQ SEQUENCE 286 AA; 31951 MW; D1A1A7F3D59439B0 CRC64;
MTELTEGNTS KFAKISEKDL SDFLIHYNEA GEGEAVIMLH GGGPGAGGWS NYYRNIGPFV
DAGYRVILKD SPGFNKSDVV VMDEQRGLVN ARAVKGLMDA LGIERAHLVG NSMGGATALN
FAIEYPERLG KMILMGPGGL GASHFAPMPM EGIKLLFKLY AEPSYETLRQ MIQVFLYDQT
NITEELLQGR WEAIQRNPEH LKNFLVSAQR APLSSWDVSP RLGEIKAKTL VTWGRDDRFV
PLDHGLKLVW GIGDARLHVF SQCGHWAQWE KADEFNRLAI DFLRQR
