BPHD_BURCE
ID BPHD_BURCE Reviewed; 286 AA.
AC Q2VLB9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Burkholderia cepacia (Pseudomonas cepacia).
OG Plasmid pIJB1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2a;
RA Sebastianelli A., Bruce I.J.;
RL Submitted (APR-2005) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ065837; AAZ08181.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2VLB9; -.
DR SMR; Q2VLB9; -.
DR ESTHER; burce-bphd; Carbon-carbon_bond_hydrolase.
DR SABIO-RK; Q2VLB9; -.
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; IPR017727; HOPD_hydrolase_BphD.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03343; biphenyl_bphD; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Hydrolase; Plasmid.
FT CHAIN 1..286
FT /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT /id="PRO_0000337774"
FT DOMAIN 36..271
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
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; 31345 MW; F580A6405A7A127A CRC64;
MTELSESTTS KFVTINEKGL SNFRIHLNDA GQGEAVIMLH GGGPGAGGWS NYYRNIGPFV
AAGYRVILPD APGFNKSDAV VMDEQRGLVN ARAVKGMMDA LGIDKAHLVG NSMGGAGALN
FALEYPERTG KVILMGPGGL GASLFNPMPM EGIKLLFKLY AEPSLETLKQ MLNVFMFDQS
LITDELLQGR WANIQRNPEH LKNFILSAQK VPLSAWDVSP RLGEIKAKTL VTWGRDDRFV
PLDHGLKLVA NMPDAQLHVF PRCGHWAQWE HADAFNRLTL DFLANG
