BPHD_PSEPU
ID BPHD_PSEPU Reviewed; 286 AA.
AC Q52036;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase;
DE Short=HOPDA hydrolase;
DE EC=3.7.1.8;
DE AltName: Full=2,6-dioxo-6-phenylhexa-3-enoate hydrolase;
GN Name=bphD;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2105297; DOI=10.1128/jb.172.2.1160-1164.1990;
RA Hayase N., Taira K., Furukawa K.;
RT "Pseudomonas putida KF715 bphABCD operon encoding biphenyl and
RT polychlorinated biphenyl degradation: cloning, analysis, and expression in
RT soil bacteria.";
RL J. Bacteriol. 172:1160-1164(1990).
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:0000269|PubMed:2105297}.
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;
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. BphD family.
CC {ECO:0000305}.
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DR EMBL; M33813; AAA25757.1; -; Genomic_DNA.
DR PIR; C35124; C35124.
DR RefSeq; WP_062538125.1; NZ_AP015030.1.
DR AlphaFoldDB; Q52036; -.
DR SMR; Q52036; -.
DR ESTHER; psepu-bph; Carbon-carbon_bond_hydrolase.
DR MEROPS; S33.016; -.
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; PF12697; Abhydrolase_6; 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_0000373815"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 42..43
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 31952 MW; 7B80919E31A73AE7 CRC64;
MTALTESSTS KFLNIKEKGL SDFKIHYNEA GNGETVIMLH GGGPGAGGWS NYYRNIGPFV
EAGYRVILKD SPGFNKSDAV VMDEQRGLVN ARAVKGLMDA LGIDRAHLVG NSMGGATALN
FAIEYPDRIG KLILMGPGGL GPSMFAPMPL EGIKLLFKLY AEPSYENLKQ MIQVFLYDQS
LITEELLQGR WEAIQRQPEH LKNFLISAQK APLSTWDVTA RLGEIKAKTF ITWGRDDRFV
PLDHGLKLLW NIDDARLHVF SKCGHWAQWE HADEFNRLAI DFLRQA
