ID   BPHD_PSEFK              Reviewed;         286 AA.
AC   Q52011;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
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 furukawaii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=1149133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=DSM 10086 / NBRC 110670 / KF707;
RX   PubMed=10900199; DOI=10.1074/jbc.m003023200;
RA   Watanabe T., Inoue R., Kimura N., Furukawa K.;
RT   "Versatile transcription of biphenyl catabolic bph operon in Pseudomonas
RT   pseudoalcaligenes KF707.";
RL   J. Biol. Chem. 275:31016-31023(2000).
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:10900199}.
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   -!- INDUCTION: By biphenyl. {ECO:0000269|PubMed:10900199}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. BphD family.
CC       {ECO:0000305}.
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DR   EMBL; D85851; BAA12881.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52011; -.
DR   SMR; Q52011; -.
DR   STRING; 1149133.ppKF707_3395; -.
DR   ESTHER; pseps-bphd; 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   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Hydrolase.
FT   CHAIN           1..286
FT                   /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT                   /id="PRO_0000373814"
FT   DOMAIN          36..271
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
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;  31946 MW;  B204AADDC7AD31AA CRC64;
     MTALTESSTS KFVKINEKGF SDFNIHYNEA GNGETVIMLH GGGPGAGGWS NYYRNVGPFV
     DAGYRVILKD SPGFNKSDAV VMDEQRGLVN ARAVKGLMDA LGIDRAHLVG NSMGGATALN
     FAIEYPERIG KLILMGPGGP GPSMFAPMPM EGIKLLFKLY AEPSYENLKQ MIQVFLYDQS
     LITEELLQGR WEAIQRQPEH LKNFLISAQK APLSTWDVTA RLGEIKAKTF ITWGRDDRFV
     PLDHGLKLLW NIDDARLHVF SKCGHWAQWE HADEFNRLAI DFLRQA