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BPHD_POLNA
ID   BPHD_POLNA              Reviewed;         286 AA.
AC   A1VUV0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=Pnap_4141;
OS   Polaromonas naphthalenivorans (strain CJ2).
OG   Plasmid pPNAP01.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000530; ABM39428.1; -; Genomic_DNA.
DR   RefSeq; WP_011797807.1; NC_008757.1.
DR   AlphaFoldDB; A1VUV0; -.
DR   SMR; A1VUV0; -.
DR   ESTHER; polna-bphd; Carbon-carbon_bond_hydrolase.
DR   MEROPS; S33.016; -.
DR   EnsemblBacteria; ABM39428; ABM39428; Pnap_4141.
DR   KEGG; pna:Pnap_4141; -.
DR   HOGENOM; CLU_020336_13_2_4; -.
DR   OMA; YWAMMHK; -.
DR   OrthoDB; 1119700at2; -.
DR   UniPathway; UPA00155; UER00253.
DR   Proteomes; UP000000644; Plasmid pPNAP01.
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; Plasmid; Reference proteome.
FT   CHAIN           1..286
FT                   /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT                   /id="PRO_0000373813"
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;  31932 MW;  4512D4B9E600948F CRC64;
     MTALTESSTS KFVKINEKGF SDFQIHYNEA GNGETVIMLH GGGPGAGGWS NYYRNIGAFV
     EAGYRVILKD SPGFNKSDAV VMDEQRGLVN ARAVKGLMDA LDIDRAHLVG NSMGGATALN
     FALEYPDRIG KLILMGPGGL GPSMFAPMPM EGIKLLFKLY AEPSYETLKQ MLQVFLYDQS
     LITEELLQGR WEAIQRNPEH LKNFLVSAQK APLSTWDVSA RLGEIKAKTF ITWGRDDRFV
     PLDHGLKLVW GINDARLHVF SKCGHWAQWE HADEFNRLVI DFLRHA
 
 
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