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}.
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; 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