BPHD_PSES1
ID BPHD_PSES1 Reviewed; 286 AA.
AC P17548;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 78.
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 Pseudomonas sp. (strain KKS102).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33, AND FUNCTION.
RX PubMed=2540155; DOI=10.1128/jb.171.5.2740-2747.1989;
RA Kimbara K., Hashimoto T., Fukuda M., Koana T., Takagi M., Oishi M.,
RA Yano K.;
RT "Cloning and sequencing of two tandem genes involved in degradation of 2,3-
RT dihydroxybiphenyl to benzoic acid in the polychlorinated biphenyl-degrading
RT soil bacterium Pseudomonas sp. strain KKS102.";
RL J. Bacteriol. 171:2740-2747(1989).
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 ECO:0000269|PubMed:2540155}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA25751.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M26433; AAA25751.1; ALT_FRAME; Genomic_DNA.
DR PIR; B32312; ESPSSK.
DR AlphaFoldDB; P17548; -.
DR SMR; P17548; -.
DR ESTHER; psesl-bphD; Carbon-carbon_bond_hydrolase.
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; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03343; biphenyl_bphD; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Hydrolase.
FT CHAIN 1..286
FT /note="2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase"
FT /id="PRO_0000207053"
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; 31589 MW; 4A4D74EC718042A7 CRC64;
MSELNESSTS KFVTINEKGL SNFRIHLNDA GQGERVIMLH GGGPGAGGWS NYYRNIGPFV
EAGYRVLLPD APGFNKSDTV VMDEQRGLVN ARSVKGMMDV LGIEKAHLVG NSMGGAGALN
FALEYPERTG KLILMGPGGL GNSLFTAMPM EGIKLLFKLY AEPSLETLKQ MLNVFLFDQS
VITDELLQGR WANIQRNPEH LKNFILSAQK VPLSAWDVSA RLGEIKAKTL VTWGRDDRFV
PLDHGLKLIA NMQDAHVHVF PRCAHWAQWE HADAFNRLTL DFLANG
