PHY_EUBRA
ID PHY_EUBRA Reviewed; 274 AA.
AC Q715L4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Phloretin hydrolase {ECO:0000303|PubMed:15466559};
DE EC=3.7.1.4 {ECO:0000269|PubMed:15466559};
GN Name=phy;
OS Eubacterium ramulus.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=39490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15466559; DOI=10.1128/aem.70.10.6131-6137.2004;
RA Schoefer L., Braune A., Blaut M.;
RT "Cloning and expression of a phloretin hydrolase gene from Eubacterium
RT ramulus and characterization of the recombinant enzyme.";
RL Appl. Environ. Microbiol. 70:6131-6137(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Catalyzes the hydrolytic C-C cleavage of phloretin to
CC phloroglucinol and 3-(4-hydroxyphenyl)propionic acid during flavonoid
CC degradation. Also hydrolyzes other C-acylated phenols.
CC {ECO:0000269|PubMed:15466559}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate;
CC Xref=Rhea:RHEA:23396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16204, ChEBI:CHEBI:16331, ChEBI:CHEBI:17276; EC=3.7.1.4;
CC Evidence={ECO:0000269|PubMed:15466559};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q4K423};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for phloretin {ECO:0000269|PubMed:15466559};
CC Note=kcat is 10 sec(-1) for phloretin. {ECO:0000269|PubMed:15466559};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15466559};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15466559};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15466559}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15466559}.
CC -!- SIMILARITY: Belongs to the DAPG/phloretin hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AF548616; AAQ12341.1; -; Genomic_DNA.
DR STRING; 39490.ERS852448_03037; -.
DR KEGG; ag:AAQ12341; -.
DR BRENDA; 3.7.1.4; 17131.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050180; F:phloretin hydrolase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0046275; P:flavonoid catabolic process; IDA:UniProtKB.
DR InterPro; IPR041526; DAPG_hydrolase.
DR Pfam; PF18089; DAPG_hydrolase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..274
FT /note="Phloretin hydrolase"
FT /id="PRO_0000430447"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4K423"
SQ SEQUENCE 274 AA; 30923 MW; FB19CA698ACE3297 CRC64;
MEEDFNMSTP GVKVGVXEEE KKLSYYKYYE QDLAPVPAEK IAILQGGPIA PEKCIPFDER
NKFLKGEDDE YANIGFGVAA DGTALVCNTT YMPGVTGEML DWWFPWHSVG SDLRYKIWDP
EDHYFARAYP ASYVVDPNVP MNQKTWGVDH YIMEDVGPGP EFLKLCFKRP ADFGYDESII
GTEKCESLVC AIGESSCAAA MTHKWHPYKD GVLFESRFWI GYRIDEEGNI VKAIPEGVSI
PPFVPQGLFA HNIKEFTNLA AILPTLYAEE KDTF