PHNPP_EGGLE
ID PHNPP_EGGLE Reviewed; 262 AA.
AC C8WJZ5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase {ECO:0000305};
DE EC=3.1.4.57 {ECO:0000269|PubMed:24147537};
DE AltName: Full=Cyclic phosphate dihydrolase {ECO:0000303|PubMed:24147537};
DE Short=cPDH {ECO:0000303|PubMed:24147537};
GN Name=phnPP {ECO:0000303|PubMed:24147537};
GN OrderedLocusNames=Elen_0235 {ECO:0000312|EMBL:ACV54227.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC
RC 11813 / VPI 0255 / 1899 B;
RX PubMed=24147537; DOI=10.1021/ja409376k;
RA Ghodge S.V., Cummings J.A., Williams H.J., Raushel F.M.;
RT "Discovery of a cyclic phosphodiesterase that catalyzes the sequential
RT hydrolysis of both ester bonds to phosphorus.";
RL J. Am. Chem. Soc. 135:16360-16363(2013).
CC -!- FUNCTION: Involved in degradation of methylphosphonate. Catalyzes the
CC hydrolysis of the phosphate ester at carbon-1 of 5-phospho-D-ribose
CC 1,2-cyclic phosphate to form ribose 2,5-bisphosphate. This intermediate
CC is then hydrolyzed to ribose-5-phosphate and inorganic phosphate.
CC {ECO:0000269|PubMed:24147537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1,2-cyclic phosphate 5-phosphate + H2O = D-
CC ribose 2,5-bisphosphate + H(+); Xref=Rhea:RHEA:41612,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:68687,
CC ChEBI:CHEBI:78345; EC=3.1.4.57;
CC Evidence={ECO:0000269|PubMed:24147537};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribose 2,5-bisphosphate + H2O = D-ribose 5-phosphate +
CC phosphate; Xref=Rhea:RHEA:41616, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:78345, ChEBI:CHEBI:78346; EC=3.1.4.57;
CC Evidence={ECO:0000269|PubMed:24147537};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q7NXD4};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for 5-phospho-alpha-D-ribose 1,2-cyclic phosphate
CC {ECO:0000269|PubMed:24147537};
CC KM=23 uM for D-ribofuranose 2,5-bisphosphate
CC {ECO:0000269|PubMed:24147537};
CC Note=kcat is 2.0 sec(-1) for 5-phospho-alpha-D-ribose 1,2-cyclic
CC phosphate. kcat is 7.4 sec(-1) for D-ribofuranose 2,5-bisphosphate.
CC {ECO:0000269|PubMed:24147537};
CC -!- SIMILARITY: Belongs to the PHP family. {ECO:0000305}.
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; CP001726; ACV54227.1; -; Genomic_DNA.
DR RefSeq; WP_015759891.1; NC_013204.1.
DR AlphaFoldDB; C8WJZ5; -.
DR SMR; C8WJZ5; -.
DR STRING; 479437.Elen_0235; -.
DR EnsemblBacteria; ACV54227; ACV54227; Elen_0235.
DR GeneID; 56791170; -.
DR KEGG; ele:Elen_0235; -.
DR eggNOG; COG0613; Bacteria.
DR HOGENOM; CLU_067347_1_0_11; -.
DR OMA; DGIEVYY; -.
DR OrthoDB; 1309717at2; -.
DR BioCyc; ELEN479437:G1GFY-244-MON; -.
DR BioCyc; MetaCyc:MON-18308; -.
DR BRENDA; 3.1.4.57; 2185.
DR Proteomes; UP000001377; Chromosome.
DR GO; GO:0102560; F:5-phospho-alpha-D-ribose 1,2-cyclic phosphate 1-phosphohydrolase activity; IDA:GO_Central.
DR GO; GO:0102561; F:D-ribose 2,5-bisphosphate 2-phosphohydrolase activity; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..262
FT /note="Phosphoribosyl 1,2-cyclic phosphate 1,2-
FT diphosphodiesterase"
FT /id="PRO_0000430723"
FT BINDING 6
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 38
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
SQ SEQUENCE 262 AA; 28613 MW; 88E6E602FCB79EFC CRC64;
MIEDLHVHST MSDGSDTFEQ VLEQAAQRGV ERLAFTNHDT TAGLTAAREL GERLGVQVVG
GIEVSAYDFE RGRKVHILGL GVEEGAPALA ALCGSTLERR HANSLWQLDR LVEAGYEVDV
ERALELGRAS TCLYKQHLMA ALTSEPYPSA AYRTLYRSLF KNGGICDRDI DYVDARDAVR
VVVEDGGLAV LAHPGQLDSY DLLPDLVECG LGGIERFHPD HTLADHARCA ELAVRYRLVC
TGGSDYHGKF GRVPHVGFRV PA
