ID CPDB_ECOLI Reviewed; 647 AA. AC P08331; Q2M692; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase; DE EC=3.1.3.6; DE EC=3.1.4.16; DE Flags: Precursor; GN Name=cpdB; OrderedLocusNames=b4213, JW4171; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=3005231; DOI=10.1128/jb.165.3.1002-1010.1986; RA Liu J., Burns D.M., Beacham I.R.; RT "Isolation and sequence analysis of the gene (cpdB) encoding periplasmic RT 2',3'-cyclic phosphodiesterase."; RL J. Bacteriol. 165:1002-1010(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. RC STRAIN=K12; RX PubMed=2172762; DOI=10.1007/bf00283039; RA Liu J., Beacham I.R.; RT "Transcription and regulation of the cpdB gene in Escherichia coli K12 and RT Salmonella typhimurium LT2: evidence for modulation of constitutive RT promoters by cyclic AMP-CRP complex."; RL Mol. Gen. Genet. 222:161-165(1990). RN [6] RP PROTEIN SEQUENCE OF 20-31. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). CC -!- FUNCTION: This bifunctional enzyme catalyzes two consecutive reactions CC during ribonucleic acid degradation. Converts a 2',3'-cyclic nucleotide CC to a 3'-nucleotide and then the 3'-nucleotide to the corresponding CC nucleoside and phosphate. {ECO:0000269|PubMed:3005231}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 3'- CC phosphate + H(+); Xref=Rhea:RHEA:19621, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66949, ChEBI:CHEBI:66954; EC=3.1.4.16; CC Evidence={ECO:0000269|PubMed:3005231}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 3'-phosphate + H2O = a ribonucleoside + CC phosphate; Xref=Rhea:RHEA:10144, ChEBI:CHEBI:13197, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474; EC=3.1.3.6; CC Evidence={ECO:0000269|PubMed:3005231}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:3005231}. CC -!- MISCELLANEOUS: Two kinetically distinguishable active sites for the two CC substrates (2',3'-cyclic nucleotides and 3'-nucleotides) have been CC identified. CC -!- SIMILARITY: Belongs to the 5'-nucleotidase 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; M13464; AAA23597.1; -; Genomic_DNA. DR EMBL; U14003; AAA97109.1; -; Genomic_DNA. DR EMBL; U00096; AAC77170.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78214.1; -; Genomic_DNA. DR EMBL; X54008; CAA37954.1; -; Genomic_DNA. DR PIR; H65232; ESECPC. DR RefSeq; NP_418634.1; NC_000913.3. DR RefSeq; WP_000589431.1; NZ_LN832404.1. DR AlphaFoldDB; P08331; -. DR SMR; P08331; -. DR BioGRID; 4262719; 40. DR DIP; DIP-9311N; -. DR IntAct; P08331; 4. DR STRING; 511145.b4213; -. DR jPOST; P08331; -. DR PaxDb; 511145-b4213; -. DR EnsemblBacteria; AAC77170; AAC77170; b4213. DR GeneID; 75169736; -. DR GeneID; 948729; -. DR KEGG; ecj:JW4171; -. DR KEGG; eco:b4213; -. DR PATRIC; fig|1411691.4.peg.2488; -. DR EchoBASE; EB0158; -. DR eggNOG; COG0737; Bacteria. DR HOGENOM; CLU_005854_4_1_6; -. DR InParanoid; P08331; -. DR OMA; EKAQYPM; -. DR OrthoDB; 9803927at2; -. DR PhylomeDB; P08331; -. DR BioCyc; EcoCyc:CPDB-MONOMER; -. DR BioCyc; MetaCyc:CPDB-MONOMER; -. DR BRENDA; 3.1.3.6; 2026. DR PHI-base; PHI:7020; -. DR PRO; PR:P08331; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IMP:EcoCyc. DR GO; GO:0008254; F:3'-nucleotidase activity; IMP:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki. DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro. DR CDD; cd07410; MPP_CpdB_N; 1. DR Gene3D; 3.60.21.10; -; 1. DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1. DR InterPro; IPR008334; 5'-Nucleotdase_C. DR InterPro; IPR036907; 5'-Nucleotdase_C_sf. DR InterPro; IPR006146; 5'-Nucleotdase_CS. DR InterPro; IPR006179; 5_nucleotidase/apyrase. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR041827; CpdB_N. DR InterPro; IPR006294; Cyc_nuc_PDE_nucleotidase. DR InterPro; IPR029052; Metallo-depent_PP-like. DR NCBIfam; TIGR01390; CycNucDiestase; 1. DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1. DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1. DR Pfam; PF02872; 5_nucleotid_C; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR01607; APYRASEFAMLY. DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1. DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Hydrolase; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Periplasm; Reference proteome; KW Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:9298646" FT CHAIN 20..647 FT /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'- FT nucleotidase" FT /id="PRO_0000000035" FT BINDING 31 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 33 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 76 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 76 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 225 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 257 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 259 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 440 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 544..550 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CONFLICT 316 FT /note="A -> G (in Ref. 1; AAA23597)" FT /evidence="ECO:0000305" FT CONFLICT 528..552 FT /note="GKPIDPNAMFLVATNNYRAYGGKFA -> ASRLIRTPCSWLPPITIALTGQI FT C (in Ref. 1; AAA23597)" FT /evidence="ECO:0000305" SQ SEQUENCE 647 AA; 70832 MW; 4B26DC3563473827 CRC64; MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIN DARNEVKNSV LVDNGDLIQG SPLADYMSAK GLKAGDIHPV YKALNTLDYT VGTLGNHEFN YGLDYLKNAL AGAKFPYVNA NVIDARTKQP MFTPYLIKDT EVVDKDGKKQ TLKIGYIGVV PPQIMGWDKA NLSGKVTVND ITETVRKYVP EMREKGADVV VVLAHSGLSA DPYKVMAENS VYYLSEIPGV NAIMFGHAHA VFPGKDFADI EGADIAKGTL NGVPAVMPGM WGDHLGVVDL QLSNDSGKWQ VTQAKAEARP IYDIANKKSL AAEDSKLVET LKADHDATRQ FVSKPIGKSA DNMYSYLALV QDDPTVQVVN NAQKAYVEHY IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS YVEVEKGQLT FRNAADLYLY PNTLIVVKAS GKEVKEWLEC SAGQFNQIDP NSTKPQSLIN WDGFRTYNFD VIDGVNYQID VTQPARYDGE CQMINANAER IKNLTFNGKP IDPNAMFLVA TNNYRAYGGK FAGTGDSHIA FASPDENRSV LAAWIADESK RAGEIHPAAD NNWRLAPIAG DKKLDIRFET SPSDKAAAFI KEKGQYPMNK VATDDIGFAI YQVDLSK //