ID CPDB_HAEIN Reviewed; 657 AA. AC P44764; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 149. 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=HI_0583; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 (By similarity). {ECO:0000250}. 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 -!- 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 -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. 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; L42023; AAC22242.1; -; Genomic_DNA. DR PIR; A64079; A64079. DR RefSeq; NP_438741.1; NC_000907.1. DR AlphaFoldDB; P44764; -. DR SMR; P44764; -. DR STRING; 71421.HI_0583; -. DR DNASU; 949588; -. DR EnsemblBacteria; AAC22242; AAC22242; HI_0583. DR KEGG; hin:HI_0583; -. DR PATRIC; fig|71421.8.peg.604; -. DR eggNOG; COG0737; Bacteria. DR HOGENOM; CLU_005854_4_1_6; -. DR OrthoDB; 9803927at2; -. DR PhylomeDB; P44764; -. DR BioCyc; HINF71421:G1GJ1-596-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0008254; F:3'-nucleotidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Hydrolase; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Periplasm; Reference proteome; Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..657 FT /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'- FT nucleotidase" FT /id="PRO_0000000037" FT BINDING 41 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 43 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 86 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 126 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 235 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 267 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 269 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 450 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 554..559 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 657 AA; 72763 MW; 201CAAB415014499 CRC64; MMNRRHFIQI SATSILALSA NRFAMAKGKS DVDLRIVATT DVHSFLTDFD YYKDAPTDKF GFTRAASLIR QARAEVKNSV LVDNGDLIQG NPIADYQAAQ GYKEGKSNPA IDCLNAMNYE VGTLGNHEFN YGLNYLADAI KQAKFPIVNS NVVKAGTEEP YFTPYVIQEK SVVDNQGKTH KLKIGYIGFV PPQIMVWDKA NLQGKVETRD IVKTAQKYVP EMKKKGADIV VALAHTGPSD EPYQEGAENS AFYLADVPHI DAVIFGHSHR LFPNKEFAKS PNADIVNGTV KGIPESMAGY WANNISVVDL GLTEHKGKWI VTSGKAVLRP IYDIETKKAL AKNDPEITAL LKPVHEATRK YVSQPIGKAT DNMYSYLALL QDDPTIQIVN QAQKAYVEKV APSIAAMAGL PILSAGAPFK AGGRKNDPTG YTEVNKGKLT FRNAADLYLY PNTLVVVKAT GEQLKEWLEC SAGMFKQIDP TSDKPQSLID WEGFRTYNFD VIDGVNYEYD LTKPARYDGE CKLINPESHR VVNLTYQGKP VDPKAEFLIA TNNYRAYGNK FPGTGDKHIV YASPDESRQI LADYIKATSE KEGSVNPNAD KNWRFVPITG NDKLDVRFET SPSEQAAKFI AEKAQYPMKQ VGTDEIGFAV YQIDLSK //