CPDB_HAEIN
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 03-AUG-2022, entry version 142.
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; Proteobacteria; 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}.
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DR EMBL; L42023; AAC22242.1; -; Genomic_DNA.
DR PIR; A64079; A64079.
DR RefSeq; NP_438741.1; NC_000907.1.
DR RefSeq; WP_005694555.1; 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 OMA; EKAQYPM; -.
DR PhylomeDB; P44764; -.
DR BioCyc; HINF71421:G1GJ1-596-MON; -.
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; IBA:GO_Central.
DR CDD; cd07410; MPP_CpdB_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 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 PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR01390; CycNucDiestase; 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
