CPDB_YEREN
ID CPDB_YEREN Reviewed; 652 AA.
AC P53052;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
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;
OS Yersinia enterocolitica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51871 / WA-314 / Serotype O:8;
RA Truelzsch K.S.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; X85742; CAA59745.1; -; Genomic_DNA.
DR PIR; S52695; S52695.
DR AlphaFoldDB; P53052; -.
DR SMR; P53052; -.
DR STRING; 1443113.LC20_04778; -.
DR eggNOG; COG0737; Bacteria.
DR BRENDA; 3.1.4.16; 6741.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; -; 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; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..652
FT /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-
FT nucleotidase"
FT /id="PRO_0000000038"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 549..555
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 71492 MW; 8781369575794E17 CRC64;
MFKRPLTLSL LASLIALTTS TAQAATVDLR VLETTDLHSN MMDFDYYKDK PTEKFGLVRT
ASLIEAARQQ ATNSVLVDNG DLIQGSPLGD YMAAKGLKAG EIHPVYKAMN TLDYAVGNIG
NHEFNYGLDY LKKSLAGAKF PYVNANVIDV KTGKPLFQPY LIVDTPVKDR DGKNHNLRIG
YIGFGPPQVM IWDKANLTGK VTVDDITETA KKWVPEMRKQ GANLVVAIPH SGLSSDPYKT
MAENSVYYLS QVPGIDAIMF GHAHAVFPSK DFATIKGADI AQGTLNGIPA VMPGQWGDHL
GVVDFVLNND QGQWQVTQAK AEARPIFDKA TQKSLAAENA NLMKVLAADH QGTRDFVSQP
IGTASDNMYS YLSLIQDDPT VQIVNNAQRA YTEHFIQGDP DLADLPVLSA AAPFKAGGRK
NDPASFVEVE KGELTFRNAA DLYLYPNTLV VVKASGADVK QWLECSAAQF NQIDVNSSKP
QSLINWDSFR TYNFDVIDGV NYEIDVSQPA RYDGECALIN DKAERIKNLT FNGKPIDPQA
TFLIGTNNYR AYSGKFAGTG DSHIAFASPD ENRAVLSAYI SAETKKHGQV TPQADNNWRL
ATLNSQQPLD IRFETSPSTK AAEFIKQKAQ YPMKAMGTDE IGFAVFKIDL QK
