CPDB_SALTY
ID CPDB_SALTY Reviewed; 647 AA.
AC P26265;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
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=STM4403;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
RC STRAIN=LT2;
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).
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.
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 -!- 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}.
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DR EMBL; AE006468; AAL23223.1; -; Genomic_DNA.
DR EMBL; X54009; CAA37956.1; -; Genomic_DNA.
DR PIR; S11915; S11915.
DR RefSeq; NP_463264.1; NC_003197.2.
DR RefSeq; WP_000589395.1; NC_003197.2.
DR AlphaFoldDB; P26265; -.
DR SMR; P26265; -.
DR STRING; 99287.STM4403; -.
DR PaxDb; P26265; -.
DR EnsemblBacteria; AAL23223; AAL23223; STM4403.
DR GeneID; 1255929; -.
DR KEGG; stm:STM4403; -.
DR PATRIC; fig|99287.12.peg.4628; -.
DR HOGENOM; CLU_005854_4_1_6; -.
DR OMA; EKAQYPM; -.
DR PhylomeDB; P26265; -.
DR BioCyc; SENT99287:STM4403-MON; -.
DR Proteomes; UP000001014; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..647
FT /note="2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-
FT nucleotidase"
FT /id="PRO_0000000036"
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 51
FT /note="G -> A (in Ref. 2; CAA37956)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..89
FT /note="GDYMAA -> RLYGG (in Ref. 2; CAA37956)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..98
FT /note="DVH -> GIQ (in Ref. 2; CAA37956)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="A -> G (in Ref. 2; CAA37956)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="I -> N (in Ref. 2; CAA37956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 70517 MW; E9F7FE7D6681DB34 CRC64;
MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIH
AARNEVKNSV LVDNGDLIQG SPLGDYMAAK GLKDGDVHPV YKALNTLDYA VGNLGNHEFN
YGLDYLHNAL AGAKFPYVNA NIIDVKTQKP LFTPYLIKET SVIDKDGNPQ TLKIGYIGFV
PPQIMIWDKA NLSGKVTVND ITETARKYVP EMREKGADIV VVIAHSGLSA DPYHSMAENS
VYYLSEVPGV DAIMFGHAHA VFPGKDFADI KGADIAKGTL NGIPAVMPGM WGDHLGVVDL
VLNNDSGKWQ VTQAKAEARP IYDAAAKKSL AAEDSKLVGI LKADHDATRE FVSKPIGKSA
DNMYSYLALV QDDPTVQVVN NAQKAYVEHF IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS
FVEVEKGQLT FRNAADLYLY PNTLVVVKAS GKEVKEWLEC SAGQFNQIDI HSNKPQSLIN
WDGFRTYNFD VIDGVNYQID VSQPARYDGE CQMVNPQAER IKNLTFNGKP VDPNATFLVA
TNNYRAYGGK FAGTGDSHIA FASPDENRAV LAAWIGAESK RAGEIHPAAD NNWRLAPIHS
DTALDIRFET SPGDKAAAFI KAKGQYPMKK VAVDDIGFAI YQVDLSK
