P26265 (CPDB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
EC=3.1.3.6
EC=3.1.4.16

Gene names

Name:	cpdB
Ordered Locus Names:	STM4403

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	647 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2',3'-cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to the corresponding nucleoside and phosphate.
Catalytic activity	Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate. A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
Cofactor	Divalent cations By similarity.
Subcellular location	Periplasm.
Miscellaneous	Two kinetically distinguishable active sites for the two substrates (2',3'-cyclic nucleotides and 3'-nucleotides) have been identified.
Sequence similarities	Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Metal-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	nucleotide catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Inferred from electronic annotation. Source: EC 3'-nucleotidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 647	628	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase		PRO_0000000036
Regions
	Region	544 – 550	7	Substrate binding By similarity
Sites
	Metal binding	31	1	Divalent metal cation 1 By similarity
	Metal binding	33	1	Divalent metal cation 1 By similarity
	Metal binding	76	1	Divalent metal cation 1 By similarity
	Metal binding	76	1	Divalent metal cation 2 By similarity
	Metal binding	116	1	Divalent metal cation 2 By similarity
	Metal binding	225	1	Divalent metal cation 2 By similarity
	Metal binding	257	1	Divalent metal cation 2 By similarity
	Metal binding	259	1	Divalent metal cation 1 By similarity
	Binding site	440	1	Substrate By similarity
Experimental info
	Sequence conflict	51	1	G → A in CAA37956. Ref.2
	Sequence conflict	84 – 89	6	GDYMAA → RLYGG in CAA37956. Ref.2
	Sequence conflict	96 – 98	3	DVH → GIQ in CAA37956. Ref.2
	Sequence conflict	133	1	A → G in CAA37956. Ref.2
	Sequence conflict	174	1	I → N in CAA37956. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P26265 [UniParc]. Last modified December 13, 2001. Version 2. Checksum: E9F7FE7D6681DB34	FASTA	647	70,517
	10 20 30 40 50 60 MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIH 70 80 90 100 110 120 AARNEVKNSV LVDNGDLIQG SPLGDYMAAK GLKDGDVHPV YKALNTLDYA VGNLGNHEFN 130 140 150 160 170 180 YGLDYLHNAL AGAKFPYVNA NIIDVKTQKP LFTPYLIKET SVIDKDGNPQ TLKIGYIGFV 190 200 210 220 230 240 PPQIMIWDKA NLSGKVTVND ITETARKYVP EMREKGADIV VVIAHSGLSA DPYHSMAENS 250 260 270 280 290 300 VYYLSEVPGV DAIMFGHAHA VFPGKDFADI KGADIAKGTL NGIPAVMPGM WGDHLGVVDL 310 320 330 340 350 360 VLNNDSGKWQ VTQAKAEARP IYDAAAKKSL AAEDSKLVGI LKADHDATRE FVSKPIGKSA 370 380 390 400 410 420 DNMYSYLALV QDDPTVQVVN NAQKAYVEHF IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS 430 440 450 460 470 480 FVEVEKGQLT FRNAADLYLY PNTLVVVKAS GKEVKEWLEC SAGQFNQIDI HSNKPQSLIN 490 500 510 520 530 540 WDGFRTYNFD VIDGVNYQID VSQPARYDGE CQMVNPQAER IKNLTFNGKP VDPNATFLVA 550 560 570 580 590 600 TNNYRAYGGK FAGTGDSHIA FASPDENRAV LAAWIGAESK RAGEIHPAAD NNWRLAPIHS 610 620 630 640 DTALDIRFET SPGDKAAAFI KAKGQYPMKK VAVDDIGFAI YQVDLSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Transcription and regulation of the cpdB gene in Escherichia coli K12 and Salmonella typhimurium LT2: evidence for modulation of constitutive promoters by cyclic AMP-CRP complex." Liu J., Beacham I.R. Mol. Gen. Genet. 222:161-165(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251. Strain: LT2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006468 Genomic DNA. Translation: AAL23223.1. X54009 Genomic DNA. Translation: CAA37956.1.
PIR	S11915.
RefSeq	NP_463264.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P26265.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM4403.
Proteomic databases
PaxDb	P26265.
PRIDE	P26265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL23223; AAL23223; STM4403.
GeneID	1255929.
KEGG	stm:STM4403.
PATRIC	32387729. VBISalEnt20916_4628.
Phylogenomic databases
eggNOG	COG0737.
HOGENOM	HOG000248800.
KO	K01119.
OMA	EKAQYPM.
ProtClustDB	PRK09420.
Family and domain databases
Gene3D	3.90.780.10. 1 hit.
InterPro	IPR008334. 5'-Nucleotdase_C. IPR006146. 5'-Nucleotdase_CS. IPR006179. 5_nucleotidase/apyrase. IPR006294. Cyc_nuc_PDE_nucleotidase. IPR004843. Metallo_PEstase_dom. [Graphical view]
PANTHER	PTHR11575. PTHR11575. 1 hit.
Pfam	PF02872. 5_nucleotid_C. 1 hit. PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR01607. APYRASEFAMLY.
SUPFAM	SSF55816. 5'-Nucleotdase_C. 1 hit.
TIGRFAMs	TIGR01390. CycNucDiestase. 1 hit.
PROSITE	PS00785. 5_NUCLEOTIDASE_1. 1 hit. PS00786. 5_NUCLEOTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CPDB_SALTY

Accession

Primary (citable) accession number: P26265

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 13, 2001
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program