P53052 (CPDB_YEREN) 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

Organism

Yersinia enterocolitica

Taxonomic identifier

630 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	652 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 By similarity.
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.
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	Multifunctional enzyme
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 – 24	24	Potential
	Chain	25 – 652	628	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase		PRO_0000000038
Regions
	Region	549 – 555	7	Substrate binding By similarity
Sites
	Metal binding	36	1	Divalent metal cation 1 By similarity
	Metal binding	38	1	Divalent metal cation 1 By similarity
	Metal binding	81	1	Divalent metal cation 1 By similarity
	Metal binding	81	1	Divalent metal cation 2 By similarity
	Metal binding	121	1	Divalent metal cation 2 By similarity
	Metal binding	230	1	Divalent metal cation 2 By similarity
	Metal binding	262	1	Divalent metal cation 2 By similarity
	Metal binding	264	1	Divalent metal cation 1 By similarity
	Binding site	445	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53052 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8781369575794E17	FASTA	652	71,492
	10 20 30 40 50 60 MFKRPLTLSL LASLIALTTS TAQAATVDLR VLETTDLHSN MMDFDYYKDK PTEKFGLVRT 70 80 90 100 110 120 ASLIEAARQQ ATNSVLVDNG DLIQGSPLGD YMAAKGLKAG EIHPVYKAMN TLDYAVGNIG 130 140 150 160 170 180 NHEFNYGLDY LKKSLAGAKF PYVNANVIDV KTGKPLFQPY LIVDTPVKDR DGKNHNLRIG 190 200 210 220 230 240 YIGFGPPQVM IWDKANLTGK VTVDDITETA KKWVPEMRKQ GANLVVAIPH SGLSSDPYKT 250 260 270 280 290 300 MAENSVYYLS QVPGIDAIMF GHAHAVFPSK DFATIKGADI AQGTLNGIPA VMPGQWGDHL 310 320 330 340 350 360 GVVDFVLNND QGQWQVTQAK AEARPIFDKA TQKSLAAENA NLMKVLAADH QGTRDFVSQP 370 380 390 400 410 420 IGTASDNMYS YLSLIQDDPT VQIVNNAQRA YTEHFIQGDP DLADLPVLSA AAPFKAGGRK 430 440 450 460 470 480 NDPASFVEVE KGELTFRNAA DLYLYPNTLV VVKASGADVK QWLECSAAQF NQIDVNSSKP 490 500 510 520 530 540 QSLINWDSFR TYNFDVIDGV NYEIDVSQPA RYDGECALIN DKAERIKNLT FNGKPIDPQA 550 560 570 580 590 600 TFLIGTNNYR AYSGKFAGTG DSHIAFASPD ENRAVLSAYI SAETKKHGQV TPQADNNWRL 610 620 630 640 650 ATLNSQQPLD IRFETSPSTK AAEFIKQKAQ YPMKAMGTDE IGFAVFKIDL QK

References

[1]	Truelzsch K.S. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 51871 / WA-314 / Serotype O:8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X85742 Genomic DNA. Translation: CAA59745.1.
PIR	S52695.
3D structure databases
ProteinModelPortal	P53052.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.1.4.16. 6741.
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_YEREN

Accession

Primary (citable) accession number: P53052

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	March 6, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program