Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase

Gene

cpdB

Organism
Yersinia enterocolitica
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate.
A 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Divalent metal cation 1By similarity
Metal bindingi38 – 381Divalent metal cation 1By similarity
Metal bindingi81 – 811Divalent metal cation 1By similarity
Metal bindingi81 – 811Divalent metal cation 2By similarity
Metal bindingi121 – 1211Divalent metal cation 2By similarity
Metal bindingi230 – 2301Divalent metal cation 2By similarity
Metal bindingi262 – 2621Divalent metal cation 2By similarity
Metal bindingi264 – 2641Divalent metal cation 1By similarity
Binding sitei445 – 4451SubstrateBy similarity

GO - Molecular functioni

  1. 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Source: UniProtKB-EC
  2. 3'-nucleotidase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. nucleotide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.4.16. 6741.

Names & Taxonomyi

Protein namesi
Recommended name:
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase (EC:3.1.3.6, EC:3.1.4.16)
Gene namesi
Name:cpdB
OrganismiYersinia enterocolitica
Taxonomic identifieri630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 6526282',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidasePRO_0000000038Add
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni549 – 5557Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR006294. Cyc_nuc_PDE_nucleotidase.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01390. CycNucDiestase. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53052-1 [UniParc]FASTAAdd to basket

« Hide

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

QK
Length:652
Mass (Da):71,492
Last modified:October 1, 1996 - v1
Checksum:i8781369575794E17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85742 Genomic DNA. Translation: CAA59745.1.
PIRiS52695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85742 Genomic DNA. Translation: CAA59745.1.
PIRiS52695.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.4.16. 6741.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProiIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
IPR006294. Cyc_nuc_PDE_nucleotidase.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PANTHERiPTHR11575. PTHR11575. 1 hit.
PfamiPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR01607. APYRASEFAMLY.
SUPFAMiSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01390. CycNucDiestase. 1 hit.
PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCPDB_YEREN
AccessioniPrimary (citable) accession number: P53052
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.