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Protein

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

Gene

cpdB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: -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.

Miscellaneous

Two kinetically distinguishable active sites for the two substrates (2',3'-cyclic nucleotides and 3'-nucleotides) have been identified.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31Divalent metal cation 1By similarity1
Metal bindingi33Divalent metal cation 1By similarity1
Metal bindingi76Divalent metal cation 1By similarity1
Metal bindingi76Divalent metal cation 2By similarity1
Metal bindingi116Divalent metal cation 2By similarity1
Metal bindingi225Divalent metal cation 2By similarity1
Metal bindingi257Divalent metal cation 2By similarity1
Metal bindingi259Divalent metal cation 1By similarity1
Binding sitei440SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme
LigandMetal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSENT99287:G1FZD-4447-MONOMER

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
Ordered Locus Names:STM4403
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000003620 – 6472',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidaseAdd BLAST628

Proteomic databases

PaxDbiP26265
PRIDEiP26265

Interactioni

Protein-protein interaction databases

STRINGi99287.STM4403

Structurei

3D structure databases

ProteinModelPortaliP26265
SMRiP26265
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni544 – 550Substrate bindingBy similarity7

Sequence similaritiesi

Belongs to the 5'-nucleotidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107RNS Bacteria
COG0737 LUCA
HOGENOMiHOG000248800
KOiK01119
OMAiMVWDKAN
PhylomeDBiP26265

Family and domain databases

Gene3Di3.60.21.10, 1 hit
3.90.780.10, 1 hit
InterProiView protein in InterPro
IPR008334 5'-Nucleotdase_C
IPR036907 5'-Nucleotdase_C_sf
IPR006146 5'-Nucleotdase_CS
IPR006179 5_nucleotidase/apyrase
IPR004843 Calcineurin-like_PHP_ApaH
IPR006294 Cyc_nuc_PDE_nucleotidase
IPR029052 Metallo-depent_PP-like
PANTHERiPTHR11575 PTHR11575, 1 hit
PfamiView protein in Pfam
PF02872 5_nucleotid_C, 1 hit
PF00149 Metallophos, 1 hit
PRINTSiPR01607 APYRASEFAMLY
SUPFAMiSSF55816 SSF55816, 1 hit
TIGRFAMsiTIGR01390 CycNucDiestase, 1 hit
PROSITEiView protein in PROSITE
PS00785 5_NUCLEOTIDASE_1, 1 hit
PS00786 5_NUCLEOTIDASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P26265-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF
60 70 80 90 100
GLVRTASLIH AARNEVKNSV LVDNGDLIQG SPLGDYMAAK GLKDGDVHPV
110 120 130 140 150
YKALNTLDYA VGNLGNHEFN YGLDYLHNAL AGAKFPYVNA NIIDVKTQKP
160 170 180 190 200
LFTPYLIKET SVIDKDGNPQ TLKIGYIGFV PPQIMIWDKA NLSGKVTVND
210 220 230 240 250
ITETARKYVP EMREKGADIV VVIAHSGLSA DPYHSMAENS VYYLSEVPGV
260 270 280 290 300
DAIMFGHAHA VFPGKDFADI KGADIAKGTL NGIPAVMPGM WGDHLGVVDL
310 320 330 340 350
VLNNDSGKWQ VTQAKAEARP IYDAAAKKSL AAEDSKLVGI LKADHDATRE
360 370 380 390 400
FVSKPIGKSA DNMYSYLALV QDDPTVQVVN NAQKAYVEHF IQGDPDLAKL
410 420 430 440 450
PVLSAAAPFK VGGRKNDPAS FVEVEKGQLT FRNAADLYLY PNTLVVVKAS
460 470 480 490 500
GKEVKEWLEC SAGQFNQIDI HSNKPQSLIN WDGFRTYNFD VIDGVNYQID
510 520 530 540 550
VSQPARYDGE CQMVNPQAER IKNLTFNGKP VDPNATFLVA TNNYRAYGGK
560 570 580 590 600
FAGTGDSHIA FASPDENRAV LAAWIGAESK RAGEIHPAAD NNWRLAPIHS
610 620 630 640
DTALDIRFET SPGDKAAAFI KAKGQYPMKK VAVDDIGFAI YQVDLSK
Length:647
Mass (Da):70,517
Last modified:December 13, 2001 - v2
Checksum:iE9F7FE7D6681DB34
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51G → A in CAA37956 (PubMed:2172762).Curated1
Sequence conflicti84 – 89GDYMAA → RLYGG in CAA37956 (PubMed:2172762).Curated6
Sequence conflicti96 – 98DVH → GIQ in CAA37956 (PubMed:2172762).Curated3
Sequence conflicti133A → G in CAA37956 (PubMed:2172762).Curated1
Sequence conflicti174I → N in CAA37956 (PubMed:2172762).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA Translation: AAL23223.1
X54009 Genomic DNA Translation: CAA37956.1
PIRiS11915
RefSeqiNP_463264.1, NC_003197.2
WP_000589395.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL23223; AAL23223; STM4403
GeneIDi1255929
KEGGistm:STM4403
PATRICifig|99287.12.peg.4628

Similar proteinsi

Entry informationi

Entry nameiCPDB_SALTY
AccessioniPrimary (citable) accession number: P26265
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 13, 2001
Last modified: March 28, 2018
This is version 133 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health