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P44764 (CPDB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:HI_0583
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 By similarity.

Sequence similarities

Belongs to the 5'-nucleotidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 6576312',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
PRO_0000000037

Regions

Region554 – 5596Substrate binding By similarity

Sites

Metal binding411Divalent metal cation 1 By similarity
Metal binding431Divalent metal cation 1 By similarity
Metal binding861Divalent metal cation 1 By similarity
Metal binding861Divalent metal cation 2 By similarity
Metal binding1261Divalent metal cation 2 By similarity
Metal binding2351Divalent metal cation 2 By similarity
Metal binding2671Divalent metal cation 2 By similarity
Metal binding2691Divalent metal cation 1 By similarity
Binding site4501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P44764 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 201CAAB415014499

FASTA65772,763
        10         20         30         40         50         60 
MMNRRHFIQI SATSILALSA NRFAMAKGKS DVDLRIVATT DVHSFLTDFD YYKDAPTDKF 

        70         80         90        100        110        120 
GFTRAASLIR QARAEVKNSV LVDNGDLIQG NPIADYQAAQ GYKEGKSNPA IDCLNAMNYE 

       130        140        150        160        170        180 
VGTLGNHEFN YGLNYLADAI KQAKFPIVNS NVVKAGTEEP YFTPYVIQEK SVVDNQGKTH 

       190        200        210        220        230        240 
KLKIGYIGFV PPQIMVWDKA NLQGKVETRD IVKTAQKYVP EMKKKGADIV VALAHTGPSD 

       250        260        270        280        290        300 
EPYQEGAENS AFYLADVPHI DAVIFGHSHR LFPNKEFAKS PNADIVNGTV KGIPESMAGY 

       310        320        330        340        350        360 
WANNISVVDL GLTEHKGKWI VTSGKAVLRP IYDIETKKAL AKNDPEITAL LKPVHEATRK 

       370        380        390        400        410        420 
YVSQPIGKAT DNMYSYLALL QDDPTIQIVN QAQKAYVEKV APSIAAMAGL PILSAGAPFK 

       430        440        450        460        470        480 
AGGRKNDPTG YTEVNKGKLT FRNAADLYLY PNTLVVVKAT GEQLKEWLEC SAGMFKQIDP 

       490        500        510        520        530        540 
TSDKPQSLID WEGFRTYNFD VIDGVNYEYD LTKPARYDGE CKLINPESHR VVNLTYQGKP 

       550        560        570        580        590        600 
VDPKAEFLIA TNNYRAYGNK FPGTGDKHIV YASPDESRQI LADYIKATSE KEGSVNPNAD 

       610        620        630        640        650 
KNWRFVPITG NDKLDVRFET SPSEQAAKFI AEKAQYPMKQ VGTDEIGFAV YQIDLSK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22242.1.
PIRA64079.
RefSeqNP_438741.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44764.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0583.

Protocols and materials databases

DNASU949588.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22242; AAC22242; HI_0583.
GeneID949588.
KEGGhin:HI0583.
PATRIC20189723. VBIHaeInf48452_0604.

Phylogenomic databases

eggNOGCOG0737.
KOK01119.
K08693.
OMAEKAQYPM.
OrthoDBEOG696BW0.
PhylomeDBP44764.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
3.90.780.10. 1 hit.
InterProIPR008334. 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]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
SSF56300. SSF56300. 1 hit.
TIGRFAMsTIGR01390. CycNucDiestase. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
PS00786. 5_NUCLEOTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDB_HAEIN
AccessionPrimary (citable) accession number: P44764
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names