Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P44764

- CPDB_HAEIN

UniProt

P44764 - CPDB_HAEIN

Protein

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

Gene

cpdB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Divalent cations.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi41 – 411Divalent metal cation 1By similarity
    Metal bindingi43 – 431Divalent metal cation 1By similarity
    Metal bindingi86 – 861Divalent metal cation 1By similarity
    Metal bindingi86 – 861Divalent metal cation 2By similarity
    Metal bindingi126 – 1261Divalent metal cation 2By similarity
    Metal bindingi235 – 2351Divalent metal cation 2By similarity
    Metal bindingi267 – 2671Divalent metal cation 2By similarity
    Metal bindingi269 – 2691Divalent metal cation 1By similarity
    Binding sitei450 – 4501SubstrateBy 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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Nucleotide-binding

    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:HI_0583
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 6576312',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidasePRO_0000000037Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi71421.HI0583.

    Structurei

    3D structure databases

    ProteinModelPortaliP44764.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni554 – 5596Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the 5'-nucleotidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0737.
    KOiK01119.
    K08693.
    OMAiEKAQYPM.
    OrthoDBiEOG696BW0.
    PhylomeDBiP44764.

    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.

    P44764-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMNRRHFIQI SATSILALSA NRFAMAKGKS DVDLRIVATT DVHSFLTDFD    50
    YYKDAPTDKF GFTRAASLIR QARAEVKNSV LVDNGDLIQG NPIADYQAAQ 100
    GYKEGKSNPA IDCLNAMNYE VGTLGNHEFN YGLNYLADAI KQAKFPIVNS 150
    NVVKAGTEEP YFTPYVIQEK SVVDNQGKTH KLKIGYIGFV PPQIMVWDKA 200
    NLQGKVETRD IVKTAQKYVP EMKKKGADIV VALAHTGPSD EPYQEGAENS 250
    AFYLADVPHI DAVIFGHSHR LFPNKEFAKS PNADIVNGTV KGIPESMAGY 300
    WANNISVVDL GLTEHKGKWI VTSGKAVLRP IYDIETKKAL AKNDPEITAL 350
    LKPVHEATRK YVSQPIGKAT DNMYSYLALL QDDPTIQIVN QAQKAYVEKV 400
    APSIAAMAGL PILSAGAPFK AGGRKNDPTG YTEVNKGKLT FRNAADLYLY 450
    PNTLVVVKAT GEQLKEWLEC SAGMFKQIDP TSDKPQSLID WEGFRTYNFD 500
    VIDGVNYEYD LTKPARYDGE CKLINPESHR VVNLTYQGKP VDPKAEFLIA 550
    TNNYRAYGNK FPGTGDKHIV YASPDESRQI LADYIKATSE KEGSVNPNAD 600
    KNWRFVPITG NDKLDVRFET SPSEQAAKFI AEKAQYPMKQ VGTDEIGFAV 650
    YQIDLSK 657
    Length:657
    Mass (Da):72,763
    Last modified:November 1, 1995 - v1
    Checksum:i201CAAB415014499
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22242.1.
    PIRiA64079.
    RefSeqiNP_438741.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC22242; AAC22242; HI_0583.
    GeneIDi949588.
    KEGGihin:HI0583.
    PATRICi20189723. VBIHaeInf48452_0604.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC22242.1 .
    PIRi A64079.
    RefSeqi NP_438741.1. NC_000907.1.

    3D structure databases

    ProteinModelPortali P44764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0583.

    Protocols and materials databases

    DNASUi 949588.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC22242 ; AAC22242 ; HI_0583 .
    GeneIDi 949588.
    KEGGi hin:HI0583.
    PATRICi 20189723. VBIHaeInf48452_0604.

    Phylogenomic databases

    eggNOGi COG0737.
    KOi K01119.
    K08693.
    OMAi EKAQYPM.
    OrthoDBi EOG696BW0.
    PhylomeDBi P44764.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    3.90.780.10. 1 hit.
    InterProi IPR008334. 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 ]
    PANTHERi PTHR11575. PTHR11575. 1 hit.
    Pfami PF02872. 5_nucleotid_C. 1 hit.
    PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR01607. APYRASEFAMLY.
    SUPFAMi SSF55816. SSF55816. 1 hit.
    SSF56300. SSF56300. 1 hit.
    TIGRFAMsi TIGR01390. CycNucDiestase. 1 hit.
    PROSITEi PS00785. 5_NUCLEOTIDASE_1. 1 hit.
    PS00786. 5_NUCLEOTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiCPDB_HAEIN
    AccessioniPrimary (citable) accession number: P44764
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 112 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3