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Protein

Cobalt-dependent inorganic pyrophosphatase

Gene

CPE2055

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Co2+1 Publication, Mn2+1 PublicationNote: Binds tightly a transition metal ion; prefers Co2+ over Mn2+.1 Publication
  • Mg2+1 PublicationNote: Mg2+ ions are required for optimal catalytic activity.1 Publication

Enzyme regulationi

Inhibited by AMP and ADP with 25% and 35% of activity remaining, respectively, at saturating conditions. Activated 5-fold by diadenosine polyphosphates(Ap[n]A) with n>2 (Ap3A, Ap4A, Ap5A, Ap6A) at saturating conditions.2 Publications

Kineticsi

  1. KM=50 µM for pyrophosphate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei100AMP1 Publication1
    Binding sitei253AMP1 Publication1
    Binding sitei258AMP; via amide nitrogen and carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi116 – 119AMP1 Publication4
    Nucleotide bindingi278 – 280AMP1 Publication3

    GO - Molecular functioni

    • AMP binding Source: UniProtKB
    • cobalt ion binding Source: UniProtKB
    • inorganic diphosphatase activity Source: UniProtKB
    • manganese ion binding Source: UniProtKB

    GO - Biological processi

    • phosphate-containing compound metabolic process Source: UniProtKB

    Keywordsi

    Molecular functionHydrolase
    LigandManganese, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cobalt-dependent inorganic pyrophosphatase1 PublicationImported (EC:3.6.1.12 Publications)
    Alternative name(s):
    CBS domain-containing pyrophosphatase1 Publication
    Short name:
    cpCBS-PPase1 Publication
    Nucleotide-regulated inorganic pyrophosphatase
    Pyrophosphate phospho-hydrolaseBy similarity
    Short name:
    PPaseBy similarity
    Gene namesi
    Ordered Locus Names:CPE2055
    OrganismiClostridium perfringens (strain 13 / Type A)
    Taxonomic identifieri195102 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    Proteomesi
    • UP000000818 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004218521 – 549Cobalt-dependent inorganic pyrophosphataseAdd BLAST549

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1549
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi70 – 72Combined sources3
    Helixi87 – 96Combined sources10
    Beta strandi100 – 105Combined sources6
    Beta strandi110 – 116Combined sources7
    Helixi117 – 125Combined sources9
    Helixi132 – 135Combined sources4
    Helixi140 – 146Combined sources7
    Beta strandi150 – 153Combined sources4
    Beta strandi165 – 167Combined sources3
    Helixi172 – 177Combined sources6
    Beta strandi184 – 187Combined sources4
    Helixi191 – 199Combined sources9
    Beta strandi203 – 207Combined sources5
    Helixi215 – 224Combined sources10
    Beta strandi227 – 230Combined sources4
    Helixi235 – 241Combined sources7
    Helixi242 – 245Combined sources4
    Helixi248 – 251Combined sources4
    Helixi266 – 276Combined sources11
    Beta strandi279 – 284Combined sources6
    Beta strandi289 – 295Combined sources7
    Helixi296 – 298Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3L2BX-ray2.27A/B66-306[»]
    3L31X-ray2.30A/B66-306[»]
    ProteinModelPortaliQ8XIQ9.
    SMRiQ8XIQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8XIQ9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini74 – 130CBS 1PROSITE-ProRule annotationAdd BLAST57
    Domaini252 – 310CBS 2PROSITE-ProRule annotationAdd BLAST59

    Sequence similaritiesi

    Belongs to the PPase family.Sequence analysis

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    HOGENOMiHOG000223999.
    KOiK15986.
    OMAiTRYRSYP.
    OrthoDBiPOG091H00ML.

    Family and domain databases

    InterProiView protein in InterPro
    IPR000644. CBS_dom.
    IPR001667. DDH_dom.
    IPR004097. DHHA2.
    IPR010766. DRTGG.
    IPR028979. Ser_kin/Pase_Hpr_N-like.
    PfamiView protein in Pfam
    PF00571. CBS. 2 hits.
    PF01368. DHH. 1 hit.
    PF02833. DHHA2. 1 hit.
    PF07085. DRTGG. 1 hit.
    SMARTiView protein in SMART
    SM00116. CBS. 2 hits.
    SM01131. DHHA2. 1 hit.
    SUPFAMiSSF75138. SSF75138. 1 hit.
    PROSITEiView protein in PROSITE
    PS51371. CBS. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q8XIQ9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKDVIYITGH KNPDSDSICA ALAYAEFKNK TQDTPAIPVR LGNVSQETQY
    60 70 80 90 100
    ILDYFGVEAP QFLETVKLKV EDLEMDKIAP LAPEVSLKMA WNIMRDKNLK
    110 120 130 140 150
    SIPVADGNNH LLGMLSTSNI TATYMDIWDS NILAKSATSL DNILDTLSAE
    160 170 180 190 200
    AQNINEERKV FPGKVVVAAM QAESLKEFIS EGDIAIAGDR AEIQAELIEL
    210 220 230 240 250
    KVSLLIVTGG HTPSKEIIEL AKKNNITVIT TPHDSFTASR LIVQSLPVDY
    260 270 280 290 300
    VMTKDNLVAV STDDLVEDVK VTMSETRYSN YPVIDENNKV VGSIARFHLI
    310 320 330 340 350
    STHKKKVIQV DHNERGQSVH GLEDAEVLEI IDHHRVADIQ TGNPIYFRNE
    360 370 380 390 400
    PLGSTSTIVA KRFFENGIRP SREAAGLLCG AIISDTLLFK SPTCTPQDVK
    410 420 430 440 450
    MCRKLAEIAG IVPETFAKEM FKAGTSLKGK SIEEIFNADF KPFTIEGVKV
    460 470 480 490 500
    GVAQVNTMDI EGFMPLKGEM LDYMNQKAES MGLEMIMLLL TDIINEGSQI
    510 520 530 540
    LVAGRSPEIA EEAFKVKLED STTFLPGVLS RKKQVVPPLT QIITTRVSK
    Length:549
    Mass (Da):60,528
    Last modified:March 1, 2002 - v1
    Checksum:i05BDFE4E42A24F4B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000016 Genomic DNA. Translation: BAB81761.1.
    RefSeqiWP_003451432.1. NC_003366.1.

    Genome annotation databases

    EnsemblBacteriaiBAB81761; BAB81761; BAB81761.
    GeneIDi29570581.
    KEGGicpe:CPE2055.

    Similar proteinsi

    Entry informationi

    Entry nameiIPYR_CLOPE
    AccessioniPrimary (citable) accession number: Q8XIQ9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: March 1, 2002
    Last modified: June 7, 2017
    This is version 91 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families