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Database: UniProt
Entry: IPYR_CLOPE
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Original site: IPYR_CLOPE 
ID   IPYR_CLOPE              Reviewed;         549 AA.
AC   Q8XIQ9;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Cobalt-dependent inorganic pyrophosphatase {ECO:0000303|PubMed:20303981, ECO:0000312|EMBL:BAB81761.1};
DE            EC=3.6.1.1 {ECO:0000269|PubMed:20303981, ECO:0000269|PubMed:22348476};
DE   AltName: Full=CBS domain-containing pyrophosphatase {ECO:0000303|PubMed:20303981};
DE            Short=cpCBS-PPase {ECO:0000303|PubMed:20303981};
DE   AltName: Full=Nucleotide-regulated inorganic pyrophosphatase;
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000250|UniProtKB:P0A7A9};
DE            Short=PPase {ECO:0000250|UniProtKB:P0A7A9};
GN   OrderedLocusNames=CPE2055;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1] {ECO:0000312|EMBL:BAB81761.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2] {ECO:0000305, ECO:0000312|PDB:3L31}
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY
RP   (2.27 ANGSTROMS) OF 66-306 IN COMPLEX WITH AMP.
RX   PubMed=20303981; DOI=10.1016/j.jmb.2010.03.019;
RA   Tuominen H., Salminen A., Oksanen E., Jamsen J., Heikkila O., Lehtio L.,
RA   Magretova N.N., Goldman A., Baykov A.A., Lahti R.;
RT   "Crystal structures of the CBS and DRTGG domains of the regulatory region
RT   of Clostridiumperfringens pyrophosphatase complexed with the inhibitor,
RT   AMP, and activator, diadenosine tetraphosphate.";
RL   J. Mol. Biol. 398:400-413(2010).
RN   [3] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22348476; DOI=10.1134/s0006297912020071;
RA   Jamsen J., Baykov A.A., Lahti R.;
RT   "Fast kinetics of nucleotide binding to Clostridium perfringens family II
RT   pyrophosphatase containing CBS and DRTGG domains.";
RL   Biochemistry (Mosc.) 77:165-170(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000269|PubMed:20303981,
CC         ECO:0000269|PubMed:22348476};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:22348476};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:22348476};
CC       Note=Binds tightly a transition metal ion; prefers Co(2+) over Mn(2+).
CC       {ECO:0000269|PubMed:22348476};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22348476};
CC       Note=Mg(2+) ions are required for optimal catalytic activity.
CC       {ECO:0000269|PubMed:22348476};
CC   -!- ACTIVITY REGULATION: Inhibited by AMP and ADP with 25% and 35% of
CC       activity remaining, respectively, at saturating conditions. Activated
CC       5-fold by diadenosine polyphosphates(Ap[n]A) with n>2 (Ap3A, Ap4A,
CC       Ap5A, Ap6A) at saturating conditions. {ECO:0000269|PubMed:20303981,
CC       ECO:0000269|PubMed:22348476}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 uM for pyrophosphate {ECO:0000269|PubMed:22348476};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20303981}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255}.
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DR   EMBL; BA000016; BAB81761.1; -; Genomic_DNA.
DR   RefSeq; WP_003451432.1; NC_003366.1.
DR   PDB; 3L2B; X-ray; 2.27 A; A/B=66-306.
DR   PDB; 3L31; X-ray; 2.30 A; A/B=66-306.
DR   PDBsum; 3L2B; -.
DR   PDBsum; 3L31; -.
DR   AlphaFoldDB; Q8XIQ9; -.
DR   SMR; Q8XIQ9; -.
DR   STRING; 195102.gene:10491325; -.
DR   GeneID; 69449991; -.
DR   KEGG; cpe:CPE2055; -.
DR   HOGENOM; CLU_025243_1_0_9; -.
DR   BRENDA; 3.6.1.1; 1503.
DR   SABIO-RK; Q8XIQ9; -.
DR   EvolutionaryTrace; Q8XIQ9; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016208; F:AMP binding; IDA:UniProtKB.
DR   GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:UniProtKB.
DR   CDD; cd04597; CBS_pair_inorgPPase; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   InterPro; IPR010766; DRTGG.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   Pfam; PF07085; DRTGG; 1.
DR   SMART; SM00116; CBS; 2.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR   SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   3D-structure; CBS domain; Hydrolase; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..549
FT                   /note="Cobalt-dependent inorganic pyrophosphatase"
FT                   /id="PRO_0000421852"
FT   DOMAIN          74..130
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          252..310
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   BINDING         100
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:20303981"
FT   BINDING         116..119
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:20303981"
FT   BINDING         253
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:20303981"
FT   BINDING         258
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:20303981"
FT   BINDING         278..280
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000269|PubMed:20303981"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           87..96
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           117..125
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           132..135
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           140..146
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          165..167
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           172..177
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           191..199
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           215..224
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          227..230
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           235..241
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           242..245
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           248..251
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           266..276
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          279..284
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   STRAND          289..295
FT                   /evidence="ECO:0007829|PDB:3L2B"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:3L31"
SQ   SEQUENCE   549 AA;  60528 MW;  05BDFE4E42A24F4B CRC64;
     MKDVIYITGH KNPDSDSICA ALAYAEFKNK TQDTPAIPVR LGNVSQETQY ILDYFGVEAP
     QFLETVKLKV EDLEMDKIAP LAPEVSLKMA WNIMRDKNLK SIPVADGNNH LLGMLSTSNI
     TATYMDIWDS NILAKSATSL DNILDTLSAE AQNINEERKV FPGKVVVAAM QAESLKEFIS
     EGDIAIAGDR AEIQAELIEL KVSLLIVTGG HTPSKEIIEL AKKNNITVIT TPHDSFTASR
     LIVQSLPVDY VMTKDNLVAV STDDLVEDVK VTMSETRYSN YPVIDENNKV VGSIARFHLI
     STHKKKVIQV DHNERGQSVH GLEDAEVLEI IDHHRVADIQ TGNPIYFRNE PLGSTSTIVA
     KRFFENGIRP SREAAGLLCG AIISDTLLFK SPTCTPQDVK MCRKLAEIAG IVPETFAKEM
     FKAGTSLKGK SIEEIFNADF KPFTIEGVKV GVAQVNTMDI EGFMPLKGEM LDYMNQKAES
     MGLEMIMLLL TDIINEGSQI LVAGRSPEIA EEAFKVKLED STTFLPGVLS RKKQVVPPLT
     QIITTRVSK
//
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