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 03-AUG-2022, entry version 111.
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; Firmicutes; 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 EnsemblBacteria; BAB81761; BAB81761; BAB81761.
DR GeneID; 29570581; -.
DR KEGG; cpe:CPE2055; -.
DR HOGENOM; CLU_025243_1_0_9; -.
DR OMA; TIIANMF; -.
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 diphosphatase 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 Gene3D; 3.10.310.20; -; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.1390.20; -; 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 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; SSF54631; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
DR SUPFAM; SSF75138; SSF75138; 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
