ID   PPAC_METTP              Reviewed;         311 AA.
AC   A0B5R0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Manganese-dependent inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=ppaC; OrderedLocusNames=Mthe_0236;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RX   PubMed=22927778; DOI=10.1155/2012/315153;
RA   Berger S., Welte C., Deppenmeier U.;
RT   "Acetate activation in Methanosaeta thermophila: characterization of the
RT   key enzymes pyrophosphatase and acetyl-CoA synthetase.";
RL   Archaea 2012:315153-315153(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;
CC         Evidence={ECO:0000269|PubMed:22927778};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:22927778};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000305|PubMed:22927778};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for diphosphate (with manganese as cofactor)
CC         {ECO:0000269|PubMed:22927778};
CC         Vmax=157 umol/min/mg enzyme with magnesium as cofactor
CC         {ECO:0000269|PubMed:22927778};
CC         Vmax=726 umol/min/mg enzyme with manganese as cofactor
CC         {ECO:0000269|PubMed:22927778};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22927778}.
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR   EMBL; CP000477; ABK14034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B5R0; -.
DR   SMR; A0B5R0; -.
DR   STRING; 349307.Mthe_0236; -.
DR   EnsemblBacteria; ABK14034; ABK14034; Mthe_0236.
DR   KEGG; mtp:Mthe_0236; -.
DR   HOGENOM; CLU_025243_0_1_2; -.
DR   OMA; IMLCAIL; -.
DR   BRENDA; 3.6.1.1; 11925.
DR   SABIO-RK; A0B5R0; -.
DR   Proteomes; UP000000674; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.310.20; -; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; SSF64182; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Manganese-dependent inorganic pyrophosphatase"
FT                   /id="PRO_0000429049"
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  33963 MW;  C796D6ECEC7BFE9B CRC64;
     MADNIYVVGH KSPDTDSVTS AITYANLKNQ LGMKDVVPAA AGEINNETKY VLEYFKIAPP
     VVLNDATDKK VILVDHNEVG QAVDNIMKAD ILEIIDHHKI GDIQTGKPIF FHNEPVGATG
     TIIASMYELN GVAISKEMAG LMMAAILSDT VLFKSPTCTD KDKATVEKLS KICGEDPQKF
     GMEMLKAKSD IKSKTAKDIL FGDFKKFDFS GVKAGVGQIE VMDLADLAPK REEILAEMRK
     ALESEKLDMI VLMLTDVIKE ASDLLFVGTA AAKEGFEKAF GGKVTNNSIY KEKVLSRKKQ
     VIPPLESAFK K