ID   A0A2I0NT40_9EURY        Unreviewed;       540 AA.
AC   A0A2I0NT40;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=inorganic diphosphatase {ECO:0000256|ARBA:ARBA00012146};
DE            EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|ARBA:ARBA00032535};
GN   ORFNames=CVV35_01590 {ECO:0000313|EMBL:PKL57125.1};
OS   Methanomicrobiales archaeon HGW-Methanomicrobiales-6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=2013822 {ECO:0000313|EMBL:PKL57125.1, ECO:0000313|Proteomes:UP000233331};
RN   [1] {ECO:0000313|EMBL:PKL57125.1, ECO:0000313|Proteomes:UP000233331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGW-Methanomicrobiales-6 {ECO:0000313|EMBL:PKL57125.1};
RX   PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA   Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA   Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT   "Potential for microbial H2 and metal transformations associated with novel
RT   bacteria and archaea in deep terrestrial subsurface sediments.";
RL   ISME J. 11:1915-1929(2017).
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:0000256|ARBA:ARBA00000926};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKL57125.1}.
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DR   EMBL; PGYH01000010; PKL57125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0NT40; -.
DR   Proteomes; UP000233331; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 2.
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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167}.
FT   DOMAIN          73..130
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          251..308
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   540 AA;  58657 MW;  FF3AEF6BBC178460 CRC64;
     MGQNKIVIIG HKQPDTDSIC SVIGYAELRN RAEPGKYIPA RCGEVSPEAK FALETFGVEA
     PAYVASVEPT VSDIPLDTRS VRQDVPTVDV AALMDTYDMR NMPITDGDET LVGLVSEYGL
     ARAYVRKNPR EQLSLIPMPL ETLARILDAR IVVPARETLG EGRVYTVIDA LHVTLSRMTP
     DDIAIVGDNE PAQLALISAG VAALIIAEGA PVGERVIDAA RTRGASVLST TLDAFSVGKM
     ISLSLPASMI METDVPTVRM EDSLEYAKSV VSNSKFRTAC VVGEGGRHIG LVSRTTLMQE
     VQKSVILLDH NEYSQAVDGI EQADILEIID HHRLGAISTL KPVRFLNDPV GSTSTIVANK
     FVEACVEPTP STAGLLLSGI LSDTMVMKLS TTTPADIRAA DYLAGIAGVD PAEYGPELIR
     KGMDLDALPK EELLTRDMKR YNLFGRSIMV SQVMTSSFSF AETHADEIRA ELDHLRTTMG
     VDCFFALFTN VFSNASDLFA AGDEGCITKL ELRDQPVRLD GVMSRKKDFI PKFGQMFRQL
//