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Database: UniProt
Entry: A0A139STN1_9BACT
LinkDB: A0A139STN1_9BACT
Original site: A0A139STN1_9BACT 
ID   A0A139STN1_9BACT        Unreviewed;       579 AA.
AC   A0A139STN1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=AXK12_01105 {ECO:0000313|EMBL:KXU37791.1};
OS   Cephaloticoccus capnophilus.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC   Cephaloticoccus.
OX   NCBI_TaxID=1548208 {ECO:0000313|EMBL:KXU37791.1, ECO:0000313|Proteomes:UP000071392};
RN   [1] {ECO:0000313|EMBL:KXU37791.1, ECO:0000313|Proteomes:UP000071392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CV41 {ECO:0000313|EMBL:KXU37791.1,
RC   ECO:0000313|Proteomes:UP000071392};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:KXU37791.1}.
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DR   EMBL; LSZP01000004; KXU37791.1; -; Genomic_DNA.
DR   RefSeq; WP_068710818.1; NZ_LSZP01000004.1.
DR   AlphaFoldDB; A0A139STN1; -.
DR   STRING; 1548208.AXK12_01105; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000071392; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000071392}.
FT   DOMAIN          87..144
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          272..328
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   579 AA;  63508 MW;  2848FB5CEC3A65D0 CRC64;
     MSPATPAPAA PTNSREITYV IGHKNPDADA ICAAIAYTAF KEQRGEPNFV AARCGNSNVR
     IDTILHRFNQ PLPLYLSDVF PRVHDLMTSD VVHISDDATC FEALEVFERR GVSVLPITDK
     DRKILGSLSL AQMGGFFVPH TQDPRRMREV HTSLSRIVRS LSATILTATD IDRLETLYVH
     IAAMDIASFW KMSERENIPA SQSITIVGDR KNVQLRAIEI GSRALIVSGG RAVDPEVVAL
     ATERGTCILS SPHDTATTAW IVRTASTLER IIDRDFKTLS ADLPLTLARK QFSPHSSHAL
     LVADANGTLQ GILTKSDLLR PVGKRLVLVD HNEMTQAVPG ADQARIVEII DHHRLGPINT
     QQPILFINEP VGSTCTIVAD LYRREGLTPT PDLAGIMMSG LITDTLLLKG PTATAKDAEI
     LRWLSGIAAV DPNQLADQIF SSGSVILGNP AKQVVRADFK IYTEEGVRFS VSQVEELGFR
     NFWKHATAIE QALQDLRDTE ALAFACLLVT DINTQNSVLL VKGDPSVISR ITYPHVKNEE
     SFELPGIVSR KKQLIPYLGS LLREMADDDE LPANPAPHR
//
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