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Database: UniProt
Entry: A0A1B8UPC8_9BACL
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ID   A0A1B8UPC8_9BACL        Unreviewed;       309 AA.
AC   A0A1B8UPC8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Probable manganese-dependent inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00207};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00207};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00207};
DE            Short=PPase {ECO:0000256|HAMAP-Rule:MF_00207};
GN   Name=ppaC {ECO:0000256|HAMAP-Rule:MF_00207};
GN   ORFNames=BBG47_17760 {ECO:0000313|EMBL:OBY78173.1};
OS   Paenibacillus sp. KS1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY78173.1, ECO:0000313|Proteomes:UP000092663};
RN   [1] {ECO:0000313|EMBL:OBY78173.1, ECO:0000313|Proteomes:UP000092663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS1 {ECO:0000313|EMBL:OBY78173.1,
RC   ECO:0000313|Proteomes:UP000092663};
RA   Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT   "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT   isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT   Florida, USA.";
RL   Submitted (JUN-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, ECO:0000256|HAMAP-
CC         Rule:MF_00207};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00207};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00207};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00207}.
CC   -!- SIMILARITY: Belongs to the PPase class C family.
CC       {ECO:0000256|ARBA:ARBA00007350, ECO:0000256|HAMAP-Rule:MF_00207}.
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:OBY78173.1}.
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DR   EMBL; MAIS01000054; OBY78173.1; -; Genomic_DNA.
DR   RefSeq; WP_065292812.1; NZ_MAIS01000054.1.
DR   AlphaFoldDB; A0A1B8UPC8; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000092663; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   HAMAP; MF_00207; PPase_C; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   InterPro; IPR022934; Mn-dep_inorganic_PyrPase.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE-RELATED; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00207}; Reference proteome {ECO:0000313|Proteomes:UP000092663}.
FT   DOMAIN          181..307
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
SQ   SEQUENCE   309 AA;  33414 MW;  B35E459AB88F0450 CRC64;
     MEKVLIFGHK NPDTDTICSA IAYADLKTQL GFNVEPVRLG SVNGETQFAL DTFQAEAPRL
     VETVANEVKG VILVDHNERQ QSANDIEQVE VLEVIDHHRI ANFETSGPLY YRAEPVGCTA
     TILNKMYKEN GKTISKNIAG LMLSAIISDS LLFKSPTCTE QDVAAARELA EIAGVDVEKY
     GLDMLKAGAD LSQKTIAELI SLDAKEFSMG SSKVEIAQVN AVDVNDVLSR QAEVEAALND
     IIATKGLDLF VFVVTDILNS DSVALALGSK TEAVEKAYNV TLENNTALLK GVVSRKKQIV
     PVLTDTLSK
//
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