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Database: UniProt
Entry: A0A269PLX3_9GAMM
LinkDB: A0A269PLX3_9GAMM
Original site: A0A269PLX3_9GAMM 
ID   A0A269PLX3_9GAMM        Unreviewed;       306 AA.
AC   A0A269PLX3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CJF42_15720 {ECO:0000313|EMBL:PAJ73432.1};
OS   Pseudoalteromonas sp. NBT06-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=2025950 {ECO:0000313|EMBL:PAJ73432.1, ECO:0000313|Proteomes:UP000215836};
RN   [1] {ECO:0000313|EMBL:PAJ73432.1, ECO:0000313|Proteomes:UP000215836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBT06-2 {ECO:0000313|EMBL:PAJ73432.1,
RC   ECO:0000313|Proteomes:UP000215836};
RA   Wei Y.;
RT   "Pseudoalteromonas hadalis sp. nov., a facultative psychrophile isolated
RT   from New Britain Trench.";
RL   Submitted (AUG-2017) 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:PAJ73432.1}.
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DR   EMBL; NQMR01000081; PAJ73432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269PLX3; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000215836; 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; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   4: Predicted;
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:UP000215836}.
FT   DOMAIN          180..305
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   306 AA;  33741 MW;  B2ED46A8DDAD00E6 CRC64;
     MPAYYVVGHK VPDSDSIVGA IALAYLKNQI GEEAIPARLG EPSPETQFIL DKFGFEAPLL
     KMSYAGESLY IVDHSDIALA PDDIAEATIL GIVDHHKLGD LTSDTPLECW IRPVGCSNTV
     IKMMYDFHNV EIPKDIAGMM MCAILSDTVI FKSPTCTTAD IRCVEILAEI AGIEDYKELG
     MDMFKVKSAV LNTPMRDLVM RDFKNFNMNG TKIGIGQLEV IDLAIFDEMK PDLEADIAKL
     KQEEGQHSII LLLTDIMKEG SELLVVSDDL SQIESAFAAT TDNKVWLDGV LSRKKQVVPP
     LEKIFA
//
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