ID A0A3B7A6Z8_9RHOO Unreviewed; 500 AA.
AC A0A3B7A6Z8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN Name=ppx {ECO:0000313|EMBL:AXS80399.1};
GN ORFNames=HYN24_10430 {ECO:0000313|EMBL:AXS80399.1};
OS Dechloromonas sp. HYN0024.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=2231055 {ECO:0000313|EMBL:AXS80399.1, ECO:0000313|Proteomes:UP000257259};
RN [1] {ECO:0000313|EMBL:AXS80399.1, ECO:0000313|Proteomes:UP000257259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0024 {ECO:0000313|EMBL:AXS80399.1,
RC ECO:0000313|Proteomes:UP000257259};
RA Kim M., Yi H.;
RT "Genome sequencing of Dechloromonas sp. HYN0024.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC ChEBI:CHEBI:43474; EC=3.6.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000209};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC {ECO:0000256|ARBA:ARBA00007125}.
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DR EMBL; CP031842; AXS80399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7A6Z8; -.
DR KEGG; dey:HYN24_10430; -.
DR OrthoDB; 9793035at2; -.
DR Proteomes; UP000257259; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006793; P:phosphorus metabolic process; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR022371; Exopolyphosphatase.
DR InterPro; IPR048950; Ppx_GppA_C.
DR InterPro; IPR003695; Ppx_GppA_N.
DR InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR NCBIfam; TIGR03706; exo_poly_only; 1.
DR PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR PANTHER; PTHR30005:SF14; EXOPOLYPHOSPHATASE; 1.
DR Pfam; PF02541; Ppx-GppA; 1.
DR Pfam; PF21447; Ppx-GppA_III; 1.
DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:AXS80399.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000257259}.
FT DOMAIN 21..305
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 312..478
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 500 AA; 54961 MW; D6E33E27003CA70E CRC64;
MIYETVAAVD LGSNSFRLQV GRVVDNQIYT LDSMKEPVRL ASGLMPDKRL DAPAQARALD
ALRRFGERLG GLDKGAVRAV ATNTLRVAKN AFEFLPLAEE ALGFPIEVIA GREEARLIYI
GASHSLPSAA HKRLVVDIGG GSTEFIIGKR HEPQLMESLY MGCVSYTLRF FPDRRIDRKR
LREAQVAAAK EIELIAADYQ RLGWKEAIGS SGSARAIADV LEMNGLNPNG ESGITRVGLA
TLCELLVKAG SAEALDLPGV KGDRLPVFPG GVAIMSAIFE ELDIERMTYA DGALRLGVLY
DLLGRFHHHD MRDSTVAQFR RRYQVEGDQV ERVEASALSA LTQLSDGSPG EADVQFLSWA
CRVHEIGISV AHNAYHKHGA YILTYADMPG FSKKDQARLA MLVLGHRGKL EKLGGMPASD
SAWDLIFCLR LAVLLHRTRD DRAIPAWRVS RGDNGFIIEL PADWLAANPW TAAAFGEEAN
VWKQLGREYV LRSKSTRKIA
//
