ID A0A160DWB5_9GAMM Unreviewed; 503 AA.
AC A0A160DWB5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN ORFNames=I596_2719 {ECO:0000313|EMBL:ANB18714.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB18714.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB18714.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB18714.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) 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; CP015249; ANB18714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160DWB5; -.
DR STRING; 1300342.I596_2719; -.
DR KEGG; dko:I596_2719; -.
DR PATRIC; fig|1300342.3.peg.2645; -.
DR OrthoDB; 9793035at2; -.
DR Proteomes; UP000076830; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000076830}.
FT DOMAIN 26..309
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 316..488
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 503 AA; 55410 MW; F7E37D8403F99B90 CRC64;
MTDANEIRNG ELLAAVDIGS NSFHMIVARY EHGELRVIDR LRDSVRLAMG LGPDGSLATT
QRQRALACLA QFGQRLRGLP HSRVHAVATN AVRQLANPQA FLLPAETALG HPIEIVSGRE
EARLIYLGVA NGLPRGKQRR LIVDIGGGST EFIIGQDFEA LERESIQVGC VASTRRFFED
GKLTPKRWRQ AATEIGVELQ QFAADYRSRG WAEAFGSSGT VRAIGSIVQA NRWSDAGISF
DSLERLRDAL IAAGSIQALN LPGLSEERAQ VIAGGVVILE SVFAALGVVQ MGVCETSMRE
GLLYDMLGRA MHRDPRSGAI AALVERYAVD RSQAARVRET ALILFDQAAA DWQLEPIDRD
VLGWCADIHE IGLAIAHSQH HVHGAYIVAH SDLAGFSQQG QQLLETILRS QRRRPHRGGF
EALPERLQTI ARRLTALLRL AVLLHRGRTN EPLPRLLLQA GERSLRLTLP SLWLEQHPLT
RADLEQESDY FKPLGLKLQI GTR
//
