ID A0A0X8CIF1_9BRAD Unreviewed; 500 AA.
AC A0A0X8CIF1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=exopolyphosphatase {ECO:0000256|ARBA:ARBA00012451};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN ORFNames=BCCGELA001_17175 {ECO:0000313|EMBL:AMA57830.1};
OS Bradyrhizobium sp. CCGE-LA001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA57830.1, ECO:0000313|Proteomes:UP000019052};
RN [1] {ECO:0000313|EMBL:AMA57830.1, ECO:0000313|Proteomes:UP000019052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA57830.1,
RC ECO:0000313|Proteomes:UP000019052};
RX PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT related Phaseolus species.";
RL Mol. Phylogenet. Evol. 79:1-11(2014).
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 -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC {ECO:0000256|ARBA:ARBA00007125}.
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DR EMBL; CP013949; AMA57830.1; -; Genomic_DNA.
DR RefSeq; WP_060735866.1; NZ_CP013949.1.
DR AlphaFoldDB; A0A0X8CIF1; -.
DR STRING; 1223566.BCCGELA001_17175; -.
DR KEGG; brc:BCCGELA001_17175; -.
DR Proteomes; UP000019052; Chromosome.
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; IPR048951; Ppx_C.
DR InterPro; IPR003695; Ppx_GppA_N.
DR NCBIfam; TIGR03706; exo_poly_only; 1.
DR PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1.
DR PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1.
DR Pfam; PF02541; Ppx-GppA; 1.
DR Pfam; PF21697; Ppx_C; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE 3: Inferred from homology;
FT DOMAIN 24..303
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 312..497
FT /note="Exopolyphosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21697"
SQ SEQUENCE 500 AA; 54653 MW; E3F166B8DACB25CD CRC64;
MKRPRKRGAS VAVIDIGSNS VRLVVYEALA RSLIPVFNEK TLCGLGREVQ STGLLAPDAV
DKALTSLKRF RALCRVMQVG RVFAIATAAC RDASNGPDFI AKAERICAVK IEILSGPREA
RLSALGVISG IHHPDGIVGD LGGGSLELID VRRNSVRSGV TLPLGGLALQ DLAHKSLKRA
DRIVREAIDG VPQLAAGGGR IFYAVGGTWR ALARIHIIQS GYPLQVMHGY SIPAAEALDF
SRRLRRLAAA DMLADIEIVA DARRPLLTYA ALVLEHIIRV AKPKTIVFST FGVREGLLHE
KLSETERNKD GLICAAEELN QLLSRSAKHA RELIAWTDRL ARVVKLRETE EDRRLRHAAC
LLSDIGWRVH PDHRGEQTLS LVVNGNFGAI THTERAFVGL SVFYRYAGLS EENQPPATMQ
GLLTPAQLER ARLLGAAFRV AHLVSAARPG VLPATHFRSQ GRKLMLVFEH RLGDLVADRV
GSRFRQLARL IGRAGSIVRR
//
