ID A0A160FMG6_9BURK Unreviewed; 541 AA.
AC A0A160FMG6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN ORFNames=AYM40_14380 {ECO:0000313|EMBL:ANB73416.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB73416.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB73416.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB73416.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
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; CP014578; ANB73416.1; -; Genomic_DNA.
DR RefSeq; WP_063496806.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FMG6; -.
DR STRING; 1804984.AYM40_14380; -.
DR KEGG; buz:AYM40_14380; -.
DR Proteomes; UP000076852; Chromosome 1.
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:SF0; RETROGRADE REGULATION PROTEIN 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000076852}.
FT DOMAIN 64..349
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 357..523
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 58715 MW; 8237AA9B76504AC7 CRC64;
MASLNSAVGH KAPKAPSGYP APSASNAAAH ARMESAYSMA TTPQLLAAVD LGSNSFRLIV
GRVEETDAGS QIYQVDALRE PVRLAAGLSR DKMLDRASQV RGWDALKRFG ERLRDFHPDH
VRAVATNTLR IAKNAGEFLG EAQAALGFPI EVIAGREEAR LIYAGAAHSV PASAGKRLVV
DIGGGSTEFI IGSHYTPIKM ESLYIGCVSH SRAFFPAGNV DEYTMRQAEL AAGREIQIIS
AEYKKTGWEQ AIGSSGTARA LAELVEANGF NDAGVTHGIS RGGLERLKRA LIKAENVNRL
KLVALKADRI PVLAGGLSIM MAVFDELGVD YVDTTDGALR LGVLYDLLGR SQHEDMRTVT
AEGFMRRYGV DRAQAGRIGE LAVRFYDQFA EPDEERRAEN RMFLGWAAAL HEIGLSISHS
AYHKHSAYIA SNADMPGFSR TDQARLAALV LGHAGKLGKL SQTREVEWPL LFCLRLAALL
CRRRADVGLP GIAVAQVNGG YEVRLPNEWV ANNPLTDYSL IQEAAEWEKV GIPYRVVYTD
D
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