ID D9SK89_GALCS Unreviewed; 491 AA.
AC D9SK89;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Exopolyphosphatase {ECO:0000256|ARBA:ARBA00020416};
DE EC=3.6.1.11 {ECO:0000256|ARBA:ARBA00012451};
GN OrderedLocusNames=Galf_2502 {ECO:0000313|EMBL:ADL56501.1};
OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS capsiferriformans (strain ES-2)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL56501.1, ECO:0000313|Proteomes:UP000001235};
RN [1] {ECO:0000313|EMBL:ADL56501.1, ECO:0000313|Proteomes:UP000001235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL56501.1,
RC ECO:0000313|Proteomes:UP000001235};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA Woyke T.;
RT "Complete sequence of Gallionella capsiferriformans ES-2.";
RL Submitted (AUG-2010) 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 -!- SIMILARITY: Belongs to the GppA/Ppx family.
CC {ECO:0000256|ARBA:ARBA00007125}.
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DR EMBL; CP002159; ADL56501.1; -; Genomic_DNA.
DR RefSeq; WP_013294421.1; NC_014394.1.
DR AlphaFoldDB; D9SK89; -.
DR STRING; 395494.Galf_2502; -.
DR KEGG; gca:Galf_2502; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_4; -.
DR OrthoDB; 9793035at2; -.
DR Proteomes; UP000001235; 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; 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 Hydrolase {ECO:0000313|EMBL:ADL56501.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001235}.
FT DOMAIN 21..300
FT /note="Ppx/GppA phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02541"
FT DOMAIN 309..475
FT /note="Ppx/GppA phosphatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21447"
SQ SEQUENCE 491 AA; 54118 MW; 6DE99509C27F2F20 CRC64;
MEQHPVLAAV DLGSNSFRLQ VAKVEGEQLY MLDGLREPVR LAAGLTADNY LDEAARQRAL
AALARFGERL RDLPPEAVRV VGTNSLRVAV NAAEFIAEAE QVLGFPIEVI AGREEARLIY
MGVAHGLPQS DDQLLVMDIG GGSTEFIIGH GLTPLKLESL YMGCVSFSSR YFPMGKITKN
NLARAELAAR SELQNIVADY KGQWQKAIGS SGTAKAIAEI LELNGWSRSG ITREGLDLFR
AHLLKVGDVH KLTLLGLRPD RLPALAGGFA IMYAAFDELG IEHMQLGLSA LREGVLYDLW
GRFHNNDMRD VTVRHFMRRY HVDVKQVERV TRLSDVLARQ FFGSEVNAQA LQVLGWVASL
HGVGIRVAHN GYQKHTAYIL ANADMPGFSK KEQNRLSLLA LAHRGSLKKL QGLLTETEDC
LLVMSLRLAA LFYRNRSDVV LPDMAASCNG AKFSLAIDAG WLKQNPLTET ALQEEVKQWK
SLGVAVQLIK K
//
