ID   PK21C_RUEPO             Reviewed;         301 AA.
AC   Q5LSN8;
DT   20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=NDP-polyphosphate phosphotransferase 3 {ECO:0000305};
DE            EC=2.7.4.- {ECO:0000269|PubMed:24930102};
DE   AltName: Full=Polyphosphate kinase PPK2 3 {ECO:0000305};
DE   AltName: Full=RpPPK2-3 {ECO:0000303|PubMed:24930102};
GN   OrderedLocusNames=SPO1727 {ECO:0000312|EMBL:AAV95009.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=24930102; DOI=10.1007/s10529-014-1566-6;
RA   Achbergerova L., Nahalka J.;
RT   "Degradation of polyphosphates by polyphosphate kinases from Ruegeria
RT   pomeroyi.";
RL   Biotechnol. Lett. 36:2029-2035(2014).
CC   -!- FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert
CC       NDP to NTP. PolyP hydrolysis is slightly faster with UDP, but it can
CC       also use ADP, GDP and CDP. {ECO:0000269|PubMed:24930102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP;
CC         Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + CTP = [phosphate](n+1) + CDP;
CC         Xref=Rhea:RHEA:55408, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + GTP = [phosphate](n+1) + GDP;
CC         Xref=Rhea:RHEA:55412, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphate](n) + UTP = [phosphate](n+1) + UDP;
CC         Xref=Rhea:RHEA:55404, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280,
CC         ChEBI:CHEBI:16838, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:24930102};
CC       Note=Also accepts various divalent metal ions.
CC       {ECO:0000269|PubMed:24930102};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.6 mM for UDP {ECO:0000269|PubMed:24930102};
CC         Note=kcat is 294 min(-1) with UDP as substrate.
CC         {ECO:0000269|PubMed:24930102};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:24930102};
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 2 (PPK2) family. Class
CC       I subfamily. {ECO:0000305}.
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DR   EMBL; CP000031; AAV95009.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5LSN8; -.
DR   SMR; Q5LSN8; -.
DR   STRING; 246200.SPO1727; -.
DR   EnsemblBacteria; AAV95009; AAV95009; SPO1727.
DR   KEGG; sil:SPO1727; -.
DR   eggNOG; COG2326; Bacteria.
DR   HOGENOM; CLU_048699_2_1_5; -.
DR   OMA; RTHYENV; -.
DR   BRENDA; 2.7.4.1; 8123.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016898; Polyphosphate_phosphotransfera.
DR   InterPro; IPR022488; PPK2-related.
DR   InterPro; IPR022486; PPK2_PA0141.
DR   Pfam; PF03976; PPK2; 1.
DR   PIRSF; PIRSF028756; PPK2_prd; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03707; PPK2_P_aer; 1.
PE   1: Evidence at protein level;
KW   Kinase; Reference proteome; Transferase.
FT   CHAIN           1..301
FT                   /note="NDP-polyphosphate phosphotransferase 3"
FT                   /id="PRO_0000442595"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  34740 MW;  FBD3DAAD77205069 CRC64;
     MNRNGSTKDP RRMTGAATGE ISRYFNDKAP KDIRRAIEKA DKDDILSTTY PYDAEMTAKD
     YRAQMEALQI ELVKLQAWIK QSGARVALLF EGRDAAGKGG TIKRFRENLN PRGARVVALS
     KPTEAERSQW YFQRYIQHLP SAGELVFYDR SWYNRGVVEH VFGWCDEEQR ERFFRQVMPF
     EHDLVDDGIH LFKFWLNVGR AEQLRRFHDR ERDPLKQWKL SPVDIAGLDK WEAYTTAISQ
     TLTRSHSDRA PWTVIRSDDK KRARLAAIRT VLSGIDYDNK DRAAVGQPDA AICGGPDIWD
     A