PK21A_RUEPO
ID PK21A_RUEPO Reviewed; 305 AA.
AC Q5LX16;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=NDP-polyphosphate phosphotransferase 1 {ECO:0000305};
DE EC=2.7.4.- {ECO:0000269|PubMed:24930102};
DE AltName: Full=Polyphosphate kinase PPK2 1 {ECO:0000305};
DE AltName: Full=RpPPK2-1 {ECO:0000303|PubMed:24930102};
GN OrderedLocusNames=SPO0224 {ECO:0000312|EMBL:AAV93549.1};
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, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP 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 GDP, but it can
CC also use ADP, CDP and UDP. {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 -!- ACTIVITY REGULATION: Shows little dependence on metals.
CC {ECO:0000269|PubMed:24930102}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for GDP {ECO:0000269|PubMed:24930102};
CC Note=kcat is 251 min(-1) with GDP as substrate.
CC {ECO:0000269|PubMed:24930102};
CC pH dependence:
CC Has two pH optima at 8 and 10. {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; AAV93549.1; -; Genomic_DNA.
DR RefSeq; WP_011045992.1; NC_003911.12.
DR AlphaFoldDB; Q5LX16; -.
DR SMR; Q5LX16; -.
DR STRING; 246200.SPO0224; -.
DR PRIDE; Q5LX16; -.
DR EnsemblBacteria; AAV93549; AAV93549; SPO0224.
DR KEGG; sil:SPO0224; -.
DR eggNOG; COG2326; Bacteria.
DR HOGENOM; CLU_048699_3_0_5; -.
DR OMA; ESTQWYY; -.
DR OrthoDB; 953793at2; -.
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..305
FT /note="NDP-polyphosphate phosphotransferase 1"
FT /id="PRO_0000442593"
SQ SEQUENCE 305 AA; 36711 MW; 46E32B3FA063BD4B CRC64;
MTHESDDPSL DWLEAELEDS LDEDFEIEFS EPMLSMEIRR IYKDQRPDLL DRQVYFRNLL
RLQAELIKLQ DWVQHTNSKV LIIMEGRDAA GKGGVIKRIT QRLNPRIARV VALPAPSRRE
QSQWYFQRYV PYLPSGGEMV LFDRSWYNRA GVERVMGFAT EDQVEQFFQD VPEFERMLVR
SGIILLKYWF SITDEEQQLR FLMRVHDPMK QWKLSPMDLE SRIRWEQYTK AKEQMFSRTN
IPEAPWYIVE GNDKKRERLN CIEHLLSKIP YEDIPHEKVT LPDRRYNPDY ERQVLPDELY
VPKVY
