PPK1_SYNY3
ID PPK1_SYNY3 Reviewed; 728 AA.
AC Q55898;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Polyphosphate kinase {ECO:0000255|HAMAP-Rule:MF_00347};
DE EC=2.7.4.1 {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00347};
DE AltName: Full=Polyphosphoric acid kinase {ECO:0000255|HAMAP-Rule:MF_00347};
GN Name=ppk {ECO:0000255|HAMAP-Rule:MF_00347}; OrderedLocusNames=sll0290;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC of ATP to form a long-chain polyphosphate (polyP). {ECO:0000255|HAMAP-
CC Rule:MF_00347}.
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; EC=2.7.4.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00347};
CC -!- PTM: An intermediate of this reaction is the autophosphorylated ppk in
CC which a phosphate is covalently linked to a histidine residue through a
CC N-P bond. {ECO:0000255|HAMAP-Rule:MF_00347}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC {ECO:0000255|HAMAP-Rule:MF_00347}.
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DR EMBL; BA000022; BAA10660.1; -; Genomic_DNA.
DR PIR; S76968; S76968.
DR AlphaFoldDB; Q55898; -.
DR SMR; Q55898; -.
DR STRING; 1148.1001781; -.
DR PaxDb; Q55898; -.
DR EnsemblBacteria; BAA10660; BAA10660; BAA10660.
DR KEGG; syn:sll0290; -.
DR eggNOG; COG0855; Bacteria.
DR InParanoid; Q55898; -.
DR OMA; NIKWARK; -.
DR PhylomeDB; Q55898; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1840.10; -; 1.
DR HAMAP; MF_00347; Polyphosphate_kinase; 1.
DR InterPro; IPR003414; PP_kinase.
DR InterPro; IPR041108; PP_kinase_C_1.
DR InterPro; IPR024953; PP_kinase_middle.
DR InterPro; IPR036830; PP_kinase_middle_dom_sf.
DR InterPro; IPR025200; PPK_C_dom2.
DR InterPro; IPR025198; PPK_N_dom.
DR InterPro; IPR036832; PPK_N_dom_sf.
DR PANTHER; PTHR30218; PTHR30218; 1.
DR Pfam; PF02503; PP_kinase; 1.
DR Pfam; PF13090; PP_kinase_C; 1.
DR Pfam; PF17941; PP_kinase_C_1; 1.
DR Pfam; PF13089; PP_kinase_N; 1.
DR PIRSF; PIRSF015589; PP_kinase; 1.
DR SUPFAM; SSF140356; SSF140356; 1.
DR TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..728
FT /note="Polyphosphate kinase"
FT /id="PRO_0000128665"
FT REGION 694..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 408
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 728 AA; 82607 MW; 65F0A501464F6CC7 CRC64;
MIQAMPSAPT VDFKDPAYYF NRELSWLAFN QRVLHEGLDD RTPLLERLKF LAIFCSNLDE
FFMVRVAGLK QQVEANVTKL TADGRTPSQQ LKEISKSLRP LVYQQNQVFE YVLKEKLADE
GIFLNDYVDL SQEERQYLHQ FYDDHIFPVL TPLAVDPSHP FPYISNLSLN LGVVVRDPDT
DEELFARVKV PPTLPRFVAL PEDVCQPDPN KPWLWTGVPL EQVIAHNLAS LFPGMIIQEC
HLFRVTRNAD IAVEEDEADD LLLAIEEELR KRRVGKSAVR LEINASTPKN IRDRLMTDLG
LEEIDVYDID GLLGLKDLFF FLSLPAPHLK DEPWASVIPP RLKHVYEFVD GDEDGRVQQE
GIDIFTLIRQ GDILVHHPYQ SFTASVQQFI TQAAYDPHVL TIKMTLYRTS GDSPIVNALI
AAAENGKQVA VLVELKARFD EENNINWARK LEQYGVHVVY GLVGLKTHTK TVLVVRQEGP
DIRRYVHIGT GNYNPKTAKL YTDLGLITCR PELGNDLTNL FNFLTGYSRQ KDYQKLLVAP
VNMRERMVAM IEREADHCLN GGTGRIVAKM NSLVDTQIIR ALYAASQAGV QIDLIVRGIC
CLRPGVENVS ENIRVISVIG RLLEHSRIFY FHNGGEEEIY IGSADWMSRN LTRRVEAVVP
VEQPDLKQEL QSILGILLAD NRQAWELQPD GTYVQRRPAS PEQSQSSQAI FTAQAIAETT
EDPELRSV
