ID   PPK1_APHBL              Reviewed;         387 AA.
AC   Q93AK9;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Polyphosphate kinase {ECO:0000250|UniProtKB:P0A7B1};
DE            EC=2.7.4.1 {ECO:0000250|UniProtKB:P0A7B1};
DE   AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000250|UniProtKB:P0A7B1};
DE   AltName: Full=Polyphosphoric acid kinase {ECO:0000250|UniProtKB:P0A7B1};
DE   Flags: Fragment;
GN   Name=ppk;
OS   Aphanizomenon baltica.
OC   Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Aphanizomenon.
OX   NCBI_TaxID=173580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Singer A., Soderback E.;
RT   "Aphanizomenon baltica polyphosphate kinase (ppk) partial sequence.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       of ATP to form a long-chain polyphosphate (polyP).
CC       {ECO:0000250|UniProtKB:P0A7B1}.
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:0000250|UniProtKB:P0A7B1};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0A7B1};
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:0000250|UniProtKB:P0A7B1}.
CC   -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC       {ECO:0000250|UniProtKB:P0A7B1}.
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DR   EMBL; AF421132; AAL16921.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q93AK9; -.
DR   SMR; Q93AK9; -.
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-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1840.10; -; 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; IPR025198; PPK_N_dom.
DR   InterPro; IPR036832; PPK_N_dom_sf.
DR   PANTHER; PTHR30218; PTHR30218; 1.
DR   Pfam; PF02503; PP_kinase; 1.
DR   Pfam; PF17941; PP_kinase_C_1; 1.
DR   Pfam; PF13089; PP_kinase_N; 1.
DR   SUPFAM; SSF140356; SSF140356; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           <1..>387
FT                   /note="Polyphosphate kinase"
FT                   /id="PRO_0000128632"
FT   BINDING         347
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7B1"
FT   BINDING         377
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0A7B1"
FT   NON_TER         1
FT   NON_TER         387
SQ   SEQUENCE   387 AA;  44024 MW;  03DB115172813079 CRC64;
     VFHGGVAGLK QQVEATVNLL TTDGRTPQKQ LDDIRLHLHP QLKKQNTEFQ EVLQPLLRQQ
     GICILDYIEL NQQQRNYLDN YFQEQIFPVL TPLAVDPSHP FPHISNLSLN LAVVVKNPDT
     EEEFFARVKV PQVLPRFLPL PPELRTEDNG KTANWSGIPL EQAIAHNLES LFPGMSIQEY
     HPFRITRDAD LELEEDEAED LLLAIEQELR KRGMGGTPVR LEIRSQTPES IRSRLLQDLG
     LTENDIYEVD GLLGLRDLMY FLLLPLPDLK DPPRQSVVPS RLQRLKEPCI NPDVPEPEDG
     KDFFSVIREK DLLVHHPYQS FSGTVVRFIT SAAHDPNVLA MKMTLYRTSG DSPIVNALIA
     AAENGKQVSV LVELKARFDE ENNIYWA