PPK1_RHOPT
ID PPK1_RHOPT Reviewed; 736 AA.
AC B3Q9Q6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Rpal_3458;
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) 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). {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; CP001096; ACF01959.1; -; Genomic_DNA.
DR RefSeq; WP_012496515.1; NC_011004.1.
DR AlphaFoldDB; B3Q9Q6; -.
DR SMR; B3Q9Q6; -.
DR PRIDE; B3Q9Q6; -.
DR EnsemblBacteria; ACF01959; ACF01959; Rpal_3458.
DR GeneID; 66894130; -.
DR KEGG; rpt:Rpal_3458; -.
DR HOGENOM; CLU_009678_5_0_5; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR BioCyc; RPAL395960:RPAL_RS17090-MON; -.
DR Proteomes; UP000001725; 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; Transferase.
FT CHAIN 1..736
FT /note="Polyphosphate kinase"
FT /id="PRO_1000120507"
FT REGION 703..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 423
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 736 AA; 82733 MW; 8C28277774392193 CRC64;
MDSEQVIAIE EKKGETEPAS MIAAGPERFI NRELSWLHFN RRVLEESVNP HHPVLERVRF
LSISANNLDE FFMVRVAGIK AQIREGITER SPDGLTPSEQ LGLINEAVSK LASDQQSIWR
DLRGVLADSG ILLLDGKDVT KAERAWIEDH FLHNIFPLLT PLAIDPAHPF PFIPSLGFTI
GLQLARVSDG RPMNALIRMP ARIDRFIRLP GNGRDQTVRV MTLEQATSLF IGRLFPGYHV
KGQGSFRIIR DSELEIEEEA EDLVRLFETA LKRRRRGSVI RMEVDSSMPE ELRVFVQRAL
TAADDEVFLV DGVLAMNELS QLTRVDRPDL EFVPYVPRHP ERVRDHGGDI FAAIRQKDLI
VHHPYESFDV VVQFLQQAAR DPDVVAIKQT LYRTSNNSPI VRALAEAAEA GKSVTALVEL
KARFDEEANI RWARDLERAG VQVVYGFLQL KTHAKLSLVV RREGGSLTTY IHTGTGNYHP
VTARIYTDLS YFTSDPILGR DAARVFNYIT GYAEPSDIEK MAVSPITLRK TMLEHIRGET
AFAKHGKPAA IWLKMNALVD PEIIDALYEA SRAGVSVELV VRGICCLRPG VPGLSDNIRV
KSIIGRFLEH GRIYCFGNGY GLPSAKAAVY ISSADMMPRN LDRRVEVLCP MLNPTVHQQV
LEQIMVANLK DTEQSWRLLP DGSSTRMKAA KGEEPFNVHN YFMTNPSLSG RGKSLQESSP
RRLTRRAERQ QSQQSS
