PPK1_ERYLH
ID PPK1_ERYLH Reviewed; 715 AA.
AC Q2NC49;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=ELI_03250;
OS Erythrobacter litoralis (strain HTCC2594).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=314225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2594;
RX PubMed=19168610; DOI=10.1128/jb.00026-09;
RA Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC62742.1; -; Genomic_DNA.
DR RefSeq; WP_011413618.1; NC_007722.1.
DR AlphaFoldDB; Q2NC49; -.
DR SMR; Q2NC49; -.
DR STRING; 314225.ELI_03250; -.
DR PRIDE; Q2NC49; -.
DR EnsemblBacteria; ABC62742; ABC62742; ELI_03250.
DR KEGG; eli:ELI_03250; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_5; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000008808; 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; Transferase.
FT CHAIN 1..715
FT /note="Polyphosphate kinase"
FT /id="PRO_1000120502"
FT ACT_SITE 440
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 569
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"
SQ SEQUENCE 715 AA; 80561 MW; DF70F4CB70F4490B CRC64;
MGSHPITQDN DLDPPTEPGE RYFNRELSWL AFNDRVLAEA CNDSYPLLER LRFLSISGSN
LDEFVMIRVA GLVGQVQRGI DEVSDDGRSP REQLNAVVAR LEELSERQQD IWRNLRVQLA
DAGVHVADEE RVNAEAYGWL KQHFFESILP LLTPQALDPA HPFPFISNEG LGLLFTLRRG
GEELVEMVLI PSALPRFIRV PGEDALYISI ESLITRFAKE LFPGFEIVGD GTFRVLRDSD
IEIQEEAEDL VRTFRSAIQR RRRGQVIQLE IEEEFDPTAE ALLREKLDTP GATFVKTDGM
LGIAGLADIV DEDRPDLKFD SYSPRYPERV LEHDGDIFAA IREKDIVIHH PYESFNVVVD
FIRRAAIDPD VVAIKQALYR AGTQSEVVDA LVEAAENGKS VTAVVELKAR FDEEQNLYWA
NKLERAGVQV IYGFVDWKTH AKVAMVVRRE EEGFRTYCHF GTGNYHPITA KIYTDLSYFT
ADPRLGRDAA KLFNFVTGYV EPRELEMLAV SPIDLRETIY AAIDNEMVNA QAGKPAAIWM
KMNQITDVDM IDRLYEASQA GVEIQLVVRG ICNLRPGVPG MSDNIRVKSI IGRFLEHSRI
YAFANGEPMP GTSSTVYISS ADLMVRNLDR RVEQLVPIDN QTVHDQVLQQ VLLANLLDNE
QSWELQPDGS YFRVEVGEKS FNCHRYFMTN PSLSGRGGAL EAGAVPKLAL RKGAV
