PPK1_ACICJ
ID PPK1_ACICJ Reviewed; 727 AA.
AC A5G1J3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=Acry_2534;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ31725.1; -; Genomic_DNA.
DR RefSeq; WP_012040123.1; NC_009484.1.
DR AlphaFoldDB; A5G1J3; -.
DR SMR; A5G1J3; -.
DR STRING; 349163.Acry_2534; -.
DR EnsemblBacteria; ABQ31725; ABQ31725; Acry_2534.
DR KEGG; acr:Acry_2534; -.
DR eggNOG; COG0855; Bacteria.
DR HOGENOM; CLU_009678_5_0_5; -.
DR OMA; NIKWARK; -.
DR OrthoDB; 76567at2; -.
DR Proteomes; UP000000245; 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..727
FT /note="Polyphosphate kinase"
FT /id="PRO_1000133401"
FT ACT_SITE 445
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 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 415
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
FT BINDING 602
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00347"
SQ SEQUENCE 727 AA; 81408 MW; ECBB9382B8963F63 CRC64;
MDQETLPRTA TEPMPAGDSD RFINRELSWL AFNSRVVAAA ENPRYPLLER LRFISISGSN
LDEFYSVRVA GLIGQARAGL ALRSSDGLTP TQQLGEINRC ARALMETQQR VLGTVLAELA
GAGLTIIAPH ELNEADRAFL DQHFMERVFP VLTPLAIDPA HPFPFVQNMG LVLALKLIRQ
EDSGVMRALI PLPAQIRRFI RLPDPSPETI RFVKLEDLVI LFLDRLFHGF RLAGSGLFRV
CRDTDVEFEE EAEDLVQSYE TALKRRRRGA AIELTLAADL PDDLRTLVID EVEAPEDQLF
VEPGMLGLVD LKEMIVDDRP ELLFPAYTPR FPERIRDFGG DCFAAIRNKD IIVHHPFESF
DVVVQFLRQA ASDPNVVAIK QTLYRTSRDS PIVGALIEAA ESGKSVTAMV ELRARFDEEA
NIRLARALEA AGVQVVYGFL GLKTHAKLSL VVRREGSAMR AYAHFGTGNY HPITARIYTD
LSFFTCDQQL TRDAARLFNY MTGYARPEQM DQLVYSPITT RRVIAALIDA EIEAARAGRP
SGIWLKLNSL VDERLIDHLY RASAAGVPVS CVVRGICCLR PGVPGLSENI RVKSIIGRFL
EHARIAVFAN GARMPDRENK VFISSADWMA RNMDWRVETF VPIHNPTVHA QVLDQIMAVD
LRDDVDSWTL GPDGVWTRVL PGDPPVSAHE YFMTNPSLSG RGSALRGPLT QQQRDQIRYR
KTFLTND
