ID A0A4P6UKD4_9BURK Unreviewed; 733 AA. AC A0A4P6UKD4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 22-FEB-2023, entry version 13. DE RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800}; DE EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800}; DE AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00347}; DE AltName: Full=Polyphosphoric acid kinase {ECO:0000256|HAMAP-Rule:MF_00347}; GN Name=ppk1 {ECO:0000313|EMBL:QBK05828.1}; GN Synonyms=ppk {ECO:0000256|HAMAP-Rule:MF_00347}; GN ORFNames=DW355_14830 {ECO:0000313|EMBL:QBK05828.1}; OS Hylemonella gracilis. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Hylemonella. OX NCBI_TaxID=80880 {ECO:0000313|EMBL:QBK05828.1, ECO:0000313|Proteomes:UP000292939}; RN [1] {ECO:0000313|EMBL:QBK05828.1, ECO:0000313|Proteomes:UP000292939} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NS1 {ECO:0000313|EMBL:QBK05828.1, RC ECO:0000313|Proteomes:UP000292939}; RA Tyc O., Kulkarni P., Gawehns F., Hundscheid M., Zweers H., Garbeva P.; RT "Exploring interactions and the metabolic potential of the ultra-small soil RT bacteria Hylemonella gracilis."; RL Submitted (JUL-2018) 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:0000256|HAMAP- CC Rule:MF_00347, ECO:0000256|RuleBase:RU003800}. 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:0000256|HAMAP-Rule:MF_00347, CC ECO:0000256|RuleBase:RU003800}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00347, CC ECO:0000256|RuleBase:RU003800}. CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family. CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP031395; QBK05828.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4P6UKD4; -. DR EnsemblBacteria; QBK05828; QBK05828; DW355_14830. DR OrthoDB; 9761456at2; -. DR Proteomes; UP000292939; 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 CDD; cd09168; PLDc_PaPPK1_C2_like; 1. DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2. DR Gene3D; 3.30.1840.10; Polyphosphate kinase middle domain; 1. DR Gene3D; 1.20.58.310; Polyphosphate kinase N-terminal domain; 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; POLYPHOSPHATE KINASE; 1. DR PANTHER; PTHR30218:SF0; POLYPHOSPHATE KINASE; 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; SSF56024; Phospholipase D/nuclease; 2. DR SUPFAM; SSF143724; PHP14-like; 1. DR SUPFAM; SSF140356; PPK N-terminal domain-like; 1. DR TIGRFAMs; TIGR03705; poly_P_kin; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00347}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00347}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00347}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00347}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00347}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_00347}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00347}. FT DOMAIN 27..128 FT /note="Polyphosphate kinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF13089" FT DOMAIN 137..342 FT /note="Polyphosphate kinase middle" FT /evidence="ECO:0000259|Pfam:PF02503" FT DOMAIN 367..539 FT /note="Polyphosphate kinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF17941" FT DOMAIN 547..718 FT /note="Polyphosphate kinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF13090" FT ACT_SITE 471 FT /note="Phosphohistidine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 64 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 411 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 441 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 512 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 608 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" FT BINDING 636 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00347" SQ SEQUENCE 733 AA; 81993 MW; 2F2FEC0433DBD3AB CRC64; MNTNLPTVIS DIAGAAASGK AAALPLLDRD HSVLAFNWRV FDWACRADVP LLERLRYLCI VSSNLDEFFE VRSEPHLMAY QRKDTQGLYT AASFTRLSAA IHELVARQYA LYNDELTPAF RKEGIEIVSH GDRNAAQRRW VRQYFEQEVQ PLLIPVGLDP SHPFPQVANK SLNFIVRLGG KDAFGRENDI AIVKVPRALP RLIPMPDKLC GHGSRRRRLF VSLSSVIRAH LEELFPGREM LHFSQFRVTR HSDLAVDEED VKNLRTALRQ GLEHRHYGQA VRLEVSAGCP QDLADFLLSQ FDLPEGALYR VHGPVNLGRM GQLVDLLSDP QLEKRLRFPS YRASYPSQLA GTAQGGASAS GAAGVQSIFE RLERGDVLIH QPYERFDGVL DFLREAVNDP QVLAIRQTVY RTGANSALMD LLREAVRRGK EVTVVLELKA RFDEEVNIDW AERLEFIGVQ VLYGVVGLKT HAKAMLVTRR VPGAGGEAGG PSLRRYAHLS TGNYNPATAR FYTDWSHLTA DPQITADVEQ VFIHLAGQNR LPRLHQLWMA PFHLHKKLLE KIETLQAAAA AGRPARLIAK MNALTDEALI RALIEAGQQG VKIDLIVRGA CMLPAGVPGQ TENIRVRSII GRFLEHARVF YFRHGEGVEA DESLYLASAD WMNRNMLRRV ELAWPVLDPA LRQRVIDETL SAALQDNDGA WELMPDGRYE RLQPASGAPA LSVQRALMGR YGA //