ID A0A4P6UKD4_9BURK Unreviewed; 733 AA. AC A0A4P6UKD4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. DE RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008191}; DE EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008191}; 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 RT soil bacteria Hylemonella gracilis."; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal CC phosphate of ATP to form a long-chain polyphosphate (polyP). CC {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, CC ECO:0000256|SAAS:SAAS00537780}. 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; CC EC=2.7.4.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00347, CC ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS01115515}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00347}; CC -!- PTM: An intermediate of this reaction is the autophosphorylated CC ppk in which a phosphate is covalently linked to a histidine CC residue through a 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 ECO:0000256|SAAS:SAAS00944215}. 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 Proteomes; UP000292939; Chromosome. 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: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 {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00420136}; KW Complete proteome {ECO:0000313|Proteomes:UP000292939}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008214, ECO:0000313|EMBL:QBK05828.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00347}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00347}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008167}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|RuleBase:RU003800}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008129, KW ECO:0000313|EMBL:QBK05828.1}. FT DOMAIN 27 128 PP_kinase_N. {ECO:0000259|Pfam:PF13089}. FT DOMAIN 137 342 PP_kinase. {ECO:0000259|Pfam:PF02503}. FT DOMAIN 367 539 PP_kinase_C_1. {ECO:0000259|Pfam: FT PF17941}. FT DOMAIN 547 723 PP_kinase_C. {ECO:0000259|Pfam:PF13090}. FT ACT_SITE 471 471 Phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00347}. FT METAL 411 411 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT METAL 441 441 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT BINDING 64 64 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 512 512 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 608 608 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 636 636 ATP. {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 //