ID A0A3A9NHE7_MORCA Unreviewed; 715 AA. AC A0A3A9NHE7; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 08-MAY-2019, entry version 5. 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:RKL89374.1}; GN Synonyms=ppk {ECO:0000256|HAMAP-Rule:MF_00347}; GN ORFNames=D6D77_03485 {ECO:0000313|EMBL:RKL89374.1}; OS Moraxella catarrhalis (Branhamella catarrhalis). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Moraxella. OX NCBI_TaxID=480 {ECO:0000313|EMBL:RKL89374.1, ECO:0000313|Proteomes:UP000270318}; RN [1] {ECO:0000313|EMBL:RKL89374.1, ECO:0000313|Proteomes:UP000270318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=COPD_M112 {ECO:0000313|EMBL:RKL89374.1, RC ECO:0000313|Proteomes:UP000270318}; RA George L., Haigh R., Mistry V., Haldar K., Barer M., Oggioni M., RA Brightling C.; RT "Sputum M. catarrhalis strains exhibit diversity within and between RT COPD subjects."; RL Submitted (SEP-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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RKL89374.1}. 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; QZGP01000003; RKL89374.1; -; Genomic_DNA. DR RefSeq; WP_064603541.1; NZ_QZGX01000008.1. DR Proteomes; UP000270318; Unassembled WGS sequence. 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: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:UP000270318}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00347, KW ECO:0000256|SAAS:SAAS00008214, ECO:0000313|EMBL:RKL89374.1}; 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:RKL89374.1}. FT DOMAIN 38 143 PP_kinase_N. {ECO:0000259|Pfam:PF13089}. FT DOMAIN 152 350 PP_kinase. {ECO:0000259|Pfam:PF02503}. FT DOMAIN 363 527 PP_kinase_C_1. {ECO:0000259|Pfam: FT PF17941}. FT DOMAIN 536 696 PP_kinase_C. {ECO:0000259|Pfam:PF13090}. FT ACT_SITE 467 467 Phosphohistidine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00347}. FT METAL 407 407 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT METAL 437 437 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00347}. FT BINDING 76 76 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 500 500 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 596 596 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. FT BINDING 624 624 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}. SQ SEQUENCE 715 AA; 80779 MW; 2BF70EABBFD36DC1 CRC64; MINTMNDVNQ ANHADHTNPM TQIDHLFDEK GAFTPKCYIN RDLSALRFQL RVLAQAANPN HPLLERMFFL TIFSSNLDEF FEIRVAGLLQ KMKQGDQVSS LDGRKPSEIL QIISDIAHGA VTQQYQILND EILPELAKHE IRYLRRDELN AKQRAWLKDY FVSQVKPVLT PISIDPAHPF PRLVNKSLNF IISLEGKDAF GRDINRAIVP APRSLPRVIR LPDEITDGKE HHVMLSAVIH EHINELFLGM KVTGCYQFRL TRNADLALAD DVDDIAKALE GELDNRRFGH EVRLEVTTNC PQDICDFLLD EFELDKSQLY RVNGPVNLTR LLTSFDRPEL KFKPFTPAMP KAFRDMDMSS AGSMFAAISR QDVLVHHPFH TFNPVINLLW QAASDPNVLA IKQTIYRSGV NSEIVQALAA AARSGKEVTA VIELRARFDE ASNIAVANML QEAGAVVVYG IVGYKTHAKM MLIVRRENGK IRRYVHLGTG NYHAGNAKAY TDYGLFTANA EVTEDVAGVF QQLTGMGRPL PSKQILHAPF TLHDTLMRLI DHEIAHVKAG KKGRIIMKFN ALTERKIINK LYEASIAGVQ IDLIVRSICC LRPQVAGLSE NIRVRSIVGR FLEHTRVYYF ANGGEERLYC SSADLMDRNL LHRVEVAFPI LDKKIFKKIY EDGLMNYLKD DVQAWELLGD GKWQPLLASG GTHDAQKTLL EKITL //