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Polyphosphate kinase (EC 2.7.4.1) (ATP-polyphosphate phosphotransferase) (Polyphosphoric acid kinase)

 Q1PJF5_PROMR            Unreviewed;       692 AA.
Q1PJF5;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
27-SEP-2017, entry version 53.
RecName: Full=Polyphosphate kinase {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008280};
EC=2.7.4.1 {ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008280};
AltName: Full=ATP-polyphosphate phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00347};
AltName: Full=Polyphosphoric acid kinase {ECO:0000256|HAMAP-Rule:MF_00347};
Name=ppk {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000313|EMBL:ABE11424.1};
ORFNames=HOT0M-3E5_0009 {ECO:0000313|EMBL:ABE11424.1};
uncultured Prochlorococcus marinus clone HOT0M-3E5.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379388 {ECO:0000313|EMBL:ABE11424.1};
[1] {ECO:0000313|EMBL:ABE11424.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11424.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the reversible transfer of the terminal
phosphate of ATP to form a long-chain polyphosphate (polyP).
{ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800,
ECO:0000256|SAAS:SAAS00537780}.
-!- CATALYTIC ACTIVITY: ATP + (phosphate)(n) = ADP + (phosphate)(n+1).
{ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800,
ECO:0000256|SAAS:SAAS00008307}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00347};
-!- PTM: An intermediate of this reaction is the autophosphorylated
ppk in which a phosphate is covalently linked to a histidine
residue through a N-P bond. {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|RuleBase:RU003800}.
-!- SIMILARITY: Belongs to the polyphosphate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00347, ECO:0000256|RuleBase:RU003800,
ECO:0000256|SAAS:SAAS00537783}.
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EMBL; DQ366736; ABE11424.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJF5; -.
GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008976; F:polyphosphate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0006799; P:polyphosphate biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1840.10; -; 1.
HAMAP; MF_00347; Polyphosphate_kinase; 1.
InterPro; IPR003414; PP_kinase.
InterPro; IPR024953; PP_kinase_middle.
InterPro; IPR025200; PPK_C_dom.
InterPro; IPR025198; PPK_N_dom.
Pfam; PF02503; PP_kinase; 1.
Pfam; PF13090; PP_kinase_C; 1.
Pfam; PF13089; PP_kinase_N; 1.
PIRSF; PIRSF015589; PP_kinase; 1.
SUPFAM; SSF140356; SSF140356; 1.
TIGRFAMs; TIGR03705; poly_P_kin; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|SAAS:SAAS00008173};
Kinase {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|SAAS:SAAS00008205, ECO:0000313|EMBL:ABE11424.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00347};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00347};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|SAAS:SAAS00008173};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|RuleBase:RU003800};
Transferase {ECO:0000256|HAMAP-Rule:MF_00347,
ECO:0000256|SAAS:SAAS00008205, ECO:0000313|EMBL:ABE11424.1}.
DOMAIN 8 112 PP_kinase_N. {ECO:0000259|Pfam:PF13089}.
DOMAIN 123 321 PP_kinase. {ECO:0000259|Pfam:PF02503}.
DOMAIN 344 687 PP_kinase_C. {ECO:0000259|Pfam:PF13090}.
ACT_SITE 448 448 Phosphohistidine intermediate.
{ECO:0000256|HAMAP-Rule:MF_00347}.
METAL 388 388 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00347}.
METAL 418 418 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00347}.
BINDING 46 46 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
BINDING 481 481 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
BINDING 577 577 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
BINDING 605 605 ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
SEQUENCE 692 AA; 79928 MW; 867D5712E2CFA6C4 CRC64;
MKSQVDVFIN RELSWIEFNK RVLLTGMEKE YKILDKVKFF SIFSNNLDEF FMVRVASLKA
QVEAGITKKS IDGLTPKEQL TKINKEVKNL TILQENYVNN ELKNELKEKG VILKKYKHLC
ENQRNWCNNF FKTSIFPLLT PLVVDPAHPF PFISNLSLNL AALIKDEEDS KNQFVRVKIP
TKNIPRFIRI PNEITQISDE SSHCFIIVED LIGNNINTLF KGMECLNYSF FRVTRDADLE
LKELEADDLL LAVEQSLQKR RLGGDVVRLE VESDMPENIL KLLIESISIQ KEYIYFCKSL
LGLDDLNQLT KIDREDLKDN LLIGKTHPEL KHLDLPSNKN SNSIFKILRK KNILLHHPYD
LFKTSVEEFI NRAADDPLVM AIKITLYRVS QDSPIIAALM RAANNGKEVM TLVELKARFD
EDNNIQWAKQ LEQAGIHVVY GIIGFKTHTK IALIVRKEKG RLRNYFHIGT GNYNSNTSKF
YTDLGLLSTD PEIASDLLEL FNYLSGFSKQ KSYQKLLVSP SSMREKFIFL IKREIKNAGE
GKKAEIIAKM NSLVDPEIIN LLYSASESGV KISLIVRGIC CLYPQRKNLS ENIKVISIIG
HFLEHSRIFW FCNNDDNEVF IGSADWMRRN LDRRIEAITP IEDSELKSQL KTLLQTYMKD
DYFSWIMKED GSYAKYTLDS TNNRSQIDLI NQ


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