(data stored in ACNUC7421 zone)

SWISSPROT: Q4ZZQ6_PSEU2

ID   Q4ZZQ6_PSEU2            Unreviewed;       736 AA.
AC   Q4ZZQ6;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 98.
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=ppk {ECO:0000256|HAMAP-Rule:MF_00347};
GN   OrderedLocusNames=Psyr_0293 {ECO:0000313|EMBL:AAY35366.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35366.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35366.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35366.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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}.
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DR   EMBL; CP000075; AAY35366.1; -; Genomic_DNA.
DR   RefSeq; WP_011266303.1; NC_007005.1.
DR   RefSeq; YP_233404.1; NC_007005.1.
DR   STRING; 205918.Psyr_0293; -.
DR   EnsemblBacteria; AAY35366; AAY35366; Psyr_0293.
DR   GeneID; 3365769; -.
DR   KEGG; psb:Psyr_0293; -.
DR   PATRIC; fig|205918.7.peg.295; -.
DR   eggNOG; ENOG4105CUU; Bacteria.
DR   eggNOG; COG0855; LUCA.
DR   HOGENOM; HOG000248948; -.
DR   KO; K00937; -.
DR   OMA; MTLYRVG; -.
DR   BioCyc; PSYR205918:G1G4J-294-MONOMER; -.
DR   Proteomes; UP000000426; 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: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;
DR   PRODOM; Q4ZZQ6.
DR   SWISS-2DPAGE; Q4ZZQ6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00420136};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00008214, ECO:0000313|EMBL:AAY35366.1};
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:AAY35366.1}.
FT   DOMAIN       53    158       PP_kinase_N. {ECO:0000259|Pfam:PF13089}.
FT   DOMAIN      169    369       PP_kinase. {ECO:0000259|Pfam:PF02503}.
FT   DOMAIN      377    540       PP_kinase_C_1. {ECO:0000259|Pfam:
FT                                PF17941}.
FT   DOMAIN      549    721       PP_kinase_C. {ECO:0000259|Pfam:PF13090}.
FT   ACT_SITE    481    481       Phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   METAL       421    421       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   METAL       451    451       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   BINDING      91     91       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     514    514       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     610    610       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     638    638       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
SQ   SEQUENCE   736 AA;  82684 MW;  5B4AD639DB904964 CRC64;
     MNTEALIEAA VQVDVPEATP VVEPDIEVIP AIEAPAAVVP AIVAPNLDDS SLYIHRELSQ
     LQFNIRVLEQ ALDESYPLLE RLKFLLIFSS NLDEFFEIRV AGLKKQITFA REQAGADGLQ
     PHQALARISE LVHGHVDRQY AILNDILLPE LEKHQVRFIR RRHWTAKLKA WVRRYFRDEI
     APIITPIGLD PTHPFPLLVN KSLNFIVELE GIDAFGRDSG LAIIPAPRLL PRVIKVPEEV
     CGPGDNFVFL SSMIHAHADD LFQGMKVKGC YQFRLTRNAD LALDSEDVED LARALRGELF
     SRRYGDAVRL EVADTCPKHL SDYLLKQFNL HESELYQVNG PVNLTRLFSI TGLDSHPELQ
     YPPFTPAIPK LLQNSENVFS VVSKQDILLL HPFESFTPVV DLLRQAAKDP HVLAVRQTLY
     RSGANSEIVD ALVDAARNGK EVTAVIELRA RFDEESNLQL ASRLQAAGAV VIYGVVGFKT
     HAKMMLILRR EAGEIVRYAH LGTGNYHAGN ARLYTDYSLL TSDDALCEDV GKLFSQLIGM
     GKTLRMKKLL HAPFTLKKGM LDMIARETQF ALDGKPAHII AKFNSLTDPK IIRALYKASQ
     SGVRIDLVVR GMCCLRPGIA GVSHNIHVRS IIGRFLEHTR VFYFLNGGDE QMFLSSADWM
     ERNLDKRVET CFPVEGKKLI LRVKKELESY LTDNTHSWLL QSDGRYVRST PTGNQNPRSA
     QATLLERLSN PVLSVR
//

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