(data stored in ACNUC7421 zone)

SWISSPROT: Q47T56_THEFY

ID   Q47T56_THEFY            Unreviewed;       702 AA.
AC   Q47T56;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
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=Tfu_0323 {ECO:0000313|EMBL:AAZ54361.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54361.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54361.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0323; -.
DR   EnsemblBacteria; AAZ54361; AAZ54361; Tfu_0323.
DR   KEGG; tfu:Tfu_0323; -.
DR   eggNOG; ENOG4105CUU; Bacteria.
DR   eggNOG; COG0855; LUCA.
DR   HOGENOM; HOG000248948; -.
DR   KO; K00937; -.
DR   OMA; MTLYRVG; -.
DR   BioCyc; TFUS269800:G1G4Q-325-MONOMER; -.
DR   Proteomes; UP000000434; 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; Q47T56.
DR   SWISS-2DPAGE; Q47T56.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00420136}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|SAAS:SAAS00008214, ECO:0000313|EMBL:AAZ54361.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00347,
KW   ECO:0000256|RuleBase:RU003800, ECO:0000256|SAAS:SAAS00008129,
KW   ECO:0000313|EMBL:AAZ54361.1}.
FT   DOMAIN       29    133       PP_kinase_N. {ECO:0000259|Pfam:PF13089}.
FT   DOMAIN      141    334       PP_kinase. {ECO:0000259|Pfam:PF02503}.
FT   DOMAIN      342    508       PP_kinase_C_1. {ECO:0000259|Pfam:
FT                                PF17941}.
FT   DOMAIN      515    680       PP_kinase_C. {ECO:0000259|Pfam:PF13090}.
FT   COILED      244    264       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    446    446       Phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   METAL       386    386       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   METAL       416    416       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00347}.
FT   BINDING      67     67       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     480    480       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     576    576       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
FT   BINDING     604    604       ATP. {ECO:0000256|HAMAP-Rule:MF_00347}.
SQ   SEQUENCE   702 AA;  80132 MW;  9CDACDC22B36557B CRC64;
     MVQKKTAAVA VNAAQMLTRD RDLLPPDRFM NREIGWLRFN QRVLELAEDT TLPLLERALF
     LSIFSSNLDE FFMVRVAGLK RRLATGVPVS SRQDPREQLR EISKVTHELM ERHAACFHTS
     VAPALAEAGI RIVRWNDLTT EEKQQMHRFF RRTIYPVLTP LAVDPAHPFP YISGRSLNLA
     VRVCDPHTGR QTFARIKVPP ALPRFTELGG QRFVPVEDVI SAHLPQLFEG MEILEHHAFR
     VTRNADLEVD EDETDDLVKS LERELLRRRF GPLVRLEVEE TISDEILTLL REELGADEEE
     TYRVPGPLDL SGLAQLHELD RPELKYPPMV PVEPRVLAHN DFFEVLRRSE LLVHHPYESF
     ATTTQRFIEL AASDPKVRAI KQTLYRTSGD SPIMEALIEA ARSGKEVIVL VEIKARFDEQ
     NNIRWARKLE MAGCHVVYGV VGLKTHCKLA LVVREEDDGS LRRYCHIGTG NYNPRTARIY
     EDFGLFSADP EVGEDLSDLF NHLTGFSRKK HYRRLLVAPH ALREALLRQI QHEIANHEQG
     LPARIRIKTN SLVDEEIVDA LYLASRAGVP IDLWVRGSCV LRPGVPGLSE TIRVRSILGR
     FLEHSRIFVF ANGGEPQVWI GSADLMPRNL DRRVEVLVRI VDPGQRSRLM TLMDLAMADS
     TSSWHLNPDG SWTRFTHDEE GNPLVDVQST LRGDRYLRVV DD
//

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