PPK1_DICDI
ID PPK1_DICDI Reviewed; 1053 AA.
AC Q54BM7; Q9U6U8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Polyphosphate kinase;
DE EC=2.7.4.1;
DE AltName: Full=ATP-polyphosphate phosphotransferase;
DE AltName: Full=Polyphosphate kinase 1 {ECO:0000303|PubMed:17940044};
DE Short=PPK1 {ECO:0000303|PubMed:17940044};
DE AltName: Full=Polyphosphoric acid kinase;
GN Name=ppkA; ORFNames=DDB_G0293524;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Myc-1;
RA Sims M.D., Katz E.R.;
RT "Polyphosphate kinase is required for normal growth and development gene in
RT Dictyostelium discoideum.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15701689; DOI=10.1073/pnas.0500023102;
RA Zhang H., Gomez-Garcia M.R., Brown M.R., Kornberg A.;
RT "Inorganic polyphosphate in Dictyostelium discoideum: influence on
RT development, sporulation, and predation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2731-2735(2005).
RN [4]
RP CHARACTERIZATION, SUBCELLULAR LOCATION, FUNCTION, AND SUBUNIT.
RX PubMed=17940044; DOI=10.1073/pnas.0706847104;
RA Zhang H., Gomez-Garcia M.R., Shi X., Rao N.N., Kornberg A.;
RT "Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote,
RT Dictyostelium discoideum, with a role in cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16486-16491(2007).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC of ATP to form a long-chain polyphosphate (polyP). Produces polyP in a
CC broad range of chain lengths (50-300 Pi residues). Involved in
CC development (growth and fruiting body formation), sporulation,
CC phagocytosis, cell division and the late stages of cytokinesis.
CC {ECO:0000269|PubMed:15701689, ECO:0000269|PubMed:17940044}.
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; EC=2.7.4.1;
CC Evidence={ECO:0000269|PubMed:17940044};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19574;
CC Evidence={ECO:0000269|PubMed:17940044};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.5 umol/min/mg enzyme;
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.;
CC -!- SUBUNIT: Hexamer. May form higher oligomeric structures in the presence
CC of ATP. {ECO:0000269|PubMed:17940044}.
CC -!- SUBCELLULAR LOCATION: Vesicle {ECO:0000269|PubMed:17940044}.
CC -!- DEVELOPMENTAL STAGE: Enzymatic activity is higher during the stationary
CC vegetative phase and on the spores. {ECO:0000269|PubMed:15701689}.
CC -!- SIMILARITY: Belongs to the polyphosphate kinase 1 (PPK1) family.
CC {ECO:0000305}.
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DR EMBL; AF176830; AAD53165.1; -; Genomic_DNA.
DR EMBL; AAFI02000218; EAL60574.1; -; Genomic_DNA.
DR RefSeq; XP_629002.1; XM_629000.1.
DR AlphaFoldDB; Q54BM7; -.
DR SMR; Q54BM7; -.
DR BioGRID; 1254289; 1.
DR DIP; DIP-46221N; -.
DR STRING; 44689.DDB0216190; -.
DR PaxDb; Q54BM7; -.
DR EnsemblProtists; EAL60574; EAL60574; DDB_G0293524.
DR GeneID; 8629286; -.
DR KEGG; ddi:DDB_G0293524; -.
DR dictyBase; DDB_G0293524; ppk1.
DR eggNOG; ENOG502QUEZ; Eukaryota.
DR HOGENOM; CLU_290615_0_0_1; -.
DR InParanoid; Q54BM7; -.
DR OMA; AHPFPQV; -.
DR PhylomeDB; Q54BM7; -.
DR BRENDA; 2.7.4.1; 1939.
DR PRO; PR:Q54BM7; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0009358; C:polyphosphate kinase complex; IEA:InterPro.
DR GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008976; F:polyphosphate kinase activity; IDA:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; IDA:dictyBase.
DR GO; GO:0006797; P:polyphosphate metabolic process; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0009847; P:spore germination; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:dictyBase.
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 SUPFAM; SSF140356; SSF140356; 1.
DR TIGRFAMs; TIGR03705; poly_P_kin; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding;
KW Phagocytosis; Phosphoprotein; Reference proteome; Sporulation; Transferase.
FT CHAIN 1..1053
FT /note="Polyphosphate kinase"
FT /id="PRO_0000328623"
FT REGION 23..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 800
FT /note="Phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 49
FT /note="T -> I (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Missing (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="E -> G (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="K -> E (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="L -> F (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
FT CONFLICT 880..882
FT /note="IQL -> Q (in Ref. 1; AAD53165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1053 AA; 118182 MW; 9E26984706E5A278 CRC64;
MITNSKMENK ILDEFDEEEL NKLKINSNNK ESTTTTTSTT TTTTTTTSTS GEESDDEHTG
SSSSTAAMEL HRYKISQECP VDFEDDYDEE SSSFDEEDED SAAESNGGNG KLIPNPNDKK
KKRSSKSSSK SSKSKSKSKN KETTANPVQN CQLMESGTLF SPTEFVKSST VNPSKSPVQP
IKLSSMLGLS ELGTSNVLTV QNPQPISEPL KNDISSGSSS SSSSNNNNSN SNSNGNCNSD
STKSKFTSLN SWDAPPLANV LPDPSYCQDI VDSENNFIVP SVKHTILDVD NLFNNLIQNT
NNNNNNDFKS STMIGKPFSS GGDGSTSPLI SGLSSSSIIP NGNGSLAEQQ QQQQQSIPES
EIPIDIKVLQ LSGSRMFFNR ELSELIYFYR ILYEAYNPTY PILERVRFIA ITSQNLDMYF
CKRALKLRLG YISTRKTLKP EEHYINMVLN TTRNLINEIY NIYMNILAPE LSNNNVFIIK
YSDLTEPEKI QLRGFFLQHV FPLMTPLVVD AGHPFPNLSN LSLNIAVLLK HDEDTTRFVR
IKVPQRIPRF VHIKQRSNYS IIPMEEIILA NLDTLFPNTK ILTKSLFRVS RHNDLKLSGE
DQANDLLELI KTELHKRKFA PMVRLEVSHN MPAEILDMLK TQLALDAYDV YVINGPLGLQ
DLFELCKLNL PHLKFQPWVP HIPSRLVNLA KYPSEDVFSV IRKGELLVNL PYLSFNSSVQ
FFIESAVKDP KVLAIKIAIY RTNSNSQLIR ALCEAASHKE VMVLVDLKAS GDEEQNTKFA
RLLEQAGCHV SYGLVGLKTH AKIAMVVREE ENGLREYLNI STGNYNASTS DVYADICLFS
CDPDLGEDMC NLFNYLTGYS RVSSFKKLLI APMNMRSTLI QLIDNEAKNA REGKDATINA
VMNGLDDKRL VNALYQASIA GVKITLVVRG RCRILPGIKG ISENIKVISI LGRFLEHSRI
YCFHNNGKPK AYIASADWLH RNLKRRVEVM VPVDDANNIK QLYEIINVYC NDSNAWEMLS
DGRYKKRSSP IDEDSQTQFM NQTNQKHPVI WSK
