ID J4C2S2_THEOR Unreviewed; 1666 AA.
AC J4C2S2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN ORFNames=TOT_010001190 {ECO:0000313|EMBL:BAM39186.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39186.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39186.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39186.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU365032}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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DR EMBL; AP011946; BAM39186.1; -; Genomic_DNA.
DR RefSeq; XP_009689487.1; XM_009691192.1.
DR STRING; 869250.J4C2S2; -.
DR EnsemblProtists; BAM39186; BAM39186; TOT_010001190.
DR GeneID; 20713990; -.
DR KEGG; tot:TOT_010001190; -.
DR VEuPathDB; PiroplasmaDB:TOT_010001190; -.
DR eggNOG; KOG1057; Eukaryota.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000003786; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 4..90
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 243..302
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 354..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 186005 MW; BF9793EC587700FD CRC64;
MKFTLGVCAM ESKVESSPMK SILKHLEDSG DFIIIIFPEE MILNEPITKW PVVECLISFY
SVKFPQEKAI EYVKLVKPII LNDLEKQRIL RSRINVYREL QACRIPHPNY LLVDHEMVKK
GLHTFEEHYD YIVYNNVRLN KPFIEKPIDS DDHNNWIYYP SNTGGGCKKL FRKIHDRSSK
YCPEIHNVRR NGTYIYEEFM LTFGTDIKVY AVGSMFAHAE ARKSPTLDGK VKRYSDGKEY
RYPVILTSEE KTIAYRIVDH FKQTVCGFDI LRTFDGPYVC DVNGWSFVKR NKKYHIDCSQ
IIRAIFLLKL QSKYNILIDG VLQNKPTGYK PVGAESGLLS EGAIETNTYE KLEASEASDG
AVDESGAKGP GRMQSRPRDQ EKSIKNKSHE ELCSVIVVMR HADRRPKNKL KFFTQQKEIL
NYFKGNESEV KLKSTEELIK LNQLNDQIIE ELEEPNRAAT TCVAALNRAN SNAAGLNELL
VELNYHKEFQ RMLRKGYEFS GINRKVQLKA VYKPKSVMDM DKSGTREGTE SASGEGIFVG
TTKVGGSTGR ETPVRQLEKV LVVAKWGGDL TDVGKSQAED LGRRLRQTLY PADSSALIRL
HSTYRHDFKI FSSDEGRCQI TGAAFTKGIL DLEGELTPIL VAMTIRNKKA YQLLNETVVV
EERSKCRYKL DELITHHGTP EYDEILQELS ENERYYYSKA LEDADFSQDD LVNLSNLIRY
YINTIHREET MWSSLYSVDD YAFHIVNKLS SLQTRWTQLL LKFHRPSFGG FGRVKSGGFY
KSHRGLNRVN SSLLERIYGD ISGLELDSLY GANTLDPSCA KNIAASTRDD RGADAGRGVS
RVSRTRHGTD AGIRGVAGDN GATKTQRAGH ATIELRGNGS NRNDNPANGG TRDGTAENMK
EASFQSGTNY STGIHGGNKE HGTVGNNTGG MRTAGGRGRT LSRDEEMHSS DYCPEERYDY
TKLSDIVDNI RYDLIHLHHL LGQALEIAFE IYRIVERLSS VISPCEYGVT PMEKLQIGAK
IAWNLLKKIQ HDVSHQRVRM SPYTDQEKLL TSSNASTTHD RSSESTQNNV NVTKGSSPKT
VTGEGGQRTV TRESGVRDSP KKVASSKATE YSSNAISGTT HVDSTSRHAV SGGNGQYDSG
AQDTKNLNVS SSLEHLEYDI DFMVNNDTSA SSIAVNSLAS SGTYLDSSKI FETGKCFIGG
VRPTEMYLFN SSTRTEILWY NMRIAKSVAT GTKSKGDSRG KGKAYSSNSS DSGKDESVIL
NSYSLWSHLS PSNSMENITD KSVDVSKTTE MDSSTVVGAD EAATSSSGST KWASREDTSK
AVPVMTGPKR SAAYNILTAT GTIRGKNDGA GNMGSVNLTD LNQGWGWDEK IFDELVRLGT
DDDLGIRSQQ RVVRSRYYVT SASHMFSVFN FFKYAHLLDD SFDTNLKHIE SINDLHYLSH
IVLRVWRSRS SEGFFNRLEI LVSSGAKDGF GQNLSLLEQS AKNQKNKYKR HIQRYKLRTL
QSSNCSYCPI TLNRSGSGRH VDTETVGRSN DAIGAFTGTG TMATGSDIVD KYNLMVTNPA
NKKFKCFKCF LEQYKLSEAS AVSSPIKASA GKRTQKKDHA SSNASNLDTA GSCASGVDNR
EDDGASNKTV PPYCELNNLV LMNRNFGLDR LNNLIQRTYE EIISKG
//
