ID W2ZPZ8_PHYPR Unreviewed; 1128 AA.
AC W2ZPZ8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=F442_05007 {ECO:0000313|EMBL:ETP49452.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP49452.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP49452.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP49452.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00004514, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP49452.1}.
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DR EMBL; ANIY01001096; ETP49452.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZPZ8; -.
DR EnsemblProtists; ETP49452; ETP49452; F442_05007.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:InterPro.
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; IPR033379; Acid_Pase_AS.
DR InterPro; IPR011761; ATP-grasp.
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; 2.
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.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Coiled coil {ECO:0000256|SAM:Coils};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 104..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 755..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 713..740
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1128 AA; 128016 MW; 57D430EE1D009D1D CRC64;
MTPFDAPDAR YTLGVCVMER KARSAPMLEI LGRLPPELFR IEFFGDETIL HQPVDVWPRC
DALIAFFSKG FPLQKTQDYV ALRRPVVVND LDTQYLLQDR REVYRVLQEH GVPTPRHVFV
SRDGYGGQTE PPEVIEREDF IQVDGVRINK PFVEKPVDGE DHNIHIYYPM SAGGGCKRLF
RKIGNRSSEY DPQVNTVRTG GGSYIYEEFL STQGTDVKVY TVGPHYAHAE ARKSPVLDGR
VVRDADGKEV RYPVMLSTEE KQIAYRVCRA FKQTVCGFDI LRVRDASYVC DVNGWSFVKN
SEKYYDDCGI LLTQYLEQAL TSGGVMAGED FGTDSSAFSS VTFRFAPDAP PPSAELSEPP
TAHRHAMLRG PSTSIAESEV SEADSITDGA EDTVYQEEEL RCVLAIIRHG DRTPKQKMKM
NVCHPAFLQF YEDRLRESQQ ENGDGNDSKK KKKMDLKIKA VANLERLLQV SKDLLDKYEN
RDPAFMEFLE QREVKCGEDA TDRVKGYRTL RDVLQRWQLV GINRKVQLKP KEFVSVPVDG
TDENGEQLTT RRVSKLLLII KWGGDLTHTG EEQAEHLGQK FRRMMYPGGA GGLNRLHSTF
RHDLKIYTSD EGRVQKTAAS FAKGLLELEG DIIPILVGLV LKSKDADSML DQSGSSAQEI
IMRVKQRLHK IIHREDHCSQ LIDSNSRLIR SVALALTKVD QPIKKMGIMH KLLQSLKEQL
TRMIQEKAQY KSEIDRWQQK KATAGRLLAP VMGRSASVNE LSQPRSRHVH SYSPRKKHSE
GSNIPSDAAN SSVGLRKMRP QESLSPEEIK YPEPCGRETL EVMRERWAKL YRDFYVKKRD
TYDLSKIPDI HDCIRYDAVH NAHLNLTDVR ELLEISSALS HALVPQEYGI NVDEKIFIGS
AMCRTLLSKI NTDLDLARGL KPDVLKDHNT HRLNPSYAKK IKSTHRSVRT RLYFTSESHL
HSLLNVLRYG REECAIKSPI GEESRKWIED IPELCYMTHF VVRVFERVQY SLDDPQRFRV
EISVSPGADQ DPLNSDPEKQ LEVAPLKIIS HEGLTCQELV DYVADCIDFA EQNEIKEMIS
RTVAAKSNSS PENTNGDSSS NSGDVTPVKR SMYSLSNNSS DSNFSSDN
//
