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Database: UniProt
Entry: A0A093Y0J1_9PEZI
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ID   A0A093Y0J1_9PEZI        Unreviewed;       482 AA.
AC   A0A093Y0J1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
DE   Flags: Fragment;
GN   ORFNames=O988_04326 {ECO:0000313|EMBL:KFX98485.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX98485.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFX98485.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX98485.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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|ARBA:ARBA00034629};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC         Evidence={ECO:0000256|ARBA:ARBA00034629};
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|ARBA:ARBA00033696};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC         Evidence={ECO:0000256|ARBA:ARBA00033696};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
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}.
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:KFX98485.1}.
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DR   EMBL; JPJR01000784; KFX98485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Y0J1; -.
DR   STRING; 1391699.A0A093Y0J1; -.
DR   HOGENOM; CLU_000914_3_1_1; -.
DR   Proteomes; UP000029329; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; 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   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR037446; His_Pase_VIP1.
DR   InterPro; IPR029033; His_PPase_superfam.
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   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW   Kinase {ECO:0000256|RuleBase:RU365032};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW   Transferase {ECO:0000256|RuleBase:RU365032}.
FT   REGION          184..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          6..33
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFX98485.1"
SQ   SEQUENCE   482 AA;  54136 MW;  4F576C3AB1FDF56D CRC64;
     DFITIRKDLL DDSNAAKDEM DKVKKKLKVL LREGHGPPPQ FAWPANLPEP SIVQRQVIQL
     MNFHRKVMRH NYQKLYGGAA TSLHNIVNPG DKASGDSSPV GAMGQATAIN NIQARWCCGE
     DAELFRERWE KLFIEFCDAD KVDPSKISEL YDTMKFDALH NRQFLEWVFT PSKSMLEEED
     SAVVVEDAKV PEDKSDKTSE KSERSDSTAT TEKSEPSKSV SRRLFRRRSG NMKNVVEETP
     ESYFHLFTGS TKTKAKTDAR FEKLRELYNL AKVLFDFICP QEYGITDSEK LEIGLLTSLP
     LLKEIVADLE EMQASDDAKS FIYFTKESHI YTLLNCILEG GIQTKIARSA IPELDYLSQI
     CFELYESETT PSPLPKAHSA PELAPPADLA ALADLAANPP SVPEPPPSPA PPEQTFAYSI
     RITISPGCHT YDPLDVQLDS KHCIGCAPRR SLTQHMDWKE VIETLRAKFH QSYVSSEGGG
     EE
//
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