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Database: UniProt
Entry: A0A0N5CGY8_STREA
LinkDB: A0A0N5CGY8_STREA
Original site: A0A0N5CGY8_STREA 
ID   A0A0N5CGY8_STREA        Unreviewed;       391 AA.
AC   A0A0N5CGY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001711300.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001711300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
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|RuleBase:RU365032}.
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DR   AlphaFoldDB; A0A0N5CGY8; -.
DR   STRING; 174720.A0A0N5CGY8; -.
DR   WBParaSite; SPAL_0001711300.1; SPAL_0001711300.1; SPAL_0001711300.
DR   Proteomes; UP000046392; Unplaced.
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   Gene3D; 3.40.50.11950; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR037446; His_Pase_VIP1.
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; PF18086; PPIP5K2_N; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU365032};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365032};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365032};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT   DOMAIN          8..98
FT                   /note="VIP1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18086"
FT   DOMAIN          168..301
FT                   /note="ATP-grasp fold RimK-type"
FT                   /evidence="ECO:0000259|Pfam:PF08443"
SQ   SEQUENCE   391 AA;  45742 MW;  8013AE6E01C6B346 CRC64;
     MEIKTKKIVV GVCAMNRKTM RKPMISILES IKKNYGIYLD IIHFNDSTIL FRQIEEWPVV
     DALITFYSTG YPIEKVMKYI EKYQPYLIND LEKQLKIMNR DCVLSVLNSV GINHPEYGIV
     RRNDNGDLLN NFEEYEDHIV IDGKIFLKPF VEKPISGEDH NINIYYHSSQ GSGCRMLFRK
     RNNMSSLFST SSNVRRDKSY IYEKFIVTSD IDVKCYAVGE EYCYAESRKA PAVDGMIDRD
     HNGKEKREEV VLTDDEMEMA AKIVKVFKHT VCGFDILRDT EKSYVCDVNG FSFVKNVPKY
     YETAGKIIGE KIFKHFISIN TKDNNKECYE SNENFILLDD WQSKPLDKNK LINQQMEENC
     HDSVKEEFSR NQRTYNDIME LAKIKVLKSQ F
//
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