ID   A0A075AYI1_ROZAC        Unreviewed;      1042 AA.
AC   A0A075AYI1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   12-AUG-2020, entry version 28.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.21 {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN   ORFNames=O9G_000738 {ECO:0000313|EMBL:EPZ35342.1};
OS   Rozella allomycis (strain CSF55).
OC   Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC   Cryptomycota incertae sedis; Rozella.
OX   NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ35342.1, ECO:0000313|Proteomes:UP000030755};
RN   [1] {ECO:0000313|EMBL:EPZ35342.1, ECO:0000313|Proteomes:UP000030755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSF55 {ECO:0000313|EMBL:EPZ35342.1,
RC   ECO:0000313|Proteomes:UP000030755};
RX   PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA   James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA   Stajich J.E.;
RT   "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT   microsporidia.";
RL   Curr. Biol. 23:1548-1553(2013).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC       group-containing inositol pyrophosphates diphosphoinositol
CC       pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC       tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC       respectively called InsP7 and InsP8, regulate a variety of cellular
CC       processes, including apoptosis, vesicle trafficking, cytoskeletal
CC       dynamics, exocytosis, insulin signaling and neutrophil activation.
CC       Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to
CC       produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC       (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4.
CC       {ECO:0000256|RuleBase:RU365032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-diphospho-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP +
CC         H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate +
CC         ADP; Xref=Rhea:RHEA:37467, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:74946, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.21; Evidence={ECO:0000256|ARBA:ARBA00001046,
CC         ECO:0000256|RuleBase:RU365032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-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:ARBA00000685,
CC         ECO:0000256|RuleBase:RU365032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC         inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC         ChEBI:CHEBI:456216; EC=2.7.4.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001444,
CC         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|ARBA:ARBA00000261,
CC         ECO:0000256|RuleBase:RU365032};
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}.
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DR   EMBL; KE560848; EPZ35342.1; -; Genomic_DNA.
DR   EnsemblFungi; EPZ35342; EPZ35342; O9G_000738.
DR   HOGENOM; CLU_000914_3_1_1; -.
DR   OrthoDB; 93740at2759; -.
DR   Proteomes; UP000030755; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
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:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
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; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR040557; VIP1_N.
DR   PANTHER; PTHR12750; PTHR12750; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   Pfam; PF08443; RimK; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, 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|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|RuleBase:RU365032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030755};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT   DOMAIN          340..549
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   COILED          20..40
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1042 AA;  120389 MW;  DDE1933D5B800656 CRC64;
     MNGMPDMYAQ ALEESILQAA SVVEAQIDEK IRELENADEN SLESIRRQRI QQMKNAALQK
     AHWRSLGHGS YSELLSEKAF FEEGKKSKDL VCHFYRTSTF RCKILDRHLE ALSKAHLEAK
     FVKIDAEKSP FLCERLGVRV LPTLVIVKDR KPVDQIVGFA EIGNNDDFET IALARRIAKS
     GVIRFEENED YSEYGVMMNK NNFYGCVFRS SSLRKLIIGV CAMDTKARSK PMRNILDRIT
     ATSDFEVVIF GDKTILDDPI EEWPQCQFLI SFFSKGFPLQ KAIEYVALRR PFCINDLPLQ
     QLLWDRRWVL SVLDAIDVPT PKRIIVNRDE GPKYYKGVIE ELNKNLGIDL GNMTNFSREN
     VIQIDKDTIM VGKQRLEKPF VEKPVDGEDH NIYIYYPESM GGGVRKLFRK VGNKSSEFFP
     DEWEIRKEGS FIYETFIDVE KAEDIKVYTI GPYYAHAETR KSPVVDGIVR RNTDGKEVRH
     LTDLSEEEQE LARRVSMAFG QTICGFDLVR CGSKSMVIDV NGWSFVKGND NYYDMCAKIM
     SQTFLKIARK RRTTILKEPL NENQWKLKSF ISIFRHADRT PKQKMKFNVS SAPFLDLIVK
     GKEETMIRNP DGLERIEKAA EASLSLGIEE KSKLLQLMEI LSKKKKSPGT KVQIKPSYSK
     SREIEKAQLI VKWGGEFTHA GRHHSKDFGE NLRKDLLLMN RKMIDDVKVY TSSERRVMAT
     ADIFSKALMF VAELPDDFLS IKKEMLDDNF DAKEKLDKIP ENVQFLNVHP EFKNPRVTLD
     EVFITLKDLR QVMRSNFDTL DVDSLSHRWC CAESSILFKE RWEKLFKDFC DVEINNFDPS
     KVSELYDSLK YDALHHREFF ERIFVKNQNC PNEKAALADL IRKAKILFDF IAPQEFGLFP
     EEKVEIGKII ANRLLAQILD DLNEAKIHAT DPCTRLYFTK ESHVHALLNI VRFGGLECSI
     GNWDELDYLT QITFEVYERF KSNTSGFEYS IRIGFSPGAH DSNILDVQID QKHALSVAPR
     RWITEHIPLD HAISIIEKML NK
//