ID A0A075AYI1_ROZAC Unreviewed; 1042 AA.
AC A0A075AYI1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-APR-2020, entry version 27.
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|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|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|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, cytoskeleton
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 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:0005623; C:cell; IEA:GOC.
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 GO; GO:0045454; P:cell redox homeostasis; 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|PROSITE-ProRule:PRU00409,
KW ECO:0000256|RuleBase:RU365032}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000030755};
KW Transferase {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
//