ID A0A075AYI1_ROZAC Unreviewed; 1042 AA. AC A0A075AYI1; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 03-MAY-2023, entry version 37. 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=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 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, 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KE560848; EPZ35342.1; -; Genomic_DNA. DR AlphaFoldDB; A0A075AYI1; -. DR STRING; 988480.A0A075AYI1; -. DR EnsemblFungi; EPZ35342; EPZ35342; O9G_000738. DR HOGENOM; CLU_000914_3_1_1; -. DR OMA; IQERWCC; -. DR OrthoDB; 5476261at2759; -. 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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:EnsemblFungi. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi. DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:EnsemblFungi. 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:0000830; F:inositol hexakisphosphate 4-kinase activity; IEA:EnsemblFungi. DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IEA:EnsemblFungi. DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IEA:EnsemblFungi. DR GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi. DR GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006020; P:inositol metabolic process; IEA:EnsemblFungi. DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051516; P:regulation of bipolar cell growth; IEA:EnsemblFungi. DR GO; GO:0110162; P:regulation of mitotic spindle elongation (spindle phase three); IEA:EnsemblFungi. DR CDD; cd02989; Phd_like_TxnDC9; 1. DR Gene3D; 3.40.50.11950; -; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1. DR PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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}; 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: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" 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 //