ID A0A0E0C8G4_9ORYZ Unreviewed; 1062 AA.
AC A0A0E0C8G4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G29890.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G29890.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI01G29890.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G29890.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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|ARBA:ARBA00004514, 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 AlphaFoldDB; A0A0E0C8G4; -.
DR STRING; 40149.A0A0E0C8G4; -.
DR EnsemblPlants; OMERI01G29890.1; OMERI01G29890.1; OMERI01G29890.
DR Gramene; OMERI01G29890.1; OMERI01G29890.1; OMERI01G29890.
DR eggNOG; KOG1057; Eukaryota.
DR Proteomes; UP000008021; Chromosome 1.
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 CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF15; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
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,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 14..103
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 810..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 120296 MW; EEF3F26CD75775BD CRC64;
MERRNDGCDG GGKIKIGVCV MEKKVWCSPM EQILERLRAF GEFEIIIFGD KIILEDPIES
WPLCDCLIAF YSAGYPLEKA EKYAALRRPF LVNELDPQYL LHDRSKVYEH LKLFGVPVPT
YAVVRREYPN QELKYFVEQD DFIEIHGKRF CKPFVEKPID GDDHNIMIYY PSSAGGGMKE
LFRKVGNRSS EFYPDVRKVR RDGSYIYEEF MPTGGTDVKV YTVGPGYAHA EARKSPVVDG
VVMRNSDGKE VRYPVLLTPT EKQIARNICQ AFGQAVCGFD LLRCDLGEAR SYVCDVNGWS
FVKSSHKYYD DAACILRKMF LDDKAPHISS TIPANLPWKV SEPVQPFDAV RNRERGTVGI
SRQSEELRCV IAVIRHGDRT PKQKVKLKVT EEKLLKLMLK YNGGKTHAEA KLKSALQLQD
LLDATRILVP RARSGRESDS DAEIEHAEKL RQVRAVLEEL KPSNWVHIPK SNSNGEEEYP
IEALMVLKYG GVLTHAGRKQ AEELGRYFRN NMYPSEGPGL LRLHSTYRHD LKIYSSDEGR
VQMSAAAFAK GLLDLEGELT PILVSLVSKD SSMLDGLQDG SIEIDEAKAR LHNIILSSKI
ANGETMEFPW MVDGAGVPPN AANLLTNLKL AHLKQPNVKI ITSIMVTNKL PLSQLSNQAQ
LTKEITAQVK LLSDNEDEEA VTDSDSPSYP YDQAKALGKT AIDMDRIASG LPCGSESFLL
MFARWKKLER DLYNERKNIL DRYDLLHNSH LKLNGLSDLF RVSQSLADGV IPNEYGINAK
QKLKIGSKIA RRLLGKILID LHNTRREVAA SGGESNACHD PTIVPSSKRK DRGYYGDVKN
EGFDRPNSNK KSIDLDDSHK ETKYCLDPKY ANVMEPERRV RTRLYFTSES HIHSLMNVLR
YCNFDESMDG EESLVCKNAL DNLFKTRELD YMSYIVLRMF ENTEVSLEDP KRFRIEMTYS
RGADISSLQS EHGKDSLLPD DHTMKIMEPE RLQEVGSYLT LDKFDKMVRP FAMPAEDFPP
AAPSQSLAVR FCKDNGLQGA RLQDKSDMVS GMPKRKTKKL QE
//
