ID A0A1S3VEW5_VIGRR Unreviewed; 870 AA.
AC A0A1S3VEW5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN Name=LOC106774350 {ECO:0000313|RefSeq:XP_014516820.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014516820.1};
RN [1] {ECO:0000313|RefSeq:XP_014516820.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014516820.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_014516820.1; XM_014661334.2.
DR AlphaFoldDB; A0A1S3VEW5; -.
DR GeneID; 106774350; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000087766; 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 PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF26; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 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|RuleBase:RU365032, ECO:0000313|RefSeq:XP_014516820.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Transferase {ECO:0000256|RuleBase:RU365032}.
SQ SEQUENCE 870 AA; 98521 MW; A16228AA5E0205CE CRC64;
MIYYPSSAGG GMKELFRKVG NRSSEFHPDV RRVRREGSYI YEEFMPTGGT DVKVYTVGPE
YAHAEARKSP VVDGVVMRNP DGKEVRYPVL LSPAEKEMAR DVCIAFSQAV CGFDLLRSQG
RSYVCDVNGW SFVKNSYKYY DDSACVLRKM LLDAKAPHLS SVVPPTLPWK VNELTQPSEP
LTREPLTRQG SGINGTFGQS EELRCVIAVI RHGDRTPKQK VKLKVTEEKL LNLMLKYNGG
RPKSETKLKS AVQLQDLLDA TRMLVPRTRP DSDSEAEDVD HAEKLRQVKV VLEEGGHFSG
IYRKVQLKPL KWIKVTKGNG EIEEQPVEAL MILKYGGVLT HAGRKQAEEL GRYFRNKMYP
GEGTGLLRLH STYRHDMKIY SSDEGRVQMS AAAFAKGLLD LEGQLTPILV SLVSKDSSML
DGLENASFEM DEAKARLNEI ITCKATTSDT NGSSEFPWTV DGAGLPPNAS ELLSTLVKLT
KKVTEQVRLL AKDENDKLTE RNLYDIVPPY DQANALGKTN IDVDRIAAGL PCGSEGFLLM
YARWKKLETD LYNERKERYD ITQIPDVYDS CKYDLLHNAH LNLEGLDELF KVAQMLADGV
IPNEYGINPK QKLKIGAKVA RRLLGKLLID LRNTREEAIN VIKNNEDLSL SEKIKKDAEA
KSKLFHKNDE IDQDDDDDKE TKYRLDPKYA NVKTPDRHVR TRLYFTSESH IHSLMNVLRY
CNLDESLQEE EGLVCHSALE RLSKTKELDY MSHIVLRMFE NTEVALEDPK RYRIELSYSR
GADLSPLEKE GSECTLHQEH TLPIMGPERL QQVGSYLTLE TMENMIRPFA MPAEDFPPTP
AGFSGYFSKS VLDRLVNLWP FHRQFSNLGK
//
