ID V7C1G2_PHAVU Unreviewed; 1029 AA.
AC V7C1G2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PHAVU_004G025600g {ECO:0000313|EMBL:ESW23183.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW23183.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 EMBL; CM002291; ESW23183.1; -; Genomic_DNA.
DR RefSeq; XP_007151189.1; XM_007151127.1.
DR AlphaFoldDB; V7C1G2; -.
DR STRING; 3885.V7C1G2; -.
DR EnsemblPlants; ESW23183; ESW23183; PHAVU_004G025600g.
DR GeneID; 18631810; -.
DR Gramene; ESW23183; ESW23183; PHAVU_004G025600g.
DR KEGG; pvu:PHAVU_004G025600g; -.
DR eggNOG; KOG1057; Eukaryota.
DR OMA; YEDNTRV; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000000226; Chromosome 4.
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:SF26; 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:UP000000226};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 9..98
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
SQ SEQUENCE 1029 AA; 117020 MW; C5BF60717BB6369C CRC64;
MAVVLAEKVK IGVCVMEKKV FSAPMGQIFD RLQAFGEFEV IHFGDKVILE EPIESWPICD
CLIAFYSSGY PLEKAEAYAA LRKPFVVNEL EPQHLLHDRR KVYERLEMFG IPVPKYALVI
REVPYQQLDY FNEEEDFVEV HGMRFYKPFV EKPVDADNHS IMIYYPSSAG GGMKELFRKV
GNRSSEFHPD VRRVRREGSY IYEEFMPTGG TDVKVYTVGP EYAHAEARKS PVVDGVVMRN
PDGKEVRYPV LLSPAEKEMA RDVCIAFSQA VCGFDLLRSE GRSYVCDVNG WSFVKNSYKY
YDDSACVLRK MLLDAKAPHL SSVVPPTLPW KVNELIQPSE TLTRQGSGIN GTFGQSEELR
CVIAVIRHGD RTPKQKVKLK VTEEKLLNLM LKYNGGRPKS ETKLKSAVQL QDLLDATRML
VPRTRRDLES DSEAEDVEHA EKLRQVKAVL EEGGHFSGIY RKVQLKPLKW VKVTKANGEI
EERPIEALMI LKYGGVLTHA GRKQAEELGR YFRNKMYPGE GTGLLRLHST YRHDLKIYSS
DEGRVQMSAA AFAKGLLDLE GQLTPILVSL VSKDSSMLDG LENASSEMEE AKARLNEIIT
CKAKPVDSNG SSEFPWTVDG AGLPPNASEL LPNLVKLTKK VTEQVRLLAK DENEKLTERN
LYDIIPPYDQ ANALGKTTID VDRIAAGLPC GSEGFLLMYA RWKKLETDLY NERKERYDIT
QIPDVYDSCK YDLLHNAHLN LEGLDELFKV AQMLADGVIP NEYGINPKQK LKIGSKIARR
LLGKLLIDLR NTREEAINVI KNNQDLSLSE KIKEDAEANS KLFHKIDEID QDDDDDKETK
YRLDPKYANV KTPDRHVRTR LYFTSESHLH SLMNVLRYCN LDESLQEEEG LVCHNALERL
SNTKELDYMS HIVLRMFENT EIALEDPRRY RVELTYSRGA DLSPLEKEGS ECTSLHQEHT
LPIMGPERLQ GIGSYLTLET MDNMIRPFAM PAEDFPPTPA GFSGYFSKSV LDRLVNLWPF
HRQSSNLGK
//
