ID A0A1U7WQJ7_NICSY Unreviewed; 1046 AA.
AC A0A1U7WQJ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-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};
GN Name=LOC104226272 {ECO:0000313|RefSeq:XP_009776519.1,
GN ECO:0000313|RefSeq:XP_009776520.1, ECO:0000313|RefSeq:XP_009776521.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009776520.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009776519.1, ECO:0000313|RefSeq:XP_009776520.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009776519.1,
RC ECO:0000313|RefSeq:XP_009776520.1};
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_009776519.1; XM_009778217.1.
DR RefSeq; XP_009776520.1; XM_009778218.1.
DR RefSeq; XP_009776521.1; XM_009778219.1.
DR STRING; 4096.A0A1U7WQJ7; -.
DR GeneID; 104226272; -.
DR KEGG; nsy:104226272; -.
DR eggNOG; KOG1057; Eukaryota.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000189701; Unplaced.
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:SF9; 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:UP000189701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 5..100
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
SQ SEQUENCE 1046 AA; 118566 MW; 0E54AE964D3B2E57 CRC64;
MEKKIRIGVC VMEKKVKCGP EVFSAPMGQI LDRLQSFGEF EVVHFGDKVI LEDPIESWPV
CDCLIAFHSS GYPLEKVEEY AALRKPFIVN ELEPQHLLHD RRKVYEHLDM FGIPVPRYAC
VNREVPYQEL DYFVEEDDFV EVHGNRFCKP LVEKPVNGDD HRIMIYYPSS AGGGMKELFR
KVGNRSSEFH PEVRRVRREG SYIYEEFMPT GGTDVKVYTV GPEYAHAEAR KSPVVDGVVM
RNPDGKEVRY PVLLTPVEKQ MAREVCIAFR QAVCGFDLLR CEGRSYVCDV NGWSFVKNSY
KYYDDAACVL RKIFLDAKAP HLSSTIPPTL PWKVNEPVQP SEGLTRQGSG LIGTFGQSEE
LRSVIAIIRH GDRTPKQKVK FKVTEEKLLN LMLKYNGGRP RSETKLKSAV QLQDLLDATR
ALVPRTRPGR GSDSEAEDFE HAEKLRQVKA VLEEGGHFSG IYRKVQLKPL KWVMVPKSNG
EGEEERPVEA LMVLKYGGVL THAGRKQAEE LGRYFRNNIY PGEGTGLLRL HSTYRHDLKI
YSSDEGRVQM SAAAFAKGLL DLEGQLTPIL VSLVSKDSSM LDGLANASIE IKEAKARLND
VIISGSKTLH NSGSAEKPWM VDGAGLPPNA SELLPKLVKL TKRVTEQVKL LAKDEDEELA
ETSSYDVIPP YDQAKALGKT NIDVDRIAAG LPCGSEGFLL MFARWRKLER DLYNERKDRY
DITQIPDVYD SCKYDRLHNS HLNLEGLGEL FEFAQLLADG VIPNEYGINP KQKLKIGSKI
ARRLLGKILI DLRNTREEAL SVADLKSCED HHSAVNKTGS DPKLNARSED LRKSSFTSVK
STDQDDDEDK ETKYRLDPKY ANVRTPERHV RTRLYFTSES HIHSLMNVLR YCNLDESLHG
EASLVCDNAL DRLFKTKELD YMSYIVLRMF ENTEVALEDP KKFRIEMTFS RGADLSPLEK
NDKDAASWHQ EHTVPIMGPE RLQEVGSYLT WENMEKMIHP FAMPAEDFPP PSIPQGFSGY
FSKSAAVLER LANLWPFHKY GNTNGK
//
