ID A0A1W0VZX1_SORBI Unreviewed; 1063 AA.
AC A0A1W0VZX1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SORBI_3003G315166 {ECO:0000313|EMBL:OQU87662.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU87662.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU87662.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000762; OQU87662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W0VZX1; -.
DR STRING; 4558.A0A1W0VZX1; -.
DR EnsemblPlants; OQU87662; OQU87662; SORBI_3003G315166.
DR Gramene; OQU87662; OQU87662; SORBI_3003G315166.
DR InParanoid; A0A1W0VZX1; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000000768; Chromosome 3.
DR ExpressionAtlas; A0A1W0VZX1; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
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:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
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:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 23..112
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 813..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 120254 MW; CDAEFB7EA225AAE5 CRC64;
MSKGGDGEGM ARRNDGWGDG DKIKIGVCVM EKKVSCSPME QILERLRAFG EFEIIIFGDK
VILEDPIESW PICDCLIAFY SSGYPLEKAE KYAALRRPFL VNELAPQYLL HDRSKVYQQL
KLYGVPVPTY AVVRREYPNQ ELSYFVEEDD FIEIHGKRFC KPFVEKPIDG DDHNIMIYYP
SSAGGGMKEL FRKVGNRSSE FYPYVRKVRR DGSYIYEEFM PTGGTDVKVY TVGPVYAHAE
ARKSPVVDGV VMRNSDGKEV RYPVLLTPSE KQIARSICQA FRQAVCGFDL LRCDLGEATS
YVCDVNGWSF VKSSYKYYDD AACILRKIFL DEKAPHIPST IPTSLPWKIS EPVQPSDAVR
CRERGTVGIS RPSEELRCVI AVIRHGDRTP KQKVKLKVTE EKLLKLMLKY NGGKAHAEAK
LKSALQLQDL LDATRILVPR ARSGRESDSD VEVEHAEKLR QVRAVLEEGG HFSGIYRKVQ
LKPSNWVHVP KDNREGEEYP VEALMVLKYG GVLTHAGRKQ AEELGRYFRN NMYPSEGPGL
LRLHSTYRHD LKIYSSDEGR VQMSAAAFAK GLLDLEGELT PILVSLVSKD SSMLDGLQDG
TIDINEAKAQ LHDIITSSEV ANCNVPMKVP WMVDGARVPK NAAQLLTDLA ELTKEITTQV
KMLSDNEDEK AAIGSDSPNP PYDIATALGN AEIDMDRISA GLPCGSESFL LMFARWKKLE
RGLYNERKKR FDTSQIPDVY DSCKYDLLHN SHLNLTGLSD LFKVSQLLAD GVIPNEYGIN
PKQKLKIGSK IARRLLGKIL IDLHNTRREV TAAAAESNTH NDTTTVSSAK RKERSYYEEV
RNECIERSSS NKKAIDLDDS HEETKYCLDP KYANVVDPER RVRTRLYFTS ESHIHSLMNI
LRYCNLDESL NGEESLVCRS SLDLLFKTRE LDYMSYIVLR MFENTEVPLE HPKRFRIEMT
FSRGADISSL ESGGKESLLP DDHTMPIMEP ERLQEVGSYI TLDKFDKMAR PFAMPAEDFP
PAAPSQPLPV RFCKDIELQA GKLQHKSDML SGILKRKTNK LQE
//
