ID A0A0L0VQZ8_9BASI Unreviewed; 988 AA.
AC A0A0L0VQZ8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=PSTG_05135 {ECO:0000313|EMBL:KNF01708.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNF01708.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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, cytoskeleton
CC {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNF01708.1}.
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DR EMBL; AJIL01000028; KNF01708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0VQZ8; -.
DR STRING; 1165861.A0A0L0VQZ8; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
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 Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 159..361
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 753..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 111517 MW; 2B3B3C3EBFA3335C CRC64;
MSRPSDEKKD RKSPAPIQNL PEAIEDENHL IKIGIAAMDR KARSKPMRNI LSRLVATNKF
ECIIFGDKVI LDEDIENWPV CDFLISFFST GFPMDKAIRY VKLRNPIPIN DLPLQKLLWD
RRLVLAVLDK IGVPTPKRCE LNRDGGPKVD KEVASEMERR FGLKLNTPRS PPKSFQVQND
TALLIDGVRM EKPFVEKPVS GEDHNINIYF GGGNGGRKLF RKIANQSSIL DPELSDPRTE
GSFIYEQFMK TDNYEDIKIY TLGPDIVHAE TRKSPVVDGI VKRNLDGKEI RYVVELTPEE
REIARKISTA FSQTVCGFDI LRVKGKSYVI DVNGWSFVKG NDSYYDKCAD TLAKFCLKAM
SSLTVPPPTP GQDVTPKPTV SSWKLKAMIC VFRHADRTPK NKLKFNFNAD EPGAEPFIKL
LQGRKDEIIL RTSDHLQLIA TATEEAIAIV ESDQIKLERL KSILCSKMGK QGLKAQLKPS
FQSEDESLEK ITIVIKWGGE FTHAARYQSR DIAENFAKDL RVMSKTMLDD VTIFTSSESR
VVATAEIFSA GLREACKAHS KTEPKTIPLV TRKDLLDDSN AAKEPMDRVK KRLKVLLRHN
QGIEVDWPIA DKEPFDVVQE VIVTLQEQRD VMHTNWETLD VEQIQSRWCC GECPVLFRER
WEKLFSDWCD GALDPSRVCE LYDSLKYDSL HNRTFLETIF SSSSTWPSPV CSDASSLLAI
MPGSAPSMMP SSSSFSSHSH FSPIGLIRTG DTSLASTPAV SPGQHHHPRQ VSLKYPAPPS
PSGTIKEEDG GWSETESLKR LRKLYKDAKL LFDLIAPQEY GIDQSEKREI ALLTSLPLLQ
KIVSDLNAAK ESQGGLARFY FTKESHMHTL VNLIKLSKLK LAHRDVMELD YMAYLSFEVY
ERTSEVGKSE HSVRISLSEG AHGIPLDTSL DAKHALQVIP RRQLIPHKDL DEVIESLQDW
GENTFELKKS TTPHDGFLPL EGEDIFSK
//
