ID A0A024UVW4_9STRA Unreviewed; 1087 AA.
AC A0A024UVW4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=H310_00273 {ECO:0000313|EMBL:ETW09793.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW09793.1};
RN [1] {ECO:0000313|EMBL:ETW09793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW09793.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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, 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; KI913952; ETW09793.1; -; Genomic_DNA.
DR RefSeq; XP_008861204.1; XM_008862982.1.
DR AlphaFoldDB; A0A024UVW4; -.
DR STRING; 157072.A0A024UVW4; -.
DR EnsemblFungi; H310_00273-t26_1; H310_00273-t26_1-p1; H310_00273.
DR EnsemblProtists; ETW09793; ETW09793; H310_00273.
DR GeneID; 20077323; -.
DR VEuPathDB; FungiDB:H310_00273; -.
DR eggNOG; KOG1057; Eukaryota.
DR OrthoDB; 5476261at2759; -.
DR GO; GO:0005829; C:cytosol; 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 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; 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; 2.
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.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 141..356
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 714..744
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1087 AA; 123288 MW; 58B6A5D4F0BFD298 CRC64;
MGAQIAREDR RESIDGSQAS GGEQRGSGMF NFPGNIGPEA MSTQGSRFVI GVCAMDKKAN
SKPMSEILSR LPKHTFTIVL FGDDLILNHP VEDWPLCDAL IAFFSTGFPL EKAMEYVELR
QPIVVNDLSK QYLLMDRRDV YRVLEDHDIP TPRHIFVDRD NGREEGNFIE SEDYVELDGV
RIHKPFVEKP VNGENHNIYI YYPTNAGGGC KHLFRKIGNR SSEFHPNVIN VRREPGQSYI
YEEFISTQGT DVKVYTVGPN YAHAEARKSP VLDGKVMRDA VGKEIRYPVI LSTHEKEIAY
KVVRAFGQTV CGFDILRVGN ESYVCDVNGW SFVKNSPKYY DDCSVLLRQF LERALAGFAD
PYESMHSPQD RILVNSSSMS LLDVGDGSNG AENDETDVHS ERKSSGYHDP LENDGQEEEL
RCVLAVIRHG DRTPKQKMKM LVTHRKFLTF YEDRVGQGKK KDLKIKAIKD LEELLAVSKQ
MIDIYEDRQR KLNGDDDDSN ELEKDQLKGI CTLRDVLERW QLCGINRKVQ MKPRAWSNDD
NVKSIDDDAK DLDDYSPRKE SRVTQLLVIV KWGGDLTHSG IQQAETLGQH FRQIMYPGGD
GGLLRLHSTY RHDLKIYTSD EGRVQKTAAS FAKGLLELEG DIVPILVSLV LKSKDADSML
DQSGSSAQEM ILAVKERLHN ILHRGDDCGH LRTNSSSRLV RSVAAALDVV EQPMKKMERM
HKLLNSLKEQ LTKLLDNEAT EKAENVITAT EFEREQSAWA YKPPQLERQG SETSVVSCLE
LEPVGAAIEN RATVSSAGAR PKKPAEHMAN KTHSPKQNHS HSKKREPCGR ETLEMMRERW
AKLYRDFYSK KQNTYDLSKI PDIHDCIRYD AMHNAHLYLS GIRELLNISA SLAHALVPQE
YGIDVHEKLH IGTNMCRSLL KKVRDDLDLA RGFNITHRLN PTFATTDHRI KSAHRSVRTR
LYFTSESHLH TLLNVLRHSV TGHEEEAPVS REAVKMIEEI PELCYMTHIV VRVFERGGYH
NMDPKRFRVE LSLSPGATGD PLTEFSPKVP LSVAPLKIIS REGLTCQEFQ DYICNVISFG
SSKQQPE
//
