ID A0A0V0VJD6_9BILA Unreviewed; 1335 AA.
AC A0A0V0VJD6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 28.
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=T09_12960 {ECO:0000313|EMBL:KRX63642.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX63642.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX63642.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX63642.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00034629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000256|ARBA:ARBA00034629};
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|ARBA:ARBA00033696};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000256|ARBA:ARBA00033696};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
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:KRX63642.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDN01000029; KRX63642.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0VJD6; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; 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.
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:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 138..228
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 153679 MW; 2491C7332C278EF7 CRC64;
MMRMKRSCSW PSMSDQKPCL SMKSKSEEIR TNSASALYKT DRKQFAEKDK REIEISSGSS
DDDPTLYRAR ETSSLFDANS YFLNSIRPLW CNTKTHGSQT QKASSAPAAV SKSSDDSSEF
SSVELLSKRR CSEDAKRIVV AICAMHRKVK SKPMKEILSR IIEYYGDKMY IMVFNETMIM
NDPVEKWPIC DCFISFYSQG FPIAKAIDYI RLRNPYVIND VHRQYDLLSR IKVYKILEKA
YIELPRYTVL HRNPTSSKTS TYVEHEDSIE IDGKCFNKPF VEKPISAEDH NIYIYYPSSA
GGGSQRLFRK VDNRSSIYSP ESHIRKEGSY IYEEFMPTDG TDVKVYAVGP DYAHAEARKS
PALDGKVDRD SDGKEIRYPV ILSSREKLIA RKIVWAFRQT VCGFDLLRAN GRSYVCDVNG
FSFVKTSTRY YDDSALILGN MILRYLAPTL HIPWVRPFQL DDPPLVSTTY GTVMELRCVL
GIIRHGDRTP KQKLKMEVSH KKFFDLFSTY DGFKWGELKL KRPAQLQEVL DIVRYLLLQI
RDNTDQRRFI TEQEAKLEQV KTVLEMHGHF SGINRKVQLK YHKRAKNESD DLSTGEKPDN
NENRCLILIV KWGGELTNAG KIQAEELGRA FRCLYPGGQG KGQSNNDSRG LGFLRLHSTY
RHDLKIYASE EGRVQMTAAA FAKAIYTFSY KLQMVKSANT DGLLDDDKDA RLYQNRVKSF
LHSFLQCDAD LTEEDFEWLN PTNSITMHNA LRFIQNPRQM CIRIHEMIKN MFETIQLRRT
KLKNNTLYMG ESWDLIERRW GKLVKDFRCV KPNGDVVFDI SKIPDIYDCI KYDLEHNASV
LLAVEEMEEL YLCSKHMADI VVFQEYGITK EEKILIGKGI CTPLIKKLRS DLNRCIDGIV
DEENATRLDP RASKDIATPF RHVRTRLYFT SESHIHSLMN LLQFGGLFEY PYDNQWKSAL
NFLSSVTEYN YMAQLVLMLY EDTTKDARSE DRFHVELHFS PGALPCIQTT HVAGLGYRPK
SYRSAMNETL MNINDLIKAL DDERVSDNKL SIDRSFNRRK EKQISPTQSS GTSIGVVAIG
DKENKPITNE ELALHSPDRV PSPDRTLPVI KSSSDISCLK SRYFSHTSYK KKRTSTLGKK
NETEEQPNYY SNIVSVEEPL GARQYPHKRA IYQRQAVKYL WQQDAKLIST AVISGSFSVA
RDAAPALLST AVVSRGSSAP DLRLSSRAEE LDKNVHIYLK SFIKQLLQWF TYLKNLDIAF
MVPPLRSLET LHNQLSLRQI DDFFEAIVAS KSPDGKLPEN SSEEYLKDEL SESWLYQIED
MQYEEISDRN SHCME
//
