ID A0A0V1MTA4_9BILA Unreviewed; 1301 AA.
AC A0A0V1MTA4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 24.
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=T10_7330 {ECO:0000313|EMBL:KRZ74847.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74847.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ74847.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74847.1};
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:KRZ74847.1}.
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; JYDO01000045; KRZ74847.1; -; Genomic_DNA.
DR Proteomes; UP000054843; 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 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:UP000054843};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 145..235
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
SQ SEQUENCE 1301 AA; 149478 MW; EEC48E619E884176 CRC64;
MEINYTKMMR MKRSYSWPSV SEQKQYLSLK PKSEEMRTNS ANALYQIVRK QLAEPDIREM
EISSGSSDDD PTLYRARETS DLFDANSYFL NCIRPLWCNT KTHGSQTQKA SSAPAAVSKS
SDDSSEFASI ELLFKRRCSE EAKRIVVAIC AMHRKVKSKP MKEILSRIIE YYGDKMYIIV
FNEAMIMNDP VEKWPICDCF ISFYSQGFPI AKAIDYIRLR NPYVINDVHR QYDLLSRIKV
YKILEKAYIE LPRYTVLHRE PTSSKTSTYI EHEDSIEIDG KCFNKPFVEK PISAEDHNIY
IYYPSCAGGG SQRLFRKVDN RSSIYSPESH IRKEGSYIYE EFMPTDGTDV KVYAVGPDYA
HAEARKSPAL DGKVDRDSDG KEIRYPVILS SREKLIARKI VWAFRQTVCG FDLLRANGRS
YVCDVNGFSF VKTSTRYYDD SALILGNMIL RYLAPTLHIP WVRPFQLDDP PLVSTTYGTV
MELRCVLGII RHGDRTPKQK LKMEVSHKKF FDLFSTYDGF KWGELKLKRP AQLQEVLDIV
RYLLLQIRDN TDQRRFITEQ EAKLEQVKTV LEMHGHFSGI NRKVQFKYHK RAKSGPDDLS
TDEKSDNDEN KCLILIVKWG GELTNAGKIQ AEELGRAFRC LYPGGQGKGQ SNNDSRGLGF
LRLHSTYRHD LKIYASEEGR GLLALEGQLP PILVQMVKSA NTDGLLDDDK DARLYQNRVK
SFLHSFLQCD ADLTEEDFEW LNPTNSITMH NALRFIQNPR QMCIRIHEMI KNIFETIQLR
RTKLKNNTLY MGESWDLIER RWGKLVKDFR CVKPNGDVVF DISKIPDIYD CIKYDLEHNA
SVLLVVEEME ELYLCSKHMA DIVVFQEYGI TKEEKVLIGK GICTPLIKKL RSDLNRCIDG
IVDEENATRL DPRASKDIAT PFRHVRTRLY FTSESHIHSL MNLLQFGGLF EYPYDNQWKS
ALNFLSSVTE YNYMAQLVLM LYEDTTKDAR SEDRFHVELH FSPGALPCIQ TTHVAGLGYR
PKSYRNAMNE TLMNINDLIK ALDDERVSNK KLSIDRNFNL KKEKQISPTQ SSGTSIGVVA
IGDKENKPIT NEELALHSPD RVPSPDRTLP VIKSSCKKKR TSTLGKKNEI EEQPNYYSNI
VSVEEPLGAR QYPHKRAIYQ RQAVKYLWQQ DAKLISTAVI SGSFSVARDA APALLSTAVV
SRGSSAPDLR LSSRAEELDK SDIAFMVPPL RSLETLHNQL SLRQIDDFFE AIVASKSPDG
KLPENSCEEY LKEDELSQSW VHQIEDVQFE ESLDSYSHSL E
//
