ID A0A158PN80_ANISI Unreviewed; 1271 AA.
AC A0A158PN80;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 03-MAY-2023, entry version 29.
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=ASIM_LOCUS10802 {ECO:0000313|EMBL:VDK43673.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001124401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001124401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK43673.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|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; UYRR01031019; VDK43673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PN80; -.
DR WBParaSite; ASIM_0001124401-mRNA-1; ASIM_0001124401-mRNA-1; ASIM_0001124401.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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; 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: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.
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 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,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 16..80
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 911..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..445
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 915..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 144534 MW; 0B37AEAB5507941F CRC64;
MPATASSSTC SISSRKKDWL EYIVFPEEVI LNEPVERWPL CDCLISFHAT DFPLHKAIEY
ERLRRPYVIN DLHRQYDLLD RRKVFRALAR AGIEHPRHGV LIRDQNGKVV NFTEGELIEH
NDHIEVNGMV FNKPFVEKPL SAEDHNVYIY YPSSVGGGSQ RLFRKINNRS SWYSPVSTVR
RDGSFIYEDF IPADGTDVKV YAVGPYYAHA EARKAPGLDG KVERDSHGKE VRYPVILSSK
EKTIARKVVI AFGQTVCGFD LLRANGKSYV CDVNGFSFVK TSTKYYEDTA KILGNTILRR
LASSMSIPWQ IPYQDDDPPL VSTPSGKVME LRCVLAVIRH GDRTPKQKMK VVVTDGRFFE
LFRKYDGFKK NEIKMKRPTQ LMEVLELARQ ILHEQQMRRT ELVRLIERCE KNGEIVQTKN
KSNNLRRFER DFERCEEDIK KWDQMRTVLE MYGHFSGINR KVQLKYLKPR EIKGSSDRSD
SEEQHQSAAL MLILKWGGEL TTAGNLQAEA LGKLFRTLYP GIRRTDGKSS PEDTQGLGFL
RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILMQMVKSAN TDGLLDDDCN
ARDFQNELKS YLHSALQVDR EWTADDYESL NPSGNRSIAN AMEFIKNPRK MCDEIAGYVQ
RMVDVINWHK INRLNHSLYL NETWDLAERR WSKELREFRR VNKAGEVEFD ISKIPDIYDN
IKYDMEHNPD LCVNNEGEFE RMYLCVKNMA DIVVPQEYGI SESSKISIAQ RVCTPLIKKI
RSDLHRCIES SDEDESQTRL DPRASQGIAT PLRHVRTRLY FTSESHIHTL MNLIRYGGLC
SIDDKKWQRA MHFLAGVTEF NYMTQVVLMV YEDSRADSEK RGTDRFHIEL LFSPGLYPCF
QSEKERIYET RFPNTNGKPG PSVTKLSSRA QFNGSNTSLS SMGTVSGDKG VSESPPATTV
VSKDVSTLPS TDSLNEYTVG KSSTQAMTLT KKCLEMNDSE DDLNDESVNL VVLDEVANNN
NQYTSDELAR HSPTAVSTSH STRRRHMTSG EAIANVVGEC NAAPSRIQSS SIACDSYSSV
CDANDPVNHV SHLNIADTRH VGLMKSVSDI SCEKAAQEVR WTLATDDSAD GDENARRSRF
PYRFKHHTVN LLKEVDNRLI STDVLFGSSD AARRRMSNSS AVLSTAIIAR SSSAPRLQTY
KAEDEISVGE IRRFWPPLRS LETLHDGIKF SQLDQFLERL LTIRTPLPSP PKTPILREVF
ESGDANPLNV A
//
