ID A0A0N4X3S0_HAEPC Unreviewed; 1073 AA.
AC A0A0N4X3S0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HPLM_LOCUS19002 {ECO:0000313|EMBL:VDO74459.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001901201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001901201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO74459.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO74459.1,
RC ECO:0000313|Proteomes:UP000268014};
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; UZAF01020980; VDO74459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4X3S0; -.
DR STRING; 6290.A0A0N4X3S0; -.
DR WBParaSite; HPLM_0001901201-mRNA-1; HPLM_0001901201-mRNA-1; HPLM_0001901201.
DR OMA; FRIELTC; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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:UP000268014};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 3..65
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 1049..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..431
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1073 AA; 122954 MW; 2ABE1B08F2E1E236 CRC64;
MVDWLEYFIF PESVIIHEPV DRWPLCDCLI SFHSTDFPLH KAIEYVKLRK PYVINDLKRQ
YDLLDRRKVF RTLAKEGIEH PRHGVLIRSD SNEEDGILVE HNDHIEVNGM VFNKPFVEKP
VSAEDHNIYI YYPSSVGGGS QRLFRKINNR SSWYSPVSEV RKDGSYIYED FIPADGTDVK
VYAVGPYYAH AEARKAPGLD GKVERDADGK EVRYPVILSH KEKMIARRVV LAFGQTVCGF
DLLRANGKSY VCDVNGFSFV KTSTKYYEDT AKILGNTIMR RLASTMSVRI PYQLPVGEQE
APPLLDLGLG DDPPIVSTPS GKLMELRCVL AVIRHGDRTP KQKMKVIVHD ERFFALFKKY
DGFKKNEIKM KRPNQLMEVL ELAREILAEH IALRNSLLMS LEACEDSGEE SQRVEHELEE
VEDAIKRWDQ MRAVLEMYGH FSGINRKVQL KYLKAREFRS GENEEAQQQG PALLLILKWG
GELTTAGNLQ AEALGKLFRT LYPGIRRADG KSSPEDTQGL GFLRLHSTYR HDLKIYASDE
GRVQMTAAAF AKGMLALEGE LTPILMQMVK SANTDGLLDD DCHARDFQSE LKGYLHQALQ
VDRDWTPEDY QALNPDGLKS INNAMEFIKN PKKMCHEIAG YVQRMCDIIN HNKYTKPHRT
LYLNETWDLA ERRWGKELRE FRRENKGGDV EYDISKIPDI YDNIKYDMEH NPDLCVNNEG
EFERMYVCVK NMADIVVPQE YGIRKENKIC VAQRVCTPLL KKIRNDLHRC IECSEEDESQ
TRLDPRASQG IATPLRHVRT RLYFTSESHI HTLMNLIRYG GLCSVDDKKW QRAMNFLSGV
TEFNYMTQVV LMVYEDSRTD SNATGMERFH IELLFSPGLY PCFLTEKERI YENRLKWDLS
TCTSFFYLFK SNGMTKSHSR EGNCNGSVSP ASAEGAKTTS IHIKKATHQR GSSFRPTFNL
LPLFYCYTFQ ENKEEAQPIF INVPSVPADD VSVSSANDDQ KAAETTGYLI EVSVGDDECQ
ATVGHGRGKW ANELVDETRK AMNSITEVEE KQMERRDSGC KSNPSLIIDR GYE
//
