ID A0A0N4XDU3_NIPBR Unreviewed; 399 AA.
AC A0A0N4XDU3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase {ECO:0000256|ARBA:ARBA00012023, ECO:0000256|RuleBase:RU364126};
DE EC=2.7.1.158 {ECO:0000256|ARBA:ARBA00012023, ECO:0000256|RuleBase:RU364126};
GN ORFNames=NBR_LOCUS696 {ECO:0000313|EMBL:VDL63612.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000069501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000069501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL63612.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). {ECO:0000256|RuleBase:RU364126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000256|RuleBase:RU364126};
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2. {ECO:0000256|RuleBase:RU364126}.
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DR EMBL; UYSL01000365; VDL63612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4XDU3; -.
DR STRING; 27835.A0A0N4XDU3; -.
DR WBParaSite; NBR_0000069501-mRNA-1; NBR_0000069501-mRNA-1; NBR_0000069501.
DR OMA; FAYSVKI; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR PANTHER; PTHR14456; INOSITOL POLYPHOSPHATE KINASE 1; 1.
DR PANTHER; PTHR14456:SF2; INOSITOL-PENTAKISPHOSPHATE 2-KINASE; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|RuleBase:RU364126};
KW Kinase {ECO:0000256|RuleBase:RU364126}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364126};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 225..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 399 AA; 45406 MW; 3F09C34BA7B2D684 CRC64;
MVDIVDPRQF RAFCFRGEGR ANFVISAKHA ASGTRIVWRF AKSRKSGLLT WKAKSELVNQ
YMERFVSPFF DSHFLVNPRI VEMAISDVHQ LAKIPSLPTN FKVEKFEELL TFPDSMSFFP
LVNPPRTVVR LSALEMLDAT RIPKHLIFYI GPTITVEIKP KQGFFQNHAS VDLPFCNNCI
LQLEKCGSDH YEEMYDFCPL DLFSGNLSRM KSAIEALFKV PHRNFLWFIN FTTIIVAASI
SSFFQLCFVL AGCDDVRDFS LKEHSVLGQI LAAQKIDTVG IVKAHQIYKG LSSSVQKELH
DKSRLPLRGL EVLEEKDDRS LLEQYLLAAT MKDCSVSEKS IRILTVKSRL GLCFAYSVKI
VDLDPKTPKN LVNAYARFMA GVKMIRLESV TREPCLKTL
//
