ID   A0A182F3B5_ANOAL        Unreviewed;       549 AA.
AC   A0A182F3B5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Inositol-pentakisphosphate 2-kinase {ECO:0000256|ARBA:ARBA00014846, ECO:0000256|RuleBase:RU364126};
DE            EC=2.7.1.158 {ECO:0000256|ARBA:ARBA00012023, ECO:0000256|RuleBase:RU364126};
OS   Anopheles albimanus (New world malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB000950-PA, ECO:0000313|Proteomes:UP000069272};
RN   [1] {ECO:0000313|EnsemblMetazoa:AALB000950-PA}
RP   IDENTIFICATION.
RC   STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB000950-PA};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
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}.
CC   -!- SIMILARITY: Belongs to the IPK1 type 2 family.
CC       {ECO:0000256|ARBA:ARBA00007229}.
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DR   AlphaFoldDB; A0A182F3B5; -.
DR   STRING; 7167.A0A182F3B5; -.
DR   EnsemblMetazoa; AALB000950-RA; AALB000950-PA; AALB000950.
DR   VEuPathDB; VectorBase:AALB000950; -.
DR   VEuPathDB; VectorBase:AALB20_033650; -.
DR   OrthoDB; 8233at2759; -.
DR   Proteomes; UP000069272; Chromosome 2L.
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   Gene3D; 3.30.200.110; Inositol-pentakisphosphate 2-kinase, N-lobe; 1.
DR   InterPro; IPR009286; Ins_P5_2-kin.
DR   InterPro; IPR043001; IP5_2-K_N_lobe.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364126};
KW   Kinase {ECO:0000256|RuleBase:RU364126};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364126};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
SQ   SEQUENCE   549 AA;  62606 MW;  EE1A969612149762 CRC64;
     MGKINASHSS YCYDSTLLGT DEGCYPHRGQ SGKCCCIVGK STQFCFPDPC CGERSKEEQE
     SLVGHAVLQV DERCLVYRAE GNANIVLSLS DNKHVLRLRK SKIATRDGKA ESNVNLDRFV
     KYSEVMSNLF SSCYVPTLQL AHLNTGDLEA FNRRLSKARP VSRQDKEIRE LDGIIFPDVA
     FLPAWLYPAG DQDIHQEGKI HSPLSHYQTY CVEIKPKQGW YSYEFCDNIP APGLAYVGDG
     DLRKCRYCFL QYLKLQQKSI AKISKYCPLD LFSGKPIRVL QAVKGLIGAP QNNFKLLKNG
     KIVYDETREK SAFNKILKEM FPRDGRTKEE RKNIFLNLIK EVLLKDFSTS NADDENNRKL
     LTIRKDRKKK DKNQLHERCC NGVGQNFLPE RCVLREILDV QSLVKSNFAA FDPSQLASSS
     SSPCSYVDDM YEKYLDYRED VGYSDASMMS GTFCSEYLST EEKYQFGATA LDCSVMITFR
     RLAADRSVED RLSPEARNHI VVIEGMKFLV KVTITDLDPK SHQHHKKYVD QLAESVVAYR
     DFMSKLMKR
//