ID S8B9F4_DACHA Unreviewed; 391 AA.
AC S8B9F4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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};
GN ORFNames=H072_10869 {ECO:0000313|EMBL:EPS35708.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS35708.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35708.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35708.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has kinase activity and phosphorylates inositol-1,3,4,5,6-
CC pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-
CC hexakisphosphate (InsP6), also known as phytate.
CC {ECO:0000256|ARBA:ARBA00003979}.
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 1 family.
CC {ECO:0000256|ARBA:ARBA00008305}.
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:EPS35708.1}.
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DR EMBL; AQGS01001056; EPS35708.1; -; Genomic_DNA.
DR RefSeq; XP_011116285.1; XM_011117983.1.
DR AlphaFoldDB; S8B9F4; -.
DR STRING; 1284197.S8B9F4; -.
DR eggNOG; ENOG502S7VH; Eukaryota.
DR HOGENOM; CLU_031304_2_0_1; -.
DR OMA; DCTMFIR; -.
DR OrthoDB; 2714244at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
SQ SEQUENCE 391 AA; 43658 MW; 4BC449480414C76C CRC64;
MSTVPATGPH AEPPVPVLPD GLTLKKLTRT IARIKVIWRI SLPQAHPHTP PQTDLSEYTN
STPPPSEIDL LATTSGENGV AKANGVNFQP PTDYSHVLLR LRKCLPSSES NLLAYEYLSS
VIMPLFPPGV MVGQTLVQVP SKLISRANDT LHDLEESGVR PSHRLNLYLA GDPRPSEQHM
EEHYAFLLED MTPDTSRGEF LLEFKAKWLV QSPNAPVEWK RCRNCALRLR KYAKSLKKGK
SADWRGLCPF DLVSGDTKRA CNGVKRILGY PRSEDEKLVE RVTQALMSCS QLSILKELQA
HLDPLGILKA NHKSKEFLTA MTLRDCTFFV KVSPTDVQAR LGDFDVKSGE GGKSDYWVRV
ENELISEGWY NGTEEGDFPW KADGLEVVCR V
//
