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Database: UniProt
Entry: A0A1V8T7E9_9PEZI
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ID   A0A1V8T7E9_9PEZI        Unreviewed;       327 AA.
AC   A0A1V8T7E9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=B0A48_07680 {ECO:0000313|EMBL:OQO07112.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO07112.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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|ARBA:ARBA00001774,
CC         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:OQO07112.1}.
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DR   EMBL; NAJO01000015; OQO07112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8T7E9; -.
DR   STRING; 1507870.A0A1V8T7E9; -.
DR   InParanoid; A0A1V8T7E9; -.
DR   OrthoDB; 2714244at2759; -.
DR   Proteomes; UP000192596; 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   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; 2.
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:UP000192596};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
SQ   SEQUENCE   327 AA;  36190 MW;  17FC89E78B57AD3F CRC64;
     MSITVYFSEQ NCLPSIGVEP LTSTNQLKLT YLSEGGANFV FRIIAQGPGS DNPLNGKLLR
     LRKDLSHVQS AKAQLEAFDA NFRPLFPAHH VVQQELIVLG PGLAEALNAF VKTVSRPTHR
     LDDVLPLDET HGLLVTDMTP SGSEDVLLQL KPKWLAQSPS APADAKRCRT CALRAQRGAN
     RIHTATDRQE TCPLRLVSDV ERHATEVATS LTDDKTIANF LIGDGRQLLV TLRSHQEMLD
     PLGALAVDDE DAIRNVCRAM TLRDCTLFVK SSSGRIEARL GDLDLKLAEK LSYWKEVEVK
     LREDGWYLNV EAKAVWAEET VCLLSRS
//
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