ID A0A0K3CLX5_RHOTO Unreviewed; 484 AA.
AC A0A0K3CLX5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=FGENESH: predicted gene_7.452 {ECO:0000313|EMBL:CTR08206.1};
GN ORFNames=BN2166_0040670 {ECO:0000313|EMBL:CTR08206.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR08206.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR08206.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR08206.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) 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|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}.
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DR EMBL; CWKI01000007; CTR08206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CLX5; -.
DR STRING; 5286.A0A0K3CLX5; -.
DR OMA; WKYISEG; -.
DR Proteomes; UP000199069; 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; 1.
PE 4: Predicted;
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:UP000199069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
SQ SEQUENCE 484 AA; 53065 MW; E6302F229FBD1657 CRC64;
MPLPPLETTS PSDWKYTAEG GANLVASFAG PASSPFWGHA LRLRKRKKRA GGTKEAEDAV
PSEVDVDFGA RVIAPLLGEA NVVEMEKVRL ERGWLEELVE DMRAKAVRPV ERESEDEIDL
DAPEGVVVED LIAGRGVLAV EIKPKWGFLP SPTHLSPSNA SIKTTYCRTC MHRHYKASED
GGSDGFCPLD LYSGDPPRVH KALEQLHATW VSSEGAINNL RIFLDGKKVL PGDASQAAAL
NQAFHHLTAT ISPASPVSPA TLFARALAPT LLHSPALPLL RDLQSLLDVL DIEGLASFLS
RTTGVDLAEK YGPEEVERLG GQPRLEEWVE WVGRYAPVLG RREEEEPAPL KHDEWERAKA
TLESRFLASA TPDQDSPTPP WREAILAYLL SATFKDCSLI IRLPLDLAAS TVGTVKAIDL
DPKPINRLGK YFRMDREIVE CWKERLERSK TEGRAGEVRK CSEAACEATA EGCSPKMTTR
TASS
//
