ID A0A1J9Q6V1_9EURO Unreviewed; 411 AA.
AC A0A1J9Q6V1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AJ78_08218 {ECO:0000313|EMBL:OJD10885.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD10885.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD10885.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD10885.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) 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:OJD10885.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGRN01000668; OJD10885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9Q6V1; -.
DR STRING; 1447872.A0A1J9Q6V1; -.
DR VEuPathDB; FungiDB:AJ78_08218; -.
DR OrthoDB; 2714244at2759; -.
DR Proteomes; UP000182235; 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; 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:UP000182235};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..411
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012317742"
FT REGION 385..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46546 MW; 37820A22DFA0056F CRC64;
MLGLILFLAL STLIFIVRFT SQYKKPSPAL ALTHRNLDQR TQTTEPWNGN LASMGHVNSD
ETTAHTSYMA SHAISKLPTG TRPSYLAEGG ANIVYRFSIP NDIASSITPH GDGQQRASRK
LLRLRKHIDS GTPYPDTVNN FDRYVRPMFD DHELVDQELV RLPRGFIAYC NEQLRADEAR
NLRPQGRRGV YLAVREPFGL MITDMTPAPG SGECLWEFKP KWLLQSPSAP SDAKRCRTCA
LREMKNYNAR EAGNSEKQSF CPLDLVSDNF EDVLRATRFI RGGHGRARVA AFLYRNSTLL
KLQACQRQMN AVGLPGLQAH FRERAISMTL RDCTMFVKVP RDELEPLEAR LGDLDFKSGI
GGKLRYWRET EKRLIEEGWY SGNRKDQEFS ECSLQGPRRD LGTSAEAITE Q
//
