ID A0A2H3CJZ2_9AGAR Unreviewed; 423 AA.
AC A0A2H3CJZ2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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};
DE Flags: Fragment;
GN ORFNames=ARMSODRAFT_850765 {ECO:0000313|EMBL:PBK78718.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK78718.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293415; PBK78718.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3CJZ2; -.
DR STRING; 1076256.A0A2H3CJZ2; -.
DR OrthoDB; 8233at2759; -.
DR Proteomes; UP000218334; 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:UP000218334};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PBK78718.1"
FT NON_TER 423
FT /evidence="ECO:0000313|EMBL:PBK78718.1"
SQ SEQUENCE 423 AA; 47106 MW; E7E371BC4AC66255 CRC64;
SSITATLPSH WKYISEGGAT IVFSYVGPPN PDFDGMVLRL RKSGVQTPVL EKQAFGTVAE
EEEPDDSSIV FQETCMKRLI PSVHLPKLQS VQVEKAWLEE LSRAHQQDRP LQRTASGGID
TTKSKAVLAT DLVGGSGLAV EIKPKWSFLP NKMYLSAASC SLKANTCRFC MHSRMKSKEG
ETVSLGYCPL DLFSSNRGRM KQAVHSLYDN WLTSDGTVNN LKIFVKGTKI GVDQKLSMFS
PEAYEVSDEN VRETFSEAIL TLLVNTPVLR VLNKVQRTLD SLDIEGLSLL WREAHSPANP
PQSTNGYTRS GRAIGVGEPN PSLADWSAFI DEYLSRSPDL EDLRYHLLAY LLSATFKDCS
IMIRMDLLDP RHSQEDVDPS KVTVIDLDPK NMTRLSKWEK LDETIVKAYS AIPLADRKTC
LDD
//
