ID J3KLD5_COCIM Unreviewed; 348 AA.
AC J3KLD5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 57.
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=CIMG_02434 {ECO:0000313|EMBL:EAS37080.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS37080.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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 ---------------------------------------------------------------------------
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; GG704911; EAS37080.3; -; Genomic_DNA.
DR RefSeq; XP_001248663.1; XM_001248662.1.
DR AlphaFoldDB; J3KLD5; -.
DR STRING; 246410.J3KLD5; -.
DR GeneID; 4566079; -.
DR KEGG; cim:CIMG_02434; -.
DR VEuPathDB; FungiDB:CIMG_02434; -.
DR InParanoid; J3KLD5; -.
DR OMA; DCTMFIR; -.
DR OrthoDB; 2714244at2759; -.
DR Proteomes; UP000001261; 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:UP000001261};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
SQ SEQUENCE 348 AA; 39463 MW; 3FEB4E50E3AED298 CRC64;
MAPMQVDIAA NSFSMPISEL PADTEVEYLA EGGANIVYKM TVPESNRTNS EIRGQRAIYH
GKLLRLRKRI DSGTPYTETA RNFDSQIRTL FRDNELVAQE LIKLPKNFVS SCNERLKEDE
TNGRRPKQRH GVYLSTKEPF GLLITDMSPS LGSGADLWEF KPKWLIQSPS APLNAKRCRT
CALRAMKNHQ ARQKGEKARQ GFCPLDLVSD DFEHVLRAVK SIKGPQHGRI RVTKFLHRNP
TLLKLRDCQQ RMNAVGLPGL DADYRDRAVS MTLRDCTMFV KVPRDEAETP EVRLGDLDFK
SGTGGKLEYW RGIETRLIED GWYQGTDAAM EDGDCSLQNN RKDTTRGE
//
