ID C5MGN6_CANTT Unreviewed; 1159 AA.
AC C5MGN6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN ORFNames=CTRG_05240 {ECO:0000313|EMBL:EER30788.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30788.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER30788.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC IP6K kinases to synthesize the diphosphate group-containing inositol
CC pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-
CC diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-
CC InsP4, also respectively called InsP7 and InsP8, may regulate a variety
CC of cellular processes, including apoptosis, vesicle trafficking,
CC cytoskeletal dynamics, and exocytosis. Phosphorylates inositol
CC hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-
CC inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946,
CC ChEBI:CHEBI:456216; EC=2.7.4.24;
CC Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
CC + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate
CC + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU365032}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609,
CC ECO:0000256|RuleBase:RU365032}.
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; GG692402; EER30788.1; -; Genomic_DNA.
DR RefSeq; XP_002550942.1; XM_002550896.1.
DR AlphaFoldDB; C5MGN6; -.
DR STRING; 294747.C5MGN6; -.
DR EnsemblFungi; CTRG_05240-t43_1; CTRG_05240-t43_1-p1; CTRG_05240.
DR GeneID; 8299559; -.
DR KEGG; ctp:CTRG_05240; -.
DR VEuPathDB; FungiDB:CTRG_05240; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_1_1; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IEA:InterPro.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0006020; P:inositol metabolic process; IEA:EnsemblFungi.
DR GO; GO:0043647; P:inositol phosphate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:EnsemblFungi.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051516; P:regulation of bipolar cell growth; IEA:EnsemblFungi.
DR GO; GO:0110162; P:regulation of mitotic spindle elongation (spindle phase three); IEA:EnsemblFungi.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.11950; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR037446; His_Pase_VIP1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR040557; VIP1_N.
DR PANTHER; PTHR12750; DIPHOSPHOINOSITOL PENTAKISPHOSPHATE KINASE; 1.
DR PANTHER; PTHR12750:SF9; INOSITOL HEXAKISPHOSPHATE AND DIPHOSPHOINOSITOL-PENTAKISPHOSPHATE KINASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF18086; PPIP5K2_N; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365032};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU365032};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365032};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365032};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 202..290
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 408..509
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 62..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 130920 MW; 525025029F6CB613 CRC64;
MRADPTLHSI SSIVQFSFNH SLNFFFRSFH RCFFVFSFFH KLAAKTLFGS IVPMSDKSES
LPIPVPGTEK HSSTKASPPV KPKSQPISPL SISLDHLSMT KHTDATPTTE KAMASIAPML
EAYTPKTNAE DSVSRLNSIS SASGHPSEDD LVQPLTTENL SGIKSHSNSF SDGHRIMKTI
SNTSNASRKS HADVPKLPKI GTIGVCAMDA KALSKPCRRI LGRLIETGEF ETVIFGDKVI
LDEAIENWPT CDFLISFFSN GFPLDKAIAY VNYRKPYIIN DLVFQKALWD RRVVLAILNH
ANVPSPSRLE ISRDGGPFLE PQLLERLKEI GMSEEKLYNL THQEEPDWEM VDEDTLRVGD
RVMKKPFVEK PVDGEDHNVY IYYPTATGGG GRKLFRKIGN KSSEFDPTLS SPRTDGSFIY
EEFMDTDNFE DVKAYTVGPN FCHAETRKSP VVDGIVRRNT HGKEIRYVTE LADDEKAMAR
NISNAFKQTI CGFDLLRVHG KSYVIDVNGF SFVKDNDEYY SSCAKILRGL FIEAKKSRDL
LSKHIPKTLN ASQFEQKGQK WVFKGMVTVI RHADRTPKQK FKYSFRSPLF ISLLKGHREE
VIIRAVSDLQ VVLETVKVAE AKGLEDLAKL KQLRGALEKK MNFPGTKIQL KPTLNSENPE
IVDKVQLILK WGGEPTHSAK HQATDLGEQI RQKLQLLNRE ALENVKIYTS SERRVIASAQ
YFTDSLLELD EPLPDDFLIV RKDLLDDSNA AKDLMDKVKK KLKPLLREGA EAPPQFAWPP
KMPQPFEVIS RVCELMNFYH QIMNYNFETK NVDEFQKEWC TGEDPFLFKE RWDKLFLEFI
TAEKTHPSKI SELYDTMKYD ALHNRQFLQM IFSYDPNDEE LLARLKSTCG GTVNSSGLVS
EYPINLLAMN NFKIPDSVST STNNSSVNLN ASPSSTTGSL GWVLSGATPN GGKGNEKTPQ
TPFDDPTFAR LRELYRLSKV LFDFICPQEY GIKDEEKLDI GLLTSLPLAK QILSDIHDMK
KNDRPALVNY FTKESHIYTL LNIIYGSQLP MKIARNALPE LDYLSQIVFE LYEADDPTSP
SGKKHSIRLS LSPGCHTQDP LDVQLDDDHY IACIPRISLT RHLDMDLVTQ RLKSRFSRVS
LPKKFTPVNI SSPLVSGSS
//
