(data stored in SCRATCH zone)

SWISSPROT: Q757D1_ASHGO

ID   Q757D1_ASHGO            Unreviewed;      1142 AA.
AC   Q757D1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.21 {ECO:0000256|RuleBase:RU365032};
DE            EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN   ORFNames=AGOS_AER082W {ECO:0000313|EMBL:AAS52766.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52766.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52766.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Bifunctional inositol kinase that acts in concert with the
CC       IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate
CC       group-containing inositol pyrophosphates diphosphoinositol
CC       pentakisphosphate, PP-InsP5, and bis-diphosphoinositol
CC       tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also
CC       respectively called InsP7 and InsP8, regulate a variety of cellular
CC       processes, including apoptosis, vesicle trafficking, cytoskeletal
CC       dynamics, exocytosis, insulin signaling and neutrophil activation.
CC       Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to
CC       produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce
CC       (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5,
CC       produced by IP6Ks from InsP6, to produce (PP)2-InsP4.
CC       {ECO:0000256|RuleBase:RU365032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-diphospho-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP +
CC         H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate +
CC         ADP; Xref=Rhea:RHEA:37467, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:74946, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC         EC=2.7.4.21; Evidence={ECO:0000256|RuleBase:RU365032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-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=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC         inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC         ChEBI:CHEBI:456216; EC=2.7.4.21;
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|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; AE016818; AAS52766.1; -; Genomic_DNA.
DR   RefSeq; NP_984942.1; NM_210296.1.
DR   STRING; 33169.AAS52766; -.
DR   EnsemblFungi; AAS52766; AAS52766; AGOS_AER082W.
DR   GeneID; 4621146; -.
DR   KEGG; ago:AGOS_AER082W; -.
DR   HOGENOM; HOG000177917; -.
DR   InParanoid; Q757D1; -.
DR   KO; K13024; -.
DR   OMA; PWLFRER; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0101011; F:inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate 1-diphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IBA:GO_Central.
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:0000830; F:inositol hexakisphosphate 4-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR   GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi.
DR   GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   CDD; cd07061; HP_HAP_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; PTHR12750; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   Pfam; PF18086; PPIP5K2_N; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757D1.
DR   SWISS-2DPAGE; Q757D1.
KW   ATP-binding {ECO:0000256|RuleBase:RU365032};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365032};
KW   Kinase {ECO:0000256|RuleBase:RU365032};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU365032};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transferase {ECO:0000256|RuleBase:RU365032}.
FT   DOMAIN          211..299
FT                   /note="PPIP5K2_N"
FT                   /evidence="ECO:0000259|Pfam:PF18086"
FT   DOMAIN          422..522
FT                   /note="RimK"
FT                   /evidence="ECO:0000259|Pfam:PF08443"
FT   REGION          33..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          743..763
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        33..51
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..204
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1142 AA;  129392 MW;  4367C53AF3DB5A07 CRC64;
     MSEDNCLQPQ LSPLFLSCST KKAMESIAPI LEGFTPKTSS SENTSLKLPP ASLTTDEEED
     ADENLDPNAL ARTVSVQSQQ SAVGGTGAVT YNSLAAPDEN AETFAKHGAA HGLEQITSSQ
     ALEECACEEG NCTDACQAVS PGAYKGQSPR KPADDATEKN EGWQHSVHPP VQQTGHEGAN
     SDSATPAPSS SSSSRKSSTS ITKPQLPRVG KIGVCAMDAK VLSKPCRHIL NRLIENGEFE
     TIIFGDKVIL DENIENWPTC DFLISFFSSG FPLNKAIDYV MLRKPFMIND LIMQKVLWDR
     RLCLRLLEAA QVPTPPRLEI TRDGGPRVDD ALRSKLLERG VHVKPIREPI WRMLDNDTLE
     VNGEIMTKPF VEKPVDGEDH NIYIYYHSKN GGGGRRLFRK VGNKSSEFDP ALVAPRSEGS
     YIYEKFMDTD NFEDVKAYTV GESFCHAETR KSPVVDGIVR RNTHGKEIRY VTELTEEEKQ
     MAARVSKTFS QMICGFDLLR VNGKSFVIDV NGFSFVKDNS MYYDSCAKIL RDTFVNAKKQ
     IDLEKRNLPV IQEEKRQKWF FKGLVTVIRH ADRTPKQKFK HSFRSQIFIS LLKGHKEEVV
     IRNVSDLQIV LQALRIAMEE GVEDPNKLEV LANALEKKLN FPGTKIQLKP VLNDDNEVEK
     VQFILKWGGE PTHSARYQAQ ELGEQMRQDF DLLNKNILRN IKIFSSSERR VLASAQLWAM
     ALFGADELGS DEISIRKDLL DDSNAAKDLM DKVKKQLKAL LREGKEAPPQ FAWPLKMPQP
     YLVIKRVVEL MNYHKKIMDH NFSHKSLEEM QRRWCCGEDP TLFKERWDKL FKEFVSVDKV
     DPAKISELYD TMKYDALHNR SFLERIFSPD EADELNEDAA CQHSLVDRYP INILAKNNFK
     IPETTLGKTT SNSVGSLGWV LEKESGMKAH CSNPNSIFDH PRYMQLRELY RLSKVLFDFI
     CPQEYGIEDN EKLDIGLLTS LPLSKQILND IDDMKSKDTP ACIAYFTKES HIYTLLNIIY
     EAGLPMRIAR NALPELDYLS QINFELYESA DSGGQKSHAI RLKMSPGCHT QDPLDVQLDE
     KHYISCIPRI SLTKHLDMDY VSQKLRNKFS RVNMPQKFTP VHITQPDLSY KRPAMKDSST
     ES
//

If you have problems or comments...

PBIL Back to PBIL home page