ID A0A094IZ95_9PEZI Unreviewed; 1487 AA.
AC A0A094IZ95;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=V501_09699 {ECO:0000313|EMBL:KFZ01993.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ01993.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ01993.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KFZ01993.1}.
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DR EMBL; JPKD01003198; KFZ01993.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094IZ95; -.
DR HOGENOM; CLU_000914_2_0_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000029315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 303..390
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 530..619
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1038..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 163060 MW; AE3786D9819DA84A CRC64;
MEEEGQTNPP SSTVAAEAKF GSAREPSHQL GPEEAAKMSS HRLSTASSEN PSAVNLKSSI
SEPVEREAFV EPASFSLPRG PTYGTESSRA SSTISHRGSV SDMSEAWTEG TNTSINDGAV
EESETPRMLS GSTSDLTKHA PLPEPAMSKS GSTTSESKRM SSSSLYSLQS ARAGGVAPSS
NFSSGDAIPR LNPGNIPGTR SLGVSPDAAP IVSVTSPSVT PPTAQGAANP QQAAPKDGAP
PGDAPKRSRQ EGTSRASIPR SRSRVKRRFS VSTGASSHSP SSERGIHQVK EKEGPKPAPY
GIIGVCALDI KARSKPSRNI LNKLIAKGEF SVVVFGDKVI LDEDIENWPV CDYLISFYSE
GFPLDKAIAY VKARKPFCVN DVPMQQILWD RRICLRILDK INVPSPSRVE VNRDGGPRVM
SQDLARHLKE TSGVIVQGPE DGDKLFAPPP RKVELLDDGD TLSVDGVLLR KPFVEKPVSG
EDHNICIYYP KSQGGGARKL FRKIGNKSSE HIDGLTIPRA ILEEGSSYVY EKFMRVDNAE
DVKAYTVGTG FCHAETRKSP VVDGLVRRNT HGKEIRYVTS LTKDEAAMAA RISTSFGQRV
CGFDLLRAEG KSYVIDVNGW SFVKDNDAYY DQCSSILRNM FIQERERRQA KAAAAEQAKI
SESVAQSAEA SESEMPPPTR KESSLKENHR STLQTILGRS PSISKLAHLH HNHGKSSEQR
STSPDRAVLT MPLSTASSME KPVSSMVSSL PHVSSRASIS GPASAAGSVR TSQILEPNPE
EEEDKELPPP APKHAWKLKG MVSVIRHADR TPKQKYKYTF HTKPFIELLK GHQEEVLLTG
EAALDSVLDA VDVALREGIE DSTKLKALRN VLVKKGGWVG TKVQIKPMFR KRKVEDSPKP
TFATIADIPV DVSKVIPPVP TTPGATDDSQ DPEDRPLKRA DSLTGVTLSR ITAAEERLVL
DKLQLIVKWG GEPTHSARYQ AQELGENMRN DLYLMNKEVL DEVHVFSSSE RRVTTSAQIF
SASFLDKKDL ASDFITIRKD LLDDSNAAKD EMDKVKKKLK VLLREGQGPP PQFAWPANLP
EPSIVQQQVI QLMKFHRKVM RHNYQKLYGG AATSLNNIVN PGDKAASESP QVGAMGQATA
INNIQARWCC GEDAELFRER WEKLFIEFCD AEKVDPSKIS ELYDTMKFDA LHNRQFLEWV
FTPSKSMLEE EDSAVVVEDA SSAKASEDKS DKSERSDSTN TTEKSESSKS VSRRLFRRRS
GNMKNVVEET PESYFHLFTG STKTKAKTDA RFEKLRELYN LAKVLFDFIC PQEYGITDSE
KLEIGLLTSL PLLKEIVADL EEMQASDDAK SFIYFTKESH IYTLLNCILE GGIQTKIARS
AIPELDYLSQ ICFELYESET TPSPAPKAQS APELAPPADV AALAELAANM PSAPEPIPSP
APPPEQTFAY SIRITISPGC HTYDPLDVQL DSKHCIGCQV AEELFGY
//
