ID A0A094G252_9PEZI Unreviewed; 1603 AA.
AC A0A094G252;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=V498_02265 {ECO:0000313|EMBL:KFY97121.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY97121.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY97121.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFY97121.1}.
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DR EMBL; JPKA01000356; KFY97121.1; -; Genomic_DNA.
DR HOGENOM; CLU_000914_2_0_1; -.
DR Proteomes; UP000029270; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 306..393
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 533..622
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1044..1071
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 177007 MW; 8BB2D60A3E76B18B CRC64;
MEEEGPTNPH SSTVAAEAKF GSPREPSRQL GPEEAAKMSS HRLSTASSEN PSAVNLKSNI
SEPVEREAYV EPASFSLPRG PTYGTESSRA SSTISHRGSV SDMSEAWTEG TNTSTNDGAV
EESETPRMLS GSMSDLTKHE PLPEPAMPKA MSTTSESKRM SSSSLYSLQS ARAGGVGPSS
NSSSGGGDAI PRLNPGNISG SRSVGVSPPD AATPVVSVIS PSVSPPTPQG TINPQQPTNK
DGVPGDAPKR SRQEGTSRAS IPRSRSRVKR RFSVSTGASS HSPSSERGVH QPKEKEEPKP
APYGIIGVCA LDIKARSKPS RNILNKLIAK GEFSVVVFGD KVILDEDIEN WPVCDYLISF
YSEGFPLDKA IAYVKARKPF CVNDVPMQQI LWDRRICLRI LDKINVPSPS RVEVNRDGGP
RVMSQDLARY LKETSGVIVQ GPDDGDKLLA PPPRKVELLD DGDTLSVDGV LLRKPFVEKP
VSGEDHNICI YYPKSQGGGA RKLFRKIGNK SSEHVEGLTI PRAILEEGSS YVYEKFMRVD
NAEDVKAYTV GTNFCHAETR KSPVVDGLVR RNTHGKEIRY VTSLTKDESA MAARISTSFG
QRVCGFDLLR ADGKSYVIDV NGWSFVKDND AYYDQCSSIL RNMFIQERER RQAKAADQLR
AAEQAKVPES VAPSAEASET EMAPPTRKES SLKDNHRSTL QSILGRSPSI SKLTHLHHNH
GKPSEKRSTS PERSVPTIPL STASSIEKPA SQMVSSLPHV PSRSSISGPV SAAPSVRTSQ
ILEPNPEEED KELPPPAPKH AWKLKGMVSV IRHADRTPKQ KYKYTFHTKP FIELLKGHQE
EVLLTGEAAL DSVLDAVDVA LREGIEDKTK LKALRNVLVR KGGWVGTKVQ IKPMFRKRKV
EDSPTPNFAT IADIPVDISK VIPSVPSTDG ASEESQDPEN RPLKRADSLT GVTLSRITAA
EERLVLDKLQ LIVKWGGEPT HSARYQAQEL GENMRNDLYL MNKEVLDEVH VFSSSERRVT
TSAQIFSASF LDKKDLASDF ITIRKDLLDD SNAAKDEMDK VKKQLKVLLR EGQGPPPQFA
WPANLPEPSI VQRQVIQLMK FHRKVMRHNY QKLYGGAATS LHNIVNPGDK STGETTPVSA
MGQATAINNI QARWCCGEDA ELFRERWEKL FIEFCDAEKV DPSKISELYD TMKFDALHNR
QFLEWVFTPS KSMLEEEDSA VVVEDASSTK VSEDKSDKSE RSDSTNTTEK SESSKSVSRR
LFRRRSGNMK NVVEEAPESY FHLFTGSTKT KAKTDARFEK LRELYNLAKV LFDFICPQEY
GITDSEKLEI GLLTSLPLLK EIVADLEEMQ ASDDAKSFIY FTKESHIYTL LNCILEGGIQ
TKIARSAIPE LDYLSQICFE LYESETTPSP APKAHSAPEL GPPSDLADLA ANPPSAPEPL
PSPAPPEQTF AYSIRITISP GCHTYDPLDV QLDSKHCIGC APRRSLTQHM DWKEVIETLR
AKFHQVRLPK SFLAINLSES HTFHRREEER SEGEEGGKEG EAEKSSLCVD GGEVERGRTE
EKVEGVKGEE KTKEKKEKKE KEKREGEEGE EDASVPEKVN VVF
//
