ID A0A0G4M8W6_9PEZI Unreviewed; 1491 AA.
AC A0A0G4M8W6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BN1708_000901 {ECO:0000313|EMBL:CRK30370.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK30370.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK30370.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK30370.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVQH01021417; CRK30370.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4M8W6; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000044602; 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:UP000044602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 367..447
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 545..638
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 928..955
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1491 AA; 162659 MW; AF71FFCBAAACDC22 CRC64;
MDQQAPCTGR AVNNSSSLSQ SQTTSTSTPA SPPRTLSTLS SSLTASSSVL TSASSATLAS
SVGAPSTSST STTPTPTPVA TTPVQRPRDR SKRSASLSHT LSSFASGTAT ALSRKSRHAE
PGTTDAHADP ASLSMPPPPP PSQASGAASS NPLRSPRSSL CRSRRDSNKS VEAGIDSESF
ASDIVQKSPN PDLDVTRSGL GISSSTSTFQ PDRPLTTRSS FTDSDIKRAS ISSVYSLASA
RGVAPSSAAS AAGSETGAAP RSVSGIMSSG KPVAGSVPPN PELSNVTVTT SSTNQHLAPR
ETLDVMKRTP APVRTDSTIR SQPTRSRSRA KRRFSGSTAA SSHSPSSDRG PYHKEREEAK
PAPWGVIGIC ALDVKARSKP SRNILNRLIA NREFDVVVFG DKVILDEDFE NWPMCDYLIS
FYSDGFPLDK AISYVKARKP MLTPDIAKYI KDVSGVDFDP DEPRWRCAPH KVELLDDDDI
LSVDGALLKK PFVEKPVSGE DHNIIIYFPK SSGGGARRLF RKIGNKSSEY DPELNVPRAI
LEPENSYLYE KFMRVENAED VKAYTVGPNY CHAETRKSPV VDGVVRRNTH GKEVRYVTAL
NPEERDIASK ISTSFGQRVC GFDFLRADDK SYVIDVNGWS FVKDNDDYYE QSAKILKDLF
VKERLRRGGV TPPMPSPAVS DVIDPLALRG KEKENGQASV PALPITKSTG QLPASQSAEK
GLLEPKTDEL RPPSSTLTTK SESAATSGAM SLGSSPSSLP PPPPLVETGP GSVPSATPSA
LASAAASLKG DAAPEPEEAP APPPPPPPKH SWKLKGIVSV IRHADRTPKQ KYKFTFHTAP
FIELLKGHQE EVLLIGEAAL ASVIHAVDVA VTQGIEDPNK LKSLRNVLVK KGGWAGTKVQ
IKPMFRKKAT DEVVPPEEVA QILKEGVEAK FSEKADETKD EMDKVKKKLK GLLRKGNERP
SQFAWPDKMP EPSEVQTRVV QLMNFHRRVM QHNFGKLYSG AVNSLNAISN PSIDKSQPGE
SSAGSMSSAL SQANGINNIQ ARWCCGEDAE LFRERWEKLF QEFCDGEKVD PSKISELYDT
MKFDALHNRQ FLEWVFTPPK QMLEEEYGIK DTKDSKESSF KEGSIKEGKE GRSAGKESEE
AKVSQDSREE RRDILDKSDK TAEGNKSSSS VRRIFRRRSF LNGIRHVGEG APPEQYFHLY
KGNTQSKAKT DARFEPLREL YQLAKMLFDF ICPQEYGISD TEKLEIGLLT SLPLLKEIVQ
DLEEMQASND AKSFFYFTKE SHIYTLLNTI LEGGLETKIK RSTIPELDYL SQICFELYES
ETKVPAEVAT RGDEATFAYS IRITISPGCH VYDPLDVQLD SKHSISCAPR RSLTLHADWM
EVIRTLRAKF NQVKLPKTFL AINLSDLFSY DEQEKKDVDS DGLEMKSLAR QSASKDVQGE
AGDVSGLGDI TAGDVLDSST ELAMTPNEGH GQPSEPSLSL RGGPHIWRPG A
//
