ID A0A0A2W8J0_BEABA Unreviewed; 1541 AA.
AC A0A0A2W8J0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BBAD15_g5358 {ECO:0000313|EMBL:KGQ09299.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ09299.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ09299.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ09299.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ09299.1}.
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DR EMBL; ANFO01000470; KGQ09299.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2W8J0; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_2_0_1; -.
DR Proteomes; UP000030106; 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:EnsemblFungi.
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:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IEA:EnsemblFungi.
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; 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:UP000030106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 309..396
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 530..623
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1541 AA; 169930 MW; A7F7E502FB10E44F CRC64;
MEPLNFTTTG SENGAKPLPC STTISSSISV NKDNADSSVP LTSADPKKPS TRAHARILSI
PAVIGSVTNT RSRHAEPGTS DIHPARASLP TTAHGSIQLT STRALLAHTR RQSTTSATST
DDSPAPRFYH DSDAQRTRLA TIDDPARSSA TLVTPQRPPR SQSDSRRLSN NSIYSLASAR
GIINSCSQGI DKRATARSAS ASLMSSVKGS GSGQSESGVS NVTVTTSSNS QATGPAGPQL
TPRDPHSQPL DMMRRPQRAE TMRTQPDRSR SRVKRRFSGS TANSSHSPSS DRGNHHYREE
AKPAQWGVIG ICALDIKARS KPSRNILNRI IANREFDVVV FGDKVILDEE VENWPICDYL
ISFYSDGFPL EKAIAYVKAR KPFCVNDVPM QQILWDRRIC LRLLDKIHVR TPKRLEVSRD
GGPSLLTPEV AKYIKEVSGV SLEPVDPTKT ATPKLVELVD NGDALSVDGV VLRKPFVEKP
TSAEDHNVII YFPKSAGGGA RKLFRKIGNK SSDFVADLDT PRCITEPENS YVYESFMQVD
NAEDVKAYTV GPTFCHAETR KSPVVDGIVR RNTHGKELRY VTALSTEERD VAGKISTAFG
QRVCGFDLLR AAGKSYVIDV NGWSFVKDNE DYYEHCASIL KDMFIKEKLR RLSLTPPLPS
PTVSDVDSMS KTTASIKEKE LQSANTSQAT TASPAPTGEP ESAVTTAPHS TFATSLPISD
SALTSALQST ITSLHLPPPA SDPTLPVPAA AASSAPGSVK STTTANTSGH QVPIDENPPA
VPPPKHSWKL KGMVSVIRHA DRTPKQKYKF TFHTEPFIAL LKGHQEEVLL IGEAALASVM
QAVDIAFEQG VEDRGKLKSL RNVLVKKGSW AGTKVQIKPM FRKKKTDKSA MSLPNVNEEE
ESAAQGDSDH VAENGTHRVS PRRHDSLSGV TMSKFTAAEE SLVLDKLQLV IKWGGEPTHS
ARYQAQELGE NMRNDLMLMN RDILDEVHVF SSSERRVTAS AQIWAASFLA QKEMPEDFIT
VRKDLLDDSN AAKDETDKVK KKLKGLLRKG NERPEQFAWP ENMPEPSEVQ TRVVQLMNFH
RRVMQYNYGK LYSGAATSLG AISNPSTEKL NGESSSASIS SALSHANAVT SIQSRWCSGE
DAELFRERWE KLFSEFCDGE KVDPSKISEL YDTMKFDALH NRQFLEWVFT PPKGMLEEEY
GTKERSKDGE DGKDGKESKD SKESKASEDA KGANSDNSDK SDQSNRSVRK LFRRRSFINS
VRGSNDEAQP EQYFRLYKGT NQATTKSDPR HEPLQELYRL AKILFDFICP QEYGISDSEK
LEIGLLTSLP LLKEIVHDLE EMQASNDAKS FFYFTKESHI YTLLNCIIEG GIETKIKRST
IPELDYLSQI CFELYESEVT PPAGSVADEQ PAFTYSIRIT ISPGCHVFDP LHVQLDSRHC
IGCAPRRSLT AHQDWLQVIK TLRAKFTQVK LPKTFLAVNL SEAFDFEEND KLFADDAPLE
MKATTPKEAV VLDMADVAPP FSEAEVRNGG ETPTSKQDAP Q
//
