ID A0A0D2BXF1_9EURO Unreviewed; 1507 AA.
AC A0A0D2BXF1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PV05_05687 {ECO:0000313|EMBL:KIW57086.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57086.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW57086.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57086.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-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; KN847319; KIW57086.1; -; Genomic_DNA.
DR RefSeq; XP_013317670.1; XM_013462216.1.
DR STRING; 348802.A0A0D2BXF1; -.
DR GeneID; 25327595; -.
DR HOGENOM; CLU_000914_2_1_1; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000054342; 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 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:UP000054342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 256..344
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 479..575
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1507 AA; 166611 MW; E7B3B1EB6EF4EF8A CRC64;
MDQSAPLRRT PTSNSDNALD DTASLTAVHS GASSSTSSRP HFPNGRTPST HSLLAAHKNP
DVRKAAHTET TKASADRSSI SMPPPISKPL ADRRLSTSLN SPRSQRRSED DARSPPASLK
SLDGDRALFG ASPTAQTSTT GYDRTVVTTA STSKAPGLPL LSPPAFNPSI PNQSDIVSTL
SSQVTSPSSA TKSDTSIPAG QTLGSIPRPD ISETILPNRV PRVPKPRSIS SSRRLSGTGP
SKNDAASTES KVSMGRIGVC ALDVKARSRP SRQILTRLQG DGDFEVIVFG DKAILDEDVE
NWPICDFLIS FFSDGFPLDK AIAYVKLRKP FVVNDLPMQK VLWDRRLCLK ILDHMQIPTP
RRIEVNRDGG PRLESPELAQ HVYNMTGVVL EGPEDGTGGG TPITKSVELT DEGDTIVVDG
KSLKKPFVEK PVNGEDHNVI IYFPRSQDGG ARRLFRKIGN KSSEYDPNLN VPRSITEPNS
SYIYEQFLRT ENAEDVKAYT VGPDYCHAET RKSPVVDGLV RRNTHGKELR YVTKLNDAER
DIAAKVARAF GQRICGFDML RTGNASYIID VNGWSFVKDN EDYYNDCAKI LRGMFVSEKF
KQENGMLDEL PAESSDDLPA RRQGTSHSHR SALKTILKSP SMTKLSQHLP HSNRHHSVTA
AGSPKSSTMT TPLSSPPSLE RHPNALAMPN AAENIESLPP PIVNTAPTSA TENESLPSAR
EQEAPAPMPS SKHSWKLKGF VTVIRHADRT PKQKIKFTAH SQVFADLLKG HHEEVLLKGE
AALASVEAAV KIAQRDHLED PDKLHNLRVA LAKKGSQPGT KVQIKPMFRK RRPEEMSANT
NVAAHPSSPS VLSISETEPF QISESPLAER SSSISETRDT AQLRRLQTRS DSISGATFSR
FSAAENDLVL DKLQLVMKWG GEPTHSARYQ SQDLGANMRD DFKLLNREVF NDVRIFTSSE
KRVKTSAQIW TAAFLDRQDI AEDFIQVRKD LLDDSNAAKD VMDKVKKKLK HLLREGNVPE
AFAWPKDVAS PFVVMHNVID LLKFHRRVMR HNFKKLTTGA AASLAALNGS PDSKDTNKDT
VTVASIQSRW CTGEDAELFK ERWEKLFTEF CDTEKADPSK ISELYDTMKY DALHNKQFLE
WVFTPSQSLL DEMAREEGLA LSASPPESEH VEGSASPVSK SRQESIVSAA GSLTDKHSFA
QKIGLRRQSV LKQPVPAPPL YSWEQGASYF KLFSGPPETK SSLDQRLGRL RELYRYSKIL
FDYIGPQEYG ISDEEKLEIG LLTSLPLLRE IVDDLEELQA SGDAKSFIYF TKESHIYTLL
NCIMEGGIHT KIKRSTIPEL DYLSQICFEL YEAKDADTAE STYSIRISIS PGCHTIDPLD
VSLDSKHAIG SAPRRSLTNH QDWKEVISTL KAKFNTVQLP KSFLAVNVSE KHEQEAERRA
SYLQSEAAKQ RHERGEDLEG EWVVNDNEDE GPSGHGVQDV NDNADTEPLS PRDVTATDSN
ATTTEEQ
//
