ID A0A0M9F1Q2_FUSLA Unreviewed; 1601 AA.
AC A0A0M9F1Q2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=FLAG1_02846 {ECO:0000313|EMBL:KPA44233.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA44233.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA44233.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA44233.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-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}.
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:KPA44233.1}.
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DR EMBL; JXCE01000029; KPA44233.1; -; Genomic_DNA.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000037904; 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; 2.
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 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:UP000037904};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 379..466
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 601..692
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1091..1118
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1601 AA; 176944 MW; 948F86D30A62FC66 CRC64;
MSSPPDTNLV STASSDQCPE KAPTQTQAQV QGQGKAGPGP STSPSTSASG EPSAADFSTS
PRRSNPHSLP PTSALAFGYV PVEQHQIQIK PPRQARALSY SSASLLANSS AAAATRKSRG
AEPVTRESYA RRSSFTTAPN STTAVSSLPI KNPRARASTR RESMTSDTAA EDQVLTDSQL
SDEPHHQRTR LPSAIENSHT VSSETPSATN NRFSSSSDLQ SRRLSGTSIY SLASARGVLS
GSSSAQGSEL GTPPRSVPGF LSTSKSTGIF QSEAEVSNVT VTTSSLQTGQ SVATNPNQHN
LTARDHNSQP LDFAKRTIRH DNMQNATSGL RNQGPDRSRS RAKRRFSGST ATSSHSPSSD
RAPQHREREE VKPSRWGVIG VCALDIKARS KPSRNILNRL IANREFDVVV FGDKVILDEE
VENWPICDYL ISFYSDGFPL DKAIAYVKAR KPFCVNDVPM QQILWDRRLC LHLLDKINVR
TPKRVEVTRD GGPGYLTPEM SKHIKEISGV TLDPIDPEQM PPPQKVELID DGNTISVDGQ
TLRKPFVEKP TSGEDHNIII YFPSEDGGGA RKLFRKIGNK SSDYIQDLNV PRAITEPDSS
YIYESFMQVD NAEDVKAYTV GPSYCHAETR KSPVVDGVVR RNTHGKELRY VTALGTEEKE
MASRISTAFG QRVCGFDMLR ASGKSYVIDV NGWSFVKDND DYYDHCSNIL KDLFIKEKLR
RGGVTPPIPS PAPSESGTDP FTRASNAFKD REQQSQPGTN GVRTSIASIP ATTDSQPDDT
SRRATSGTVT PLMPPETGLP SKAQSSSATP VIPTTPTEVN LPGILSAPAV PQSAIADPPS
EDTPAVPEPP LPTHSWKLKG MVSVIRHADR TPKQKYKFTF HSEPFIALLK GHQEEVLLIG
EAALGSVIQA VDLAYEQGIE DRAKLRSLRN VLVKKGSWPG TKIQIKPMFR KKKTEQPVIS
EELVAMTEKE NDKAEEGGDS SKEDKPPGAP RRQDSLSGVT MSKFTAAEER LVLDKLQLII
KWGGEPTHSA RYQAQELGEN MRNDLMLLNR DILDEVHVFS SSERRVTTSA QIWAASFLGK
KDIAEDFITI RKDLLDDSNA AKDEMDKVKK KLKGLLRKGN ERPAQFTWPE NMPEPSEVQT
RVVQLMNFHR RVMDHNYKKL CSGAVTSLNA ISNPSTEKLS GDNSSSSIAS SMSQANTINQ
IQSRWCCGED AELFRERWEK LFQEFCDGDK VDPSKISELY DTMKFDALHN RQFLEWVYTP
PNHMLDEYTA AGTKEGKPKE SEDGKSIDEK TDKSHQNSPE GSDKVDAGSR SASVKKLFRR
RSFLNNLRHF NEEAPPEQYF RLYKGTKQTA SQTDAQNEPL QELYRLAKVL FDFICPQEYG
ISDSEKLEIG LLTSLPLLKE IVQDLEEMQA SDDAKSFFYF TKESHIYTLL NCIIEGGVET
KIKRSTIPEL DYLSQICFEL YEAEMKTTGD DSSPHNAPTF TYSIRITISP GCHVFDPLHV
QLDSRHCIGC APRRSLTPHA DWLQVIKTLR AKFNQVKLPK TFLAVNLSDA FTFEDLERQG
SDSDVLEMKA APSRGLTDQP KSPGQEDSEQ LATGAGEVMI S
//
