ID W9PZS9_FUSOX Unreviewed; 1544 AA.
AC W9PZS9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FOVG_05215 {ECO:0000313|EMBL:EXA48506.1};
OS Fusarium oxysporum f. sp. pisi HDV247.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1080344 {ECO:0000313|EMBL:EXA48506.1};
RN [1] {ECO:0000313|EMBL:EXA48506.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA48506.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXA48506.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HDV247 {ECO:0000313|EMBL:EXA48506.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum HDV247.";
RL Submitted (MAY-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}.
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DR EMBL; JH650970; EXA48506.1; -; Genomic_DNA.
DR Proteomes; UP000030751; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 382..469
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 605..695
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1091..1118
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1544 AA; 170807 MW; C758DE20C66572E7 CRC64;
MNKNNPLDPD LNAASLADTD DSPAQAQAQA QEPEPEQEPS VSSSVSASGE PSAADFSSSP
RRFHPHSHPP SSSLTFGYVS VEQHNIQPNP PRQSRALSST SASLLANSSA AAITRKSRGA
EPVTRDAYAT ARRASFTAAP SSTTVVSSLP IRNPRPLART RRESMTSDTA SEEQTLADSQ
LSGPGEEPHQ LRTRLPSTNE NSHTVSPEAS NAAYHRLSSS SDYQSRRLSG TSIYSLASAR
GVLSGSSSAH GSELGTPPRS VPGLLSTGKS TATGQSEAEV SNITVTTSSN QPGQSVVGHP
NQHHLTPRDL HSQPLDFTKR AIRHDNMQSS TSGLRQGPDR SRSRAKRRFS GSTATSSHSP
SSDRGPHHRE REEVKPSRWG VIGVCALDVK ARSKPSRNIL NRLIANREFD VVVFGDKVIL
DEEVENWPIC DYLISFYSDG FPLDKAIAYV KARKPFCVND VPMQQILWDR RLCLHLLDKI
EVRTPKRVEV TRDGGPQYLT PEMVKHIKDV SGVSLDPIDP SQTPPPQKVE LIEDGNTISV
DGQTLRKPFV EKPTSGEDHN IIIYFPTEEG GGARKLFRKI GNKSSDYIKD LNVPRAITEP
GSSYIYESFM QVDNAEDVKA YTVGPNYCHA ETRKSPVVDG VVRRNTHGKE LRYVTALGAE
EKEMASRIST AFGQRVCGFD MLRASGKSYV IDVNGWSFVK DNDDYYDHCS NILKDLFIKE
KMRKGGVTPP MPSPAPSDTD PFTRASNAFK DREQTQSGTN GVRTSINSIA GTTDSQPDDS
SRRAPSGTVT PLLPPDSGLP SKTHSTLATP AIPPTPVDVT LPGISSAPPT QQSAVAEPPS
EQASIVPEPP LPTHSWKLKG MVSVIRHADR TPKQKYKFTF HSEPFIALLK GHQEEVLLIG
EAALGSVVQA VDLAYEQGIE DRAKLRSLRN VLVKKGSWPG TKIQIKPMFR KKKTEEPVIS
EELVAMTEEK KDITEEAGDS SREDKSHQGP KRQDSLSGVT MSKFTAAEER LVLDKLQLIV
KWGGEPTHSA RYQSQELGEN MRNDLMLLNR DILDEVHVFS SSERRVTTSA QIWAASFLGK
KDIPEDFITI RKDLLDDSNA AKDEMDKVKK KLKGLLRKGN ERPAQFTWPE NMPEPSEVQT
RVVQLMNFHR RVMDHNYKKL QSGAVTSLNA ISNPSTEKLS GENSSSSIAS SLSQANTLNQ
IQSRWCCGED AELFRERWEK LFQEFCDGEK VDPSKISELY DTMKFDALHN RQFLEWVYTP
PNHMLDEYTA AGASSVPGGS NGTKDGKSKE SEDGKTSDDK SDKSHHHSPE GSDKVDAGSR
SASVKKLFRR RSFLNNLRHF NEEAPPEQYF RLYKGTKQTA STADAHNEPL QELYRLAKVL
FDFICPQEYG ISDSEKLEIG LLTSLPLLKE IVQDLEEMQA SDDAKSFFYF TKESHIYTLL
NCIIEGGVET KIKRSTIPEL DYLSQICFEL YEAEMKSGDG SSPHDAPTFT YSIRITISPG
CHVFDPLHVQ LDSRHCIGCA PRRSLTPHAD WLQVIKTLRA KFNQ
//
