ID W9WSJ8_9EURO Unreviewed; 1237 AA.
AC W9WSJ8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A1O5_06176 {ECO:0000313|EMBL:EXJ71182.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ71182.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ71182.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ71182.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) 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:EXJ71182.1}.
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DR EMBL; AMGX01000008; EXJ71182.1; -; Genomic_DNA.
DR RefSeq; XP_007744961.1; XM_007746771.1.
DR AlphaFoldDB; W9WSJ8; -.
DR STRING; 1182543.W9WSJ8; -.
DR GeneID; 19190888; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_3_1; -.
DR OrthoDB; 2220091at2759; -.
DR Proteomes; UP000019471; 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; 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 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:UP000019471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 311..399
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 196..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 872..899
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 209..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 139935 MW; F3804A355166775F CRC64;
MEHASTEEQL YAPSVAESNS TVASSYTGKE LHVAVLPRPT AEDGTELEDF ECPYCMLMKT
IRTKHQWKKH VMEDIQPYVC TFSGCDMSEQ LFENREQWFR HELSAHRATW YCNEDGHPEF
EAQIDFIKHM SDYHDTRLTE QKLQLSKDMF QRPLKSVGGK CNLCQMFSSR LKSHVSRHLE
QVALFALPRN NEIEGSGKAE LDGCSSRLGG SRGSGSQSSS EDSDDKLAPS QNAAGEESLA
TEGPEPSPQT YSVVEEEEEQ VGVPELAMGV DWDQLGMTKH LQAEEKQSLQ SLPQPTHEAP
SNKYSPARPG TVGFCALDIK ARSRQSRQLL TRQLSPGELE VVVFGDKVIL DDDVEDWPLC
DFFLAWYSDG FPLEKAIAYT RLRKPFVVND LWMQSALWDR RLCLRILDKL QVLTPKRLEI
NRDGGPIFAS TQQAQYVQRM TGVMLPGPED NDDGFASAQS VSISENGDTL YANGKSISKP
FVEKPVNGAD HNIVVYFSTS QGGGARRLLH KPSNKSSEFD PHCTIPRCIT EKTSSYIYEE
FLQADNAEDV KVYTVGPHYY HAETRKSPVV DGIVRLNTYR REIRYVRTLS LAERDIAATI
AKGFGQCVCS FGMLRAGNRS FVINVKGFKF AKDNDTYFDE CAKNLRSMFL NHLGPTNVHV
GPEIRSDMPA QEAASSWRLK GVSMAIRNGD HTPRQSILFL SSSEFLVGKA TDDGMISLEN
DEVVATVIHA TRETLARQYG IMHADSVEYI LRTSRRAQVK MIEQHPSLDL LVELGFQDPG
IVFQVPLQSL FELSWGEEAL HSLRYQSQDL GTSMRKDYIL LNKATLEDVR VFCGRDKAST
VSAQIWTDAF LGHSSLPENF ITVRTDLLSN ISSFARDELV QAEKKLQDLQ EFKNLLSRTI
TCVQEHQRVI DYNSAKLDGQ SDGARAIQRR WCAGEDWQLF RLRWELLFHK FFWNHGSCSR
ISNLYINMKH DAFHNLPISS WIATTPVRTD STEMSTTDNS GEGETGPRPQ SRFHILESPS
ENDFTSPSRA ISSSLQKTYT AVKALTDYVK ARQYGITDDE KPRIGLLISL PLLREVVDDF
EELQASGEAK AFIYFTDESH MRGLFDSIVL GLPQTRIKTM PEFDNLSQMC FELWESATET
EDGPEYKYSI QVSVSPGCHV DDPFSIEMDS KHFIPSQHRV PIASHLDWKE FMTTLKQKYN
TVQLPKEFLP VNVSEEHKNA TEDRARLLLS TEDQHTS
//
