ID J8ZR99_EDHAE Unreviewed; 1177 AA.
AC J8ZR99;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=EDEG_03341 {ECO:0000313|EMBL:EJW02223.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW02223.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW02223.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW02223.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-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:EJW02223.1}.
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DR EMBL; AFBI03000083; EJW02223.1; -; Genomic_DNA.
DR AlphaFoldDB; J8ZR99; -.
DR STRING; 1003232.J8ZR99; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_03341; -.
DR HOGENOM; CLU_273421_0_0_1; -.
DR InParanoid; J8ZR99; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000003163; 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 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; 2.
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 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:UP000003163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 9..96
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 755..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 135753 MW; 07A8EB25F8F5B1D4 CRC64;
MSESTHKKMR ICVCIMPPKL NRPHLQKLLD RLKKHHNIEI LDEECILNVP VCLWPQSDVL
ISFYHNHLPF AKVLSYINLT NIHCINDFNM QYCLFDRRVV YMILQKLKIP VPCHIFINRD
NINMPPSIAK YVSDRFNLNL EIPKLADETN LIECYCEIKK EGYIKVGEKI LHRPFIEKPV
NSEDHNIFVY LENNTVRKLF RKKGNVSSEI DCSIKKIRRD RSYIYEKFYK ADEYKDIKVY
ALRTDYAYAE SRKAPTVDGI VERDEFGKEK RQVVVLKEVE YEYARRITQA FKQKICGFDI
LRSGDMSYVI DVNGWSFVKN NAAYYDLCAD LLKKEIARIG SDNDVSYNID IVKMIRVYRH
SDRTPKQKIK VKLKCVSSIE EEFVFKGDFN CVGEYLQYIV EKLEKMCENL CDVNVCDECI
VLPSFIDFQN SKNSSLEDIC RKNKISSNNR SNNSNTSDSN SYPFNITNSS SNIEDLLIDS
KIDPNGDYFN TSSMIEDSRI NNQYNNHITP ININLQKKLT SNISDFIRKI NSNDIKTEEK
DLSTLKNDCK NNTITTQIDI LSEKNYKPEN DIITSTKTNN TSDKQKNKEQ KLDYRTLITD
IYDIIDILNT KNTETNVKIQ LKCLKNTTEI ILKWGGQLTH AGVWQSKELG DILRYNITEN
NTHLLNNVTF RSSAENRVYE SACHFAESLC LKKVDVIRDK NLLDSTFHAN DLIEEGRSDL
KDEFFKFIKP EDNMFLMDTI RGLVCDDIGD EYNSGNSHSS NNSSSNNSSN NSSSNNSSSN
SSSNNSSSNN SSSSNSSSNN SNTGIDYNND RNNSKGTENG NSAINNDKNK LDMSIDLNRI
ALDKKSNTIK NILPKNINLK FPHKPYTTNK NKELQNIYAR WRRLKHNILK DTKMLYNRVS
EIYDNLKYDI THNNAHIHKI LSNDKITKFL LIINKLYNFV IQNEYGKGVH EKVRISYGIC
KPFFDVIINN LEGQDILSLY FAKESRIYTL FNVLNFVGGK SVPIKEFDYG SMIGLDVYTT
KKDNIYGNMS NLENDKNNNI NHNIFSDINS ICNNNSSTNT ISSNNSIALA NSNTNCNTIT
NKNNDNNNIN NLTTDTNCNS KSNNHNTNNN IYTNISDIKN IETRIRVVYN RGANCKDIID
GCLDARHRIP EKPDEILYDM SLDEFLQSIE IMRKNIQ
//
