ID A0A0D2LXK6_9CHLO Unreviewed; 538 AA.
AC A0A0D2LXK6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
DE Flags: Fragment;
GN ORFNames=MNEG_11821 {ECO:0000313|EMBL:KIY96139.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIY96139.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIY96139.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIY96139.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
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, cytosol
CC {ECO:0000256|ARBA:ARBA00004514, 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; KK103143; KIY96139.1; -; Genomic_DNA.
DR RefSeq; XP_013895159.1; XM_014039705.1.
DR AlphaFoldDB; A0A0D2LXK6; -.
DR STRING; 145388.A0A0D2LXK6; -.
DR GeneID; 25729122; -.
DR KEGG; mng:MNEG_11821; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:InterPro.
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; IPR033379; Acid_Pase_AS.
DR InterPro; IPR011761; ATP-grasp.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 147..366
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 538
FT /evidence="ECO:0000313|EMBL:KIY96139.1"
SQ SEQUENCE 538 AA; 59575 MW; B7649C41B8D0397F CRC64;
MDGHGTPVER AARVGSAVLT PHSAPGHKGG SKRKGMKRSS SAPNCNRPSI LPIKVGICAM
DKKATSKPMR EITGRLTQAG EFEIIVFGDK IIQEEPVEKW PLCDVLLSWH SDGFPLRKAQ
AYAALRRPFM VNDVGMQDML LDRRRVYKLL QDSSIPVPTH IVVSRDRLPP GEADPPGFLE
GEDYVELDGV RIEKPFVEKP VSGEDHNIYI YYPHSMGGGV KRLFRKVENK SADYDPNHPG
TVRRLGSFIY EQFLTTGGTD VKVYTVGPRY AHAEARKSPV VDGKVNRDAE GKEVRFPVLL
SPQEKEIARM VCAAFGQRVC GFDLLRSENG RSYVCDVNGW SFVKNSKKYY DDTADVLRTM
ILSQLAPHRL AAIIPEPLRQ LRLPEECGHA PEEGCSCAEE QAAAEAAAGM REVASLQDMA
SMGEEEALDD DDSSSTNFGG EPSSNRFLEL RCVLAVVRHG DRTPKQKMKM PVTQPAMLEL
FNKHKDSKGK QAKLKSPLQL QELLDVTRQL LADMERQQKA AARGPDGGAA GEEERDQL
//
