ID A0A329T1C8_9STRA Unreviewed; 1063 AA.
AC A0A329T1C8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=JG687_00000440 {ECO:0000313|EMBL:KAG6974251.1}, PC110_g1179
GN {ECO:0000313|EMBL:RAW42675.1}, PC113_g3349
GN {ECO:0000313|EMBL:KAG2865802.1}, PC118_g2514
GN {ECO:0000313|EMBL:KAG2996366.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW42675.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW42675.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW42675.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG2865802.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=15-7 {ECO:0000313|EMBL:KAG2865802.1}, and P415
RC {ECO:0000313|EMBL:KAG2996366.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG6974251.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 3830 {ECO:0000313|EMBL:KAG6974251.1};
RA Mcdougal R., Panda P., Williams N., Studholme D.J.;
RT "Phytophthora aleatoria, a newly-described species from Pinus radiata is
RT distinct from Phytophthora cactorum isolates based on comparative
RT genomics.";
RL Submitted (JAN-2021) 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, 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}.
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:RAW42675.1}.
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DR EMBL; RCMG01000051; KAG2865802.1; -; Genomic_DNA.
DR EMBL; RCML01000038; KAG2996366.1; -; Genomic_DNA.
DR EMBL; JAENGZ010000009; KAG6974251.1; -; Genomic_DNA.
DR EMBL; MJFZ01000013; RAW42675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329T1C8; -.
DR STRING; 29920.A0A329T1C8; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000688947; Unassembled WGS sequence.
DR Proteomes; UP000697107; Unassembled WGS sequence.
DR Proteomes; UP000735874; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; 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 CDD; cd07061; HP_HAP_like; 1.
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; IPR033379; Acid_Pase_AS.
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; PS00616; HIS_ACID_PHOSPHAT_1; 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:UP000251314};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 37..125
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 371..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 120351 MW; 58CA9016CB58A575 CRC64;
MERTQSLPVA PPSVLASMSP PCSPPPLCSP PSVSKYVVGV CAMEKKTRSK PMREILRRLE
KKRQFDVLVF DDETIINRPV EAWPACDALI SFYSTGFPLE KAEDYVRRVR PVLVNELGMQ
HVLFDRRKVY ALLTRHGIQV PRHVIVNRDL PGGKQDELIE HDNYVEINGV RINKPFVEKP
ADAEDHNVYI YYPTSAGGGS KRLFRKVGDR SSEFYPDVNH VRRDGSYIYE EFLNTQGTDV
KVYTVGSSYG HAEARKSPVL DGRVVRDSAG KEVRYPVILN STEKDMARKV CLAFHQTVCG
FDLLRVRGSS YVCDVNGWSF VKNSKKYYDD CGLILHNYLV SALRSRYFRQ RRANSLTSMG
TQMCPQYATE PSVGGHDWHN HTRPSSGSDV SESSVASASS AGFTLDDENR EELRCVIAVV
RHGDRTPKQK LKTLVWERDL VNFYEKRRSE RKYDEVKVKA VADLQELLDL VRSLIKAYAP
GVGSKDAVWE DEGGDSFEKL LQMKRVLERW KFAGINRKVQ FKPHKSYAAA AAAYAEAPDG
TEKPKVLMIL KWGGDLTERG KQQGEELGQS FRNSLYPVEV EEGGLLRLHS TFRHDLKIFT
SDEGRVQMTA AAFAKGFLEL DGDLTPILVS LVTTLGRDAN KMLDHSGQAD ANEEMQTIKT
KLRTLLQRDY SSIEEMKAAI APLKTESIIQ ALEIIKTPKE ALVRLLELVR KFRTEIAERV
QDKQADEATP LYMGETFSLM FERWDKIYRD FYSTKTDTFN LSKIPDVHDC IKYDLLHNSS
VGWKYGLELF KLAEALARCY VSQEYGMDTA EKQSIGNRVS QALCAKIRAD IVTVMSASAE
QEESSSSSRS LYGNGDVVED GAVDIAEQDI EHHGYRLDPS YAKELRIKSP GTQVRTRLYF
TSESHLHTLL NVLRFQCPSW RARHEGGEDD EYDISLEQEK FSNEILKRMG ISVNDHMTQR
KYVFRESKLI SDSSRRALDR VAEINYLAHV VIRVFETPSL PQDSEDRFRV EISFSPGVKD
GLADFPDGAE GVEDTIYLTK NMTGVMFEDM LAACVSSVQS TSV
//
