ID A0A420HBX4_9PEZI Unreviewed; 1386 AA.
AC A0A420HBX4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=GcM3_206010 {ECO:0000313|EMBL:RKF54883.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF54883.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF54883.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF54883.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF54883.1}.
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DR EMBL; MCBQ01020615; RKF54883.1; -; Genomic_DNA.
DR STRING; 62708.A0A420HBX4; -.
DR Proteomes; UP000283383; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:UP000283383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 193..281
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 416..510
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..941
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 573..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1386 AA; 156228 MW; 39503EAD76D6A007 CRC64;
MTFRSSGDRA EDSNLEETQL NTSSLLAKSS KYPAPNIQCD NHTSTSSTCS MLSTRAAVMS
SVNSSNGSEN GSSRSNTTRL CTSQASLAQP EISAPVVSPI TSSGQLSSQK ISRVLHRSTS
RETQASTTDM LLRSVSQRAE TGSVPQLANG RPRSQIHRRP SGSTVASSHS PNSERDLCSR
PTSTEEKASL IGVIGVCALD VKARSKPSRN ILNRLIAKGE FKVVVFGDKV ILDEDIENWP
ACDFLISFYS DGFPLDKAIA YVKARKPFCV NDVPMQKLLW DRRICLRILD KINVPTAERL
EVNRDGGPTI LSPEITKYVK ETTNIVLDEP ENRLSGRNKV PRKVELIDDG DTLSVDGALL
RKPFVEKPIN GEDHNICIYF PKSEGGGARK LFRKIGNKSS EWIEGLTVPR AIIEPNSSYL
YEKFMKVDNS EDVKAYTVGP NFCHAETRKS PVVDGLVRRN THGKEIRYIT SLSRKESAMA
RRIAISFGQR VCGFDLLRTE GKSFVIDVNG WSFVKDNDEY YDQCARILKD IFVREKQKRN
EPQLDPISSP MPIDNPKFAL VDKKKDTGTS FKEQNRTTRY QILNRSPSLT QTQYNKKRSA
TNSSSDLSCL PSPRTSPSGK LENNAAHVLV NPTPMLPPPA VSFTSRSLPS TTKSSITSGD
KIANETSPPA PKHTWKLKGM VSVIRHADRT PKQKYKFTFH SKPFFELLKG HQEEVLLTGE
AALLSVMAAV DTALQEGIED GEKLRNLKNV LIKKGGWIGT KVQIKPMFRE KFTETTLSKS
SDIREDKQSR SIILGKTEEE LDQNYDESDQ TLLERHDSLS GITLSRITAA ENCLVLDKLQ
LIVKWGGEPT HSARYQSQEL GESMRKDLIL MNPEVLDKVH VFSSSERRVT TSAQIWAAAF
TDQKEISPKS IIIRKDLLDD SNAAKDEMDK VKKQLKTLLR RGISAPPQFA WPSNMPEPSI
VQRCVVQLMK FHRKVMRYNF NKIYGGTSLS LNTIRNPGDK DGLKEKKSSS SLNYHSIPQN
GTTCSIQARW CCGEDAGLFK ERWEKLFSEF CDREKVDPSK ISELYDTMKF DALHNRQFLE
WVFTPSKSIL AEEEDGISET LKEIGKEKKQ PRPNDDTVEE QEVLTKLERS RSQHRRMFRR
GSIISGNKFT ENPPEQYFRL FTGSSDTKAK TDARLEKLRE LYKLAKVLFD FICPQEYGMT
DTEKLEIGLL TSLPLLKEIV QDLEEMQASD DAKSFIYFTK ESHIYTLLNC ILEGGITTKI
TRSAIPELDY LSQICFELYE SENKNPKGVD DMAKYEYSIR IAISPGCHTF DPLDVQLDSK
HCISCAPRRS LTAHKDWKEV IDTLRAKFHQ VKLPKSFVAI NLSESHAFHK RETQQSDLEP
QENKMI
//
