ID I2H0X0_TETBL Unreviewed; 1141 AA.
AC I2H0X0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase {ECO:0000256|RuleBase:RU365032};
DE EC=2.7.4.24 {ECO:0000256|RuleBase:RU365032};
GN Name=TBLA0C02100 {ECO:0000313|EMBL:CCH60022.1};
GN ORFNames=TBLA_0C02100 {ECO:0000313|EMBL:CCH60022.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60022.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60022.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE806318; CCH60022.1; -; Genomic_DNA.
DR RefSeq; XP_004179541.1; XM_004179493.1.
DR AlphaFoldDB; I2H0X0; -.
DR STRING; 1071380.I2H0X0; -.
DR GeneID; 14495002; -.
DR KEGG; tbl:TBLA_0C02100; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_3_1_1; -.
DR InParanoid; I2H0X0; -.
DR OMA; FRIELTC; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000002866; Chromosome 3.
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-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 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; IPR011761; ATP-grasp.
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.
DR PROSITE; PS50975; ATP_GRASP; 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:UP000002866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 315..521
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 130628 MW; 91C2FE39DD3C49BA CRC64;
MQEKNLPKEG EILPSLNDKR PGSEKDLKYL DTPINSDPLK KTKAETRSGT AKTIESFAPI
LEAFSPTPSH SENTSLKLGT PGSPRIDTLN EEEALTNLLN VGLQLNDKNQ RSSHNSVTDP
SSSANSVNFS DNFDRPDMNS GLGISSTAFD SLPPSIIKDE SPVPHAKSTS PSTSSSRKSS
LSHHKVQLPR VGKIGVCAMD AKVLSKPCTQ ILNRLQENGQ FTTIIFGDKV ILDEKVENWP
TCDFLISFFS KGFPLEKAIR YVNLRKPFMI NDLVMQKALW DRRLCLQILQ AANIPTPRRL
MIIRDGGPKV DKQLKEKLSK AGVEVDKMVE SRWKMIDDDT LEVDGHIMRK PFVEKPVDGE
DHNIFIYYHS KNGGGGRRLF RKVGNKSSEF DPSLITPRRQ GSYIYEEFMD TDNLEDVKAY
TVGEGFCHAE TRKSPVVDGI VRRNIHGKEV RYITELTDEE KEIARKVSTA FSQMICGFDL
LRVKGKSYVI DVNGFSFVKD NTSYYDSCAQ ILRDTFIKAK KEIDKKKQIL PIIKEEKMQN
WVFKGLVSII RHADRTPKQK IKYSFTTPIF IALLKGHKEE VIIRAQTDME IVLQALSFAR
EENKEDPAKL KVLYTALKKK LTFRGTKIQL KPVINKDNEV EKVQFILKWG GEPTHSAPYQ
AQDLGEEMRQ YFDLLNKDTL QDVTIYSSSE RRVVLTAQTW ANALFGEDEI SSDVINIRKD
LLDDSNAAKE LMDKVKKRLK PLLRQHKKPS RNFSWPPEMP EPYTVVKRVV ELMNFHKKVL
RYNFANEDIE NIQARWCCGE DPALFKERWE KLFKEFTSVE KLDPSKISEL YDSMKYDALH
NREFLQLVFN PNNCQDVKEE IEKHASLVDR YPINILAMNN FKISNNLKTD DADAQNTSSV
GSLGWSLEGK TMKNPNAIPD SPFNDPSFIQ FRELFKLTKV LFDFISPQEY GIEDTEKLDI
GLLTSLPLAK QILNDLKDLK EKTSPGCVAY FTKESHIYTL LNIIYESGIP MKIVRSALPE
FDYLSQINFE LYESTDPMGH KTHAIRLKMS PGCHTQDPLD VQIDEKHYIS CIPKISLTKH
LDMDYCQQKL RNKFPRVNLP PKFIPVSITN PNLIFKKEIQ AKMEKEEKCI YLHYQKRKIS
L
//
