ID A0A2P4ZYN2_9HYPO Unreviewed; 1564 AA.
AC A0A2P4ZYN2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=TGAM01_v201663 {ECO:0000313|EMBL:PON29414.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON29414.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON29414.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON29414.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(2016).
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:PON29414.1}.
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DR EMBL; JPDN02000004; PON29414.1; -; Genomic_DNA.
DR STRING; 398673.A0A2P4ZYN2; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000054821; 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 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:UP000054821};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 311..398
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 532..625
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 171897 MW; 638610DB3737EC83 CRC64;
MDPLGASGSA AIASDESPQP RQSPSYEPSA ANSSPSTLPS QPSRHSRSVS VSSFTGSVSS
KKSRYAEPGT SDIHAERSSF SSSPYSSNLL RSGRSWPYNR RHSAASEALT EELYLGEAQQ
QLFDKDTPRM RPNPDSTGNH SALPEPALTT RSSFSDSYSV QSKRLSGTSL YSLASARGVI
ASAPPSNRAS DQGEPPRSVP GLMSSSKGTA SALPEAALSN MTVTTSSAAQ PGHASPSNHS
LAARDSQTHH DLVRRNQRSE TMRSSQPDRS RSRAKRRFSG STAYSSQSPS SERGPHHREK
EEAKPAPLGV IGICALDIKA RSKPSRNILN RLIANREFDV VVFGDKTILD EEVENWPMCD
YLISFYSDGF PLEKAIAYIK TRKPFCVNDV PMQKILWDRR ACLRLLDKIQ VRTPERLEVT
RDGGPKVLSP EMTKYIKEIS GVTLEPADPE NTLPPSKVEL IDDGDVLSVD GLLLKKPFVE
KPISGEDHNI IIYFPKSSGG GGRKLFRKVG NKSSEYIPDL NIPRAITEPE ASYIYESFME
VDNAEDVKAY TVGPQYCHAE TRKSPVVDGI VRRNTHGKEL RYVTSLSTEE REVARKISTA
FGQRVCGFDL LRASGKSYVI DVNGWSFVKD NEDYYEHCAS ILKEVFIKER LRRGMPSPPV
ASPAPSSEVD PIARAGQNME QGSSSTVTVQ PIPVAKQSNR SSQAEQSDQA ESAIAPSGTA
SPTVQSTRTS VGQSSSGSPL IPQPLPPPAA ELTSPSVLSS TPASSKDVSQ SSPAGALAQE
EEEAEPSPPP PPPPKHSWKL KGMVSVIRHA DRTPKQKYKF TFHTEPFIDL LKGHQEEVLL
IGEPALASVI QAVDVAYIQG IEDREKLKSL RNVLVKKGSW AGTKVQIKPM FRKKKPQQVP
ETEEAPVIAN QTGDSTPLMP GGDAAESTPE GRASKRHDSV SEVTMSKFTA AEESLVLDKL
QLIVKWGGEP THSARYQSQE LGENMRNDLM LLNRDILDEV HVYSSSERRV TASAQIWACS
FLGEKELPED FITIRKDLLD DSNAAKDETD KVKKKLKGLL REGNDRPAQF AWPENMPEPS
EVQKRVVQLM NFHRRVMQYN YGKLYPSNAA TSLSAISNPS NEKLNGEGSS TSLSSALSQA
NAVNNIQPRW CCGEDADLFR ERWEKLFTEF CDAEKVDPSK ISELYDTMKF DALHNRQFLE
WVFTPPRSML EEEYGVKDGK TSTSSTKDGE DAKTATADDG KASSGTSPDN SDKAEGSSRS
ATVKKLFRRR SFLNSFRHID EAPPEQYFRL YKSSTSSAEK PDPRNEPLQE LYRLAKILFD
FICPQEYGIS DSEKLEIGLL TSLPLLKEIV QDLEEMQASN DAKSFFYFTK ESHIYTLLNC
IIEGGIETKI SRSTIPELDY LSQICFELYE SEVSPPAEGA PGDGEPTFAY SIRITISPGC
HVFDPLHVQL DSRHCIGCAP RRSLTPHLDW LQVIKTLRAK FNQVKLPKTF LAINLSDAFT
FEEIDKMGSD LEGAGEILEM KSLSVSTKDA TPVAAGVEAS EGCAIIDDED EDPAAAAAPS
QPAS
//
