ID B6QTN9_TALMQ Unreviewed; 1345 AA.
AC B6QTN9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=PMAA_005520 {ECO:0000313|EMBL:EEA19781.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA19781.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995905; EEA19781.1; -; Genomic_DNA.
DR RefSeq; XP_002152718.1; XM_002152682.1.
DR STRING; 441960.B6QTN9; -.
DR VEuPathDB; FungiDB:PMAA_005520; -.
DR HOGENOM; CLU_000914_2_1_1; -.
DR OrthoDB; 5476261at2759; -.
DR PhylomeDB; B6QTN9; -.
DR Proteomes; UP000001294; 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; 1.
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; 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:UP000001294};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 224..312
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 451..543
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 149558 MW; EB330DA2E40B63DF CRC64;
MSENASVSSG QPQTLATTTT ASNEGTSTAT TTSPSPQGLS VPSGTNKEDR LFPSAVITND
EPRQTYFSDR LKSSSTSCVN ELGVSDNAVQ NSTNAASVQP ESKRMSFASL RSLGSVSIAG
SVTGPHDLAA AATSNEDSQK TTSGYTRSSV SSADFPAAFR SGHALSSLNH PSHGLPTTRN
ETPSEGRRLS RPTRSSSRAP RRLSGSTAAS SASEAEPRPP YIGRIGVCAL DVKARSKPSQ
NILTRLQSKG DLDVIVFGDK VILDEAVENW PVCDFLIAFF SDGFPLDKAI AYAKLRKPFC
VNDLPMQKIL WDRRLCLKVL DQMGIPTPRR VEVNRDGGPV LESTELAQHL YHLTGVKLQG
PEDGVGGGAV KSQSISLSED GETLIVDGQT IRKPFVEKPV SGEDHNIHIY FPKDQQYGGG
GRRLFRKVGN KSSEYDPNLV VPRSITEKGT SYLYEQFLRV DNAEDVKAYT VGPDFCHAET
RKSPVVDGVV RRNTHGKELR YITNLTKEEA AMAAKISNGF GQRICGFDML RVGDRSYVID
VNGWSFVKDN NDYYDKCAKI LREMFLNERR RRDRNLEQSE PPSPDPVSSM RSVSGSHRSS
LKTILKSPSM SRIHGSPQAP RDHSVPPDII SPTSGPAGEM IKASMSQSRE ELSLPESGSA
SATHSPALSI ANEEEIVPLP ASKHSWKLKG MVAVIRHADR TPKQKFKFTF HSQPFVDLLR
GHEEEVVIKG EAALASVAAA VRVSMEQGLE DMDKLKLLKV SLEKKGNWPG TKVQIKPMFR
KRRPEEMSGG IEPPSSPQVK NAPLPEDPAT ASQESPSDSE KLARSQTRSD SISGPTFSRF
SAAENDLILD KLQLVIKWGG EPTHAARYQA QDLGMTMRDD LKLMNKEALN DVRIFTSSEP
RVSTSAQIWA CSFLDEKELP EDFIQVRKDL LDDSNAAKDV MDKVKKKLKL LLREGSAPSQ
FTWPKDNFPE PSVVLATVVQ LMKYHRVVMR HNFHRLARSD IVDVPGNPPK NPDSPSVDSI
QGRWCTGEDA ELFKERWEKL FAEFCDTEKV DPSKISELYD SMKFDALHNR QFLEWVFIPP
DGFKVKEQSG LPSQQLIESD KFEEKTDNGT LAEIISFKKR ALSIVESRRF GRLEDAYDNY
FKLHGNPNSK RKKSDERLVK LRELYKLAKV LFDYITPQEY GIKDSEKLEI GLLTSLPLLR
EIVRDLEEVQ ASPDAKSFFY FTKESHIYTL LNCILEGGIQ TKIKRRAIPE LDYLSQICFE
LYEAKDSETD TFSYSIRISI SPGCHAFDPL DVQLDSRHAI GCAPRRSLTA HQDWKEVIET
LKAKFDTVKL PKSFIAVNLS DKHAY
//
