ID A0A1B0FIZ5_GLOMM Unreviewed; 2184 AA.
AC A0A1B0FIZ5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 03-MAY-2023, entry version 32.
DE RecName: Full=diphosphoinositol-pentakisphosphate 1-kinase {ECO:0000256|ARBA:ARBA00012893};
DE EC=2.7.4.24 {ECO:0000256|ARBA:ARBA00012893};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY003791-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY003791-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY003791-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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|ARBA:ARBA00034629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460;
CC Evidence={ECO:0000256|ARBA:ARBA00034629};
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|ARBA:ARBA00033696};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277;
CC Evidence={ECO:0000256|ARBA:ARBA00033696};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00005609}.
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DR EMBL; CCAG010004256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CCAG010004257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 37546.A0A1B0FIZ5; -.
DR EnsemblMetazoa; GMOY003791-RA; GMOY003791-PA; GMOY003791.
DR VEuPathDB; VectorBase:GMOY003791; -.
DR PhylomeDB; A0A1B0FIZ5; -.
DR Proteomes; UP000092444; 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; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 156..245
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2144..2166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2184 AA; 245166 MW; 09537C8C46034B15 CRC64;
MEWTWLKDWW RLKRYRLQHR TRKNHHSTPP NVISSTHQYD NSSKNVSVFE ENDNEKFIND
GNNDKHVVMK QKRRKRRGRK KHVTIAYDGS KDNNALYCDE GVLNDTDIDI TFESDIEEVN
DFCYCDDCLN GDTDFGESND GMDSDTSTSS NPGKQVVVGV CAMSKKTQSK PMKEIITRLE
EFEFIKMVIF SEEVILKESV DNWPICDCLI SFHSKGFPLE KAIQYAQLRK PYVLNNLHMQ
YDIQDRRRVY AILEKEGIEI PRYAVLDRDS PDPKKHELIE SEDHVEVNGV IFNKPFVEKP
VSAEDHNIYI YYPTSAGGGS QRLFRKIGSR SSVYSPESRV RKTGSFIYED FMPTDGTDVK
VYTVGPDYAH AEARKSPALD GKVERDSEGK EIRYPVILNH DEKLISRKVC LAFKQTVCGF
DLLRANGKSY VCDVNGFSFV KNSNKYYDDC AKILGNMILR ELTPTLHIPW SVPFQLDDPP
IVPTTFGKMM ELRCVVAVIR HGDRTPKQKM KVEVRHPKFF EIFEKYDGFK FGHIKLKRPK
QLQEILDIAR FLLAEIETKA DAEIEEKKSK LEQLKSVLEM YGHFSGINRK VQMKYQPKGR
PRGSSSDDDA PTEPSLVLIL KWGGELTPAG RIQAEELGRI FRCMYPGGQG RYDYSGTQGL
GLLRLHSTFR HDLKIYASDE GRVQMTAAAF AKGLLALEGE LTPILVQMVK SANTNGLLDN
DCDSSKYQNM AKNRLHELMR LDREFTSDDR IAINPNNSIS INQALDFVKN PVECCQHVHK
LIKELLVIIS VKKDDPKTKD AILYHGETWD LMRCRWEKIE KDFSTKSKLY DISKIPDIYD
CIKYDLQHNQ HTLQYDQAEE LYIYAKYLAD IVIPQEYGLT TQEKLTIGQG ICTPLLKKIK
SDLQRNIEEV DDESVNRLNP QYSHGVASPG RHVRTRLYFT SESHVHSLLT VLRYGGLLNV
ATDEQWRRAM DYISMVSELN YMSQIVIMLY EDPTKDPTSE ERFHVELHFS PGVNCCVQKN
LPPGPGFRPH SRNDSNALKA VVSNILDKAH LKSKPISIGA HHTVSGHEAL DLAKRLNEEL
ASQQQTKQTG SLETPRPISP NAEPRSRSYE QHAQKSKDGI CLAIDKKFPE IFNSSHNITN
VNRTAFQIRI TDNLTLYKID SSTNELPLSE IDFTLTLNGN DNQEICSTQK TDSATEQLLK
KQSQLLTMRR MESNDSSDYI QKLREFRRMS PLSTNERPLT CNCSLHLCIN NEENSLPHNH
AKSETDLSEL IMPFMKKQNS YSEFEEDFQM SASAPAVLLS GDFLPQQHRD SKLLKVSSLT
NSPTASTLQL CKALEETASL PIIVKPADHA LIVAKHKTSL ATAQSAPIIV ELANPFKFPS
NICTATPPIA ENSTSKTSYQ NTPIHYPPDI YQQQEQSREQ FYTKHLSHHN IHLHYHSATN
SNLHTNITIP NVVVTLTSST SANNLTNLSY NTNEFNTKLI TDSSNVTTHD LRSFTDPLHN
LSSAASYTNN NNNNNVSTTP HITITSYPIT TTTTATGAMH NNNITTTTTT TIDGNATSVS
SSSSVSSSRR QRHSIAGQMS YMKMLGFGGF NKKMTTSANS LFSTAVISGS SSAPNLRDMI
PVSSSVLEGF GGVPPIRPLE TLHNALSLKQ LDNFLEKMTT APLFKTPTCT PPKNPSTPLS
MITTTIEEET CVSTPTNHLC ICTDNRYDED SHFELCTRCG RQRRFDPTRL ERNLNQSSAQ
NPSNILWSKQ SSIASSITEP SSPAVSDTCS QETPSCDMSI SLTSTEGYNM PPATTEQLAK
FFPQLDVDLN SVSVYAPLNT DTLGETNNAL DELHFSAIGA GFEAKSACLT PVSFNMDLSI
VANKGSLTLS MEGFEDDDDA TPSAATPSLP CDEPQLAFCY CCEAHVNQGQ PPDDTQKSNE
LFTIMRSKRL AAHERKTPCA CAEPPLSAGL LNPELPSLNV RKVSDPISPR IQKQISLFED
GEFDKPKDYS VLHGSINIPA QLKQDARLRK FENLTQSTSN SNFPFESNTL KRVPNKVEDF
VDAELTQSCI NLKSSGVVAS NSSSACSSPQ HKMAAFRPVT QSCSTVATDL TPASGPTSPR
PGALIVREKF IEPPRRLARS LRGKTQSMDA EFLFNEFLLV PSQSVQAPSS NETNSTVTSP
SMRPNKRFIT TKVMGDSNDY LEKK
//
