ID C1GSL8_PARBA Unreviewed; 1595 AA.
AC C1GSL8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 68.
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=PAAG_01513 {ECO:0000313|EMBL:EEH39051.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH39051.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH39051.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(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}.
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DR EMBL; KN293994; EEH39051.2; -; Genomic_DNA.
DR RefSeq; XP_015701275.1; XM_015844367.1.
DR AlphaFoldDB; C1GSL8; -.
DR STRING; 502779.C1GSL8; -.
DR GeneID; 9100065; -.
DR KEGG; pbl:PAAG_01513; -.
DR VEuPathDB; FungiDB:PAAG_01513; -.
DR eggNOG; KOG1057; Eukaryota.
DR HOGENOM; CLU_000914_2_0_1; -.
DR OMA; AQIWACS; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000002059; Partially assembled 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; 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:UP000002059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 368..456
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 596..687
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 24..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1595 AA; 173603 MW; 8AA248F37C38B2FD CRC64;
MEPLSGDSSG TAAAAAVARW LKSIDPHTMD ETQKDKGSGE KAVEGGSLLA KEKSQTQQQL
QLQQQEESLQ LSAGSAVFGS SNAGDTGRGH SDKEKEKERQ PATAQSTAAV HNRQGLAAGS
PSGLAAAGAS PEPATGNGNG SGSMSMSMPT TDGGGGGGGG GGDTTTATAT TTSATSYTSP
TTPSPGTTTT ASTAIPSSHC VSFSSLYSLG STIYSATSDR VPGTGTCASS LAGSIKGCNS
NSNSNSMDNP DGARSNPSSN PNQQCNNTNN NAIESSLPSS SPSTAAATAT ATATAADSTF
STISTSGPFP NLRADSTTTT AAATDGRSTS NWVVRPARSS SRTPRRFSGS TAASSASEAE
PKVPLIGKIG VCALDVKARS KPSQNILTRL QSKGDFEVIV FGDKVILDEA VENWPVCDFL
IAFFSDGFPL DKAIAYAKLR KPFCINDLPM QKVLWDRRLC LRILDQMGIP TPKRFEVNRD
GGPRVESKKL AQHIYDLTGV KLDGPDDGTG GGSPKTQSVT LSEDGETLIV DGKSFRKPFI
EKPVNGEDHN IHIYFPNDDH YGGGGRRLFR KIGNKSSEYD PDLTIPRSIL EKDGSYLYEQ
FLRVDNAEDV KAYTVGPDFC HAETRKSPVV DGLVRRNTHG KEIRYITKLS KEEATIATKI
SNGFGQRICG FDMLRVGDKS YVIDVNGWSF VKDNNDYYDK CAKILREMFI NHRLRREGKK
IDHLLVETHP NGELPTGRKN NGGSHRQALK SLLKSPSMTR MQNPIYNQKT HPTVSRDLAS
ATTSFPTPSS DASVLASNLK GVPIKTDRRC TVNTSDSAGS AVTSSTDTVV APPPASKHSW
KLKGMVAVIR HADRTPKQKF KFTFHTQPFI DLLRGHQEEV VIKGEMALRC VSDAVMIAME
QGIEDMEKLK LLQTSLQHKG KWPGTKVQIK PMFRQRYPDE MRDRLAAPSG NPLSSASENS
MSFNVSREVT REGGAEAAGE TEDENQEPFL SRSQTWSNSL SSPTFSRFSA VENDLILDKL
QLVIKWGGEP THAARYQSQD VGLNMRDDLK LMNKEALNDV SIFTSSERRV STSAQIFASA
FLDQKDVPED FVQVRKDLLD DSNAAKDVMD KVKKKLKLLL REGNSAPPQF AWPKENFPEP
SIVLSTVVEL MKFHRTVMRY NFARLERGDA SVSPATTTTI TTTTTTTTTT TANAIDIQGK
TDQDTPAPTL SSIQGRWCAG EDPQLFKERW EKLFAEFCDT EKVDPGKLSE LYDSMKFDAL
HNRPFLEWVF LPPESMLQTG EAGKQMSLGT DAKSRSASSE KGELGAVRGQ RLSPSGQEGG
GGGEVSAAEK EKEKAEDKNN NTFVQRLGLK RRSVADLSLM QPMGPLEDSY DSYFKLYGGS
NQTKAKLDKR LSRLRQLYKF AKVLFDFVTP QEYGIDDDEK LEIGLLTSLP LLREIVMDLE
EVQASPDAKS FFYFTKESHI YTLLNCILEG GIQTKIARRA IPELDYLSQI CFELYEAWDS
EAATFSYSIR ISISPGCHTF DPLDVQLDSR HAIGCAPRRS LTAHQDWKEV IETLKAKFDT
VKLPKSFIAV NLSDKHAAAK VDDAVKAAAG EVVQK
//
