ID A0A1V6R767_9EURO Unreviewed; 1287 AA.
AC A0A1V6R767;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=PENSOL_c012G11508 {ECO:0000313|EMBL:OQD97345.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD97345.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD97345.1}.
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DR EMBL; MDYO01000012; OQD97345.1; -; Genomic_DNA.
DR STRING; 60172.A0A1V6R767; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000191612; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:UP000191612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 120..208
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 346..439
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1287 AA; 143372 MW; 1118B30B168074B6 CRC64;
MDDAAEHSNG SFADAGPLRP TEPNHSSPLL DMDSDNNDLT PTGPVPEPTL VPNKPASHAK
STQSQSGKAD SGFDTRSASR MGQSTRPLSH APRRFSGSTA ASTAASSISE MESSSLKPWR
IGVCALDVKA RSKPSQNILT RLQSKGEFEV IVFGDKVILD EAVENWPVCD FLLAFFSDGF
PLDKAIAYAK LRKPLCVNDL PMQKVLWDRR LCLRILDHMG VPTPKRLEVN RDGGPVLESA
ELGQHIYHLT GVKLEGPESG IGGGAPQTQS VSMSEDGEAL IVDGKVFKKP FVEKPVNGED
HNIHIYFPND QQYGGGGRRL FRKVGNKSSE YDPNLTVPRS VTEKDASYLY EQFLRVDNAE
DVKAYTVGPN FCHAETRKSP VVDGLVRRNT HGKEVRYITK LGKEEAIIAS KISNGFGQRI
CGFDMLRVGD KSYVIDVNGW SFVKDNNDYY DKCANILRDI FLEERRKCEG ISESSEPPSP
DMGSSSSRRS TTGSHRQALK TLLKSPSTSR LYGQSQKPTE ASESCTPSVA SSGVESTDIG
AALSKLNSRE AYSTSRGYSP SNTKSPALSV QHANDEALPP LPASKHSWKL KGMVAVIRHA
DRTPKQKFKF TFHSQPFVDL LKGHQNEIVI KGEAALSSVS DAVKLAMEKG LEDMEKLQLL
RTSLDKKGGW PGTKVQIKPM FRKRKPEEMG EQGPPEASAP LPESKPSEEP PAPVPNEGEG
LTPEDEDLRR SQTRSDSISG ATFSRFSAAE NDLILDKLQL VIKWGGEPTH AARYQSQDLG
LNMRDDLKLM NKEALNNVRI FTSSERRVST SAQIWACSFL DQKDIPEDLI QVRKDLLDDS
NAAKDVMDKV KKKLKLLLRE GSAPSQFAWP KDRNIPEPSV VLARVVELMK FHRSVMRHNF
EKLDSAPHIF QTPSNDPETQ SQPPPVDPDI SSIQGRWCAG EDPRLFKERW EKLFAEFCDT
EKVDPSKLSE LYDSMKFDAL HNRQFLEWVF MPQDSPRDSV EEQKSKSAAK VDTIAEGKPG
QEAVNDKSEE RTESQTFAHR FGLKKRNLAL ESLPHLRALD DSYDHYFKLF PGSQSSKCKM
DERLSQLREL YKLAKVLFDY VTPQEYGITD SEKLEIGLLT SLPLLQEIVR DLEEVQASQD
AKSFFYFTKE SHIYTLLNCI LEGGIQTKIA RSAIPELDYL SQICFELYEA RDSESDSYSY
SIRISVSPGC HAFDPLDVQL DSRHSIGCTP RRSLTAHQDW KEVIETLKAK FNTVELPKTF
IAVNLSDKHS HGENSSSPPR GISPAQD
//
