ID A0A1G4MDA1_LACFM Unreviewed; 1111 AA.
AC A0A1G4MDA1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LAFE_0E08394G {ECO:0000313|EMBL:SCW01839.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW01839.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; LT598488; SCW01839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MDA1; -.
DR STRING; 4955.A0A1G4MDA1; -.
DR OMA; IQERWCC; -.
DR OrthoDB; 5476261at2759; -.
DR Proteomes; UP000190831; Chromosome e.
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 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; 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:UP000190831};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365032}.
FT DOMAIN 176..264
FT /note="VIP1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18086"
FT DOMAIN 383..477
FT /note="ATP-grasp fold RimK-type"
FT /evidence="ECO:0000259|Pfam:PF08443"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 125934 MW; AE5E418054B0E0A8 CRC64;
MAGNEQAEPQ QGSMSPLTLN SKTKKVMESI APILEGFTPK TSSSENTSLK LPPPGVPQDS
QVDDNNSEDN ALDRTLSITS QHSNASSRPA LSPSNSYENS MGSKIQRLKS NPASTQVSSS
PAGSYSGSPF LSEQNLDDVV ADVVNETPSS STASSAGSSR KPSTSNNKPQ LPKIGKIGVC
AMDAKVLSKP CRHILNRLIE HGEFETIIFG DKVILDENIE NWPTCDFLIS FFSSGFPLNK
AIDYVNLRKP FIINDLVMQK VLWDRRICLQ LLDGAKIPTP PRLEISRDGG PRVDVQLRAK
LLERNVVIKP IKEPKWRMID DDTLEVQGKV MTKPYVEKPV DGEDHNIYIY YHSKNGGGGR
RLFRKVGNKS SEFDPTLNYP RTEGSYIYEE FMDTDNFEDV KAYTVGEKFC HAETRKSPVV
DGIVRRNTHG KEIRYVTELS VEEKEIAKRV SNAFSQMICG FDLLRVNGKS YVIDVNGFSF
VKDNSSYYDS CARILRETFI AAKRKMDLEK RNLPVIKEEK TQKWVFKGLV TVIRHADRTP
KQKFKHSFRS PIFISLLKGH KEEVVIRNVS DLKVVLQALK IAQEENTEDP VKLDVLANAL
EKKLNFPGTK IQLKPVLNSE KDVEKVQFIL KWGGEPTHSA RYQAMELGEQ MRQDFDLLNK
NILQNIKIFS SSERRVLASA QIWAMALFGA DELGSDEISI RKDLLDDSNA AKDLMDKVKK
KLKPLLREGK EAPPQFAWPA KMPEPYLVIK RVVELMNYHK QIMDYNFKSK NVDDMQRRWC
CGEDPMLFKE RWDKLFKEFV SVEKVDPSKI SELYDTMKYD ALHNRQFLEN IFAPDFTTEL
ENVDVCKNSL VDRYPINILA MNNFKIPDSS ASTSNNGSSK GSSVGSLGWV LESSAKTPRS
STSSQFDDPK FMRLRELFRL SKVLFDFICP QEYGIEDGEK LDIGLLTSLP LAKQILNDID
DMKSKDTPAC TAYFTKESHI YTLLNIIYES GLPMRIARNA LPELDYLSQI NFELYESTDA
SGQKSHSIRL KMSPGCHTQD PLDVQLDEKH YISCIPKISL TRHLDMDYVS QKLRNKFSRV
ILPQKFTPVN ITSPNLSFRK PSLPEPKTEK E
//
