VTC4_ARATH
ID VTC4_ARATH Reviewed; 271 AA.
AC Q9M8S8; Q8LE95;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Inositol-phosphate phosphatase;
DE EC=3.1.3.25 {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
DE AltName: Full=L-galactose 1-phosphate phosphatase;
DE EC=3.1.3.93 {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
DE AltName: Full=Myo-inositol monophosphatase;
GN Name=VTC4; Synonyms=IMP; OrderedLocusNames=At3g02870; ORFNames=F13E7.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=15550539; DOI=10.1073/pnas.0407453101;
RA Laing W.A., Bulley S., Wright M., Cooney J., Jensen D., Barraclough D.,
RA MacRae E.;
RT "A highly specific L-galactose-1-phosphate phosphatase on the path to
RT ascorbate biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16976-16981(2004).
RN [6]
RP FUNCTION, MUTAGENESIS OF PRO-92, AND DISRUPTION PHENOTYPE.
RX PubMed=16595667; DOI=10.1074/jbc.m601409200;
RA Conklin P.L., Gatzek S., Wheeler G.L., Dowdle J., Raymond M.J.,
RA Rolinski S., Isupov M., Littlechild J.A., Smirnoff N.;
RT "Arabidopsis thaliana VTC4 encodes L-galactose-1-P phosphatase, a plant
RT ascorbic acid biosynthetic enzyme.";
RL J. Biol. Chem. 281:15662-15670(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=19339506; DOI=10.1104/pp.108.135129;
RA Torabinejad J., Donahue J.L., Gunesekera B.N., Allen-Daniels M.J.,
RA Gillaspy G.E.;
RT "VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate
RT biosynthesis in plants.";
RL Plant Physiol. 150:951-961(2009).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20960216; DOI=10.1007/s10265-010-0381-y;
RA Sato Y., Yazawa K., Yoshida S., Tamaoki M., Nakajima N., Iwai H., Ishii T.,
RA Satoh S.;
RT "Expression and functions of myo-inositol monophosphatase family genes in
RT seed development of Arabidopsis.";
RL J. Plant Res. 124:385-394(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Phosphatase acting on L-galactose 1-phosphate (L-Gal 1-P), D-
CC myoinositol 3-phosphate (D-Ins 3-P) and D-myoinositol 1-phosphate (D-
CC Ins 1-P). Can also use beta-glycerophosphate (glycerol 2-P) and, to a
CC lesser extent, D-galactose 1-phosphate (D-Gal 1-P), alpha-D-glucose 1-
CC phosphate (a-D-Glc 1-P), D-mannitol 1-phosphate and adenosine 2'-
CC monophosphate as substrates. No activity with D-fructose 1-phosphate
CC (D-Fru 1-P), fructose 1,6-bisphosphate (Fru 1,6-bisP), D-glucose 6-
CC phosphate (D-Glc 6-P), D-alpha-glycerophosphate (glycerol 3-P), D-
CC sorbitol 6-phosphate and D-myoinositol 2-phosphate. The C1 phosphate
CC position in a six-member ring substrate is important for catalysis.
CC {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:16595667,
CC ECO:0000269|PubMed:19339506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-L-galactose 1-phosphate + H2O = L-galactose + phosphate;
CC Xref=Rhea:RHEA:26349, ChEBI:CHEBI:15377, ChEBI:CHEBI:37619,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:75522; EC=3.1.3.93;
CC Evidence={ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15550539};
CC -!- ACTIVITY REGULATION: Inhibited by LiCl or CaCl(2). Not inhibited by
CC ascorbate. {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=191 uM for D-myoinositol 3-phosphate
CC {ECO:0000269|PubMed:19339506};
CC KM=107 uM for L-galactose 1-phosphate {ECO:0000269|PubMed:19339506};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19339506};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M8S8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Strongly expressed in photosynthetic tissues.
CC Expressed in pistil and seed endosperm. {ECO:0000269|PubMed:20960216}.
CC -!- DEVELOPMENTAL STAGE: Detected in globular to heart stage embryos.
CC {ECO:0000269|PubMed:20960216}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced myoinositol and
CC ascorbate levels. {ECO:0000269|PubMed:16595667,
CC ECO:0000269|PubMed:19339506, ECO:0000269|PubMed:20960216}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AC018363; AAF26973.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73869.1; -; Genomic_DNA.
DR EMBL; AY085548; AAM62772.1; -; mRNA.
DR EMBL; AY035150; AAK59654.1; -; mRNA.
DR EMBL; AY063021; AAL34195.1; -; mRNA.
DR RefSeq; NP_186936.1; NM_111155.3. [Q9M8S8-1]
DR AlphaFoldDB; Q9M8S8; -.
DR SMR; Q9M8S8; -.
DR BioGRID; 6539; 7.
DR STRING; 3702.AT3G02870.1; -.
DR iPTMnet; Q9M8S8; -.
DR PaxDb; Q9M8S8; -.
DR PRIDE; Q9M8S8; -.
DR ProteomicsDB; 242634; -. [Q9M8S8-1]
DR EnsemblPlants; AT3G02870.1; AT3G02870.1; AT3G02870. [Q9M8S8-1]
DR GeneID; 821206; -.
DR Gramene; AT3G02870.1; AT3G02870.1; AT3G02870. [Q9M8S8-1]
DR KEGG; ath:AT3G02870; -.
DR Araport; AT3G02870; -.
DR TAIR; locus:2075392; AT3G02870.
DR eggNOG; KOG2951; Eukaryota.
DR InParanoid; Q9M8S8; -.
DR OMA; RVDGYWE; -.
DR PhylomeDB; Q9M8S8; -.
DR BioCyc; ARA:AT3G02870-MON; -.
DR BioCyc; MetaCyc:AT3G02870-MON; -.
DR BRENDA; 3.1.3.25; 399.
DR BRENDA; 3.1.3.93; 399.
DR BRENDA; 3.1.3.B9; 399.
DR SABIO-RK; Q9M8S8; -.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q9M8S8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8S8; baseline and differential.
DR Genevisible; Q9M8S8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:TAIR.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0010347; F:L-galactose-1-phosphate phosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IMP:TAIR.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR00378; LIIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrolase; Lithium; Magnesium;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..271
FT /note="Inositol-phosphate phosphatase"
FT /id="PRO_0000383679"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 92
FT /note="P->L: In vtc4-1; low levels of ascorbate."
FT /evidence="ECO:0000269|PubMed:16595667"
FT CONFLICT 5
FT /note="D -> H (in Ref. 3; AAM62772)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="G -> S (in Ref. 3; AAM62772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29121 MW; 278584BF541B8F5F CRC64;
MADNDSLDQF LAAAIDAAKK AGQIIRKGFY ETKHVEHKGQ VDLVTETDKG CEELVFNHLK
QLFPNHKFIG EETTAAFGVT ELTDEPTWIV DPLDGTTNFV HGFPFVCVSI GLTIGKVPVV
GVVYNPIMEE LFTGVQGKGA FLNGKRIKVS AQSELLTALL VTEAGTKRDK ATLDDTTNRI
NSLLTKVRSL RMSGSCALDL CGVACGRVDI FYELGFGGPW DIAAGIVIVK EAGGLIFDPS
GKDLDITSQR IAASNASLKE LFAEALRLTG A
