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Inositol-phosphate phosphatase (EC 3.1.3.25) (L-galactose 1-phosphate phosphatase) (EC 3.1.3.93) (Myo-inositol monophosphatase)

 VTC4_ARATH              Reviewed;         271 AA.
Q9M8S8; Q8LE95;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 108.
RecName: Full=Inositol-phosphate phosphatase;
EC=3.1.3.25 {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
AltName: Full=L-galactose 1-phosphate phosphatase;
EC=3.1.3.93 {ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:19339506};
AltName: Full=Myo-inositol monophosphatase;
Name=VTC4; Synonyms=IMP; OrderedLocusNames=At3g02870;
ORFNames=F13E7.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, ENZYME REGULATION, COFACTOR, AND CATALYTIC ACTIVITY.
PubMed=15550539; DOI=10.1073/pnas.0407453101;
Laing W.A., Bulley S., Wright M., Cooney J., Jensen D.,
Barraclough D., MacRae E.;
"A highly specific L-galactose-1-phosphate phosphatase on the path to
ascorbate biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 101:16976-16981(2004).
[6]
FUNCTION, MUTAGENESIS OF PRO-92, AND DISRUPTION PHENOTYPE.
PubMed=16595667; DOI=10.1074/jbc.M601409200;
Conklin P.L., Gatzek S., Wheeler G.L., Dowdle J., Raymond M.J.,
Rolinski S., Isupov M., Littlechild J.A., Smirnoff N.;
"Arabidopsis thaliana VTC4 encodes L-galactose-1-P phosphatase, a
plant ascorbic acid biosynthetic enzyme.";
J. Biol. Chem. 281:15662-15670(2006).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND DISRUPTION PHENOTYPE.
PubMed=19339506; DOI=10.1104/pp.108.135129;
Torabinejad J., Donahue J.L., Gunesekera B.N., Allen-Daniels M.J.,
Gillaspy G.E.;
"VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate
biosynthesis in plants.";
Plant Physiol. 150:951-961(2009).
[8]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=20960216; DOI=10.1007/s10265-010-0381-y;
Sato Y., Yazawa K., Yoshida S., Tamaoki M., Nakajima N., Iwai H.,
Ishii T., Satoh S.;
"Expression and functions of myo-inositol monophosphatase family genes
in seed development of Arabidopsis.";
J. Plant Res. 124:385-394(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Phosphatase acting on L-galactose 1-phosphate (L-Gal 1-
P), D-myoinositol 3-phosphate (D-Ins 3-P) and D-myoinositol 1-
phosphate (D-Ins 1-P). Can also use beta-glycerophosphate
(glycerol 2-P) and, to a lesser extent, D-galactose 1-phosphate
(D-Gal 1-P), alpha-D-glucose 1-phosphate (a-D-Glc 1-P), D-manitol
1-phosphate and adenosine 2'-monophosphate as substrates. No
activity with D-fructose 1-phosphate (D-Fru 1-P), fructose 1,6-
bisphosphate (Fru 1,6-bisP), D-glucose 6-phosphate (D-Glc 6-P), D-
alpha-glycerophosphate (glycerol 3-P), D-sorbitol 6-phosphate and
D-myoinositol 2-phosphate. The C1 phosphate position in a six-
member ring substrate is important for catalysis.
{ECO:0000269|PubMed:15550539, ECO:0000269|PubMed:16595667,
ECO:0000269|PubMed:19339506}.
-!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
+ phosphate. {ECO:0000269|PubMed:15550539,
ECO:0000269|PubMed:19339506}.
-!- CATALYTIC ACTIVITY: Beta-L-galactose 1-phosphate + H(2)O = L-
galactose + phosphate. {ECO:0000269|PubMed:15550539,
ECO:0000269|PubMed:19339506}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15550539};
-!- ENZYME REGULATION: Inhibited by LiCl or CaCl(2). Not inhibited by
ascorbate. {ECO:0000269|PubMed:15550539,
ECO:0000269|PubMed:19339506}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=191 uM for D-myoinositol 3-phosphate
{ECO:0000269|PubMed:19339506};
KM=107 uM for L-galactose 1-phosphate
{ECO:0000269|PubMed:19339506};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:19339506};
-!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
inositol from D-glucose 6-phosphate: step 2/2.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q9M8S8-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Strongly expressed in photosynthetic tissues.
Expressed in pistil and seed endosperm.
{ECO:0000269|PubMed:20960216}.
-!- DEVELOPMENTAL STAGE: Detected in globular to heart stage embryos.
{ECO:0000269|PubMed:20960216}.
-!- DISRUPTION PHENOTYPE: No visible phenotype, but reduced
myoinositol and ascorbate levels. {ECO:0000269|PubMed:16595667,
ECO:0000269|PubMed:19339506, ECO:0000269|PubMed:20960216}.
-!- SIMILARITY: Belongs to the inositol monophosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC018363; AAF26973.1; -; Genomic_DNA.
EMBL; CP002686; AEE73869.1; -; Genomic_DNA.
EMBL; AY085548; AAM62772.1; -; mRNA.
EMBL; AY035150; AAK59654.1; -; mRNA.
EMBL; AY063021; AAL34195.1; -; mRNA.
RefSeq; NP_186936.1; NM_111155.3. [Q9M8S8-1]
UniGene; At.21164; -.
ProteinModelPortal; Q9M8S8; -.
SMR; Q9M8S8; -.
STRING; 3702.AT3G02870.1; -.
PaxDb; Q9M8S8; -.
EnsemblPlants; AT3G02870.1; AT3G02870.1; AT3G02870. [Q9M8S8-1]
GeneID; 821206; -.
Gramene; AT3G02870.1; AT3G02870.1; AT3G02870.
KEGG; ath:AT3G02870; -.
Araport; AT3G02870; -.
TAIR; locus:2075392; AT3G02870.
eggNOG; KOG2951; Eukaryota.
eggNOG; COG0483; LUCA.
HOGENOM; HOG000282238; -.
InParanoid; Q9M8S8; -.
KO; K10047; -.
OMA; NNYAEFC; -.
OrthoDB; EOG09360J4S; -.
PhylomeDB; Q9M8S8; -.
BioCyc; MetaCyc:AT3G02870-MONOMER; -.
BRENDA; 3.1.3.25; 399.
BRENDA; 3.1.3.93; 399.
BRENDA; 3.1.3.B9; 399.
Reactome; R-ATH-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RK; Q9M8S8; -.
UniPathway; UPA00823; UER00788.
PRO; PR:Q9M8S8; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9M8S8; baseline and differential.
Genevisible; Q9M8S8; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:TAIR.
GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0010347; F:L-galactose-1-phosphate phosphatase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006021; P:inositol biosynthetic process; IMP:TAIR.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0009409; P:response to cold; IMP:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
CDD; cd01639; IMPase; 1.
InterPro; IPR033942; IMPase.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR020552; Inositol_monoPase_Li-sen.
InterPro; IPR000760; Inositol_monophosphatase-like.
InterPro; IPR020550; Inositol_monophosphatase_CS.
PANTHER; PTHR20854; PTHR20854; 1.
Pfam; PF00459; Inositol_P; 1.
PRINTS; PR00377; IMPHPHTASES.
PRINTS; PR00378; LIIMPHPHTASE.
PROSITE; PS00629; IMP_1; 1.
PROSITE; PS00630; IMP_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Hydrolase;
Lithium; Magnesium; Metal-binding; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 271 Inositol-phosphate phosphatase.
/FTId=PRO_0000383679.
REGION 93 96 Substrate binding. {ECO:0000250}.
REGION 194 196 Substrate binding. {ECO:0000250}.
METAL 71 71 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 2. {ECO:0000250}.
METAL 93 93 Magnesium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 94 94 Magnesium 2. {ECO:0000250}.
METAL 221 221 Magnesium 2. {ECO:0000250}.
BINDING 71 71 Substrate. {ECO:0000250}.
BINDING 213 213 Substrate. {ECO:0000250}.
BINDING 221 221 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 92 92 P->L: In vtc4-1; low levels of ascorbate.
{ECO:0000269|PubMed:16595667}.
CONFLICT 5 5 D -> H (in Ref. 3; AAM62772).
{ECO:0000305}.
CONFLICT 39 39 G -> S (in Ref. 3; AAM62772).
{ECO:0000305}.
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


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