PPSP3_ARATH
ID PPSP3_ARATH Reviewed; 245 AA.
AC Q9SU92;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Thiamine phosphate phosphatase-like protein {ECO:0000303|PubMed:26537753};
DE EC=3.1.3.100 {ECO:0000269|PubMed:26537753};
GN OrderedLocusNames=At4g29530 {ECO:0000312|Araport:AT4G29530};
GN ORFNames=T16L4.40 {ECO:0000312|EMBL:CAB45313.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=26537753; DOI=10.1042/bj20150805;
RA Hasnain G., Roje S., Sa N., Zallot R., Ziemak M.J., de Crecy-Lagard V.,
RA Gregory J.F. III, Hanson A.D.;
RT "Bacterial and plant HAD enzymes catalyse a missing phosphatase step in
RT thiamin diphosphate biosynthesis.";
RL Biochem. J. 473:157-166(2016).
RN [6]
RP FUNCTION.
RX PubMed=27677881; DOI=10.1105/tpc.16.00600;
RA Mimura M., Zallot R., Niehaus T.D., Hasnain G., Gidda S.K., Nguyen T.N.,
RA Anderson E.M., Mullen R.T., Brown G., Yakunin A.F., de Crecy-Lagard V.,
RA Gregory J.F., McCarty D.R., Hanson A.D.;
RT "Arabidopsis TH2 encodes the orphan enzyme thiamin monophosphate
RT phosphatase.";
RL Plant Cell 28:2683-2696(2016).
CC -!- FUNCTION: HAD-like hydrolase that has a thiamine monophosphate
CC phosphatase activity in a heterologous system (PubMed:26537753). Does
CC not contribute to thiamine monophosphate phosphatase activity in planta
CC (PubMed:27677881). {ECO:0000269|PubMed:26537753,
CC ECO:0000269|PubMed:27677881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + thiamine phosphate = phosphate + thiamine;
CC Xref=Rhea:RHEA:47948, ChEBI:CHEBI:15377, ChEBI:CHEBI:18385,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:43474; EC=3.1.3.100;
CC Evidence={ECO:0000269|PubMed:26537753};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O33194};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 mM for thiamine monophosphate {ECO:0000269|PubMed:26537753};
CC Note=kcat is 29.9 sec(-1) for thiamine monophosphate.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26537753}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:26537753}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL079344; CAB45313.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79711.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85640.1; -; Genomic_DNA.
DR EMBL; BT006155; AAP04140.1; -; mRNA.
DR EMBL; BT008523; AAP40350.1; -; mRNA.
DR EMBL; AK229519; BAF01374.1; -; mRNA.
DR PIR; T09916; T09916.
DR RefSeq; NP_194682.1; NM_119098.3.
DR AlphaFoldDB; Q9SU92; -.
DR SMR; Q9SU92; -.
DR STRING; 3702.AT4G29530.1; -.
DR PaxDb; Q9SU92; -.
DR PRIDE; Q9SU92; -.
DR ProteomicsDB; 225982; -.
DR DNASU; 829074; -.
DR EnsemblPlants; AT4G29530.1; AT4G29530.1; AT4G29530.
DR GeneID; 829074; -.
DR Gramene; AT4G29530.1; AT4G29530.1; AT4G29530.
DR KEGG; ath:AT4G29530; -.
DR Araport; AT4G29530; -.
DR TAIR; locus:2134353; AT4G29530.
DR eggNOG; KOG3120; Eukaryota.
DR HOGENOM; CLU_068983_1_1_1; -.
DR InParanoid; Q9SU92; -.
DR OMA; HNLADCF; -.
DR OrthoDB; 1454608at2759; -.
DR PhylomeDB; Q9SU92; -.
DR BioCyc; ARA:AT4G29530-MON; -.
DR BioCyc; MetaCyc:AT4G29530-MON; -.
DR PRO; PR:Q9SU92; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU92; baseline and differential.
DR Genevisible; Q9SU92; AT.
DR GO; GO:0004427; F:inorganic diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0052732; F:phosphoethanolamine phosphatase activity; IDA:TAIR.
DR GO; GO:0042131; F:thiamine phosphate phosphatase activity; IDA:TAIR.
DR GO; GO:0006580; P:ethanolamine metabolic process; IDA:TAIR.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IDA:TAIR.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR PANTHER; PTHR20889; PTHR20889; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..245
FT /note="Thiamine phosphate phosphatase-like protein"
FT /id="PRO_0000404258"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O33194"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O33194"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O33194"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O33194"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O33194"
SQ SEQUENCE 245 AA; 28053 MW; E6A045C236816870 CRC64;
MAKIVILFDF DRTLIDGDSD NWVVTEMGLT EIFHQLRFTL PWNRLMDRMM MELQSQGRSI
DDIKSCLKKM PIDSHIIEAI KSAKSSGCDL KIVSDANQFF IEKILEHHDL VDCFSEIYTN
PTSLDDNGNL RILPYHSDAL PPHSCNLCPS NLCKGLVMDH LRASSSNDQI PRRFIYLGDG
GGDFCPTLKL RECDFVMPRT NYPLWKKISD NPLLIKAEVK EWSSAEEQQR ILLQLVSTIT
KEEDS
