TTM3_ARATH
ID TTM3_ARATH Reviewed; 210 AA.
AC Q9SIY3; B9DG04;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Triphosphate tunnel metalloenzyme 3;
DE AltName: Full=Adenosinetriphosphatase;
DE Short=ATPase;
DE EC=3.6.1.-;
DE AltName: Full=Triphosphatase;
DE Short=PPPase;
DE EC=3.6.1.25;
GN Name=TTM3; OrderedLocusNames=At2g11890; ORFNames=F23M2.5;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY REGULATION, MUTAGENESIS
RP OF GLU-2; ARG-52; GLU-154 AND GLU-171, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24004165; DOI=10.1111/tpj.12325;
RA Moeder W., Garcia-Petit C., Ung H., Fucile G., Samuel M.A., Christendat D.,
RA Yoshioka K.;
RT "Crystal structure and biochemical analyses reveal that the Arabidopsis
RT triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved
RT in root development.";
RL Plant J. 76:615-626(2013).
CC -!- FUNCTION: Involved in the hydrolysis of the beta-gamma-phosphoanhydride
CC linkage of triphosphate-containing substrates (inorganic or nucleoside-
CC linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi),
CC however it does not display significant activity towards long-chain
CC polyphosphates. The existence of PPPi in living cells is still unclear,
CC and PPPase activity might be the ancestral function of CYTH domain. It
CC also has gamma-phosphatase activity on NTP substrates, but no adenylate
CC cyclase or RNA triphosphatase activity. {ECO:0000269|PubMed:24004165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + triphosphate = diphosphate + phosphate;
CC Xref=Rhea:RHEA:14157, ChEBI:CHEBI:15377, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.25;
CC Evidence={ECO:0000269|PubMed:24004165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24004165};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24004165};
CC Note=PPPase is active in the presence of Mg(2+) ions, while no activity
CC is observed in the presence of manganese ions.
CC {ECO:0000269|PubMed:24004165};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24004165};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24004165};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:24004165};
CC Note=ATPase occurs in the presence of Mg(2+) ions as well as Mn(2+) and
CC Co(2+) ions. {ECO:0000269|PubMed:24004165};
CC -!- ACTIVITY REGULATION: Inhibited by 2.5 mM Ca(2+).
CC {ECO:0000269|PubMed:24004165}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.08 mM for ATP {ECO:0000269|PubMed:24004165};
CC KM=42.9 uM for triphosphate {ECO:0000269|PubMed:24004165};
CC pH dependence:
CC Optimum pH is 9.5 (in the presence of Mg(2+)). No activity at pH 7.5.
CC {ECO:0000269|PubMed:24004165};
CC Temperature dependence:
CC Optimum temperature is 45.50 degrees Celsius.
CC {ECO:0000269|PubMed:24004165};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24004165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIY3-2; Sequence=VSP_053969;
CC -!- TISSUE SPECIFICITY: Expressed only in the proximal meristematic zone of
CC the root. {ECO:0000269|PubMed:24004165}.
CC -!- DISRUPTION PHENOTYPE: Delayed root growth and reduced length and number
CC of lateral roots. {ECO:0000269|PubMed:24004165}.
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DR EMBL; AC007045; AAD22501.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06186.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06187.1; -; Genomic_DNA.
DR EMBL; AY045689; AAK74047.1; -; mRNA.
DR EMBL; AY055788; AAL06955.1; -; mRNA.
DR EMBL; AK316974; BAH19671.1; -; mRNA.
DR EMBL; AY088524; AAM66058.1; -; mRNA.
DR EMBL; AK229646; BAF01490.1; -; mRNA.
DR PIR; E84499; E84499.
DR RefSeq; NP_001031347.1; NM_001036270.1. [Q9SIY3-2]
DR RefSeq; NP_565353.1; NM_126867.2. [Q9SIY3-1]
DR PDB; 3V85; X-ray; 1.90 A; A=1-210.
DR PDB; 5A5Y; X-ray; 1.92 A; A/B=1-210.
DR PDB; 5A66; X-ray; 2.05 A; A/B=1-210.
DR PDB; 5A67; X-ray; 1.30 A; A=1-210.
DR PDB; 5A68; X-ray; 1.67 A; A=1-210.
DR PDBsum; 3V85; -.
DR PDBsum; 5A5Y; -.
DR PDBsum; 5A66; -.
DR PDBsum; 5A67; -.
DR PDBsum; 5A68; -.
DR AlphaFoldDB; Q9SIY3; -.
DR SMR; Q9SIY3; -.
DR STRING; 3702.AT2G11890.1; -.
DR iPTMnet; Q9SIY3; -.
DR PaxDb; Q9SIY3; -.
DR PRIDE; Q9SIY3; -.
DR ProteomicsDB; 232366; -. [Q9SIY3-1]
DR EnsemblPlants; AT2G11890.1; AT2G11890.1; AT2G11890. [Q9SIY3-1]
DR EnsemblPlants; AT2G11890.2; AT2G11890.2; AT2G11890. [Q9SIY3-2]
DR GeneID; 815664; -.
DR Gramene; AT2G11890.1; AT2G11890.1; AT2G11890. [Q9SIY3-1]
DR Gramene; AT2G11890.2; AT2G11890.2; AT2G11890. [Q9SIY3-2]
DR KEGG; ath:AT2G11890; -.
DR Araport; AT2G11890; -.
DR TAIR; locus:2045879; AT2G11890.
DR eggNOG; ENOG502QUVI; Eukaryota.
DR InParanoid; Q9SIY3; -.
DR OMA; EMGFVCL; -.
DR PhylomeDB; Q9SIY3; -.
DR PRO; PR:Q9SIY3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIY3; baseline and differential.
DR Genevisible; Q9SIY3; AT.
DR GO; GO:0005680; C:anaphase-promoting complex; IPI:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0050355; F:triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR023577; CYTH_domain.
DR InterPro; IPR033245; TTM3.
DR PANTHER; PTHR34948:SF6; PTHR34948:SF6; 1.
DR Pfam; PF01928; CYTH; 1.
DR SMART; SM01118; CYTH; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51707; CYTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..210
FT /note="Triphosphate tunnel metalloenzyme 3"
FT /id="PRO_0000426737"
FT DOMAIN 1..208
FT /note="CYTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT VAR_SEQ 100..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_053969"
FT MUTAGEN 2
FT /note="E->A: Loss of 98.9% of the ATPase activity and 97.3%
FT of the tripolyphosphatase activity."
FT /evidence="ECO:0000269|PubMed:24004165"
FT MUTAGEN 52
FT /note="R->A: Loss of 96.7% of the ATPase activity and 98.8%
FT of the tripolyphosphatase activity."
FT /evidence="ECO:0000269|PubMed:24004165"
FT MUTAGEN 154
FT /note="E->A: Loss of 98.2% of the ATPase activity and 72.7%
FT of the tripolyphosphatase activity."
FT /evidence="ECO:0000269|PubMed:24004165"
FT MUTAGEN 171
FT /note="E->A: Total loss of ATPase activity and 92.5% of the
FT tripolyphosphatase activity."
FT /evidence="ECO:0000269|PubMed:24004165"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 26..38
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5A5Y"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 134..148
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:5A67"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5A67"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:5A67"
SQ SEQUENCE 210 AA; 24163 MW; 56E70B8055143A33 CRC64;
MEVEVKLRLL TAAAHLRLTT LLTPYHLKTL HQRNTFFDTP KNDLSLRRAV LRLRFLQNAA
VSAASPSPPR CIVSLKAKPT LANGISRVEE DEEEIEYWIG KECVESPAKL SDIGSRVLKR
VKEEYGFNDF LGFVCLGGFE NVRNVYEWRG VKLEVDETKY DFGNCYEIEC ETEEPERVKT
MIEEFLTEEK IEFSNSDMTK FAVFRSGKLP
