PPSP2_ARATH
ID PPSP2_ARATH Reviewed; 279 AA.
AC Q9FZ62; A8MQ90;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Inorganic pyrophosphatase 2;
DE Short=AtPPsPase2;
DE Short=PPi phosphatase 2;
DE Short=Pyrophosphate-specific phosphatase 2;
DE EC=3.6.1.1;
GN OrderedLocusNames=At1g17710; ORFNames=F11A6.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific cleavage of pyrophosphate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Tetramer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FZ62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FZ62-2; Sequence=VSP_040549;
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC034257; AAF99814.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29624.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29625.1; -; Genomic_DNA.
DR EMBL; BT015372; AAU05495.1; -; mRNA.
DR EMBL; BT015670; AAU15169.1; -; mRNA.
DR PIR; A86312; A86312.
DR RefSeq; NP_001077556.1; NM_001084087.1. [Q9FZ62-2]
DR RefSeq; NP_173213.2; NM_101633.4. [Q9FZ62-1]
DR AlphaFoldDB; Q9FZ62; -.
DR SMR; Q9FZ62; -.
DR STRING; 3702.AT1G17710.1; -.
DR PaxDb; Q9FZ62; -.
DR PRIDE; Q9FZ62; -.
DR ProteomicsDB; 226407; -. [Q9FZ62-1]
DR EnsemblPlants; AT1G17710.1; AT1G17710.1; AT1G17710. [Q9FZ62-1]
DR EnsemblPlants; AT1G17710.2; AT1G17710.2; AT1G17710. [Q9FZ62-2]
DR GeneID; 838347; -.
DR Gramene; AT1G17710.1; AT1G17710.1; AT1G17710. [Q9FZ62-1]
DR Gramene; AT1G17710.2; AT1G17710.2; AT1G17710. [Q9FZ62-2]
DR KEGG; ath:AT1G17710; -.
DR Araport; AT1G17710; -.
DR TAIR; locus:2007958; AT1G17710.
DR eggNOG; KOG3120; Eukaryota.
DR HOGENOM; CLU_068983_1_1_1; -.
DR InParanoid; Q9FZ62; -.
DR OMA; ICCEELA; -.
DR OrthoDB; 1454608at2759; -.
DR PhylomeDB; Q9FZ62; -.
DR BioCyc; ARA:AT1G17710-MON; -.
DR BRENDA; 3.1.3.75; 399.
DR PRO; PR:Q9FZ62; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ62; baseline and differential.
DR Genevisible; Q9FZ62; 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:0052731; F:phosphocholine phosphatase activity; IDA:TAIR.
DR GO; GO:0052732; F:phosphoethanolamine phosphatase activity; IDA:TAIR.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Inorganic pyrophosphatase 2"
FT /id="PRO_0000404257"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 14
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2..49
FT /note="AKNNNIVIVFDFDKTIIDVDSDNWVVDELGFTDLFNQLLPTMPWNSLM ->
FT FISHNTKSLFGFISKQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040549"
SQ SEQUENCE 279 AA; 31570 MW; 7AE316D0DAF7E0EE CRC64;
MAKNNNIVIV FDFDKTIIDV DSDNWVVDEL GFTDLFNQLL PTMPWNSLMN RMMKELHDHG
KTIEEIKQVL RRIPIHPRVI PAIKSAHALG CELRIVSDAN TLFIETIIEH LGIGEFFSEI
NTNPGLVDEQ GRLIVSPYHD FTKSSHGCSR CPPNMCKGLI IDRIQASLTK EGKTSKMIYL
GDGAGDYCPS LGLKAEDYMM PRKNFPVWDL ISQNPMLVKA TVRDWTDGED MERILMEIIN
EIMSSEEGEE NDKMLSSENC KISVGIVHEP IQVPLNLVK
