PPSP1_ARATH
ID PPSP1_ARATH Reviewed; 295 AA.
AC Q67YC0; Q8LDK9; Q9SSM6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Inorganic pyrophosphatase 1;
DE Short=AtPPsPase1;
DE Short=PPi phosphatase 1;
DE Short=Pyrophosphate-specific phosphatase 1;
DE EC=3.6.1.1;
DE AltName: Full=Protein PHOSPHATE STARVATION-INDUCED GENE 2;
DE Short=AtPS2;
GN Name=PS2; OrderedLocusNames=At1g73010; ORFNames=F3N23.21;
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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP INDUCTION BY PHOSPHATE STARVATION.
RX PubMed=15894620; DOI=10.1073/pnas.0500778102;
RA Miura K., Rus A., Sharkhuu A., Yokoi S., Karthikeyan A.S., Raghothama K.G.,
RA Baek D., Koo Y.D., Jin J.B., Bressan R.A., Yun D.-J., Hasegawa P.M.;
RT "The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7760-7765(2005).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT,
RP INDUCTION BY PHOSPHATE STARVATION, COFACTOR, AND MUTAGENESIS OF ASP-19.
RC STRAIN=cv. Columbia;
RX PubMed=21122813; DOI=10.1016/j.bbagen.2010.11.006;
RA May A., Berger S., Hertel T., Kock M.;
RT "The Arabidopsis thaliana phosphate starvation responsive gene AtPPsPase1
RT encodes a novel type of inorganic pyrophosphatase.";
RL Biochim. Biophys. Acta 1810:178-185(2011).
CC -!- FUNCTION: Catalyzes the specific cleavage of pyrophosphate.
CC {ECO:0000269|PubMed:21122813}.
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 Evidence={ECO:0000269|PubMed:21122813};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21122813};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:21122813};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:21122813};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21122813};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21122813};
CC Note=Magnesium. Can also use iron, nickel, cobalt and manganese, but
CC not zinc ions. {ECO:0000269|PubMed:21122813};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.8 uM for pyrophosphate PPi (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:21122813};
CC Vmax=0.3 nmol/min/ug enzyme with PPi as substrate (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:21122813};
CC pH dependence:
CC Optimum pH is 8-8.5. {ECO:0000269|PubMed:21122813};
CC -!- SUBUNIT: Tetramer. {ECO:0000269|PubMed:21122813}.
CC -!- INDUCTION: Strongly induced upon phosphate (Pi) starvation.
CC {ECO:0000269|PubMed:15894620, ECO:0000269|PubMed:21122813}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55648.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008017; AAD55648.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35403.1; -; Genomic_DNA.
DR EMBL; AK176548; BAD44311.1; -; mRNA.
DR EMBL; BT030334; ABO38747.1; -; mRNA.
DR EMBL; AY085944; AAM63155.1; -; mRNA.
DR PIR; E96755; E96755.
DR RefSeq; NP_565052.1; NM_105959.3.
DR AlphaFoldDB; Q67YC0; -.
DR SMR; Q67YC0; -.
DR STRING; 3702.AT1G73010.1; -.
DR PaxDb; Q67YC0; -.
DR PRIDE; Q67YC0; -.
DR ProteomicsDB; 226293; -.
DR DNASU; 843632; -.
DR EnsemblPlants; AT1G73010.1; AT1G73010.1; AT1G73010.
DR GeneID; 843632; -.
DR Gramene; AT1G73010.1; AT1G73010.1; AT1G73010.
DR KEGG; ath:AT1G73010; -.
DR Araport; AT1G73010; -.
DR TAIR; locus:2032748; AT1G73010.
DR eggNOG; KOG3120; Eukaryota.
DR HOGENOM; CLU_068983_1_1_1; -.
DR InParanoid; Q67YC0; -.
DR OMA; RPFHSHE; -.
DR OrthoDB; 1454608at2759; -.
DR PhylomeDB; Q67YC0; -.
DR BioCyc; ARA:AT1G73010-MON; -.
DR BRENDA; 3.6.1.1; 399.
DR PRO; PR:Q67YC0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q67YC0; baseline and differential.
DR Genevisible; Q67YC0; AT.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA: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:0016462; F:pyrophosphatase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA: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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..295
FT /note="Inorganic pyrophosphatase 1"
FT /id="PRO_0000404256"
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 21
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 19
FT /note="D->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21122813"
FT CONFLICT 7..8
FT /note="Missing (in Ref. 5; AAM63155)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="A -> V (in Ref. 5; AAM63155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33515 MW; 3B353D382597E74E CRC64;
MAYNSNSNNN NNNIVVVFDF DKTIIDVDSD NWVIDELGFT DLFNQLLPTM PWNTLMDRMM
KELHDQGKTI EEIKQVLRTI PIHPRVVPAI KSAHDLGCEL RIVSDANMFF IETIVEHLGI
SELFSEINSN PGYVDERGTL KISPYHDFTK SPHSCSCGTC PPNMCKGLII ERIQQSLAKE
GKKKMIYLGD GAGDYCPSLK LNTEDYVMPR KNFPVWDLIS QNPMLIKAAI REWTDGQSME
MILIGTIEEI RLEEEKEKML TSAENNCKMQ TISIGINNVH HEPILPRALR VSQSS
