Reviewed, UniProtKB/Swiss-Prot Q9LXC9 (IPYR1_ARATH)

Names and origin

Protein names

Recommended name:
    Soluble inorganic pyrophosphatase 1, chloroplastic
    EC=3.6.1.1
Alternative name(s):
    Pyrophosphate phospho-hydrolase 1
      Short name=PPase 1
    Inorganic pyrophosphatase 1

Gene names

Name:	PPA1
Synonyms:	PPA
Ordered Locus Names:	At5g09650
ORF Names:	F17I14_160

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Diphosphate + H2O = 2 phosphate. Ref.1 Ref.2
Cofactor	Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity. UniProtKB P00817
Enzyme regulation	Inhibited by NaF. Ref.1
Subcellular location	Plastid › chloroplast stroma Ref.1.
Tissue specificity	Expressed in all tissues tested. Highest expression in flowers, leaves and roots. Lower levels of expression in siliques and stems. Ref.1
Induction	By glucose, frustose or sucrose at 300 mM, but not at 100 mM. Ref.1
Sequence similarities	Belongs to the PPase family.
Biophysicochemical properties	Kinetic parameters: KM=0.6 mM for PPi Ref.1 pH dependence: Optimum pH is 7.5. Activity is extremely low below pH 6.5. Activity decreases slightly at more basic pHs, activity at pH 9.0 was only 10% less than that found at pH 7.5. Ref.1

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from expression pattern. Source: TAIR phosphate metabolic process Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Ref.1 Inferred from direct assay. Source: TAIR thylakoid Inferred from direct assay. Source: TAIR
Molecular function	inorganic diphosphatase activity Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 300		Soluble inorganic pyrophosphatase 1, chloroplastic		PRO_0000253937
Sites
	Metal binding	173	1	Magnesium 1 By similarity UniProtKB P00817
	Metal binding	178	1	Magnesium 1 By similarity UniProtKB P00817
	Metal binding	178	1	Magnesium 2 By similarity UniProtKB P00817
	Metal binding	210	1	Magnesium 1 By similarity UniProtKB P00817
	Binding site	140	1	Inorganic pyrophosphate By similarity UniProtKB P00817
Experimental info
	Sequence conflict	194	1	K → N in AAM64828. Ref.6
	Sequence conflict	270	1	K → R in AAM64828. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9LXC9-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E5EDA94D56EDD3C4	FASTA	300	33,380
	10 20 30 40 50 60 MAATRVLTAA TAVTQTTSCF LAKQAFTLPA KKSCGGFGGL CFSRRALVLK SKRPFSCSAI 70 80 90 100 110 120 YNPQVKVQEE GPAESLDYRV FFLDGSGKKV SPWHDIPLTL GDGVFNFIVE IPKESKAKME 130 140 150 160 170 180 VATDEDFTPI KQDTKKGKLR YYPYNINWNY GLLPQTWEDP SHANSEVEGC FGDNDPVDVV 190 200 210 220 230 240 EIGETQRKIG DILKIKPLAA LAMIDEGELD WKIVAISLDD PKAHLVNDVE DVEKHFPGTL 250 260 270 280 290 300 TAIRDWFRDY KIPDGKPANR FGLGDKPANK DYALKIIQET NESWAKLVKR SVDAGDLSLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of an Arabidopsis inorganic pyrophosphatase capable of being imported into chloroplasts." Schulze S., Mant A., Kossmann J., Lloyd J.R. FEBS Lett. 565:101-105(2004) [PubMed: 15135060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[2]	"A novel subfamily of monomeric inorganic pyrophosphatases in photosynthetic eukaryotes." Gomez-Garcia M.R., Losada M., Serrano A. Biochem. J. 395:211-221(2006) [PubMed: 16313235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY. Strain: cv. Columbia. Tissue: Leaf.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S. DNA Res. 6:183-195(1999) [PubMed: 10470850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY551439 mRNA. Translation: AAS57950.1. AJ252210 mRNA. Translation: CAC19853.1. AB020752 Genomic DNA. Translation: BAB09520.1. AL353994 Genomic DNA. Translation: CAB89365.1. AY045945 mRNA. Translation: AAK76619.1. AY079355 mRNA. Translation: AAL85086.1. AY087275 mRNA. Translation: AAM64828.1.
IPI	IPI00524195.
PIR	T49933.
RefSeq	NP_196527.1.
UniGene	At.1794 At.21648 Rra.2316 Rsa.25496 Rsa.3119
3D structure databases
HSSP	HSSP built from PDB template 1WGI based on UniProtKB P00817.
SMR	Q9LXC9. Positions 66-299.
ModBase	Search...
Proteomic databases
PRIDE	Q9LXC9.
ProMEX	Q9LXC9.
Genome annotation databases
GeneID	830824.
GenomeReviews	Gene locus AT5G09650 in contig BA000015_GR.
KEGG	ath:AT5G09650.
NMPDR	fig|3702.1.peg.23086.
Organism-specific databases
TAIR	At5g09650.
Phylogenomic databases
eggNOG	KOG1626.
HOGENOM	HBG434750.
InParanoid	Q9LXC9.
OMA	WFFISGS.
PhylomeDB	Q9LXC9.
Enzyme and pathway databases
BRENDA	3.6.1.1. 302.
Gene expression databases
ArrayExpress	Q9LXC9.
Genevestigator	Q9LXC9.
GermOnline	AT5G09650. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008162. Pyrophosphatase. [Graphical view]
Gene3D	G3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
PANTHER	PTHR10286. Pyrophosphatase. 1 hit.
Pfam	PF00719. Pyrophosphatase. 1 hit. [Graphical view]
PROSITE	PS00387. PPASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IPYR1_ARATH

Accession

Primary (citable) accession number: Q9LXC9
Secondary accession number(s): Q8LBD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)