Reviewed, UniProtKB/Swiss-Prot O82796 (SERB_ARATH)

Names and origin

Protein names

Recommended name:
    Phosphoserine phosphatase, chloroplastic
      Short name=PSPase
      Short name=PSP
    EC=3.1.3.3
Alternative name(s):
    O-phosphoserine phosphohydrolase

Gene names

Name:	PSP
Ordered Locus Names:	At1g18640
ORF Names:	F26I16.2

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	295 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)

Function	Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. May be required preferentially for serine biosynthesis in non-photosynthetic tissues. Ref.1
Catalytic activity	O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.
Cofactor	Magnesium.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
Subcellular location	Plastid › chloroplast. Ref.1
Tissue specificity	Expressed in leaf and root.
Sequence similarities	Belongs to the serB family.
Biophysicochemical properties	Kinetic parameters: Approximately 60% inhibition of PSP activity by 10 mM serine was observed. KM=3.5 mM for 3-phosphoserine (at 30 degrees Celsius and pH 7.5)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Ref.1 Traceable author statement. Source: TAIR
Cellular component	chloroplast Ref.1 Inferred from direct assay. Source: TAIR
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoserine phosphatase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 62	62	Chloroplast Potential
	Chain	63 – 295	233	Phosphoserine phosphatase, chloroplastic		PRO_0000032375
Experimental info
	Sequence conflict	266	1	C → S in BAA33806. Ref.1
	Sequence conflict	266	1	C → S in BAA33807. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O82796-1 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: F14C95E636F7745E	FASTA	295	32,318
	10 20 30 40 50 60 MEALTTSRVV PVQVPCRKLS SLFANFSCLE LRRYPCRGLV SIMNHPKLLR PVTASVQPHE 70 80 90 100 110 120 LSTLGHEGNI VPSKEILDLW RSVEAVCFDV DSTVCVDEGI DELAEFCGAG KAVAEWTARA 130 140 150 160 170 180 MGGSVPFEEA LAARLSLFKP SLSKVEEYLD KRPPRLSPGI EELVKKLRAN NIDVYLISGG 190 200 210 220 230 240 FRQMINPVAS ILGIPRENIF ANNLLFGNSG EFLGFDENEP TSRSGGKAKA VQQIRKGRLY 250 260 270 280 290 KTMAMIGDGA TDLEARKPGG ADLFICYAGV QLREAVAANA DWLIFKFESL INSLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana." Ho C.-L., Noji M., Saito K. J. Biol. Chem. 274:11007-11012(1999) [PubMed: 10196182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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.
[4]	"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
EMBLGenBankDDBJ	AB018408 mRNA. Translation: BAA33806.1. AB018409 Genomic DNA. Translation: BAA33807.1. AC026238 Genomic DNA. Translation: AAF98410.1. AY065351 mRNA. Translation: AAL38792.1. AY096687 mRNA. Translation: AAM20321.1. AY087385 mRNA. Translation: AAM64935.1.
IPI	IPI00526883.
PIR	B86320. T51362.
RefSeq	NP_973858.1.
UniGene	At.356
3D structure databases
HSSP	HSSP built from PDB template 1NNL based on UniProtKB P78330.
ModBase	Search...
Protein-protein interaction databases
STRING	O82796.
Proteomic databases
PRIDE	O82796.
Genome annotation databases
GeneID	838445.
GenomeReviews	Gene locus AT1G18640 in contig CT485782_GR.
KEGG	ath:AT1G18640.
NMPDR	fig|3702.1.peg.2199.
Organism-specific databases
GeneFarm	4917.
TAIR	At1g18640.
Phylogenomic databases
OMA	PATNVFA.
Enzyme and pathway databases
BRENDA	3.1.3.3. 302.
Gene expression databases
Genevestigator	O82796.
GermOnline	AT1G18640. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR006383. HAD-SF_hydro_IB_PSP-like. IPR004469. SerB. [Graphical view]
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01488. HAD-SF-IB. 1 hit. TIGR00338. serB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SERB_ARATH

Accession

Primary (citable) accession number: O82796
Secondary accession number(s): Q9FZ85

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)