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O82796 (SERB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoserine phosphatase, chloroplastic
Short name=PSP
Short name=PSPase
EC=3.1.3.3
Alternative name(s):
O-phosphoserine phosphohydrolase
Gene names
Name:PSP
Ordered Locus Names:At1g18640
ORF Names:F26I16.2
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Binds 1 magnesium ion per subunit By similarity.

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) Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Chloroplast Potential
Chain63 – 295233Phosphoserine phosphatase, chloroplastic
PRO_0000032375

Regions

Region178 – 1792Substrate binding By similarity

Sites

Active site891Nucleophile By similarity
Active site911Proton donor By similarity
Metal binding891Magnesium By similarity
Metal binding911Magnesium; via carbonyl oxygen By similarity
Metal binding2481Magnesium By similarity
Binding site981Substrate By similarity
Binding site1341Substrate By similarity
Binding site2271Substrate By similarity

Experimental info

Sequence conflict2661C → S in BAA33806. Ref.1
Sequence conflict2661C → S in BAA33807. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O82796 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: F14C95E636F7745E

FASTA29532,318
        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

« Hide

References

« Hide '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. expand/collapse author list , 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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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.
[5]"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		AB018408 mRNA. Translation: BAA33806.1.
AB018409 Genomic DNA. Translation: BAA33807.1.
AC026238 Genomic DNA. Translation: AAF98410.1.
CP002684 Genomic DNA. Translation: AEE29738.1.
AY065351 mRNA. Translation: AAL38792.1.
AY096687 mRNA. Translation: AAM20321.1.
AY087385 mRNA. Translation: AAM64935.1.
IPIIPI00526883.
PIRB86320.
T51362.
RefSeqNP_973858.1. NM_202129.2.
UniGeneAt.356.
At.41785.

3D structure databases

ProteinModelPortalO82796.
SMRO82796. Positions 14-295.
ModBaseSearch...

Protein-protein interaction databases

IntActO82796. 1 interaction.
STRINGO82796.

Proteomic databases

PRIDEO82796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G18640.2; AT1G18640.2; AT1G18640.
GeneID838445.
GenomeReviewsGene locus AT1G18640 in contig CT485782_GR.
KEGGath:AT1G18640.
NMPDRfig|3702.1.peg.2199.

Organism-specific databases

GeneFarm4917.
TAIRAt1g18640.

Phylogenomic databases

eggNOGKOG1615.
GeneTreeEPGT00050000007509.
HOGENOMHBG482410.
OMAYAGFDES.
PhylomeDBO82796.
ProtClustDBPLN02954.

Gene expression databases

GenevestigatorO82796.
GermOnlineAT1G18640. Arabidopsis thaliana.

Family and domain databases

InterProIPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR023190. Pser_Pase_dom_2.
IPR004469. SerB.
[Graphical view]
Gene3DG3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
G3DSA:1.10.150.210. Pser_Pase_dom_2. 1 hit.
KOK01079.
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01488. HAD-SF-IB. 1 hit.
TIGR00338. SerB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSERB_ARATH
AccessionPrimary (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: December 14, 2011
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents