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Q5RB83 (SERB_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Phosphoserine phosphatase

Short name=PSP
Short name=PSPase
EC=3.1.3.3
Alternative name(s):
O-phosphoserine phosphohydrolase
Gene names
Name:PSPH
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the serB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Phosphoserine phosphatase
PRO_0000156881

Regions

Region109 – 1102Substrate binding By similarity

Sites

Active site201Nucleophile By similarity
Active site221Proton donor By similarity
Metal binding201Magnesium By similarity
Metal binding221Magnesium; via carbonyl oxygen By similarity
Metal binding1791Magnesium By similarity
Binding site291Substrate By similarity
Binding site651Substrate By similarity
Binding site1581Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RB83 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: BD5D72697747FA30

FASTA22525,008
        10         20         30         40         50         60 
MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA 

        70         80         90        100        110        120 
ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA 

       130        140        150        160        170        180 
SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG 

       190        200        210        220 
ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858770 mRNA. Translation: CAH90977.1.
RefSeqNP_001128794.1. NM_001135322.1.
UniGenePab.13544.

3D structure databases

ProteinModelPortalQ5RB83.
SMRQ5RB83. Positions 4-225.
ModBaseSearch...

Proteomic databases

PRIDEQ5RB83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100189699.
KEGGpon:100189699.

Phylogenomic databases

HOVERGENHBG057486.
InParanoidQ5RB83.

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. 2 hits.
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_PONAB
AccessionPrimary (citable) accession number: Q5RB83
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families