Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0AGB2 (SERB_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:serB
Ordered Locus Names:SF4420, S4691
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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.

Sequence similarities

Belongs to the serB family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Serine biosynthesis
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-serine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoserine phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Phosphoserine phosphatase
PRO_0000156889

Regions

Region204 – 2052Substrate binding By similarity

Sites

Active site1161Nucleophile By similarity
Active site1181Proton donor By similarity
Metal binding1161Magnesium By similarity
Metal binding1181Magnesium; via carbonyl oxygen By similarity
Metal binding2721Magnesium By similarity
Binding site1251Substrate By similarity
Binding site1611Substrate By similarity
Binding site2491Substrate By similarity
Binding site2751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AGB2 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: A09A43BD846B7DE6

FASTA32235,043
        10         20         30         40         50         60 
MPNITWCDLP EDVSLWPGLP LSLSGDEVMP LDYHAGRSGW LLYGRGLDKQ RLTQYQSKLG 

        70         80         90        100        110        120 
AAMVIVAAWC VEDYQVIRLA GSLTARATRL AHEAQLDVAP LGKIPHLRTP GLLVMDMDST 

       130        140        150        160        170        180 
AIQIECIDEI AKLAGTGEMV AEVTERAMRG ELDFTASLRS RVATLKGADA NILQQVRENL 

       190        200        210        220        230        240 
PLMPGLTQLV LKLETLGWKV AIASGGFTFF AEYLRDKLRL TAVVANELEI MDGKFTGNVI 

       250        260        270        280        290        300 
GDIVDAQYKA KTLTRLAQEY EIPLAQTVAI GDGANDLPMI KAAGLGIAYH AKPKVNEKAE 

       310        320 
VTIRHADLMG VFCILSGSLN QK 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN45834.1.
AE014073 Genomic DNA. Translation: AAP19608.1.
RefSeqNP_710127.1. NC_004337.2.
NP_839796.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AGB2.
SMRP0AGB2. Positions 11-322.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000086049; EBESCP00000082871; EBESCG00000085094.
EBESCT00000090177; EBESCP00000086813; EBESCG00000089221.
GeneID1025178.
1080889.
GenomeReviewsGene locus SF4420 in contig AE005674_GR.
Gene locus S4691 in contig AE014073_GR.
KEGGsfl:SF4420.
sfx:S4691.
PATRIC18711446. VBIShiFle31049_5118.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011712.
HOGENOMHBG645339.
OMADYQVVRL.
ProtClustDBPRK11133.

Enzyme and pathway databases

BioCycSFLE198214:AAN45834.1-MONOMER.

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_SHIFL
AccessionPrimary (citable) accession number: P0AGB2
Secondary accession number(s): P06862
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families