[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1093/nar/13.19.7025; PubMed=2997734 [NCBI, ExPASy, EBI, Israel, Japan] Neuwald A.F., Stauffer G.V.; "DNA sequence and characterization of the Escherichia coli serB gene."; Nucleic Acids Res. 13:7025-7039(1985).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H₂O = L(or D)-serine + phosphate.
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: step 3/3 .
INTERACTION:
P18843:nadE; NbExp=1; IntAct=EBI-1126007, EBI-548960;
SIMILARITY: Belongs to the serB family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03046; CAA26852.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97284.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77341.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78377.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24271; PAECS.

RefSeq

AP_004876.1; -.
NP_418805.1; -.

3D structure databases

HSSP

Q58989; 1J97. [HSSP ENTRY / PDB]

ModBase

P0AGB0.

Protein-protein interaction databases

IntAct

P0AGB0; 3.

Enzyme and pathway databases

BioCyc

EcoCyc:PSERPHOSPHA-MON; -.

Organism-specific databases

EchoBASE

EB0938; -.

EcoGene

EG10945; serB.

Ontologies

GO:0004647;	Molecular function: phosphoserine phosphatase activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006564;	Biological process: L-serine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001757; ATPase_P.
IPR005834; Dehalogen-like_hydro.
IPR006383; HAD-SF_hydro_IB_PSP-like.
IPR004469; SerB.
Graphical view of domain structure.

Pfam

PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00119; CATATPASE.

TIGRFAMs

TIGR01488; HAD-SF-IB; 1.
TIGR00338; serB; 1.

Genome annotation databases

GeneID

948913; -.

GenomeReviews

AP009048_GR; JW4351.
U00096_GR; b4388.

KEGG

ecj:JW4351; -.
eco:b4388; -.

Phylogenomic databases

HOGENOM

P0AGB0; -.

Genome annotation databases

CMR

P0AGB0; b4388.

Other

ProtoNet

P0AGB0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Hydrolase; Serine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 322`	`322`		`Phosphoserine phosphatase.`	`PRO_0000156886`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 35043 Da [This is the MW of the unprocessed precursor]

CRC64: A09A43BD846B7DE6 [This is a checksum on the sequence]

        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

P0AGB0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools