Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoserine phosphatase

Gene

serB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dephosphorylation of phosphoserine (P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr).1 Publication

Catalytic activityi

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.

Cofactori

Mg2+1 Publication, Mn2+1 Publication, Co2+1 Publication, Zn2+1 PublicationNote: Binds 1 Mg2+ ion per subunit. Can also use other divalent metal cations as Mn2+, Co2+ and Zn2+.1 Publication

Kineticsi

  1. KM=0.097 mM for P-Ser (with magnesium ions as cofactor and at pH 9)1 Publication
  2. KM=0.07 mM for imido-diphosphate (with magnesium ions as cofactor and at pH 9)1 Publication
  3. KM=6.2 mM for acetyl-phosphate (with magnesium ions as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is between 6 and 7.5.1 Publication

    Pathwayi: L-serine biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. D-3-phosphoglycerate dehydrogenase (serA)
    2. Phosphoserine aminotransferase (serC)
    3. Phosphoserine phosphatase (serB)
    This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi12 – 121MagnesiumBy similarity
    Active sitei116 – 1161NucleophileBy similarity
    Metal bindingi116 – 1161MagnesiumBy similarity
    Active sitei118 – 1181Proton donorBy similarity
    Metal bindingi118 – 1181Magnesium; via carbonyl oxygenBy similarity
    Binding sitei125 – 1251SubstrateBy similarity
    Binding sitei161 – 1611SubstrateBy similarity
    Binding sitei249 – 2491SubstrateBy similarity
    Metal bindingi272 – 2721MagnesiumBy similarity
    Binding sitei275 – 2751SubstrateBy similarity

    GO - Molecular functioni

    • magnesium ion binding Source: EcoliWiki
    • phosphatase activity Source: EcoliWiki
    • phosphoserine phosphatase activity Source: EcoliWiki

    GO - Biological processi

    • cellular amino acid biosynthetic process Source: EcoliWiki
    • dephosphorylation Source: GOC
    • L-serine biosynthetic process Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Amino-acid biosynthesis, Serine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PSERPHOSPHA-MONOMER.
    ECOL316407:JW4351-MONOMER.
    MetaCyc:PSERPHOSPHA-MONOMER.
    SABIO-RKP0AGB0.
    UniPathwayiUPA00135; UER00198.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoserine phosphatase (EC:3.1.3.3)
    Short name:
    PSP
    Short name:
    PSPase
    Alternative name(s):
    O-phosphoserine phosphohydrolase
    Gene namesi
    Name:serB
    Ordered Locus Names:b4388, JW4351
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10945. serB.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Phosphoserine phosphatasePRO_0000156886Add
    BLAST

    Proteomic databases

    PaxDbiP0AGB0.
    PRIDEiP0AGB0.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nadEP188431EBI-1126007,EBI-548960

    Protein-protein interaction databases

    BioGridi4262789. 113 interactions.
    DIPiDIP-48100N.
    IntActiP0AGB0. 3 interactions.
    STRINGi511145.b4388.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AGB0.
    SMRiP0AGB0. Positions 37-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 123Substrate bindingBy similarity
    Regioni204 – 2052Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the SerB family.Curated

    Phylogenomic databases

    eggNOGiENOG4105EAC. Bacteria.
    COG0560. LUCA.
    HOGENOMiHOG000231115.
    InParanoidiP0AGB0.
    KOiK01079.
    OMAiAQYKANT.
    OrthoDBiEOG6ZPT4H.
    PhylomeDBiP0AGB0.

    Family and domain databases

    Gene3Di1.10.150.210. 1 hit.
    3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006383. HAD-SF_hydro_IB_PSP-like.
    IPR023190. Pser_Pase_dom_2.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AGB0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPNITWCDLP EDVSLWPGLP LSLSGDEVMP LDYHAGRSGW LLYGRGLDKQ
    60 70 80 90 100
    RLTQYQSKLG AAMVIVAAWC VEDYQVIRLA GSLTARATRL AHEAQLDVAP
    110 120 130 140 150
    LGKIPHLRTP GLLVMDMDST AIQIECIDEI AKLAGTGEMV AEVTERAMRG
    160 170 180 190 200
    ELDFTASLRS RVATLKGADA NILQQVRENL PLMPGLTQLV LKLETLGWKV
    210 220 230 240 250
    AIASGGFTFF AEYLRDKLRL TAVVANELEI MDGKFTGNVI GDIVDAQYKA
    260 270 280 290 300
    KTLTRLAQEY EIPLAQTVAI GDGANDLPMI KAAGLGIAYH AKPKVNEKAE
    310 320
    VTIRHADLMG VFCILSGSLN QK
    Length:322
    Mass (Da):35,043
    Last modified:January 1, 1988 - v1
    Checksum:iA09A43BD846B7DE6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03046 Genomic DNA. Translation: CAA26852.1.
    U14003 Genomic DNA. Translation: AAA97284.1.
    U00096 Genomic DNA. Translation: AAC77341.1.
    AP009048 Genomic DNA. Translation: BAE78377.1.
    PIRiA24271. PAECS.
    RefSeqiNP_418805.1. NC_000913.3.
    WP_001132955.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77341; AAC77341; b4388.
    BAE78377; BAE78377; BAE78377.
    GeneIDi948913.
    KEGGiecj:JW4351.
    eco:b4388.
    PATRICi32124392. VBIEscCol129921_4536.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03046 Genomic DNA. Translation: CAA26852.1.
    U14003 Genomic DNA. Translation: AAA97284.1.
    U00096 Genomic DNA. Translation: AAC77341.1.
    AP009048 Genomic DNA. Translation: BAE78377.1.
    PIRiA24271. PAECS.
    RefSeqiNP_418805.1. NC_000913.3.
    WP_001132955.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP0AGB0.
    SMRiP0AGB0. Positions 37-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262789. 113 interactions.
    DIPiDIP-48100N.
    IntActiP0AGB0. 3 interactions.
    STRINGi511145.b4388.

    Proteomic databases

    PaxDbiP0AGB0.
    PRIDEiP0AGB0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77341; AAC77341; b4388.
    BAE78377; BAE78377; BAE78377.
    GeneIDi948913.
    KEGGiecj:JW4351.
    eco:b4388.
    PATRICi32124392. VBIEscCol129921_4536.

    Organism-specific databases

    EchoBASEiEB0938.
    EcoGeneiEG10945. serB.

    Phylogenomic databases

    eggNOGiENOG4105EAC. Bacteria.
    COG0560. LUCA.
    HOGENOMiHOG000231115.
    InParanoidiP0AGB0.
    KOiK01079.
    OMAiAQYKANT.
    OrthoDBiEOG6ZPT4H.
    PhylomeDBiP0AGB0.

    Enzyme and pathway databases

    UniPathwayiUPA00135; UER00198.
    BioCyciEcoCyc:PSERPHOSPHA-MONOMER.
    ECOL316407:JW4351-MONOMER.
    MetaCyc:PSERPHOSPHA-MONOMER.
    SABIO-RKP0AGB0.

    Miscellaneous databases

    PROiP0AGB0.

    Family and domain databases

    Gene3Di1.10.150.210. 1 hit.
    3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006383. HAD-SF_hydro_IB_PSP-like.
    IPR023190. Pser_Pase_dom_2.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "DNA sequence and characterization of the Escherichia coli serB gene."
      Neuwald A.F., Stauffer G.V.
      Nucleic Acids Res. 13:7025-7039(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family."
      Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.
      J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.

    Entry informationi

    Entry nameiSERB_ECOLI
    AccessioniPrimary (citable) accession number: P0AGB0
    Secondary accession number(s): P06862, Q2M5S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: April 13, 2016
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.