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Protein

Phosphoserine phosphatase

Gene

MJ1594

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.2 Publications

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=620 µM for O-phospho-L-serine (at 70 degrees Celsius and at pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius.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. no protein annotated in this organism
    3. Phosphoserine phosphatase (MJ1594)
    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
    Active sitei11 – 111Nucleophile3 Publications
    Metal bindingi11 – 111Magnesium3 Publications
    Active sitei13 – 131Proton donor3 Publications
    Metal bindingi13 – 131Magnesium; via carbonyl oxygen3 Publications
    Binding sitei20 – 201Substrate3 Publications
    Binding sitei56 – 561Substrate3 Publications
    Binding sitei144 – 1441Substrate3 Publications
    Metal bindingi167 – 1671Magnesium3 Publications
    Binding sitei170 – 1701Substrate1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Amino-acid biosynthesis, Serine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.3. 3260.
    UniPathwayiUPA00135; UER00198.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoserine phosphatase (EC:3.1.3.32 Publications)
    Short name:
    PSP
    Short name:
    PSPase
    Alternative name(s):
    O-phosphoserine phosphohydrolase
    Gene namesi
    Ordered Locus Names:MJ1594
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    Proteomesi
    • UP000000805 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111D → N: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Phosphoserine phosphatasePRO_0000156891Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi243232.MJ_1594.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116Combined sources
    Helixi12 – 165Combined sources
    Beta strandi17 – 193Combined sources
    Helixi21 – 288Combined sources
    Helixi32 – 4312Combined sources
    Helixi49 – 5810Combined sources
    Turni59 – 624Combined sources
    Helixi65 – 739Combined sources
    Helixi81 – 9010Combined sources
    Beta strandi93 – 10210Combined sources
    Helixi103 – 11311Combined sources
    Beta strandi116 – 12611Combined sources
    Beta strandi129 – 1357Combined sources
    Helixi143 – 15513Combined sources
    Helixi159 – 1613Combined sources
    Beta strandi162 – 1665Combined sources
    Helixi169 – 1713Combined sources
    Helixi172 – 1776Combined sources
    Beta strandi179 – 1857Combined sources
    Helixi188 – 1914Combined sources
    Beta strandi195 – 1984Combined sources
    Helixi203 – 2097Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F5SX-ray1.80A/B1-211[»]
    1J97X-ray1.50A/B1-211[»]
    1L7MX-ray1.48A/B1-211[»]
    1L7NX-ray1.80A/B1-211[»]
    1L7OX-ray2.20A/B1-211[»]
    1L7PX-ray1.90A/B1-211[»]
    ProteinModelPortaliQ58989.
    SMRiQ58989. Positions 2-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ58989.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1002Substrate binding3 Publications

    Sequence similaritiesi

    Belongs to the SerB family.Curated

    Phylogenomic databases

    eggNOGiarCOG01158. Archaea.
    COG0560. LUCA.
    InParanoidiQ58989.
    KOiK01079.
    OMAiRVAFCAK.
    PhylomeDBiQ58989.

    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.

    Q58989-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEKKKKLILF DFDSTLVNNE TIDEIAREAG VEEEVKKITK EAMEGKLNFE
    60 70 80 90 100
    QSLRKRVSLL KDLPIEKVEK AIKRITPTEG AEETIKELKN RGYVVAVVSG
    110 120 130 140 150
    GFDIAVNKIK EKLGLDYAFA NRLIVKDGKL TGDVEGEVLK ENAKGEILEK
    160 170 180 190 200
    IAKIEGINLE DTVAVGDGAN DISMFKKAGL KIAFCAKPIL KEKADICIEK
    210
    RDLREILKYI K
    Length:211
    Mass (Da):23,594
    Last modified:November 1, 1996 - v1
    Checksum:i8573E6D92D883AA6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77117 Genomic DNA. Translation: AAB99612.1.
    PIRiA64499.

    Genome annotation databases

    EnsemblBacteriaiAAB99612; AAB99612; MJ_1594.
    KEGGimja:MJ_1594.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L77117 Genomic DNA. Translation: AAB99612.1.
    PIRiA64499.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F5SX-ray1.80A/B1-211[»]
    1J97X-ray1.50A/B1-211[»]
    1L7MX-ray1.48A/B1-211[»]
    1L7NX-ray1.80A/B1-211[»]
    1L7OX-ray2.20A/B1-211[»]
    1L7PX-ray1.90A/B1-211[»]
    ProteinModelPortaliQ58989.
    SMRiQ58989. Positions 2-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi243232.MJ_1594.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAB99612; AAB99612; MJ_1594.
    KEGGimja:MJ_1594.

    Phylogenomic databases

    eggNOGiarCOG01158. Archaea.
    COG0560. LUCA.
    InParanoidiQ58989.
    KOiK01079.
    OMAiRVAFCAK.
    PhylomeDBiQ58989.

    Enzyme and pathway databases

    UniPathwayiUPA00135; UER00198.
    BRENDAi3.1.3.3. 3260.

    Miscellaneous databases

    EvolutionaryTraceiQ58989.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase."
      Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., Kustu S., Yan D.
      Proc. Natl. Acad. Sci. U.S.A. 98:8525-8530(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH BEF3 AND MAGNESIUM ION, CATALYTIC ACTIVITY, ACTIVE SITE.
    3. "Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution."
      Wang W., Kim R., Jancarik J., Yokota H., Kim S.-H.
      Structure 9:65-71(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND PHOSPHATE, ACTIVE SITE.
    4. "Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic 'snapshots' of intermediate states."
      Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H., Grigoriev I.V., Wemmer D.E., Kim S.-H.
      J. Mol. Biol. 319:421-431(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; SUBSTRATE; PHOSPHATE AND TRANSITION STATE ANALOG, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME MECHANISM, COFACTOR, ACTIVE SITE, MUTAGENESIS OF ASP-11.

    Entry informationi

    Entry nameiSERB_METJA
    AccessioniPrimary (citable) accession number: Q58989
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 116 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.