SERB_METJA
ID SERB_METJA Reviewed; 211 AA.
AC Q58989;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phosphoserine phosphatase;
DE Short=PSP;
DE Short=PSPase;
DE EC=3.1.3.3 {ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918};
DE AltName: Full=O-phosphoserine phosphohydrolase;
GN OrderedLocusNames=MJ1594;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH BEF3 AND MAGNESIUM
RP ION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=11438683; DOI=10.1073/pnas.131213698;
RA Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., Kustu S.,
RA Yan D.;
RT "BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on
RT aspartate: structure of a BeF(3)(-) complex with phosphoserine
RT phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8525-8530(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP PHOSPHATE, AND ACTIVE SITE.
RX PubMed=11342136; DOI=10.1016/s0969-2126(00)00558-x;
RA Wang W., Kim R., Jancarik J., Yokota H., Kim S.-H.;
RT "Crystal structure of phosphoserine phosphatase from Methanococcus
RT jannaschii, a hyperthermophile, at 1.8 A resolution.";
RL Structure 9:65-71(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM;
RP SUBSTRATE; PHOSPHATE AND TRANSITION STATE ANALOG, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME MECHANISM, COFACTOR, ACTIVE SITE, AND
RP MUTAGENESIS OF ASP-11.
RX PubMed=12051918; DOI=10.1016/s0022-2836(02)00324-8;
RA Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H.,
RA Grigoriev I.V., Wemmer D.E., Kim S.-H.;
RT "Structural characterization of the reaction pathway in phosphoserine
RT phosphatase: crystallographic 'snapshots' of intermediate states.";
RL J. Mol. Biol. 319:421-431(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate;
CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3;
CC Evidence={ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate;
CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3;
CC Evidence={ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12051918};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:12051918};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=620 uM for O-phospho-L-serine (at 70 degrees Celsius and at pH
CC 7.5) {ECO:0000269|PubMed:12051918};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12051918};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12051918};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99612.1; -; Genomic_DNA.
DR PIR; A64499; A64499.
DR RefSeq; WP_010871118.1; NC_000909.1.
DR PDB; 1F5S; X-ray; 1.80 A; A/B=1-211.
DR PDB; 1J97; X-ray; 1.50 A; A/B=1-211.
DR PDB; 1L7M; X-ray; 1.48 A; A/B=1-211.
DR PDB; 1L7N; X-ray; 1.80 A; A/B=1-211.
DR PDB; 1L7O; X-ray; 2.20 A; A/B=1-211.
DR PDB; 1L7P; X-ray; 1.90 A; A/B=1-211.
DR PDBsum; 1F5S; -.
DR PDBsum; 1J97; -.
DR PDBsum; 1L7M; -.
DR PDBsum; 1L7N; -.
DR PDBsum; 1L7O; -.
DR PDBsum; 1L7P; -.
DR AlphaFoldDB; Q58989; -.
DR BMRB; Q58989; -.
DR SMR; Q58989; -.
DR STRING; 243232.MJ_1594; -.
DR EnsemblBacteria; AAB99612; AAB99612; MJ_1594.
DR GeneID; 1452502; -.
DR KEGG; mja:MJ_1594; -.
DR eggNOG; arCOG01158; Archaea.
DR HOGENOM; CLU_036368_4_3_2; -.
DR InParanoid; Q58989; -.
DR OMA; CINEPDL; -.
DR OrthoDB; 105892at2157; -.
DR PhylomeDB; Q58989; -.
DR BRENDA; 3.1.3.3; 3260.
DR UniPathway; UPA00135; UER00198.
DR EvolutionaryTrace; Q58989; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SFLD; SFLDF00029; phosphoserine_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..211
FT /note="Phosphoserine phosphatase"
FT /id="PRO_0000156891"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11342136,
FT ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12051918"
FT MUTAGEN 11
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12051918"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1L7M"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:1L7M"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1L7M"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1L7M"
SQ SEQUENCE 211 AA; 23594 MW; 8573E6D92D883AA6 CRC64;
MEKKKKLILF DFDSTLVNNE TIDEIAREAG VEEEVKKITK EAMEGKLNFE QSLRKRVSLL
KDLPIEKVEK AIKRITPTEG AEETIKELKN RGYVVAVVSG GFDIAVNKIK EKLGLDYAFA
NRLIVKDGKL TGDVEGEVLK ENAKGEILEK IAKIEGINLE DTVAVGDGAN DISMFKKAGL
KIAFCAKPIL KEKADICIEK RDLREILKYI K
