PSPA_HYDTT
ID PSPA_HYDTT Reviewed; 211 AA.
AC D3DFG8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Phosphoserine phosphatase 1;
DE Short=PSP 1;
DE Short=PSPase 1;
DE EC=3.1.3.3;
DE AltName: Full=Metal-independent phosphoserine phosphatase 1;
DE Short=iPSP1;
DE AltName: Full=O-phosphoserine phosphohydrolase 1;
GN Name=pspA; Synonyms=pgmA; OrderedLocusNames=HTH_0103, Hydth_0104;
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobacter.
OX NCBI_TaxID=608538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=20348262; DOI=10.1128/jb.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=21677850; DOI=10.4056/sigs.1463589;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Zeytun A., Sikorski J., Nolan M., Lapidus A., Lucas S., Han J., Tice H.,
RA Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Ngatchou-Djao O.D., Land M., Hauser L., Jeffries C.D.,
RA Han C., Detter J.C., Ubler S., Rohde M., Tindall B.J., Goker M., Wirth R.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Hydrogenobacter thermophilus type strain (TK-
RT 6).";
RL Stand. Genomic Sci. 4:131-143(2011).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION AS A PHOSPHOSERINE PHOSPHATASE,
RP CATALYTIC ACTIVITY, LACK OF PHOSPHOGLYCERATE MUTASE ACTIVITY, SUBSTRATE
RP SPECIFICITY, GENE NAME, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RC STRAIN=DSM 6534 / IAM 12695 / TK-6;
RX PubMed=22337887; DOI=10.1074/jbc.m111.330621;
RA Chiba Y., Oshima K., Arai H., Ishii M., Igarashi Y.;
RT "Discovery and analysis of cofactor-dependent phosphoglycerate mutase
RT homologs as novel phosphoserine phosphatases in Hydrogenobacter
RT thermophilus.";
RL J. Biol. Chem. 287:11934-11941(2012).
CC -!- FUNCTION: Catalyzes the dephosphorylation of L-phosphoserine to serine
CC and inorganic phosphate. Is poorly or not active toward D-
CC phosphoserine, DL-phosphothreonine, 3-phosphoglycerate, para-
CC nitrophenylphosphate, and fructose-6-phosphate. Does not display
CC phosphoglycerate mutase activity. {ECO:0000269|PubMed:22337887}.
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:22337887};
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:22337887};
CC -!- ACTIVITY REGULATION: Activity is not inhibited by EDTA in vitro, nor
CC enhanced by the addition of Mg(2+). {ECO:0000269|PubMed:22337887}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for O-phospho-L-serine;
CC Vmax=56 umol/min/mg enzyme;
CC Note=Values are given for the homodimeric form of the protein.;
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 3/3. {ECO:0000269|PubMed:22337887}.
CC -!- SUBUNIT: Homodimer. Can also form a heterodimer with PspB.
CC {ECO:0000269|PubMed:22337887}.
CC -!- SIMILARITY: Belongs to the histidine phosphatase superfamily. Metal-
CC independent phosphoserine phosphatase family. {ECO:0000305}.
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DR EMBL; AP011112; BAI68570.1; -; Genomic_DNA.
DR EMBL; CP002221; ADO44514.1; -; Genomic_DNA.
DR RefSeq; WP_012962753.1; NC_017161.1.
DR PDB; 4IJ5; X-ray; 1.50 A; A/B=1-211.
DR PDB; 4IJ6; X-ray; 1.80 A; A/B=1-211.
DR PDBsum; 4IJ5; -.
DR PDBsum; 4IJ6; -.
DR AlphaFoldDB; D3DFG8; -.
DR SMR; D3DFG8; -.
DR STRING; 608538.HTH_0103; -.
DR PRIDE; D3DFG8; -.
DR EnsemblBacteria; BAI68570; BAI68570; HTH_0103.
DR KEGG; hte:Hydth_0104; -.
DR KEGG; hth:HTH_0103; -.
DR PATRIC; fig|608538.5.peg.105; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_4_0; -.
DR OMA; WLTEPAW; -.
DR OrthoDB; 1122642at2; -.
DR BRENDA; 3.1.3.3; 2722.
DR UniPathway; UPA00135; UER00198.
DR Proteomes; UP000002574; Chromosome.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Direct protein sequencing;
KW Hydrolase; Reference proteome; Serine biosynthesis.
FT CHAIN 1..211
FT /note="Phosphoserine phosphatase 1"
FT /id="PRO_0000416820"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4IJ5"
FT TURN 13..18
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:4IJ5"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:4IJ5"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4IJ5"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:4IJ5"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4IJ6"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:4IJ5"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4IJ5"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:4IJ5"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:4IJ5"
SQ SEQUENCE 211 AA; 24556 MW; 45E252C822C85242 CRC64;
MVKLILVRHA ESEWNPVGRY QGLLDPDLSE RGKKQAKLLA QELSREHLDV IYSSPLKRTY
LTALEIAEAK NLEVIKEDRI IEIDHGMWSG MLVEEVMEKY PEDFRRWVEE PHKVEFQGGE
SLASVYNRVK GFLEEVRKRH WNQTVVVVSH TVPMRAMYCA LLGVDLSKFW SFGCDNASYS
VIHMEERRNV ILKLNITCHL GEFYVEAHKA I
