PSPB_HYDTT
ID PSPB_HYDTT Reviewed; 203 AA.
AC D3DFP8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Putative phosphoserine phosphatase 2;
DE Short=PSP 2;
DE Short=PSPase 2;
DE EC=3.1.3.3;
DE AltName: Full=Metal-independent phosphoserine phosphatase 2;
DE Short=iPSP2;
DE AltName: Full=O-phosphoserine phosphohydrolase 2;
GN Name=pspB; OrderedLocusNames=HTH_0183, Hydth_0184;
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, LACK OF PHOSPHOGLYCERATE MUTASE
RP ACTIVITY, SUBSTRATE SPECIFICITY, GENE NAME, ACTIVITY REGULATION, PATHWAY,
RP 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: Part of a complex that catalyzes the dephosphorylation of L-
CC phosphoserine to serine and inorganic phosphate. Is poorly or not
CC active toward D-phosphoserine, DL-phosphothreonine, 3-phosphoglycerate,
CC para-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 -!- 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 -!- 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=1.5 mM for O-phospho-L-serine;
CC Vmax=32 umol/min/mg enzyme;
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: Heterodimer with PspA. The PspB subunit appears to have no or
CC considerably lower PSP activity compared with that of PspA.
CC {ECO:0000269|PubMed:22337887}.
CC -!- SIMILARITY: Belongs to the histidine phosphatase superfamily. Metal-
CC independent phosphoserine phosphatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011112; BAI68650.1; -; Genomic_DNA.
DR EMBL; CP002221; ADO44594.1; -; Genomic_DNA.
DR RefSeq; WP_012962833.1; NC_017161.1.
DR AlphaFoldDB; D3DFP8; -.
DR SMR; D3DFP8; -.
DR STRING; 608538.HTH_0183; -.
DR EnsemblBacteria; BAI68650; BAI68650; HTH_0183.
DR KEGG; hte:Hydth_0184; -.
DR KEGG; hth:HTH_0183; -.
DR PATRIC; fig|608538.5.peg.184; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_0_0; -.
DR OMA; FWADPYA; -.
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 Amino-acid biosynthesis; Direct protein sequencing; Hydrolase;
KW Reference proteome; Serine biosynthesis.
FT CHAIN 1..203
FT /note="Putative phosphoserine phosphatase 2"
FT /id="PRO_0000416821"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 149
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 23548 MW; 98D44BC6E9C10849 CRC64;
MKRLYLVRHA QSEYNEKGIF QGRLDSDLTP LGFVQARLLA REFLKKKVDI IYSSPQRRAY
KTALTISDML GTQLVVDERL REMSFGEYEG KHFWSMLEAH KDVFLNWLSN PVKHPLPTQE
SMEEFEKRVR SFLEDVKSSH YQNMLIVAHG GTLHAIVCLL TGIGLENLWN IHMDNAGITE
IHMEGEKSTL VYLNKLCHTR QLT
