GPMPP_PERMH
ID GPMPP_PERMH Reviewed; 269 AA.
AC C0QRP9; A9QXB5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase {ECO:0000303|PubMed:17189358};
DE Short=GpgP {ECO:0000303|PubMed:17189358};
DE Short=MpgP {ECO:0000303|PubMed:17189358};
DE EC=3.1.3.70 {ECO:0000269|PubMed:17189358};
DE EC=3.1.3.85 {ECO:0000269|PubMed:17189358};
GN Name=gpgP {ECO:0000303|PubMed:17189358}; OrderedLocusNames=PERMA_1578;
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX NCBI_TaxID=123214;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=DSM 14350 / EX-H1;
RX PubMed=17189358; DOI=10.1128/jb.00841-06;
RA Costa J., Empadinhas N., da Costa M.S.;
RT "Glucosylglycerate biosynthesis in the deepest lineage of the Bacteria:
RT characterization of the thermophilic proteins GpgS and GpgP from
RT Persephonella marina.";
RL J. Bacteriol. 189:1648-1654(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
CC -!- FUNCTION: Involved in the biosynthesis of glucosylglycerate. Catalyzes
CC the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and
CC mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and
CC mannosylglycerate (MG), respectively. {ECO:0000269|PubMed:17189358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H2O =
CC (2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate;
CC Xref=Rhea:RHEA:31343, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62510, ChEBI:CHEBI:62600; EC=3.1.3.85;
CC Evidence={ECO:0000269|PubMed:17189358};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = (2R)-2-O-
CC (alpha-D-mannosyl)-glycerate + phosphate; Xref=Rhea:RHEA:19309,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57541,
CC ChEBI:CHEBI:57744; EC=3.1.3.70;
CC Evidence={ECO:0000269|PubMed:17189358};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17189358};
CC Note=Divalent metal cations. Can use Mg(2+), Co(2+) and, to a lesser
CC extent, Mn(2+) ions. {ECO:0000269|PubMed:17189358};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for GPG (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.41 mM for GPG (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.53 mM for GPG (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.19 mM for MPG (at 85 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.21 mM for MPG (at 90 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC KM=0.43 mM for MPG (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:17189358};
CC Vmax=97 umol/min/mg enzyme with GPG as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=288 umol/min/mg enzyme with GPG as substrate (at 90 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=294 umol/min/mg enzyme with GPG as substrate (at 85 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=17.9 umol/min/mg enzyme with MPG as substrate (at 90 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=15.75 umol/min/mg enzyme with MPG as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC Vmax=19.6 umol/min/mg enzyme with MPG as substrate (at 85 degrees
CC Celsius) {ECO:0000269|PubMed:17189358};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:17189358};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:17189358};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17189358}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family.
CC {ECO:0000305}.
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DR EMBL; EU277657; ABX75858.1; -; Genomic_DNA.
DR EMBL; CP001230; ACO04040.1; -; Genomic_DNA.
DR RefSeq; WP_012676278.1; NC_012440.1.
DR AlphaFoldDB; C0QRP9; -.
DR SMR; C0QRP9; -.
DR STRING; 123214.PERMA_1578; -.
DR EnsemblBacteria; ACO04040; ACO04040; PERMA_1578.
DR KEGG; pmx:PERMA_1578; -.
DR eggNOG; COG3769; Bacteria.
DR HOGENOM; CLU_063016_0_0_0; -.
DR OMA; GPEGWNE; -.
DR OrthoDB; 1861282at2; -.
DR BRENDA; 3.1.3.85; 9181.
DR Proteomes; UP000001366; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:InterPro.
DR CDD; cd07507; HAD_Pase; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006381; HAD-SF-IIB-MPGP.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR SFLD; SFLDG01142; C2.B.2:_Mannosyl-3-phosphoglyc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR01486; HAD-SF-IIB-MPGP; 1.
DR PROSITE; PS01228; COF_1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..269
FT /note="Glucosyl-3-phosphoglycerate/mannosyl-3-
FT phosphoglycerate phosphatase"
FT /id="PRO_0000420161"
FT ACT_SITE 6
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O58690"
FT BINDING 6
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O58690"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O58690"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O58690"
FT CONFLICT 1
FT /note="M -> MANV (in Ref. 1; ABX75858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 31076 MW; 0C5444E85F1BF33E CRC64;
MVIFTDLDGT LLNHEDYSFK DAIPSLERIK KKGIPLVIVT SKTKKEVELI QKELGIEEPF
IVENGAAVFF PKGYRGFNIR CDQENRYCII KLGRDYREIR DFIEKIKDKF KIKGFGDMTV
EEIVRLTDLP YDRAELAKER DFTEPFIIED EKDIKDLEEI AEKEGFKITK GGRFYHLIGK
GQDKGRAVQI VKKVFEENYG EVPLTVGLGD SRNDIPMLRE VDIPILIPHI NKKYESVNLP
GIIKAEYPGS KGWNESIWRI LNEIERGCC
