GPMPP_METBU
ID GPMPP_METBU Reviewed; 272 AA.
AC Q12XX5;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glucosyl-3-phosphoglycerate/mannosyl-3-phosphoglycerate phosphatase {ECO:0000303|PubMed:16428406};
DE Short=GpgP {ECO:0000303|PubMed:16428406};
DE Short=MpgP {ECO:0000303|PubMed:16428406};
DE EC=3.1.3.70 {ECO:0000269|PubMed:16428406};
DE EC=3.1.3.85 {ECO:0000269|PubMed:16428406};
GN Name=gpgP {ECO:0000303|PubMed:16428406}; OrderedLocusNames=Mbur_0736;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=16428406; DOI=10.1128/jb.188.3.1022-1030.2006;
RA Costa J., Empadinhas N., Goncalves L., Lamosa P., Santos H., da Costa M.S.;
RT "Characterization of the biosynthetic pathway of glucosylglycerate in the
RT archaeon Methanococcoides burtonii.";
RL J. Bacteriol. 188:1022-1030(2006).
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:16428406}.
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:16428406};
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:16428406};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:16428406};
CC Note=Divalent cations in the following order of efficiency: cobalt,
CC magnesium, and, to a lesser extent, nickel ions.
CC {ECO:0000269|PubMed:16428406};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for GPG (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC KM=0.27 mM for GPG (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC KM=0.28 mM for MPG (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16428406};
CC Vmax=0.1 umol/min/mg enzyme with GPG as substrate (at 30 degrees
CC Celsius) {ECO:0000269|PubMed:16428406};
CC Vmax=0.25 umol/min/mg enzyme with MPG as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:16428406};
CC Vmax=0.58 umol/min/mg enzyme with GPG as substrate (at 50 degrees
CC Celsius) {ECO:0000269|PubMed:16428406};
CC pH dependence:
CC Optimum pH is between 5.5 and 6.5 with GPG and MPG as substrates.
CC {ECO:0000269|PubMed:16428406};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius with GPG and 60 degrees
CC Celsius with MPG. With GPG as substrate, the activity becomes
CC undetectable below 20 degrees Celsius and above 70 degrees Celsius,
CC and with MPG as substrate, the activity is almost undetectable at 30
CC degrees Celsius. At 50 degrees Celsius, divalent cations are
CC absolutely required for GpgP activity with GPG and MPG as the
CC substrates. {ECO:0000269|PubMed:16428406};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:C0QRP9}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family.
CC {ECO:0000305}.
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DR EMBL; CP000300; ABE51701.1; -; Genomic_DNA.
DR RefSeq; WP_011498859.1; NC_007955.1.
DR AlphaFoldDB; Q12XX5; -.
DR SMR; Q12XX5; -.
DR STRING; 259564.Mbur_0736; -.
DR EnsemblBacteria; ABE51701; ABE51701; Mbur_0736.
DR GeneID; 3996640; -.
DR KEGG; mbu:Mbur_0736; -.
DR HOGENOM; CLU_063016_0_0_2; -.
DR OMA; GPEGWNE; -.
DR OrthoDB; 58084at2157; -.
DR Proteomes; UP000001979; 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:0016151; F:nickel cation binding; IDA:UniProtKB.
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 InterPro; IPR033980; MPG_Pase_thermophiles.
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 TIGRFAMs; TIGR02461; osmo_MPG_phos; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..272
FT /note="Glucosyl-3-phosphoglycerate/mannosyl-3-
FT phosphoglycerate phosphatase"
FT /id="PRO_0000420162"
FT ACT_SITE 8
FT /note="Nucleophile"
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 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O58690"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O58690"
SQ SEQUENCE 272 AA; 30554 MW; 0B909AC970A24855 CRC64;
MKHIIFTDLD GTLIDHDTYS YDAARPALDL LKEKEIPLIF CTSKTRAELE VYVDELECHH
PFISENGGAI FIPKDHFSIE LKDVHEIGNY KVIEFGTSYT RIRGVLEDIR KKTGFKITGF
GDLDAEGVSK DTGLDIRSAK LAKLREYDEA FRLEEDENAT AKVIELIHAA GLNYTKGGRY
WHIMGDNDKG KAVRALTEIY RQQFTEVVTI ALGDSLNDLP MLKAVDIPFL VQKPDGKYDP
SIILTEIKHA EGIGPVGWNN AIMDLIGKNN NI
