MGGB_PETMO
ID MGGB_PETMO Reviewed; 503 AA.
AC A9BJC1;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Mannosylglucosyl-3-phosphoglycerate phosphatase {ECO:0000303|PubMed:20061481};
DE Short=MGPG phosphatase {ECO:0000303|PubMed:20061481};
DE EC=3.1.3.- {ECO:0000269|PubMed:20061481};
DE Flags: Precursor;
GN Name=mggB {ECO:0000303|PubMed:20061481};
GN OrderedLocusNames=Pmob_0601 {ECO:0000312|EMBL:ABX31335.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=DSM 10674 / SJ95;
RX PubMed=20061481; DOI=10.1128/jb.01424-09;
RA Fernandes C., Mendes V., Costa J., Empadinhas N., Jorge C., Lamosa P.,
RA Santos H., da Costa M.S.;
RT "Two alternative pathways for the synthesis of the rare compatible solute
RT mannosylglucosylglycerate in Petrotoga mobilis.";
RL J. Bacteriol. 192:1624-1633(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the compatible solute
CC mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes
CC the dephosphorylation of mannosylglucosyl-3-phosphoglycerate (MGPG) to
CC mannosylglucosylglycerate (MGG). Can also dephosphorylate UDP-glucose,
CC ADP-glucose, GDP-mannose, glucosyl-3-phosphoglycerate (GPG), mannosyl-
CC 3-phosphoglycerate (MPG), ADP, GDP and UDP.
CC {ECO:0000269|PubMed:20061481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-[alpha-D-mannopyranosyl-(1->2)-alpha-D-
CC glucopyranosyl]-3-phospho-glycerate + H2O = (2R)-2-O-[alpha-D-
CC mannopyranosyl-(1->2)-alpha-D-glucopyranosyl]-glycerate + phosphate;
CC Xref=Rhea:RHEA:47696, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:62602, ChEBI:CHEBI:87836;
CC Evidence={ECO:0000269|PubMed:20061481};
CC -!- ACTIVITY REGULATION: Divalent cations are not required for activity,
CC but the presence of Mn(2+), Mg(2+) or Ca(2+) stimulates activity.
CC {ECO:0000269|PubMed:20061481}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for mannosylglucosyl-3-phosphoglycerate (at 60 degrees
CC Celsius) {ECO:0000269|PubMed:20061481};
CC KM=2.6 mM for glucosyl-3-phosphoglycerate (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC KM=2.8 mM for mannosyl-3-phosphoglycerate (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:20061481};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:20061481};
CC -!- MISCELLANEOUS: MggB could be only partially purified, because it
CC completely loses activity after hydrophobic interaction chromatography
CC or size-exclusion chromatography. {ECO:0000305|PubMed:20061481}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; CP000879; ABX31335.1; -; Genomic_DNA.
DR RefSeq; WP_012208439.1; NC_010003.1.
DR AlphaFoldDB; A9BJC1; -.
DR SMR; A9BJC1; -.
DR STRING; 403833.Pmob_0601; -.
DR EnsemblBacteria; ABX31335; ABX31335; Pmob_0601.
DR KEGG; pmo:Pmob_0601; -.
DR eggNOG; COG0737; Bacteria.
DR HOGENOM; CLU_005854_7_3_0; -.
DR OMA; VQPFTNM; -.
DR OrthoDB; 1884225at2; -.
DR BioCyc; MetaCyc:MON-16137; -.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..503
FT /note="Mannosylglucosyl-3-phosphoglycerate phosphatase"
FT /id="PRO_5000287018"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P44569"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P44569"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P44569"
FT BINDING 450..456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 106
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P44569"
FT SITE 109
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P44569"
SQ SEQUENCE 503 AA; 54892 MW; 7658B56FA59DE59B CRC64;
MKRFLGILVF VVMVLSVFAG PNHLVIFHMN DTHGHVWGTE DGGGFARAAT LINQAREEVA
KEGGAVLFLH AGDVNTGIPE SDQLDAVPDF LALHYMGLDA MSLGNHEFDK PFEVLEKQYE
VAQFPFLGAN FVNEKRGGPV FEPYIIKDYG DFSVGIIGLV TEQTKVLEPI YLGENTIVDA
EETLNMYLPI VQEKADVVIV LAHLGYHADG GRPNLSVEFT TSDELAENVS GVDIIIDGHS
HTLLETPVVI NNVIVAQAGD NAENIGRIDL WIDDGRIVDW RGEVIPLTSD IPEDPFIKMF
TDAFYQLGSE ALNEVVGVTK VYLDGERAHV RSDETNLSNL IADGMIWKTG ADVALMNGGG
IRASIEAGEI TYRDILTVLP FGNTLYVLEL TGKDIMDVLN YAATIPDGQG AKLHVAGLTA
EIKGGKATNV KINGKPIDLN KTYKVVTNNY VAAGGDGYTM LAGKPGYDTY FRDADSLREY
IAHLGTIEDY TSQERLIELD QVK
