MPGP_ECOLI
ID MPGP_ECOLI Reviewed; 271 AA.
AC P76329; Q2MB01;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Mannosyl-3-phosphoglycerate phosphatase {ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000303|PubMed:25848029};
DE Short=MPGP {ECO:0000255|HAMAP-Rule:MF_00617};
DE EC=3.1.3.70 {ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000269|PubMed:25848029};
GN Name=yedP; OrderedLocusNames=b1955, JW1938;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
RN [4] {ECO:0007744|PDB:1XVI}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
RA Kim Y., Joachimiak A., Cymborowski M., Skarina T., Savchenko A.,
RA Edwards A.;
RT "Crystal Structure of YedP, phosphatase-like domain protein from
RT Escherichia coli K12.";
RL Submitted (OCT-2004) to the PDB data bank.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00617, ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00617,
CC ECO:0000269|PubMed:25848029};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00617}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family.
CC {ECO:0000255|HAMAP-Rule:MF_00617}.
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DR EMBL; U00096; AAC75021.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76555.1; -; Genomic_DNA.
DR PIR; G64959; G64959.
DR RefSeq; NP_416464.1; NC_000913.3.
DR RefSeq; WP_000491520.1; NZ_LN832404.1.
DR PDB; 1XVI; X-ray; 2.26 A; A/B=1-271.
DR PDBsum; 1XVI; -.
DR AlphaFoldDB; P76329; -.
DR SMR; P76329; -.
DR BioGRID; 4261051; 16.
DR DIP; DIP-11848N; -.
DR IntAct; P76329; 3.
DR STRING; 511145.b1955; -.
DR jPOST; P76329; -.
DR PaxDb; P76329; -.
DR PRIDE; P76329; -.
DR DNASU; 946472; -.
DR EnsemblBacteria; AAC75021; AAC75021; b1955.
DR EnsemblBacteria; BAE76555; BAE76555; BAE76555.
DR GeneID; 946472; -.
DR KEGG; ecj:JW1938; -.
DR KEGG; eco:b1955; -.
DR PATRIC; fig|1411691.4.peg.297; -.
DR EchoBASE; EB3793; -.
DR eggNOG; COG3769; Bacteria.
DR HOGENOM; CLU_063016_1_0_6; -.
DR OMA; GPEGWNE; -.
DR PhylomeDB; P76329; -.
DR BioCyc; EcoCyc:G7048-MON; -.
DR EvolutionaryTrace; P76329; -.
DR PRO; PR:P76329; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:InterPro.
DR CDD; cd07507; HAD_Pase; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_00617; MPGP_rel; 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; IPR012815; MPG_Pase.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..271
FT /note="Mannosyl-3-phosphoglycerate phosphatase"
FT /id="PRO_0000184974"
FT ACT_SITE 13
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000305"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:1XVI"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1XVI"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1XVI"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:1XVI"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1XVI"
SQ SEQUENCE 271 AA; 30439 MW; 1192A5DC83F71816 CRC64;
MFSIQQPLLV FSDLDGTLLD SHSYDWQPAA PWLTRLREAN VPVILCSSKT SAEMLYLQKT
LGLQGLPLIA ENGAVIQLAE QWQEIDGFPR IISGISHGEI SLVLNTLREK EHFKFTTFDD
VDDATIAEWT GLSRSQAALT QLHEASVTLI WRDSDERMAQ FTARLNELGL QFMQGARFWH
VLDASAGKDQ AANWIIATYQ QLSGKRPTTL GLGDGPNDAP LLEVMDYAVI VKGLNREGVH
LHDEDPARVW RTQREGPEGW REGLDHFFSA R
