MPGP_PYRHO
ID MPGP_PYRHO Reviewed; 243 AA.
AC O58690;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Mannosyl-3-phosphoglycerate phosphatase {ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000303|PubMed:11562374, ECO:0000303|PubMed:19018103};
DE Short=MPGP {ECO:0000255|HAMAP-Rule:MF_00617};
DE EC=3.1.3.70 {ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000269|PubMed:11562374};
GN Name=mngB {ECO:0000255|HAMAP-Rule:MF_00617}; OrderedLocusNames=PH0926;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=11562374; DOI=10.1074/jbc.m108054200;
RA Empadinhas N., Marugg J.D., Borges N., Santos H., da Costa M.S.;
RT "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic
RT archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of
RT key enzymes.";
RL J. Biol. Chem. 276:43580-43588(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
RP COFACTOR.
RX PubMed=19018103; DOI=10.1107/s0907444908033817;
RA Kawamura T., Watanabe N., Tanaka I.;
RT "Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus
RT horikoshii.";
RL Acta Crystallogr. D 64:1267-1276(2008).
CC -!- FUNCTION: Hydrolyzes mannosyl-3-phosphoglycerate (MPG) to form the
CC osmolyte mannosylglycerate (MG). The enzyme is absolutely specific for
CC MPG. {ECO:0000269|PubMed:11562374}.
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:11562374};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00617,
CC ECO:0000269|PubMed:11562374, ECO:0000269|PubMed:19018103};
CC -!- PATHWAY: Carbohydrate biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate
CC biosynthesis; 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose
CC (MPG route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00617}.
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; BA000001; BAA30022.1; -; Genomic_DNA.
DR PIR; H71082; H71082.
DR RefSeq; WP_010885016.1; NC_000961.1.
DR PDB; 1WZC; X-ray; 1.90 A; A/B=1-243.
DR PDB; 2ZOS; X-ray; 1.70 A; A/B=1-243.
DR PDBsum; 1WZC; -.
DR PDBsum; 2ZOS; -.
DR AlphaFoldDB; O58690; -.
DR SMR; O58690; -.
DR STRING; 70601.3257339; -.
DR EnsemblBacteria; BAA30022; BAA30022; BAA30022.
DR GeneID; 1443251; -.
DR KEGG; pho:PH0926; -.
DR eggNOG; arCOG01215; Archaea.
DR OMA; GPEGWNE; -.
DR OrthoDB; 58084at2157; -.
DR BioCyc; MetaCyc:MON-13379; -.
DR BRENDA; 2.4.1.217; 5244.
DR BRENDA; 3.1.3.70; 5244.
DR SABIO-RK; O58690; -.
DR UniPathway; UPA00130; UER00193.
DR EvolutionaryTrace; O58690; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050531; F:mannosyl-3-phosphoglycerate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051479; P:mannosylglycerate biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR033980; MPG_Pase_thermophiles.
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 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..243
FT /note="Mannosyl-3-phosphoglycerate phosphatase"
FT /id="PRO_0000184973"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617, ECO:0000305"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617,
FT ECO:0000269|PubMed:19018103"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617,
FT ECO:0000269|PubMed:19018103"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617,
FT ECO:0000269|PubMed:19018103"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00617,
FT ECO:0000269|PubMed:19018103"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2ZOS"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1WZC"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2ZOS"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1WZC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:2ZOS"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:2ZOS"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2ZOS"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:2ZOS"
SQ SEQUENCE 243 AA; 27959 MW; FE5EE94DCAAD3636 CRC64;
MIRLIFLDID KTLIPGYEPD PAKPIIEELK DMGFEIIFNS SKTRAEQEYY RKELEVETPF
ISENGSAIFI PKGYFPFDVK GKEVGNYIVI ELGIRVEKIR EELKKLENIY GLKYYGNSTK
EEIEKFTGMP PELVPLAMER EYSETIFEWS RDGWEEVLVE GGFKVTMGSR FYTVHGNSDK
GKAAKILLDF YKRLGQIESY AVGDSYNDFP MFEVVDKAFI VGSLKHKKAQ NVSSIIDVLE
VIK
