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Protein

Mannosyl-3-phosphoglycerate phosphatase

Gene

mngB

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes mannosyl-3-phosphoglycerate (MPG) to form the osmolyte mannosylglycerate (MG). The enzyme is absolutely specific for MPG.1 Publication

Catalytic activityi

2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation2 Publications

Pathwayi: 2-(alpha-D-mannosyl)-D-glycerate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose (MPG route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Mannosyl-3-phosphoglycerate synthase (mngA)
  2. Mannosyl-3-phosphoglycerate phosphatase (mngB)
This subpathway is part of the pathway 2-(alpha-D-mannosyl)-D-glycerate biosynthesis, which is itself part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-(alpha-D-mannosyl)-D-glycerate from GDP-alpha-D-mannose (MPG route), the pathway 2-(alpha-D-mannosyl)-D-glycerate biosynthesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81NucleophileUniRule annotationCurated
Metal bindingi8 – 81MagnesiumUniRule annotation1 Publication
Metal bindingi10 – 101Magnesium; via carbonyl oxygenUniRule annotation1 Publication
Metal bindingi169 – 1691MagnesiumUniRule annotation1 Publication
Metal bindingi204 – 2041MagnesiumUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13379.
PHOR70601:GJWR-919-MONOMER.
BRENDAi3.1.3.70. 5244.
SABIO-RKO58690.
UniPathwayiUPA00130; UER00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl-3-phosphoglycerate phosphatase2 PublicationsUniRule annotation (EC:3.1.3.70UniRule annotation1 Publication)
Short name:
MPGPUniRule annotation
Gene namesi
Name:mngBUniRule annotation
Ordered Locus Names:PH0926
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Mannosyl-3-phosphoglycerate phosphatasePRO_0000184973Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi70601.PH0926.

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Turni11 – 133Combined sources
Beta strandi14 – 174Combined sources
Helixi20 – 223Combined sources
Helixi23 – 319Combined sources
Beta strandi34 – 396Combined sources
Helixi44 – 5411Combined sources
Beta strandi60 – 623Combined sources
Turni63 – 664Combined sources
Beta strandi67 – 693Combined sources
Beta strandi81 – 844Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 11015Combined sources
Helixi115 – 1173Combined sources
Helixi120 – 1278Combined sources
Turni131 – 1333Combined sources
Helixi134 – 1385Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi150 – 1523Combined sources
Helixi154 – 1607Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi169 – 1757Combined sources
Helixi180 – 19213Combined sources
Beta strandi197 – 2037Combined sources
Helixi206 – 2083Combined sources
Helixi209 – 2124Combined sources
Beta strandi215 – 2239Combined sources
Beta strandi229 – 2346Combined sources
Helixi235 – 2439Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WZCX-ray1.90A/B1-243[»]
2ZOSX-ray1.70A/B1-243[»]
ProteinModelPortaliO58690.
SMRiO58690. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58690.

Family & Domainsi

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily. MPGP family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01215. Archaea.
COG3769. LUCA.
HOGENOMiHOG000224319.
KOiK07026.
OMAiPLAMERE.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
HAMAPiMF_00617. MPGP_rel.
InterProiIPR023214. HAD-like_dom.
IPR006381. HAD-SF-IIB-MPGP.
IPR006379. HAD-SF_hydro_IIB.
IPR012815. MPG_Pase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 2 hits.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.

Sequencei

Sequence statusi: Complete.

O58690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRLIFLDID KTLIPGYEPD PAKPIIEELK DMGFEIIFNS SKTRAEQEYY
60 70 80 90 100
RKELEVETPF ISENGSAIFI PKGYFPFDVK GKEVGNYIVI ELGIRVEKIR
110 120 130 140 150
EELKKLENIY GLKYYGNSTK EEIEKFTGMP PELVPLAMER EYSETIFEWS
160 170 180 190 200
RDGWEEVLVE GGFKVTMGSR FYTVHGNSDK GKAAKILLDF YKRLGQIESY
210 220 230 240
AVGDSYNDFP MFEVVDKAFI VGSLKHKKAQ NVSSIIDVLE VIK
Length:243
Mass (Da):27,959
Last modified:August 1, 1998 - v1
Checksum:iFE5EE94DCAAD3636
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30022.1.
PIRiH71082.
RefSeqiWP_010885016.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30022; BAA30022; BAA30022.
GeneIDi1443251.
KEGGipho:PH0926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30022.1.
PIRiH71082.
RefSeqiWP_010885016.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WZCX-ray1.90A/B1-243[»]
2ZOSX-ray1.70A/B1-243[»]
ProteinModelPortaliO58690.
SMRiO58690. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH0926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30022; BAA30022; BAA30022.
GeneIDi1443251.
KEGGipho:PH0926.

Phylogenomic databases

eggNOGiarCOG01215. Archaea.
COG3769. LUCA.
HOGENOMiHOG000224319.
KOiK07026.
OMAiPLAMERE.

Enzyme and pathway databases

UniPathwayiUPA00130; UER00193.
BioCyciMetaCyc:MONOMER-13379.
PHOR70601:GJWR-919-MONOMER.
BRENDAi3.1.3.70. 5244.
SABIO-RKO58690.

Miscellaneous databases

EvolutionaryTraceiO58690.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
HAMAPiMF_00617. MPGP_rel.
InterProiIPR023214. HAD-like_dom.
IPR006381. HAD-SF-IIB-MPGP.
IPR006379. HAD-SF_hydro_IIB.
IPR012815. MPG_Pase.
[Graphical view]
PfamiPF08282. Hydrolase_3. 2 hits.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes."
    Empadinhas N., Marugg J.D., Borges N., Santos H., da Costa M.S.
    J. Biol. Chem. 276:43580-43588(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  3. "Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii."
    Kawamura T., Watanabe N., Tanaka I.
    Acta Crystallogr. D 64:1267-1276(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR.

Entry informationi

Entry nameiMPGP_PYRHO
AccessioniPrimary (citable) accession number: O58690
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: August 1, 1998
Last modified: April 13, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.