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Reviewed, UniProtKB/Swiss-Prot O58690 (MPGP_PYRHO)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Mannosyl-3-phosphoglycerate phosphatase
      Short name=MPGP
    EC=3.1.3.70
Gene names
Name: mngB
Ordered Locus Names: PH0926
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes mannosyl-3-phosphoglycerate (MPG) to form the osmolyte mannosylglycerate (MG). The enzyme is absolutely specific for MPG. HAMAP MF_00617

Catalytic activity

2(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2(alpha-D-mannosyl)-D-glycerate + phosphate. HAMAP MF_00617

Cofactor

Magnesium. HAMAP MF_00617

Pathway

Carbohydrate biosynthesis; mannosylglycerate biosynthesis; 2(alpha-D-mannosyl)-D-glycerate from GDP-D-mannose (MPG route): step 2/2. HAMAP MF_00617

Subcellular location

Cytoplasm. HAMAP MF_00617

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmannosylglycerate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mannosyl-3-phosphoglycerate phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243Mannosyl-3-phosphoglycerate phosphatase HAMAP MF_00617
PRO_0000184973

Secondary structure

................................................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O58690-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: FE5EE94DCAAD3636

FASTA24327,959
        10         20         30         40         50         60 
MIRLIFLDID KTLIPGYEPD PAKPIIEELK DMGFEIIFNS SKTRAEQEYY RKELEVETPF 

        70         80         90        100        110        120 
ISENGSAIFI PKGYFPFDVK GKEVGNYIVI ELGIRVEKIR EELKKLENIY GLKYYGNSTK 

       130        140        150        160        170        180 
EEIEKFTGMP PELVPLAMER EYSETIFEWS RDGWEEVLVE GGFKVTMGSR FYTVHGNSDK 

       190        200        210        220        230        240 
GKAAKILLDF YKRLGQIESY AVGDSYNDFP MFEVVDKAFI VGSLKHKKAQ NVSSIIDVLE 


VIK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.
[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: 11562374] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA30022.1.
PIRH71082.
RefSeqNP_142849.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WZCX-ray1.90A/B1-243[»]
2ZOSX-ray1.70A/B1-243[»]
ModBaseSearch...

Genome annotation databases

GeneID1443251.
GenomeReviewsGene locus PH0926 in contig BA000001_GR.
KEGGpho:PH0926.
NMPDRfig|70601.1.peg.904.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58690.
OMAO58690. EYSETIF.

Enzyme and pathway databases

BioCycMetaCyc:MON-13379.
BRENDA3.1.3.70. 74679.

Family and domain databases

HAMAPMF_00617.
[Tree]
InterProIPR013200. HAD-SF_hydro-like_3.
IPR006379. HAD-SF_hydro_IIB.
IPR006381. HAD-SF_hydro_IIB_YedP.
IPR012813. Osmo_MPG_phos.
[Graphical view]
PfamPF08282. Hydrolase_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
TIGR01486. HAD-SF-IIB-MPGP. 1 hit.
TIGR02461. osmo_MPG_phos. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMPGP_PYRHO
AccessionPrimary (citable) accession number: O58690
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents