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Reviewed, UniProtKB/Swiss-Prot O58689 (MPGS_PYRHO)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 synthase
      Short name=MPG synthase
      Short name=MPGS
    EC=2.4.1.217
Gene names
Name: mngA
Ordered Locus Names: PH0927
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Transfers a mannosyl group from GDP-mannose to phosphoglycerate to form mannosyl-3-phosphoglycerate (MPG). The enzyme is absolutely specific for GDP-mannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration.

Catalytic activity

GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate.

Cofactor

Magnesium.

Pathway

Carbohydrate biosynthesis; mannosylglycerate biosynthesis; 2(alpha-D-mannosyl)-D-glycerate from GDP-D-mannose (MPG route): step 1/2.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete 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 synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Mannosyl-3-phosphoglycerate synthase
PRO_0000059287

Sequences

Sequence LengthMass (Da)Tools
O58689-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6C2FB4141D2CC807

FASTA39445,210
        10         20         30         40         50         60 
MLLEAPVYKE IFGAVTIHEV QKVIKMDTET EEVPIYTISN IPREKIYDLL GKMAVIVPMK 

        70         80         90        100        110        120 
NEKLHLVDGV LKAIPHKCPI IIVSNSKREG PNRYKLEVDL IRHFYNLTHS KIIMIHQKDP 

       130        140        150        160        170        180 
GLAKAFKEVG YTDILDENGM IRSGKGEGML VGLLLAKAIG AEYVGFVDAD NYIPGAVNEY 

       190        200        210        220        230        240 
VKDYAAGFLM SESEYTMVRL HWRHKPKVTK GTLYFKKWGR VSEITNHYLN LLVSEHTAFE 

       250        260        270        280        290        300 
TTIMVTGNAG EHAMTMKLAE ILPFSTGYSI EPYEIVYILE RFGKWENVEE FKDVFDQGIE 

       310        320        330        340        350        360 
IFQIETLNPH FHEDKGKEHV KEMLLLSLAT IYHSKLATDN LRKRILKDLR DHGILGENEE 

       370        380        390 
PPKPLVMRPI KEIPIKEWMD IVEGNSETLL RFEL 

« 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.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA30023.1.
PIRA71083.
RefSeqNP_142850.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT55. Glycosyltransferase Family 55.

Genome annotation databases

GeneID1443252.
GenomeReviewsGene locus PH0927 in contig BA000001_GR.
KEGGpho:PH0927.
NMPDRfig|70601.1.peg.905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58689.
OMAO58689. EIFQIET.

Enzyme and pathway databases

BioCycMetaCyc:MON-13380.
BRENDA2.4.1.217. 74679.

Family and domain databases

InterProIPR012812. Osmo_MPG_synth.
[Graphical view]
PfamPF09488. Osmo_MPGsynth. 1 hit.
[Graphical view]
TIGRFAMsTIGR02460. osmo_MPGsynth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMPGS_PYRHO
AccessionPrimary (citable) accession number: O58689
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 48 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

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