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P31353 (PMM_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphomannomutase

Short name=PMM
EC=5.4.2.8
Gene names
Name:PMM1
ORF Names:CaO19.10454, CaO19.2937
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.

Catalytic activity

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the eukaryotic PMM family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGDP-mannose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mannose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphomannomutase activity

Inferred from genetic interaction Ref.1. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Phosphomannomutase
PRO_0000199701

Sites

Active site161Nucleophile By similarity
Active site181Proton donor/acceptor Potential
Binding site251Substrate By similarity
Binding site1271Substrate By similarity
Binding site1381Substrate By similarity
Binding site1451Substrate By similarity
Binding site1831Substrate By similarity
Binding site1851Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P31353 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 25455FC315D85212

FASTA25229,019
        10         20         30         40         50         60 
MSFANKQDPK TLVLFDVDGT LTPARLTISE EMKKTLEKLR EKVVIGFVGG SDLSKQVEQL 

        70         80         90        100        110        120 
GPNVLNDFDY CFSENGLTAY KLGKELASQS FINWIGNEKY NKLVKFILRY LSDIDLPIRR 

       130        140        150        160        170        180 
GTFIEFRNGM INVSPIGRNA STQERNDYEK FDKQHHIRET MVEALKKEFP DFGLTYSIGG 

       190        200        210        220        230        240 
QISFDVFPTG WDKTYCLQHV EDEHFENIHF FGDKSYKGGN DYEIYNDPRT IGHAVNSPDD 

       250 
TIRILNETFK LQ 

« Hide

References

« Hide 'large scale' references
[1]"The Candida albicans PMM1 gene encoding phosphomannomutase complements a Saccharomyces cerevisiae sec 53-6 mutation."
Smith D.J., Cooper M., De Tiani M., Losberger C., Payton M.A.
Curr. Genet. 22:501-503(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96770 Genomic DNA. Translation: AAA34356.1.
AACQ01000017 Genomic DNA. Translation: EAL02356.1.
AACQ01000015 Genomic DNA. Translation: EAL02637.1.
RefSeqXP_721164.1. XM_716071.1.
XP_721436.1. XM_716343.1.

3D structure databases

ProteinModelPortalP31353.
SMRP31353. Positions 10-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0006021.

2D gel databases

COMPLUYEAST-2DPAGEP31353.

Proteomic databases

PRIDEP31353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3636852.
3637067.
KEGGcal:CaO19.10454.
cal:CaO19.2937.

Organism-specific databases

CGDCAL0006021. PMM1.

Phylogenomic databases

eggNOGCOG0561.
KOK17497.
OrthoDBEOG7X3R31.

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERPTHR10466. PTHR10466. 1 hit.
PfamPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePMM_CANAL
AccessionPrimary (citable) accession number: P31353
Secondary accession number(s): Q5AIB6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 11, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names