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Reviewed, UniProtKB/Swiss-Prot P34948 (MPI_CANAL)

Last modified February 9, 2010. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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Names and origin

Protein namesRecommended name:
    Mannose-6-phosphate isomerase
    EC=5.3.1.8
Alternative name(s):
    Phosphomannose isomerase
      Short name=PMI
    Phosphohexomutase
Gene names
Name: PMI1
Synonyms: MANA
ORF Names: CaO19.1390
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

D-mannose 6-phosphate = D-fructose 6-phosphate.

Cofactor

Binds 1 zinc ion per subunit.

Pathway

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

Subunit structure

Monomer.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 1 family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmannose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 441440Mannose-6-phosphate isomerase
PRO_0000194241

Sites

Active site3041 Ref.4
Metal binding1111Zinc
Metal binding1131Zinc
Metal binding1381Zinc
Metal binding2851Zinc
Site1501Its modification inactivates the enzyme

Secondary structure

1 ..................................................................................... 441
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P34948-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AEDDE2AE9EDAD5EC

FASTA44148,867
        10         20         30         40         50         60 
MSSEKLFRIQ CGYQNYDWGK IGSSSAVAQF VHNSDPSITI DETKPYAELW MGTHPSVPSK 

        70         80         90        100        110        120 
AIDLNNQTLR DLVTAKPQEY LGESIITKFG SSKELPFLFK VLSIEKVLSI QAHPDKKLGA 

       130        140        150        160        170        180 
QLHAADPKNY PDDNHKPEMA IAVTDFEGFC GFKPLDQLAK TLATVPELNE IIGQELVDEF 

       190        200        210        220        230        240 
ISGIKLPAEV GSQDDVNNRK LLQKVFGKLM NTDDDVIKQQ TAKLLERTDR EPQVFKDIDS 

       250        260        270        280        290        300 
RLPELIQRLN KQFPNDIGLF CGCLLLNHVG LNKGEAMFLQ AKDPHAYISG DIIECMAASD 

       310        320        330        340        350        360 
NVVRAGFTPK FKDVKNLVEM LTYSYESVEK QKMPLQEFPR SKGDAVKSVL YDPPIAEFSV 

       370        380        390        400        410        420 
LQTIFDKSKG GKQVIEGLNG PSIVIATNGK GTIQITGDDS TKQKIDTGYV FFVAPGSSIE 

       430        440 
LTADSANQDQ DFTTYRAFVE A

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and heterologous expression of the Candida albicans gene PMI 1 encoding phosphomannose isomerase."
Smith D.J., Proudfoot A.E.I., de Tiani M., Wells T.N.C., Payton M.A.
Yeast 11:301-310(1995) [PubMed: 7785330] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 1006.
[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: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.
[3]"Identification of Cys-150 in the active site of phosphomannose isomerase from Candida albicans."
Coulin F., Magnenat E., Proudfoot A.E.I., Payton M.A., Scully P., Wells T.N.C.
Biochemistry 32:14139-14144(1993) [PubMed: 8260497] [Abstract]
Cited for: CHEMICAL LABELLING OF CYS-150, PARTIAL PROTEIN SEQUENCE.
[4]"Arginine 304 is an active site residue in phosphomannose isomerase from Candida albicans."
Wells T.N.C., Scully P., Magnenat E.
Biochemistry 33:5777-5782(1994) [PubMed: 8180205] [Abstract]
Cited for: ACTIVE SITE ARG-304, PROTEIN SEQUENCE OF 300-312.
[5]"The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7-A resolution."
Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J., Proudfoot A.E.I., Bernard A.R., Payton M.A., Wells T.N.C.
Nat. Struct. Biol. 3:470-479(1996) [PubMed: 8612079] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X82024 Genomic DNA. Translation: CAA57548.1.
AACQ01000101 Genomic DNA. Translation: EAK95509.1.
PIRS55354.
RefSeqXP_714562.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMIX-ray1.70A2-441[»]
ModBaseSearch...

Genome annotation databases

GeneID3643795.
KEGGcal:CaO19.1390.

Organism-specific databases

CGDCAL0003967. PMI1.

Phylogenomic databases

OMADFTVMKM.
OrthoDBEOG9SN352.
PhylomeDBP34948.

Enzyme and pathway databases

BRENDA5.3.1.8. 1124.

Family and domain databases

InterProIPR011051. Cupin_RmlC_type.
IPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 2 hits.
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSPR00714. MAN6PISMRASE.
TIGRFAMsTIGR00218. manA. 1 hit.
PROSITEPS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMPI_CANAL
AccessionPrimary (citable) accession number: P34948
Secondary accession number(s): Q59YD6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

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