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P29952 (MPI_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Mannose-6-phosphate isomerase

EC=5.3.1.8
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI
Gene names
Name:PMI40
Ordered Locus Names:YER003C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

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

Cofactor

Binds 1 zinc ion per subunit.

Enzyme regulation

Can be inhibited by an excess of zinc.

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.

Induction

By D-mannose.

Miscellaneous

Present with 5220 molecules/cell in log phase SD medium.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 429428Mannose-6-phosphate isomerase
PRO_0000194247

Sites

Active site3001 By similarity
Metal binding1091Zinc By similarity
Metal binding1111Zinc By similarity
Metal binding1361Zinc By similarity
Metal binding2811Zinc By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.1
Modified residue1071Phosphoserine Ref.6

Experimental info

Sequence conflict251A → R in AAA34872. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29952 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: C95E7C06B348A02F

FASTA42948,189
        10         20         30         40         50         60 
MSNKLFRLDA GYQQYDWGKI GSSSAVAQFA AHSDPSVQIE QDKPYAELWM GTHSKMPSYN 

        70         80         90        100        110        120 
HESKESLRDI ISKNPSAMLG KDIIDKFHAT NELPFLFKVL SIEKVLSIQA HPDKALGKIL 

       130        140        150        160        170        180 
HAQDPKNYPD DNHKPEMAIA VTDFEGFCGF KPLQEIADEL KRIPELRNIV GEETSRNFIE 

       190        200        210        220        230        240 
NIQPSAQKGS PEDEQNKKLL QAVFSRVMNA SDDKIKIQAR SLVERSKNSP SDFNKPDLPE 

       250        260        270        280        290        300 
LIQRLNKQFP DDVGLFCGCL LLNHCRLNAG EAIFLRAKDP HAYISGDIME CMAASDNVVR 

       310        320        330        340        350        360 
AGFTPKFKDV KNLVSMLTYT YDPVEKQKMQ PLKFDRSSGN GKSVLYNPPI EEFAVLETTF 

       370        380        390        400        410        420 
DEKLGQRHFE GVDGPSILIT TKGNGYIKAD GQKLKAEPGF VFFIAPHLPV DLEAEDEAFT 


TYRAFVEPN 

« Hide

References

« Hide 'large scale' references
[1]"PMI40, an intron-containing gene required for early steps in yeast mannosylation."
Smith D.J., Proudfoot A.E.I., Friedli L., Klig L.S., Paravicini G., Payton M.A.
Mol. Cell. Biol. 12:2924-2930(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Phosphomannose isomerase from Saccharomyces cerevisiae contains two inhibitory metal ion binding sites."
Wells T.N.C., Coulin F., Payton M.A., Proudfoot A.E.I.
Biochemistry 32:1294-1301(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY ZINC.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85238 Genomic DNA. Translation: AAA34872.1.
U18778 Genomic DNA. Translation: AAB64536.1.
BK006939 Genomic DNA. Translation: DAA07653.1.
PIRS50461.
RefSeqNP_010918.1. NM_001178894.1.

3D structure databases

ProteinModelPortalP29952.
SMRP29952. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36733. 18 interactions.
DIPDIP-6619N.
MINTMINT-2786830.
STRING4932.YER003C.

2D gel databases

UCD-2DPAGEP29952.

Proteomic databases

PaxDbP29952.
PeptideAtlasP29952.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER003C; YER003C; YER003C.
GeneID856720.
KEGGsce:YER003C.

Organism-specific databases

SGDS000000805. PMI40.

Phylogenomic databases

eggNOGCOG1482.
GeneTreeENSGT00390000016075.
HOGENOMHOG000241277.
KOK01809.
OMAPYAEFWV.
OrthoDBEOG7WDNCR.

Enzyme and pathway databases

BioCycYEAST:YER003C-MONOMER.
SABIO-RKP29952.
UniPathwayUPA00126; UER00423.

Gene expression databases

GenevestigatorP29952.

Family and domain databases

Gene3D2.60.120.10. 3 hits.
InterProIPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR10309. PTHR10309. 1 hit.
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSPR00714. MAN6PISMRASE.
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR00218. manA. 1 hit.
PROSITEPS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982811.
PROP29952.

Entry information

Entry nameMPI_YEAST
AccessionPrimary (citable) accession number: P29952
Secondary accession number(s): D3DLP9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways