Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O43014 (MPI_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. 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:
Mannose-6-phosphate isomerase

EC=5.3.1.8
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI
Gene names
Name:pmi40
ORF Names:SPBC2G2.16
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

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

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Mannose-6-phosphate isomerase
PRO_0000314774

Sites

Active site2841 By similarity
Metal binding991Zinc By similarity
Metal binding1011Zinc By similarity
Metal binding1261Zinc By similarity
Metal binding2651Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
O43014 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: E1B4685C02B25C89

FASTA41245,590
        10         20         30         40         50         60 
MYRLKCDVKS YGWGKVGHES LAAKLAEAGY GFEVDPNTPY AELWMGSHPS GPSFVMQTGK 

        70         80         90        100        110        120 
PLSELLTPET VGEKVYKKYG KQLPFLFKVL SINKVLSIQA HPDKPLGKQL HKTNPKEYKD 

       130        140        150        160        170        180 
DNHKPEMAVA LTEFDALCGF RPVKQIEQFL DSIAPLREFV GEEAVRQFKG TVKQDERKAL 

       190        200        210        220        230        240 
ETLFNELMHK DEKRIQEFTP QLVQLAKSDA NNFGGTEYGG KAFSDLIIHL NSQFPDDIGL 

       250        260        270        280        290        300 
FVTPFLNYVR LHPGEAVFLR ALDPHAYVSG NIIECMAASD NVIRLGFTPK FKDIETLVNN 

       310        320        330        340        350        360 
LTYQTADAKS QLTQPVPFAK ACGSGKTLLY DPPIEEFSIL QTKVSPGQKQ CIRGINGPSI 

       370        380        390        400        410 
LLVTEGSGIL NGDKGDVASI SPGFVYFISA NFPLTISATS EPVVVYQAFC EI 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA17896.1.
PIRT40155.
RefSeqNP_596445.1. NM_001022364.2.

3D structure databases

ProteinModelPortalO43014.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4674647.
STRING4896.SPBC2G2.16-1.

Proteomic databases

MaxQBO43014.
PaxDbO43014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC2G2.16.1; SPBC2G2.16.1:pep; SPBC2G2.16.
GeneID2540428.
KEGGspo:SPBC2G2.16.

Organism-specific databases

PomBaseSPBC2G2.16.

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000241277.
KOK01809.
OMAQGEPWDT.
OrthoDBEOG7WDNCR.
PhylomeDBO43014.

Enzyme and pathway databases

UniPathwayUPA00126; UER00423.

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.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801555.
PROO43014.

Entry information

Entry nameMPI_SCHPO
AccessionPrimary (citable) accession number: O43014
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 1998
Last modified: May 14, 2014
This is version 94 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways