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Q66WM4 (MPI_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:pmi1
Synonyms:manA
ORF Names:AfA6E3.135c, AFUA_1G13280
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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 By similarity.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mannose metabolic process

Inferred from mutant phenotype PubMed 19574302. Source: ASPGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmannose-6-phosphate isomerase activity

Inferred from direct assay PubMed 19574302. Source: ASPGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Mannose-6-phosphate isomerase
PRO_0000194240

Sites

Active site3111 By similarity
Metal binding1081Zinc By similarity
Metal binding1101Zinc By similarity
Metal binding1351Zinc By similarity
Metal binding2921Zinc By similarity

Experimental info

Sequence conflict801I → V in AAU06585. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q66WM4 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 27C3E5F425BAA224

FASTA45749,930
        10         20         30         40         50         60 
MPPVPLLRLQ CGVNSYDWGK VGHESAAAKY AATTAASDFS IQSDKPYAEL WMGTHPSLPS 

        70         80         90        100        110        120 
KDLETQRTLL DMVQDNQALI SQEVSERYGG KLPFLFKVLS IRKALSIQAH PNKKLAEKLH 

       130        140        150        160        170        180 
ARDPRNYPDD NHKPEMTIAI TPFEGLCGFR PLVEIIHFLK AVAPLRQLVG ERAASEFENT 

       190        200        210        220        230        240 
VKGSEESEDP AVTEKNKQAL RTLFTSLMRS SPESIEAATK ELVAIAQNSP ETFTTSSSTP 

       250        260        270        280        290        300 
ETNPTNPAEL AAITVRLNGQ FPNDIGSFVF FFLNFVKLEP GEAMFLKADD IHAYISGDII 

       310        320        330        340        350        360 
ECMASSDNVV RAGFTPKFKD VDTLVDMLTY SYAPIAEQKL EPTDYPYAVL NAPAYSSGSS 

       370        380        390        400        410        420 
CILYDPPIEE FSVVKTDLKR QGAKATFDGI SGPSIVICTA GAGKITVGPK TEEVNEGYVF 

       430        440        450 
FVGANAECII ESTGEDTFTT FKAFCDLTGK EDMVNGN 

« Hide

References

« Hide 'large scale' references
[1]"Aspergillus fumigatus strain YJ-407 phosphomannose isomerase (pmi) mRNA."
Yu X., Jin C.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: YJ-407.
[2]"Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb region encompassing the nitrate assimilation gene cluster."
Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M., Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S., O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A., Salzberg S.L. expand/collapse author list , Saunders D., Seeger K., Sharp S., Warren T., Denning D.W., Barrell B.G., Hall N.
Fungal Genet. Biol. 41:443-453(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[3]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY700212 mRNA. Translation: AAU06585.1.
BX649606 Genomic DNA. Translation: CAF32047.1.
AAHF01000004 Genomic DNA. Translation: EAL90660.1.
RefSeqXP_752698.1. XM_747605.1.

3D structure databases

ProteinModelPortalQ66WM4.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ66WM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007084; CADAFUAP00007084; CADAFUAG00007084.
GeneID3510576.
KEGGafm:AFUA_1G13280.

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000241277.
KOK01809.
OMAPYAEFWV.
OrthoDBEOG7WDNCR.

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.
PS00966. PMI_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPI_ASPFU
AccessionPrimary (citable) accession number: Q66WM4
Secondary accession number(s): Q4WSC2, Q6MYF6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 13, 2013
This is version 76 of the entry and version 2 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