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

P29951 (MPI_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 100. 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:manA
ORF Names:AN0667
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length461 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.

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 Probable.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Mannose-6-phosphate isomerase
PRO_0000194244

Sites

Active site3101 By similarity
Metal binding1071Zinc By similarity
Metal binding1091Zinc By similarity
Metal binding1341Zinc By similarity
Metal binding2911Zinc By similarity

Experimental info

Sequence conflict191R → K in AAA33319. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29951 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 17E0D089A6656F79

FASTA46150,613
        10         20         30         40         50         60 
MQVPLLRLQC GVNSYDWGRV GPESAAAKYA AATAPSDFTI EADKPYAELW MGTHPSLPSK 

        70         80         90        100        110        120 
DVETQRTLLD MVQDNLALMS PEVSERYGGK LPFLFKVLSI RKALSIQAHP NKKLAEALHA 

       130        140        150        160        170        180 
RDPRNYPDDN HKPEMTIAIT PFEGLCGFRP LAEIVHFLKA VAPLRYLIGV QTATDFENAV 

       190        200        210        220        230        240 
RGFENTEDPE QTKKNKVALR TLFTSLMQSA SENIEQAARE LVAAAQSSPE TFASLVNAPD 

       250        260        270        280        290        300 
TNPTNAAELA SIIIRLNEQF PNDIGLFVFF FLNFVRLEPG EAMFLKADDI HAYISGDIIE 

       310        320        330        340        350        360 
CMASSDNVVR AGFTPKFKDV DTLTEMLTYS YAPIDEQKLQ PTDYPYTVLN AAAYSSASDS 

       370        380        390        400        410        420 
LLYDPPIEEF SVVKTSLRRT GAKATFDPLT GPSILICTGG TGKISVGHKT EEVKEGYVFF 

       430        440        450        460 
VGANAECIIE NTGTGSDEEN VFTTFKAFCD LTGKEDMANG H 

« Hide

References

« Hide 'large scale' references
[1]"Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase."
Proudfoot A.E.I., Turcatti G., Wells T.N.C., Payton M.A., Smith D.J.
Eur. J. Biochem. 219:415-423(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M85239 Genomic DNA. Translation: AAA33319.1.
AACD01000010 Genomic DNA. Translation: EAA65443.1.
BN001308 Genomic DNA. Translation: CBF89025.1.
PIRA56239.
RefSeqXP_658271.1. XM_653179.1.

3D structure databases

ProteinModelPortalP29951.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00002007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00002007; CADANIAP00002007; CADANIAG00002007.
GeneID2876445.
KEGGani:AN0667.2.

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000241277.
KOK01809.
OMAPYAEFWV.

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_EMENI
AccessionPrimary (citable) accession number: P29951
Secondary accession number(s): C8VRS9, Q5BFL3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 1, 2007
Last modified: January 22, 2014
This is version 100 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