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O35621 (PMM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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:
Phosphomannomutase 1

Short name=PMM 1
EC=5.4.2.8
Gene names
Name:Pmm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length262 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. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain. Ref.3

Catalytic activity

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Cofactor

Magnesium By similarity.

Enzyme regulation

IMP, a metabolite whose concentration is elevated in anoxia, inhibits phosphomannomutase and phosphoglucomutase activities and strongly enhances glucose-1,6-bisphosphatase activity. Ref.3

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Ref.2.

Tissue specificity

Present in brain, where it is restricted to neuronal cell bodies. Present at lower levels in pancreas, liver, lung, gonads, uterus, adrenal glands and pituitary (at protein level). Undetectable in intestine. Ref.2

Developmental stage

Highly expressed at E17 in most organs (at protein level). Ref.2

Disruption phenotype

Mice are viable and fertile and develop normally. Ref.2

Sequence similarities

Belongs to the eukaryotic PMM family.

Biophysicochemical properties

Kinetic parameters:

KM=17 µM for glucose-1,6-bisphosphate in the presence of 1 µM IMP Ref.3

KM=40 µM for glucose-1,6-bisphosphate in the presence of 20 µM IMP

Vmax=2.1 µmol/min/mg enzyme with glucose-1,6-bisphosphate as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 262261Phosphomannomutase 1
PRO_0000199693

Sites

Active site191Nucleophile By similarity
Active site211Proton donor/acceptor Potential
Metal binding191Magnesium By similarity
Metal binding211Magnesium; via carbonyl oxygen By similarity
Metal binding2181Magnesium By similarity
Binding site281Substrate By similarity
Binding site1321Substrate By similarity
Binding site1431Substrate By similarity
Binding site1501Substrate By similarity
Binding site1861Substrate; via amide nitrogen By similarity
Binding site1881Substrate By similarity
Binding site1901Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
O35621 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2967154C0FF292B0

FASTA26229,775
        10         20         30         40         50         60 
MAVAVEGARR KERILCLFDV DGTLTPARQK IDPEVSAFLQ KLRSRVQIGV VGGSDYSKIA 

        70         80         90        100        110        120 
EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR 

       130        140        150        160        170        180 
LPKKRGTFIE FRNGMLNVSP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR 

       190        200        210        220        230        240 
FSRGGMISFD VFPEGWDKRY CLDSLDEDSF DIIHFFGNET SPGGNDFEIY ADPRTVGHSV 

       250        260 
VSPQDTVQRC RELFFPETAH EA 

« Hide

References

[1]Janoueix-Lerosey I., Goud B.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not essential for normal mouse development."
Cromphout K., Vleugels W., Heykants L., Schollen E., Keldermans L., Sciot R., D'Hooge R., De Deyn P.P., von Figura K., Hartmann D., Korner C., Matthijs G.
Mol. Cell. Biol. 26:5621-5635(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
[3]"Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase."
Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G., Van Schaftingen E.
J. Biol. Chem. 283:33988-33993(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007267 mRNA. Translation: AAB62943.1.
RefSeqNP_038900.1. NM_013872.4.
UniGeneMm.18939.

3D structure databases

ProteinModelPortalO35621.
SMRO35621. Positions 13-258.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO35621.

Proteomic databases

PaxDbO35621.
PRIDEO35621.

Protocols and materials databases

DNASU29858.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023112; ENSMUSP00000023112; ENSMUSG00000022474.
GeneID29858.
KEGGmmu:29858.
UCSCuc007wxt.2. mouse.

Organism-specific databases

CTD5372.
MGIMGI:1353418. Pmm1.

Phylogenomic databases

eggNOGCOG0561.
HOGENOMHOG000181843.
HOVERGENHBG009971.
InParanoidO35621.
KOK17497.
OMANDYEIYD.
OrthoDBEOG773XH0.
PhylomeDBO35621.
TreeFamTF300874.

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.

Gene expression databases

ArrayExpressO35621.
BgeeO35621.
CleanExMM_PMM1.
GenevestigatorO35621.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERPTHR10466. PTHR10466. 1 hit.
PfamPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPMM1. mouse.
NextBio307058.
PROO35621.
SOURCESearch...

Entry information

Entry namePMM1_MOUSE
AccessionPrimary (citable) accession number: O35621
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot