PMM1

Phosphomannomutase 1

PDB rendering based on 2fuc.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2FUC, 2FUE

Identifiers

PMM1 ; Sec53

External IDs

OMIM: 601786 MGI: 1353418 HomoloGene: 90898 GeneCards: PMM1 Gene

Gene ontology
Molecular function	• phosphomannomutase activity • metal ion binding
Cellular component	• cytosol • neuronal cell body
Biological process	• mannose metabolic process • dolichol-linked oligosaccharide biosynthetic process • GDP-mannose biosynthetic process • protein N-linked glycosylation via asparagine • mannose biosynthetic process • post-translational protein modification • cellular protein metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000100417

ENSMUSG00000022474

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
41.97 – 41.99 Mb

Chr 15:
81.95 – 81.96 Mb

PubMed search

Phosphomannomutase 1 is an enzyme that in humans is encoded by the PMM1 gene.^[1]^[2]^[3]

Phosphomannomutase catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins.^[3]

This enzyme has been extracted from the venom of the wasp species Polistes major major. ^[4]

References

↑ Matthijs G, Schollen E, Pirard M, Budarf ML, Van Schaftingen E, Cassiman JJ (Jun 1997). "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is localized on chromosome 22q13". Genomics 40 (1): 41–7. doi:10.1006/geno.1996.4536. PMID 9070917.
↑ Pirard M, Collet JF, Matthijs G, Van Schaftingen E (Sep 1997). "Comparison of PMM1 with the phosphomannomutases expressed in rat liver and in human cells". FEBS Lett 411 (2-3): 251–4. doi:10.1016/S0014-5793(97)00704-7. PMID 9271215.
↑ 3.0 3.1 "Entrez Gene: PMM1 phosphomannomutase 1".
↑ Identification of three novel peptides isolated from the venom of the neotropical social wasp Polistes major major/Vaclav Cerovsky/Jan Pohl/Zhihua Yang/Naseer Alam/Athula B. Attygalle

Further reading

Wada Y, Sakamoto M (1997). "Isolation of the human phosphomannomutase gene (PMM1) and assignment to chromosome 22q13.". Genomics 39 (3): 416–7. doi:10.1006/geno.1996.4487. PMID 9119384.
Hansen SH, Frank SR, Casanova JE (1997). "Cloning and characterization of human phosphomannomutase, a mammalian homologue of yeast SEC53.". Glycobiology 7 (6): 829–34. doi:10.1093/glycob/7.6.829. PMID 9376685.
Collet JF, Stroobant V, Pirard M et al. (1998). "A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif.". J. Biol. Chem. 273 (23): 14107–12. doi:10.1074/jbc.273.23.14107. PMID 9603909.
Pirard M, Achouri Y, Collet JF et al. (1999). "Kinetic properties and tissular distribution of mammalian phosphomannomutase isozymes.". Biochem. J. 339 (1): 201–7. doi:10.1042/0264-6021:3390201. PMC 1220145. PMID 10085245.
Dunham I, Shimizu N, Roe BA et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Jensen H, Kjaergaard S, Klie F, Moller HU (2003). "Ophthalmic manifestations of congenital disorder of glycosylation type 1a.". Ophthalmic Genet. 24 (2): 81–8. doi:10.1076/opge.24.2.81.13994. PMID 12789572.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Collins JE, Wright CL, Edwards CA et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Silvaggi NR, Zhang C, Lu Z et al. (2006). "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a.". J. Biol. Chem. 281 (21): 14918–26. doi:10.1074/jbc.M601505200. PMID 16540464.
Baumbusch LO, Myhre S, Langerød A et al. (2006). "Expression of full-length p53 and its isoform Deltap53 in breast carcinomas in relation to mutation status and clinical parameters.". Mol. Cancer 5: 47. doi:10.1186/1476-4598-5-47. PMC 1636663. PMID 17054774.
Barone R, Sturiale L, Fiumara A et al. (2007). "Borderline mental development in a congenital disorder of glycosylation (CDG) type Ia patient with multisystemic involvement (intermediate phenotype).". J. Inherit. Metab. Dis. 30 (1): 107. doi:10.1007/s10545-006-0486-6. PMID 17186415.

PDB gallery

2fuc: Human alpha-Phosphomannomutase 1 with Mg2+ cofactor bound

2fue: Human alpha-Phosphomannomutase 1 with D-mannose 1-phosphate and Mg2+ cofactor bound

Isomerase: mutases (EC 5.4)

5.4.1 Acyl Groups

5.4.2 Phosphomutases

5.4.99 Other groups

Biochemistry overview
Enzymes overview
By EC number: 1.1
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2.1
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  - 2.7.10
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3.1
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4.1
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5.1
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6.1-3
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