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A0PMD3 (GLMM_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:MUL_0866
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301344

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PMD3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: F1DCCEBF1A529ABC

FASTA44545,415
        10         20         30         40         50         60 
MGRLFGTDGV RGVANRELTA ELALALGAAT AQHLASSTGP GRRVAVVGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVIAGLTSQG VDALRVGVLP TPAVAYLTGA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 

       130        140        150        160        170        180 
LDDATENRIE SLVAAGPGLR PVGSEIGRVI DAEDAADRYL RHVSKACTTR LDGLTVVVDC 

       190        200        210        220        230        240 
AHGAASEVGP RAYRAAGARV IEINADPNGL NINDDCGSTH LEAIRAAVLA HGADLGVAHD 

       250        260        270        280        290        300 
GDADRCLAVD ANGDLVDGDA IMVVLALAMQ EAGELASDTL VTTVMSNLGL HLAMREAGVN 

       310        320        330        340        350        360 
VRTTGVGDRY VLEELRAGDY SLGGEQSGHI VMPGLGSTGD GIVTGLRLMT RMVATGASLA 

       370        380        390        400        410        420 
ALASRMQTLP QVLINVQVTD KATAAAAPSV QAAVDRAETE LGDTGRILLR PSGTEPLIRV 

       430        440 
MVEAADEEAA HRLATSVADA VSAAG 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL03502.1.
RefSeqYP_904973.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PMD3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PMD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000076936; EBMYCP00000074941; EBMYCG00000076931.
GeneID4553772.
GenomeReviewsGene locus MUL_0866 in contig CP000325_GR.
KEGGmul:MUL_0866.
PATRIC18168432. VBIMycUlc37413_1078.

Organism-specific databases

GenoListMUL_0866.
CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00050000015909.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
InterProIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
IPR016066. A-D-PHexomutase_CS.
IPR005841. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_MYCUA
AccessionPrimary (citable) accession number: A0PMD3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families