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B1M3G3 (GLMM_METRJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:Mrad2831_4337
OrganismMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831) [Complete proteome] [HAMAP]
Taxonomic identifier426355 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length447 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 – 447447Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201119

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1M3G3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: A9AB96D9DD5898AD

FASTA44748,316
        10         20         30         40         50         60 
MVRKYFGTDG IRGRANGVIT PELALKVGQA AGLVFQRGDH RHRVVIGKDT RLSGYMIETA 

        70         80         90        100        110        120 
LVAGFTSVGM DVLLLGPVPT PAVAMLTRSM RADLGVMISA SHNPFEDNGI KLFGPDGFKL 

       130        140        150        160        170        180 
NDAIEHEIEG LIDADMHKRL SGSNDLGRAK RIESVHARYI EFAKRTLPRQ VTLDGLRVVV 

       190        200        210        220        230        240 
DCANGAAYRV APETLWELGA EVIAIGTEPD GFNINRDVGS TAPAALIDMV RERRADIGIA 

       250        260        270        280        290        300 
LDGDADRVLI VDEKGQVVDG DQLMAVVARS WKEDERLTQP GVVATIMSNL GLERFLGGLG 

       310        320        330        340        350        360 
LSLARTAVGD RYVLEHMRAH GYNLGGEQSG HIIMSDYTTT GDGLVAALQL LSVVQRQNRP 

       370        380        390        400        410        420 
VSEVCHCFDP LPQILKNVRY RSGEPLREDS VVSAIEHARE RLGNAGRLVI RPSGTEPVIR 

       430        440 
VMAEGDDRGL VNAVVDEVVD AVTRAAA 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium radiotolerans JCM 2831."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27329 / DSM 1819 / JCM 2831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001001 Genomic DNA. Translation: ACB26303.1.
RefSeqYP_001756986.1. NC_010505.1.

3D structure databases

ProteinModelPortalB1M3G3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1M3G3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6140396.
GenomeReviewsGene locus Mrad2831_4337 in contig CP001001_GR.
KEGGmrd:Mrad2831_4337.
PATRIC22577092. VBIMetRad70578_4415.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAIGSAKRI.
ProtClustDBPRK14315.

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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_METRJ
AccessionPrimary (citable) accession number: B1M3G3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 27 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