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B1HMT3 (GLMM_LYSSC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. 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:Bsph_4565
OrganismLysinibacillus sphaericus (strain C3-41) [Complete proteome] [HAMAP]
Taxonomic identifier444177 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus ›

Protein attributes

Sequence length450 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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000201117

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1HMT3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 9F3FDFF05E214896

FASTA45048,165
        10         20         30         40         50         60 
MGKYFGTDGV RGVANSELTP EFAFKLGRIG GYVLTKDATD RPKVLIGRDT RISGEMLEGA 

        70         80         90        100        110        120 
LVAGLLSIGV EVMRLGIIST PGVAYLTRIM SADAGVMISA SHNPVADNGI KFFGPDGFKL 

       130        140        150        160        170        180 
TDAQEEEIEV LLDAQEDTLP RPIGADLGSV SDYFEGGQKY IQYLKQTVDE EFDGIHVALD 

       190        200        210        220        230        240 
CAHGATSSLA THLFADLEAD ISTMGSSPNG LNINDGVGST HPEGLAKFVL EKDADVGLAF 

       250        260        270        280        290        300 
DGDGDRLIAV DENGKIVDGD QIMFIIGKYL NAVGRLKKQT IVSTVMSNMG FYKAVEDNGM 

       310        320        330        340        350        360 
QSIQTAVGDR YVVEEMRAND YNLGGEQSGH IVFLDFNTTG DGLLTGIQLV NIMKATGKKL 

       370        380        390        400        410        420 
SELAAEMKIY PQRLVNVRVT DKHAVTENTK VAAVIAEVEA AMAGNGRVLV RPSGTEPLVR 

       430        440        450 
VMVEAATETA CERFVERIAD VVRAEMGLTD

« Hide

References

[1]"Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species."
Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z.
J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C3-41.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000817 Genomic DNA. Translation: ACA42011.1.
RefSeqYP_001700141.1. NC_010382.1.

3D structure databases

ProteinModelPortalB1HMT3.
ModBaseSearch...

Protein-protein interaction databases

STRING444177.Bsph_4565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA42011; ACA42011; Bsph_4565.
GeneID6023252.
KEGGlsp:Bsph_4565.
PATRIC22421631. VBILysSph89750_4642.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMASGHIILF.

Enzyme and pathway databases

BioCycLSPH444177:GJEL-4557-MONOMER.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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_LYSSC
AccessionPrimary (citable) accession number: B1HMT3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 38 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

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