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B1HMT3 (GLMM_LYSSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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 › 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 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 – 450450Phosphoglucosamine mutase HAMAP MF_01554_B
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: 18296527] [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

STRINGB1HMT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6023252.
GenomeReviewsGene locus Bsph_4565 in contig CP000817_GR.
KEGGlsp:Bsph_4565.
PATRIC22421631. VBILysSph89750_4642.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAIGSAKRI.

Enzyme and pathway databases

BioCycLSPH444177:BSPH_4565-MONOMER.

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_LYSSC
AccessionPrimary (citable) accession number: B1HMT3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 28 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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