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Q73F50 (GLMM_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:BCE_0157
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length448 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 – 448448Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147840

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73F50 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F871074D653A57A6

FASTA44848,417
        10         20         30         40         50         60 
MGKYFGTDGV RGVANQELTP ELAFKIGRFG GYVLTKDTDR PKVIIGRDTR ISGHMLEGAL 

        70         80         90        100        110        120 
VAGLLSTGAE VMRLGVISTP GVAYLTKALD AQAGVMISAS HNPVQDNGIK FFGSDGFKLT 

       130        140        150        160        170        180 
DEQEAEIEAL LDKEVDELPR PTGTNLGQVS DYFEGGQKYL QYIKQTVEED FSGLHIALDC 

       190        200        210        220        230        240 
AHGATSSLAP YLFADLEADI STMGTSPNGM NINDGVGSTH PEVLAELVKE KGADIGLAFD 

       250        260        270        280        290        300 
GDGDRLIAVD EKGNIVDGDQ IMFICAKYMK ETGQLKHNTV VSTVMSNLGF YKALEANGIT 

       310        320        330        340        350        360 
SDKTAVGDRY VMEEMKRGGY NLGGEQSGHI ILLDYITTGD GMLSALQLVN IMKMTKKPLS 

       370        380        390        400        410        420 
ELAGEMTKFP QLLVNVRVTD KKLALENEKI KEIIRVVEEE MNGDGRILVR PSGTEPLIRV 

       430        440 
MAEAPTQEVC DAYVHRIVEV VKAEVGAE 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS39093.1.
RefSeqNP_976485.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ73F50.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ73F50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000027863; EBBACP00000027213; EBBACG00000027854.
GeneID2749790.
GenomeReviewsGene locus BCE_0157 in contig AE017194_GR.
KEGGbca:BCE_0157.
NMPDRfig|222523.1.peg.157.
PATRIC18849158. VBIBacCer118379_0151.
TIGRBCE_0157.

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00070000032132.
HOGENOMHBG644964.
OMAPLEDIQV.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycBCER405917:BCE_0157-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_BACC1
AccessionPrimary (citable) accession number: Q73F50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 56 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