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Reviewed, UniProtKB/Swiss-Prot A9VPC3 (GLMM_BACWK)

Last modified November 3, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Ordered Locus Names: BcerKBAB4_0151
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation By similarity.

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: UniProtKB-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Phosphoglucosamine mutase HAMAP MF_01554
PRO_1000201062

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
A9VPC3-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: F7A65942A25FF861

FASTA44848,358
        10         20         30         40         50         60 
MGKYFGTDGV RGVANKELTP ELAFKIGRFG GYVLTKDTDR PKVIIGRDTR VSGHMLEGAL 

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

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

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

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

       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 
MAEAPTQEIC DGYVHRIVEV VKAEVGAE 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000903 Genomic DNA. Translation: ABY41420.1.
RefSeqYP_001643048.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5840175.
GenomeReviewsGene locus BcerKBAB4_0151 in contig CP000903_GR.
KEGGbwe:BcerKBAB4_0151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANTIPEDL.

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_BACWK
AccessionPrimary (citable) accession number: A9VPC3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents