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Reviewed, UniProtKB/Swiss-Prot Q65P47 (GLMM_BACLD)

Last modified November 3, 2009. Version 38. 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: BLi00203, BL02703
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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_0000147845

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
Q65P47-1 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 5177B0EE99310578

FASTA44848,198
        10         20         30         40         50         60 
MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKER PKVLIGRDTR ISGHMLEGAL 

        70         80         90        100        110        120 
VAGLLSIGAE VMRLGVISTP GVAYLTKAMD AEAGVMISAS HNPVQDNGIK FFGGDGFKLS 

       130        140        150        160        170        180 
DEQELEIERL MDQPEDHLPR PVGADLGMVN DYFEGGQKYL QFLKQSADED FTGIHVALDC 

       190        200        210        220        230        240 
AHGATSSLAT HLFADLDADV STMGTSPNGL NINDGVGSTH PEALAEFVKE KGADVGMAFD 

       250        260        270        280        290        300 
GDGDRLIAVD EKGNIVDGDQ IMYICAKYLK SEGRLTDNTV VSTVMSNLGF YKALEAEGIK 

       310        320        330        340        350        360 
SVQTAVGDRY VVEAMKKGGF TLGGEQSGHL IFLDYNTTGD GLLSAIMLMN TIKMTGKPLS 

       370        380        390        400        410        420 
ELAAEMQKFP QLLLNVKVTD KHKVTENEKV KAVIEEVEKE MNGDGRILVR PSGTEPLVRV 

       430        440 
MAEAKTKELC EKYVGRIADV VKAEMGAE 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017333 Genomic DNA. Translation: AAU39167.1. Different initiation.
CP000002 Genomic DNA. Translation: AAU21822.1.
RefSeqYP_077460.1.
YP_089860.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ65P47.

Genome annotation databases

GeneID3028093.
3099927.
GenomeReviewsGene locus BLi00203 in contig AE017333_GR.
Gene locus BL02703 in contig CP000002_GR.
KEGGbld:BLi00203.
bli:BL02703.
NMPDRfig|279010.5.peg.1781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ65P47.
OMASTHPEAM.

Enzyme and pathway databases

BioCycBLIC279010:BL02703-MON.

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_BACLD
AccessionPrimary (citable) accession number: Q65P47
Secondary accession number(s): Q62ZI6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 3, 2009
This is version 38 of the entry and version 2 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