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Q65P47 (GLMM_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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:BLi00203, BL02703
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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.

Sequence caution

The sequence AAU39167.1 differs from that shown. Reason: Erroneous initiation.

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_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 [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].
Strain: DSM 13 / ATCC 14580.
[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:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017333 Genomic DNA. Translation: AAU39167.1. Different initiation.
CP000002 Genomic DNA. Translation: AAU21822.1.
RefSeqYP_077460.1. NC_006270.3.
YP_089860.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65P47.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65P47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000055820; EBBACP00000054351; EBBACG00000055811.
EBBACT00000059456; EBBACP00000057889; EBBACG00000059447.
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.
PATRIC18945889. VBIBacLic203714_0183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00070000032132.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ65P47.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI00203-MONOMER.
BLIC279010:BL02703-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_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: January 25, 2012
This is version 55 of the entry and version 2 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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