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Q9KG46 (GLMM_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:BH0267
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length447 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 – 447447Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000147844

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KG46 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AA9E7158685D4023

FASTA44748,120
        10         20         30         40         50         60 
MGKYFGTDGV RGVANTELTP ELAFKLGRIG GYVLTKDKEN PKVLIGRDTR ISGEMLEGAL 

        70         80         90        100        110        120 
VAGLLSIGVE VMRLGVISTP GVAFLTKAVS ASAGVMISAS HNPVADNGIK FFGPDGFKLL 

       130        140        150        160        170        180 
DEQEKEIETL LDQEDALPRP TGADLGQAND YFEGAQKYLQ FLKQTVDEDF TGIHIALDCA 

       190        200        210        220        230        240 
NGAASSLAPH LFADLEADIS TMGTSPNGKN INDGVGSTHP EALAAFVNAK NADIGLAFDG 

       250        260        270        280        290        300 
DADRLIAVDE KGNIVDGDKI LYICAKYMKE KGLLKQQTLV TTVMSNLGLY KALEALQIDT 

       310        320        330        340        350        360 
KQTAVGDRYV MEEMRKGGYN LGGEQSGHII FLDHITTGDG MLSALQLVNI MKQTGKKLSE 

       370        380        390        400        410        420 
LAEEWETFPQ TLVNIRVTDK HAVTDNEKVP AVIKEVEQEM NGEGRVLVRP SGTEPLVRIM 

       430        440 
VEAKTEELCD AFVNKIADVV KAELGQE 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB03986.1.
PIRC83683.
RefSeqNP_241133.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KG46.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000050406; EBBACP00000049045; EBBACG00000050397.
GeneID894435.
GenomeReviewsGene locus BH0267 in contig BA000004_GR.
KEGGbha:BH0267.
NMPDRfig|272558.1.peg.267.
PATRIC18937446. VBIBacHal18977_0282.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00070000032132.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBQ9KG46.
ProtClustDBCLSK2748835.

Enzyme and pathway databases

BioCycBHAL272558:BH0267-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_BACHD
AccessionPrimary (citable) accession number: Q9KG46
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 63 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