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A7Z0V3 (GLMM_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:RBAM_002300
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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_1000068888

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
A7Z0V3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: EC1730DB9F0191A0

FASTA44848,443
        10         20         30         40         50         60 
MGKYFGTDGV RGVANSELTP ELAFKVGRFG GYVLTKDKQR PKVLIGRDTR ISGHMLEGAL 

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

       130        140        150        160        170        180 
DEQEAEIERL MDEPEDKLPR PTGADLGLVN DYFEGVQKYL QFLKQTADED FTGIHVALDC 

       190        200        210        220        230        240 
AHGATSSIAT HLFADLDADV STMGTSPNGL NINDGVGSTH PEALSAFVKE KNADIGLAFD 

       250        260        270        280        290        300 
GDGDRLIAVD EKGNIVDGDQ IMYICAKYLK SEGRLKDDTV VSTVMSNLGF YKALEKEEIK 

       310        320        330        340        350        360 
SVQTAVGDRY VVEAMKKDGY NVGGEQSGHL IFLDYNTTGD GLLSAIMLVN TLKASGKTLS 

       370        380        390        400        410        420 
ELADEMKKFP QLLVNVKVTD KYKVEENAKV KAVISEVEKE MNGDGRILVR PSGTEPLVRV 

       430        440 
MAEARTKELC DEYVTKIVDV VRTEMGAE 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS72629.1.
RefSeqYP_001419860.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z0V3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z0V3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000004693; EBBACP00000004571; EBBACG00000004685.
GeneID5460130.
GenomeReviewsGene locus RBAM_002300 in contig CP000560_GR.
KEGGbay:RBAM_002300.
PATRIC18745351. VBIBacAmy31356_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00070000032132.
HOGENOMHBG644964.
OMAPLEDIQV.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycBAMY326423:RBAM_002300-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_BACA2
AccessionPrimary (citable) accession number: A7Z0V3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 33 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