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Q1GB12 (GLMM_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:Ldb0654
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length450 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 – 450450Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301328

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GB12 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 610BE77A2C190B12

FASTA45048,869
        10         20         30         40         50         60 
MLKYFGTDGV RGEANKVLTP EMAFKLGRMG GYVLTKEKED GGQARVLVSR DTRISGEMLE 

        70         80         90        100        110        120 
HALISGLLSV GIEVLECGVM TTPGLSYLVQ AQGADAGVQI SASHNPVEDN GIKFFGSNGL 

       130        140        150        160        170        180 
KLSDAKEEEI EELIDTKQDM LPRPSAEGLG TVTDFRDGSN KYIQFLENTI PEDLSGIKVV 

       190        200        210        220        230        240 
IDGANGAASA FISRLFADLD VDFTTISTHL NGLNINDHCG ATHTARLQEE VVKQGAQLGL 

       250        260        270        280        290        300 
AFDGDADRCI AVDENGNEVD GDHIMYVIGS YLADHGRLKK DTIVTTVMSN LGFTKALERR 

       310        320        330        340        350        360 
GIKNVRTQVG DRYVSEEMRA NGYSLGGEQS GHVIISDYHN TGDGMLTGLH LMLVMKKTGK 

       370        380        390        400        410        420 
SLTELLADFK EYPQVLVNVP VKDKNSWKNH QAVVDAIDSV EKDMAGNGRV LVRPSGTQEL 

       430        440        450 
LRVMAEGPTQ EITQEYVDRI VKVVTTEMGE 

« Hide

References

[1]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed: 16754859] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954253 Genomic DNA. Translation: CAI97483.1.
RefSeqYP_618728.1. NC_008054.1.

3D structure databases

ProteinModelPortalQ1GB12.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1GB12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4085382.
GenomeReviewsGene locus Ldb0654 in contig CR954253_GR.
KEGGldb:Ldb0654.
PATRIC22216911. VBILacDel123523_0601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMALENTIPE.
PhylomeDBQ1GB12.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycLDEL390333:LDB0654-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_LACDA
AccessionPrimary (citable) accession number: Q1GB12
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 45 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