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Q1WSZ9 (GLMM_LACS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:LSL_1144
OrganismLactobacillus salivarius (strain UCC118) [Complete proteome] [HAMAP]
Taxonomic identifier362948 [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_0000305647

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1WSZ9 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: E69399029F7CAA74

FASTA45048,571
        10         20         30         40         50         60 
MKYFGTDGVR GIANETLSPE LAFKLGRCGG YVLTQHASNK PARVLVARDT RISGQMLEQA 

        70         80         90        100        110        120 
LIAGLLSVGI EVFSLGVMTT PGVAYLVRLQ DADAGIMISA SHNPVQDNGI KFFGSDGYKL 

       130        140        150        160        170        180 
SDEKEEEIEA LLESDEDTLP RPSAEGLGTL SDYREGALKY TQFLEQTIPD DLEGMHIAVD 

       190        200        210        220        230        240 
GANGSTSALV SRLFADLGAD FDTMATNPDG LNINKGVGST HPEALAKFVV EKGAQVGVAF 

       250        260        270        280        290        300 
DGDGDRCIAV DENGEIVDGD KIMFICGKYL SERGRLKKDT IVTTVMSNIG LYKAMKENNL 

       310        320        330        340        350        360 
NSVQTKVGDR YVVEAMRKDG YNVGGEQSGH VVFLDFNTTG DGMLTALQLL NVIKQTGKKL 

       370        380        390        400        410        420 
SELAAEVKTY PQELVNIKVT DKKAALDNEK IKEAIAKVEE KMAGDGRVLV RPSGTEDLLR 

       430        440        450 
VMAEAKTQEL VHDYVMEIAD VVEAEMGVNE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000233 Genomic DNA. Translation: ABD99952.1.
RefSeqYP_536035.1. NC_007929.1.

3D structure databases

ProteinModelPortalQ1WSZ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1WSZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3977884.
GenomeReviewsGene locus LSL_1144 in contig CP000233_GR.
KEGGlsl:LSL_1144.
PATRIC22279195. VBILacSal43464_1218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMAPLEDIQV.
PhylomeDBQ1WSZ9.
ProtClustDBPRK14316.

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_LACS1
AccessionPrimary (citable) accession number: Q1WSZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 2, 2006
Last modified: January 25, 2012
This is version 42 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