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Q5M3V8 (GLMM_STRT2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. 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:stu1251
OrganismStreptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP]
Taxonomic identifier264199 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation By similarity.

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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000147980

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5M3V8 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: E45BFD8A2BF4335A

FASTA45047,931
        10         20         30         40         50         60 
MGKYFGTDGV RGEANVELTP ELAFKLGRFG GYVLSQHETG RPKVFVARDT RISGEMLESA 

        70         80         90        100        110        120 
LVAGLLSVGI EVYKLGVLAT PGVSYLVRTE NASAGVMISA SHNPALDNGI KFFGGDGFKL 

       130        140        150        160        170        180 
DDAREAEIEA LLDAAEDTLP RPSAEGLGTL VDYPEGLRKY EKFLVTTGLD LGGMKVALDA 

       190        200        210        220        230        240 
ANGAAAVSAR NIFLDLNAEI AVIGDQPDGL NINAGVGSTH PEQLQALVRE SGSAIGLAFD 

       250        260        270        280        290        300 
GDSDRLIAVD ENGDIVDGDK VMYIIGKYLS QKGELAKNTI VTTVMSNLGF HKALDREGIN 

       310        320        330        340        350        360 
KAVTAVGDRY VVEEMRKNGY NLGGEQSGHV IIMDYNTTGD GQLTAIQLTK VMVETGKSLS 

       370        380        390        400        410        420 
ELAAEVTIYP QKLVNIRVEN SMKDKAMDVP AIAAIIEKME AEMAGNGRIL VRPSGTEPLL 

       430        440        450 
RVMAEAPTDD EVNYYVDTIA DVVRAEIGLD 

« Hide

References

[1]"Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus."
Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. expand/collapse author list , Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.
Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-250 / LMG 18311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000023 Genomic DNA. Translation: AAV60885.1.
RefSeqYP_139700.1. NC_006448.1.

3D structure databases

ProteinModelPortalQ5M3V8.
ModBaseSearch...

Protein-protein interaction databases

STRING264199.stu1251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV60885; AAV60885; stu1251.
GeneID3165474.
KEGGstl:stu1251.
PATRIC19804065. VBIStrThe97850_1234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14316.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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_STRT2
AccessionPrimary (citable) accession number: Q5M3V8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 1, 2005
Last modified: May 1, 2013
This is version 57 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