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Q67T14 (GLMM_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:STH194
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XVIII. Incertae Sedis › Symbiobacterium ›

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-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 – 447447Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000147984

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67T14 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B89FFC086FD70B8E

FASTA44747,198
        10         20         30         40         50         60 
MPRMFGTDGV RGVANTEDLS PELAFALGRA AATLARERSG GRVVGVIGRD TRRSGPMLAA 

        70         80         90        100        110        120 
ALSAGICSAG GDVVDLGVIT TPGVAYVTTH LKADFGVMIS ASHNPAPDNG IKFFSGDGYK 

       130        140        150        160        170        180 
LPDEVEDQLE ALVKARPDTM PRPTGAELGS IRQSPEAVEA YVEHLVSTGS PLSGLRVVVD 

       190        200        210        220        230        240 
CGHGAAYRLS PEVLRRLGAE VIALNTAPDG LNINAGCGST HPEALQEAVR AHGADAGIAH 

       250        260        270        280        290        300 
DGDADRCIAV DERGELVDGD QIMAICALDL KARGQLPNDT LVTTVMSNMG LEMLMRRHGI 

       310        320        330        340        350        360 
RLVRTKVGDR YVLEEMLKGG HGLGGEQSGH VIFGALSTTG DGILTAVQLL SIVAREKQPL 

       370        380        390        400        410        420 
STLAGRMQRL PQWLENVRVG RKEGWEQNQA IQAAIARAEA EMAGQGRVLV RASGTEPLIR 

       430        440 
VMLEGTDMAH IQRLAASIAE VIRTELQ

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References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006840 Genomic DNA. Translation: BAD39179.1.
RefSeqYP_074023.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67T14.
ModBaseSearch...

Protein-protein interaction databases

STRING292459.STH194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD39179; BAD39179; STH194.
GeneID2980805.
KEGGsth:STH194.
PATRIC23778447. VBISymThe116959_0195.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.

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. 2 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_SYMTH
AccessionPrimary (citable) accession number: Q67T14
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 58 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

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