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Q31HG3 (GLMM_THICR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 55. 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:Tcr_0814
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira

Protein attributes

Sequence length444 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 – 444444Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000305688

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31HG3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 83A5BDE774A7E0A0

FASTA44447,701
        10         20         30         40         50         60 
MKKEKKYFGT DGIRDQVGKG LICPDKILKL GWATGKVIKD HGESVVMIGK DTRISGYMFE 

        70         80         90        100        110        120 
SALEAGFIAA GVDVMLLGPM PTPAVAYLTQ TFHADAGIVI SASHNPHHDN GIKFFSAKGQ 

       130        140        150        160        170        180 
KISDAIEHEI EAAYEQDLSI VSSSDLGRAK RIDDAAGRYI EFCKSTYEGA KKLDGFKIVL 

       190        200        210        220        230        240 
DCAQGATYHI APMVFKELGA EVVAIGVEPD GININQNCGA TDLAQLQARV VAEKADFGIA 

       250        260        270        280        290        300 
FDGDGDRVMM VDAQGDVVDG DEILYILATG TNLPIKGVAG TLMSNLGLEN ALKEKGIELV 

       310        320        330        340        350        360 
RTQVGDRYVM EALREKGWVL GAESSGHVLC LNKTTTGDGI VAALQVVSIM VNSGKTLTEL 

       370        380        390        400        410        420 
RQGMTKYPQI LQNVRVESKV GLNTNAALKK AVQDSEERMG GKGRVLIRAS GTEPLIRVMV 

       430        440 
EGDSRSMIES EVKSLVELVK TEFC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000109 Genomic DNA. Translation: ABB41410.1.
RefSeqYP_391084.1. NC_007520.2.

3D structure databases

HSSPHSSP built from PDB template 2DKD based on UniProtKB Q9P4V2.
ProteinModelPortalQ31HG3.
ModBaseSearch...

Protein-protein interaction databases

STRING317025.Tcr_0814.

Proteomic databases

PRIDEQ31HG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB41410; ABB41410; Tcr_0814.
GeneID3762141.
KEGGtcx:Tcr_0814.
PATRIC23973568. VBIThiCru83387_0843.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAHEGNEVD.

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_THICR
AccessionPrimary (citable) accession number: Q31HG3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 55 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