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C0QGV9 (GLMM_DESAH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 30. 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:HRM2_25140
OrganismDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2) [Complete proteome] [HAMAP]
Taxonomic identifier177437 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium

Protein attributes

Sequence length463 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 – 463463Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000215486

Sites

Active site1011Phosphoserine intermediate By similarity
Metal binding1011Magnesium; via phosphate group By similarity
Metal binding2561Magnesium By similarity
Metal binding2581Magnesium By similarity
Metal binding2601Magnesium By similarity

Amino acid modifications

Modified residue1011Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0QGV9 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: EF96AB514DD2E794

FASTA46349,305
        10         20         30         40         50         60 
MGKLFGTDGI RGFANIYPMT VEVALKTGRA VARFAKEHGG TVVIIGRDTR RSGDMLEAAL 

        70         80         90        100        110        120 
AAGISSMGIN VLEAGVIPTP GVAFLTATVK GAGAGVVISA SHNPFHDNGI KVFKSGGLKL 

       130        140        150        160        170        180 
TDPEEAKIES YIFDAGPDRA DSSICEPKTS DSAIEPGTIS TISNASAQYA NFLTSCYQRD 

       190        200        210        220        230        240 
LDKNTPDQPL KIVVDCSNGA SFKVAPMVFP TLGFETQFIF DTPDGKNINH NCGSQHTETL 

       250        260        270        280        290        300 
AKRVISTGAD LGLAFDGDAD RLIAIDEQGV KLTGDKILAI CANHAKAQGR LTNNLVITTV 

       310        320        330        340        350        360 
MSNIGLSKAL ERLGIDHIKT GVGDREVLKE MWATGAVMGG EDSGHMIFSE FHSTGDGILS 

       370        380        390        400        410        420 
ALCLIRVMVD TNKSLSDLAT IMTVYPQVLM NVEVDPSRPD FMKIETIARE IKRVEQALNS 

       430        440        450        460 
SGRVLVRYSG TQPLLRVMVE GPDLEATKSH CQSICDAIKQ ASI 

« Hide

References

[1]"Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate reducer oxidizing organic carbon completely to carbon dioxide."
Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.
Environ. Microbiol. 11:1038-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43914 / DSM 3382 / HRM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001087 Genomic DNA. Translation: ACN15608.1.
RefSeqYP_002603772.1. NC_012108.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING177437.HRM2_25140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN15608; ACN15608; HRM2_25140.
GeneID7502304.
KEGGdat:HRM2_25140.
PATRIC21684731. VBIDesAut25181_2629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAAQYSNIC.

Enzyme and pathway databases

BioCycDAUT177437:GHLR-2589-MONOMER.

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_DESAH
AccessionPrimary (citable) accession number: C0QGV9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 30 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