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C6BTS9 (GLMM_DESAD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 27. 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:Desal_1797
OrganismDesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763) [Complete proteome] [HAMAP]
Taxonomic identifier526222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length449 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. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

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 – 449449Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000215485

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
C6BTS9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 0A7A095BA35530D4

FASTA44949,380
        10         20         30         40         50         60 
MSKRLFGTDG LRGQVNIFPM TAEVALRMGL AAGSYFRNGK QRHKVIIGKD TRLSGYVFES 

        70         80         90        100        110        120 
ALTSGLCAMG MDVFQVGPMP TPAVSFLTRN MRADLGIVIS ASHNPFMDNG IKFFDSSGHK 

       130        140        150        160        170        180 
LPDAVEDEIA DMVLSQDTQW DYPQAEKVGR AYKIEDARGR YIVYLKYSFP QDMTLNGVKL 

       190        200        210        220        230        240 
VLDCANGAAY SLGHMFEELG AEVVRIGDKP NGLNINDKCG SLYPDILGQR VVEEHADLGL 

       250        260        270        280        290        300 
ALDGDADRLI VVDEKGQVLD GDVIMAMCAA DLMERGKLNH NMLVATVMSN MALENFMKEN 

       310        320        330        340        350        360 
GGSLLRTPVG DRYVVEAMRR EGAILGGEQS GHLIFKEFST TGDGLLAALQ LLRILCVKNR 

       370        380        390        400        410        420 
PLSELSGLLE LYPQKLQNVH VKRKRPFEEV PAVQDALKQV EQELAGKGRV LLRYSGTESV 

       430        440 
ARVMVEAEDS SKVELYTSEL AGVLEEHLR 

« Hide

References

[1]"Complete sequence of Desulfovibrio salexigens DSM 2638."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. expand/collapse author list , Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001649 Genomic DNA. Translation: ACS79859.1.
RefSeqYP_002991398.1. NC_012881.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING526222.Desal_1797.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS79859; ACS79859; Desal_1797.
GeneID8092898.
KEGGdsa:Desal_1797.
PATRIC21759091. VBIDesSal121003_1805.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
ProtClustDBPRK14314.

Enzyme and pathway databases

BioCycDSAL526222:GHES-1825-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_DESAD
AccessionPrimary (citable) accession number: C6BTS9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 29, 2013
This is version 27 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