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Q39HM9 (GLMM_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 53. 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:Bcep18194_A4441
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000301293

Sites

Active site1071Phosphoserine intermediate By similarity
Metal binding1071Magnesium; via phosphate group By similarity
Metal binding2461Magnesium By similarity
Metal binding2481Magnesium By similarity
Metal binding2501Magnesium By similarity

Amino acid modifications

Modified residue1071Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39HM9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 21C5165323BA0691

FASTA45147,240
        10         20         30         40         50         60 
MGRRYFGTDG IRGTVGEGPI TPDFVLRLGY AAGKVLASSA EVAAGSRPTV LIGKDTRVSG 

        70         80         90        100        110        120 
YMLEAALEAG FSAAGVDVML AGPMPTPGVA YLTRALRLSA GVVISASHNP YHDNGIKFFS 

       130        140        150        160        170        180 
ADGNKLPDDT EAAIEAWLDK PLECASSDGL GKARRLDDAA GRYIEFCKST FPAAFNLRGL 

       190        200        210        220        230        240 
KLVIDCAHGA AYQIAPHVFH ELGADVIPIG VAPNGFNIND GVGATAPDAL VRAVRANHAD 

       250        260        270        280        290        300 
LGIALDGDAD RLQVVDSTGR LYNGDELLYV LVKDRIATDG KVEGAVGTLM TNLAVEVALQ 

       310        320        330        340        350        360 
REGVKFVRAA VGDRYVLEQL REHGWQLGAE GSGHILSLDR HSTGDGIVSA LLVLAALKRS 

       370        380        390        400        410        420 
GQTLAQMLDG VTLFPQKLIN VRMKPGADWK GSTSIRAAID TAEAALAGSG RVLIRASGTE 

       430        440        450 
PVLRVMVEAQ QAADAVRHAE TIADAVRAAT T 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB08037.1.
RefSeqYP_368681.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39HM9.
ModBaseSearch...

Protein-protein interaction databases

STRING269483.Bcep18194_A4441.

Proteomic databases

PRIDEQ39HM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB08037; ABB08037; Bcep18194_A4441.
GeneID3749640.
KEGGbur:Bcep18194_A4441.
PATRIC19286260. VBIBurSp120713_2548.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK10887.

Enzyme and pathway databases

BioCycBSP269483:GHLS-1296-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_BURS3
AccessionPrimary (citable) accession number: Q39HM9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 22, 2005
Last modified: May 29, 2013
This is version 53 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