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C1B058 (GLMM_RHOOB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 20. 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:ROP_62320
OrganismRhodococcus opacus (strain B4) [Complete proteome] [HAMAP]
Taxonomic identifier632772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length445 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 MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

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: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000185379

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
C1B058 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: AFA7E148E13901A3

FASTA44545,066
        10         20         30         40         50         60 
MGRLFGTDGV RGLANTELTA ELALQVASAA ATVLASPGSG GRKTAVVGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVVAGLTSAG VDVLNVGVLP TPAVAFLTAE LDAALGVMIS ASHNPMPDNG IKIFAAGGHK 

       130        140        150        160        170        180 
LDDEVEDRIE SVATGTATRR APTGAGIGRV HTVPDAADRY LQHLTTALPN RLDGLTVVVD 

       190        200        210        220        230        240 
CAHGAASDVA PAAYRAAGAT VVAINAEPDG LNINENCGST HLEGLQKAVV RHGADLGLAH 

       250        260        270        280        290        300 
DGDADRCLAV DAGGSLVDGD AIMTVLALGM RDAGELVDDT LVATVMSNLG LHIAMREAGI 

       310        320        330        340        350        360 
SLVTTAVGDR YVLEGLRSGG FSLGGEQSGH VVFPAFGTTG DGVLTGLRLM GRMAETGQPI 

       370        380        390        400        410        420 
AELASAMTTL PQVLVNVKVA DKRAVAASPV VLDAVLAAER SLGENGRVLL RPSGTEQLVR 

       430        440 
VMVEASDLEV ARKLADELAG TVASV 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP011115 Genomic DNA. Translation: BAH54479.1.
RefSeqYP_002783424.1. NC_012522.1.

3D structure databases

ProteinModelPortalC1B058.
ModBaseSearch...

Protein-protein interaction databases

STRINGC1B058.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7743759.
GenomeReviewsGene locus ROP_62320 in contig AP011115_GR.
KEGGrop:ROP_62320.
PATRIC23229861. VBIRhoOpa21106_6299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGVGSTHL.
ProtClustDBPRK14318.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
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_RHOOB
AccessionPrimary (citable) accession number: C1B058
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 20 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