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A6W5X2 (GLMM_KINRD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Krad_0722
OrganismKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP]
Taxonomic identifier266940 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesKineosporiineaeKineosporiaceaeKineococcus

Protein attributes

Sequence length454 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 – 454454Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000087768

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity
Metal binding2511Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6W5X2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 6AC66FED425FE802

FASTA45446,270
        10         20         30         40         50         60 
MARLFGTDGV RGLANVDLTA DMALGLAVAA ASVLVEPGGN AHPRALVARD PRASGEFLSA 

        70         80         90        100        110        120 
AVVAGLASAG VDVLDIGVVP TPALAHLVDT SGADFGVMLS ASHNPMPDNG LKIFARGGTK 

       130        140        150        160        170        180 
LPDDVEDVVE RAYREGGGRR PTGAAVGRVH GGPDVEQDAQ DTYVAHLLST LPGGPGSLKG 

       190        200        210        220        230        240 
LHVVVDCANG AASAVSPRVL AEAGARVTTI FAAPDGLNIN DGCGSTHLGP VTAAVLAHGA 

       250        260        270        280        290        300 
DIGLAHDGDA DRCLAVDARG NAVDGDQIMA VLTLALRDRG QLTDDTLVAT VMSNLGLRLA 

       310        320        330        340        350        360 
MQREGVTMVE TGVGDRYVLE ALNAGGWSIG GEQSGHVVLP AHATTGDGVL TGLHLLARMA 

       370        380        390        400        410        420 
ETGRSLEDLT GVVQRLPQVL VNVRGVDKSR AGSDAELLGA VADAERELGE TGRVLLRPSG 

       430        440        450 
TEPLVRVMVE AAHTDHAQGV ADRLADVVRK RLAL 

« Hide

References

[1]"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000750 Genomic DNA. Translation: ABS02211.1.
RefSeqYP_001360475.1. NC_009664.2.

3D structure databases

ProteinModelPortalA6W5X2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6W5X2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5334034.
GenomeReviewsGene locus Krad_0722 in contig CP000750_GR.
KEGGkra:Krad_0722.
NMPDRfig|266940.1.peg.1871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHBG644964.
OMACANGPSA.

Enzyme and pathway databases

BioCycKRAD266940:KRAD_0722-MONOMER.

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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_KINRD
AccessionPrimary (citable) accession number: A6W5X2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 36 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