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A5U8B7 (GLMM_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:MRA_3482
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length448 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 – 448448Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_0000301343

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
A5U8B7 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 1A796BAC81742A04

FASTA44845,873
        10         20         30         40         50         60 
MGRLFGTDGV RGVANRELTA ELALALGAAA ARRLSRSGAP GRRVAVLGRD PRASGEMLEA 

        70         80         90        100        110        120 
AVIAGLTSEG VDALRVGVLP TPAVAYLTGA YDADFGVMIS ASHNPMPDNG IKIFGPGGHK 

       130        140        150        160        170        180 
LDDDTEDQIE DLVLGVSRGP GLRPAGAGIG RVIDAEDATE RYLRHVAKAA TARLDDLAVV 

       190        200        210        220        230        240 
VDCAHGAASS AAPRAYRAAG ARVIAINAEP NGRNINDGCG STHLDPLRAA VLAHRADLGL 

       250        260        270        280        290        300 
AHDGDADRCL AVDANGDLVD GDAIMVVLAL AMKEAGELAC NTLVATVMSN LGLHLAMRSA 

       310        320        330        340        350        360 
GVTVRTTAVG DRYVLEELRA GDYSLGGEQS GHIVMPALGS TGDGIVTGLR LMTRMVQTGS 

       370        380        390        400        410        420 
SLSDLASAMR TLPQVLINVE VVDKATAAAA PSVRTAVEQA AAELGDTGRI LLRPSGTEPM 

       430        440 
IRVMVEAADE GVAQRLAATV ADAVSTAR 

« Hide

References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ75267.1.
RefSeqYP_001284829.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U8B7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5U8B7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000065907; EBMYCP00000064017; EBMYCG00000065902.
GeneID5215364.
GenomeReviewsGene locus MRA_3482 in contig CP000611_GR.
KEGGmra:MRA_3482.
PATRIC18147406. VBIMycTub106795_3888.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00050000015909.
HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycMTUB419947:MRA_3482-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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_MYCTA
AccessionPrimary (citable) accession number: A5U8B7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 34 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